UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
|
|---|---|---|
B7LCS2 | MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVEVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINELIDDLMDHISLENNVLFPRALAGE | Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions. Homodimer. Belongs to the RIC family. YtfE subfamily. |
Q7A8T9 | MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVEVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHARHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHNTNNVTPPPEACTTWKAMYNGINELIDDLMDHISLENNVLFPRALAGE | Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions. Homodimer. Belongs to the RIC family. YtfE subfamily. |
B5Z3G5 | MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVEVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHARHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHNTNNVTPPPEACTTWKAMYNGINELIDDLMDHISLENNVLFPRALAGE | Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions. Homodimer. Belongs to the RIC family. YtfE subfamily. |
B7NUC3 | MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVDVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINELIDDLMEHISLENNVLFPRALAGE | Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions. Homodimer. Belongs to the RIC family. YtfE subfamily. |
B7MSU8 | MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVDVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINELIDDLMEHISLENNILFPRALAGE | Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions. Homodimer. Belongs to the RIC family. YtfE subfamily. |
B7M9H2 | MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLSRAAARKELDVEVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINELIDDLMDHISLENNVLFPRALAGE | Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions. Homodimer. Belongs to the RIC family. YtfE subfamily. |
C4ZR85 | MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVEVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINELIDDLMDHISLENNVLFPRALAGE | Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions. Homodimer. Belongs to the RIC family. YtfE subfamily. |
B1XDV9 | MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVEVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINELIDDLMDHISLENNVLFPRALAGE | Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions. Homodimer. Belongs to the RIC family. YtfE subfamily. |
A8A7W5 | MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVEVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINELIDDLMDHISLENNVLFPRALAGE | Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions. Homodimer. Belongs to the RIC family. YtfE subfamily. |
A1AJC0 | MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVDVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINELIDDLMEHISLENNVLFPRALAGE | Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions. Homodimer. Belongs to the RIC family. YtfE subfamily. |
Q0T9H5 | MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVEVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINELIDDLMEHISLENNVLFPRALAGE | Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions. Homodimer. Belongs to the RIC family. YtfE subfamily. |
Q8FAH0 | MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVDVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINELIDDLMEHISLENNVLFPRALAGE | Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions. Homodimer. Belongs to the RIC family. YtfE subfamily. |
B1ISZ1 | MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVEVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINELIDDLMDHISLENNVLFPRALAGE | Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions. Homodimer. Belongs to the RIC family. YtfE subfamily. |
Q2M696 | MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVEVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINELIDDLMDHISLENNVLFPRALAGE | Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions. Homodimer. Induced by nitric oxide. Negatively regulated by Fnr and Fur, but no obvious Fnr or Fur binding sites were found, suggesting that this regulation could be indirect. Mutants show a severe growth impairment under nitrosative and oxidative stress conditions. Mutation increases the sensitivity of the bacterium to iron starvation, increases the intracellular levels of free iron, and decreases the activity of several iron-sulfur-containing proteins. Belongs to the RIC family. YtfE subfamily. |
B7NGE7 | MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVEVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINELIDDLMEHISLENNVLFPRALAGE | Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions. Homodimer. Belongs to the RIC family. YtfE subfamily. |
O32069 | MRLDKLLANSGYGSRKEVKAVVKAGAVMIDGKPAKDVKEHVDPDTQEVTVYGEPVDYREFIYLMMNKPQGVLSATEDSRQQTVVDLLTPEEMRFEPFPAGRLDKDTEGFLLLTNDGQLAHRLLSPKKHVPKTYEVHLKSQISREDISDLETGVYIEGGYKTKPAKAEIKTNDSGNTVIYLTITEGKYHQVKQMAKAVGNEVVYLKRLSMGRVSLDPALAPGEYRELTEEELHLLNEPQA | a uridine in RNA = a pseudouridine in RNA Belongs to the pseudouridine synthase RsuA family. |
A8MT66 | MNLFCISLEGSMDSLYEPIPEQQANQENMSSRTDSPIPPFGESEQTPNNLFVGVSNLENAKPKKRKLFRRFMSENKIFEGKTVNDKIWQEHSKHKNDSHIRRPCQLKDLNENDFLSNNIHTYQGKTLQGTSYQVTSECWSPFHYQRHVETTVDELVRHFFPDVTI | Product of a dubious gene prediction. |
A8MWP4 | MQRPHRRQSQMDAASTRAPPRPSAPQQGRRQPSMPGSAQCHHRPDPHPPAPGKKKSSPVGRFFPASAMAPPWLPGIVSAAQLKPVLSDLPPHCTRAQCQPLTQRPHSLHLQDSRNASSLPHKGWRCNFPLQGPAGLTHKSACVGRMGHCCGSAGNVPELSPRPASPRGQQVTQDGPLQTPELPSECNVGPVMSRQPFPEQSQQGECAIDPRGPPRLELSWGEDPLSGV | Could be the product of a pseudogene. |
Q19753 | MKLKKRPMKLAAKPKPKQPTEKLGKAQKMKLKEDNLASAEKIMAQFESGAVHTNKKKQAQNGAAKPVAHKPANPENSNQKRQFKKILGQDGILVKHQEGTKWYSYQIDHVHDEKTEKMNASEIQKLLEEGKDEMAQDAALLQTKEKQDNGSEASWLYSVISKGTATDKRTAMQLQMHKSPVHSLEYIEKLIASCKKQGTRDVVDIIPILEDVFINHCLPENRKLIPFSKRALRELTELSSGNQRLRRKILLMWAFEHELKILYQQFIETLVEIIKRPLEEVIKRSLKTLANCLMGRPESENLILSALVNAFGHPNYKIGAFTVVLLEGISRKHPAMRIVMVEEIERLAFRKNVNERAHLYAMTFLSQMKFSKKDSDLCCRLMSIYLSLFKTIVGKKITDNRLLPIILAGANRAFPFAKDADKLLEDVKDVYFLAHNSNYRTAIPALKLLFQFHKMNDYVSDRFYNALYRKLLDNCPAGAYAQLLKLMFDTMKEDSSAQRVRTFVKRLLQVAVNSQPDFTASILILISRLQKLRGTTEKLVVLSKDIDPAARVVAQMQNDEDDEERYVDLDVEGNEISRNGVKKEEKEEEDIVIEENEDEDKKKVQPGKLGASSSGGWVHRSIGARGAKTPYDSVARNPLFVDASHTADSELLLLSKHYHPSVAVFAKALMEGREINYGGEALNDFTLMAFLDRFAFRNPKDVTKTTGTRIVRKKAHDPWGVRKLAVGSNEYTQKRREEIPADERFLHRYTSSLQKEKKVKKENGDDDWEYAESVSSAEFDQLLERFEPGELNEEFDIDYSKEFGAEKSKRNKKKDVEEDDVDMDEDDDIDLNDLNEEEDGGMEDDDEDDGDMDDDDEDDEDAEDDDEVDDDDEDDDEDGGFGGKSSANIFGDADESSDEEIGANDYEMAGDKFAEMLEDLEEDDGKRGKKKGGKKRGSTGGFKRGGAKKFRKR | Belongs to the CBF/MAK21 family. |
Q7CEG5 | MRTLVMVACAVSLAACSSPPKPPTVSGRHRIPINSPAAQEELRLQVFPQEPTAQATMWPARPPKQTVSVYFPQDVTVFRPTSAQINQLHTLLWPVPKHINVRGLTDNNCPPPGDTQVARVRALAIYNWLINQGVSASRITISYAPVKDYASNAPLSPGRVLNRRVDIEILRK | The VirB system could be required for the establishment of the replication niche in the host. Specifically induced within macrophages by phagosome acidification. Induced at 37 degrees Celsius in minimal medium, suggesting that nutritional stress is a regulating signal. Transcription of the operon is maximal in early exponential phase. |
Q9ZNK0 | MSGHSKWHNIQAKKSKVDAKRGKIFTKIGKEIAIAAKNGGPNPDANPKLRDVIAKAKANNMPKDSIERAIKKAAGELAGVNYEEILYEGYGPDGIAVLVQALTDNKNRSAGNVRHAFSKHGGNLGSTGCVSFMFQTKGQIVIEKNDELDEEELMMMALECGAEDFQSEDEVYIITTSPEDFGSVRETLEEKGLEFLEAEVKSIPDTYTVIDENTAGKFQKMLDVLEDDEDVQDVYHNAEFPEGWEE | Belongs to the TACO1 family. |
O80832 | MYQSMNLSFSSNFTNLSFLKPRLYSGISARAPKSLHFKFNPSCVSSGPKSDDSPLSEKLISLLKAVPNWSDGIKERRMQQKRSLYTHENWVRHRSSLRHLRHVSSSPSSRVILSLIPPVFFFTTVAILIAGYNSAVDLDWLPDFFPVLRASPLPYQLTAPALALLLVFRTEASYSRFEQGRKAWVKIISGTNDLARLVISSVHGSGDELIIRDALLRYIVAFPVALKCHVIYGSDIASDLKNVIEVDDLSLILQSKHRPRCVIQFISQSLQLLNLDSTKIDMLETKMMQLQEGIGVCEQLMGIPIPLSYTRLTSRFLVLWHLTLPVILWDDCHWNVVPATFISAASLFCIEEVGVLIEEPFSMLALDELCAMVLSNSDEAVESKEVIRNRIIAKKRILEIKHSSNGWHKS | Belongs to the UPF0187 family. |
Q93YZ0 | MYQSMNLSVSSNFTHRSLLESRFPIFSTGFRKSVNLKPPRVSSGPESNDSGHETLTDKLIHLLRAVPDWADEIKERGMQQKRSLYTHEKWVEHRSSLRHVRHLLSSFSSRVILSLIPPVFFFTSVAVVIASYNSAVALDWLPGIFPILRSSSLPYQLTAPALALLLVFRTEASYSRYEEGRKAWVGIIAGTNDLARQVICSVDSSGDELIIKDLLLRYIAAFPVALKCHVIYGSDIARDLRNLIEADDLSLILQAKHRPRCVIEFISQSIQLLKLDDAKRDLLESKMLHLHEGIGVCEQLMGIPIPLSYTRLTSRFLVFWHLTLPIILWDECHWIVVPATFISAASLFCIEEVGVLIEEPFPMLALDELCDLVHSNIQEAVKSEKVIRNRIIAKIKLHEFKHSSNGRHRS | Belongs to the UPF0187 family. |
O87971 | IDRKLERYDSPRYTYMVIDKKNPVDVFIVTSYPDEWADIYTSQNYQHIDPIVLTAFKRISPFAWDENITILSDLKSSKIFALSKKYNIVNGFTFVLHDHMNNLAMLSLIMDNNADKGLNSRIESDKDRLQMNLIKIHEKMLMLEQNKLGVSNGKNTDTSGKGILSPRENEVLHWASMGKTYPEIALIAGITTRTVKHHMGNVVKKLGVINARQAIRLGVELELIKPVLV | Probable transcriptional activator. Binds to an autoinducer molecule. Belongs to the autoinducer-regulated transcriptional regulatory protein family. |
Q795K9 | MALNKPKIVILGAGYGGLMTVTRLTKYVGPNDADITLVNKHNYHYETTWMHEASAGTLHHDRCRYQIKDVINQSRVNFVQDTVKAIKIDEKKVVLANGELQYDYLVIGLGAVPETFGIKGLKEYAFPIANINTSRLLREHIELQFATYNTEAEKRPDRLTIVVGGAGFTGIEFLGELAARVPELCKEYDVDRSLVRIICVEAAPTVLPGFDPELVDYAVHYLEENGVEFKIGTAVQECTPEGVRVGKKDEEPEQIKSQTVVWAAGVRGHPIVEEAGFENMRGRVKVNPDLRAPGHDNVFILGDSSLFMNEDTERPYPPTAQIAMQQGITVAKNLGRLIKGGELEEFKPDIKGTVASLGEHNAVGVVYGRKLKGTPASFMKKVIDNRSLFMIGGLGLTLKKGKFKFF | Binds 1 FAD per subunit. Belongs to the NADH dehydrogenase family. |
O32131 | MPRYRGPFRKRGPLPFRYVMLLSVVFFILSTTVSLWMINGSIKPVLMDIGEMETKRIATEVIQDSIEDYMSDSENMKDMFQMNSDENGNLTTIDFNTQVVNSVKTKVTKQLQAHLKEMETHTGHSGASENIMINIPLGQVTGNSLLGNLGPKIPVRFNLIGDAFTDVKTKIKPYGINNALIDISIFVEIKVKVIIPFASKTAVVTNNVPVSIKAVQGEVPQFYNGSGGSGVTPSVQLPSSKENGADSKKEKSSK | Required for sporulation. Expression controlled by a sigma-E-regulated promoter which needs the sigma-E factor for the binding of the RNA polymerase and subsequent transcription. |
O32133 | MKEKLRLYHTNDLHSHFENWPKIVDYIEQKRKEHQSDGEETLVFDIGDHLDRFQFVTEATFGKANVDLLNRLHIDGAAIGNNEGITLPHEELAALYDHAEFPVIVSNLFDKNGNRPSWAVPYHIKSLKNGMSIAFLGVTVPYYPVYDKLGWTVTDALESIKETILEVKGQADIIVLLSHLGILDDQAVAEAVPEIDVILESHTHHLLEDGQVVNGVLLASAEKYGHYVGCVEITVDSVQRSINSKTASVQNMAEWTGESAETKAFLNEKEREAEEKLSDAVAELAQDAEVKWFEESELPLLLAYALKEWCETDISMVNSGVILGPLKAGPVTKLDLHRICPHPINPVAVRLTGEELKETIVHAASEQMEQLRIKGLGFRGEVMGKMVYAGVEVETKRLDDGITHVTRITLNGEDIEKHKQYSVAVLDMFTLGKLFPLIRDAAEKEYFMPEFLRDLLAWKLAQ | Binds 2 divalent metal cations. Belongs to the metallophosphoesterase superfamily. |
O32134 | MSFVILVVLGLIAGTVGSLIGLGGGIVIVPSLMFLSTVTQLFQDVTPQVAIGTSLLVIIFTGLSSTLAYIKYKTVDYKSGLIFFIGSGPGSMIGAYVSKLFNSNSFSVWFGIFMILISLSLMLKAKARPINKAHKGIIRTFQDDAGEPYTYSYQASVGIAIAFVVGFLGGLFGIGGGSLMVPAMMLLFLFPPKVAVATSMFIIFLSSMTGSVSHMISGHVNWLYALALVPGAWFGGKLGAAINRKMQTKTIVMIMRIVLILIGCQLIYEGIFS | Belongs to the 4-toluene sulfonate uptake permease (TSUP) (TC 2.A.102) family. |
O32135 | MIYIGLTGWGDHDSIYPPKTASQKKLQAYSSHFPIVELDASFYAIQPARNNEKWVKETPETFQFIVKAYQGMTGHQRGEIPFDSKEEMFDAFKVSLTPYLHSNKLAMVLFQFPPWFDCKKENVAYLRWCKHQMGDIPCALEFRNRSWFSPPFYEQTLSFMKAEGWIHSVCDEPQIGEGSVPTVLRATDENKTLVRFHGRNKQGWMKPDGGKNWREVRYLYRYNQQELEDWKKHLNELQQQCKDVFVLFNNNSGGDAADNGKQMLELLDIEYSGLAPRQLDLF | Belongs to the UPF0759 family. |
P43051 | MAYNKESKQRRFLFAIDLDGTLLADSANGTVHPKTEEAIKKAVAQGHIVSIITGRPWRSTLPVYEKLGLNAIVGNYNGAHIHNPADPFFIPAITYLDLNEVLYILGDEKVKKEITNYAIEGPDWVQLMHRDPNLERVFGFNQATKFRECINLEKIPLKPTGIVFDVKPDTDVLELLTYLKRRYGDLGEFSSWSKGEGLSPVFDITSIGIDKGKVISLIMRYYNIDIDDTVAMGDSYNDLSMYNVANVCVSPANAEPLIKKMSTVVMKQTNKEGAVGYFIDHS | Belongs to the HAD-like hydrolase superfamily. Cof family. |
D6VW45 | MAKGGSLYIVGIFLPIWTFMIYIFGKELFLIRKYQKIDSTYTALSQRVKEQYDTSRRRNYFPKVKLSRNSYDDYTLNYTRQNDSDSFHLRENATILMLVRNSELEGALDSMRSLEDRFNNKYHYDWTFLNDVPFDQDFIEATTSMASGKTQYALIPPEDWNRPQWINDTLFEERLRVMEDEGVLYGGSKSYRNMCRFNSGFFFRQSILDNYDYYFRVEPNVKYYCDFPYDPFRVMRLKGKKYGFVISLYEYEETIPTLWDAVEEYLVASEETILRKEDSAYAFLTDSGLVGKHYPVVEANSDYNLCHFWSNFEIGDLNFFRSDEYKHFFETLDAKGGFYYERWGDAPVHSIGVSLLLRPDEIIHFDELGYFHSPFGTCPASYAVRLDQRCRCKSDDESVIDITPHSCLMRWWKNGSGKYFLKEEQDEI | Possible glycosyltransferase involved in N-linked glycosylation. Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage. Protein modification; protein glycosylation. Present with 6400 molecules/cell in log phase SD medium. Belongs to the glycosyltransferase 15 family. |
O32151 | MASLTFEHVKKSYHSQLTVKDFDLDVKDKELLVLVGPSGCGKSTTLRMVAGLESISEGNLLIDGERVNDLPPKERDIAMVFQNYALYPHMTVFDNMAFGLKLRKMAKQEIAERVHAAARILEIEHLLKRKPKALSGGQRQRVALGRSIVREPKVFLMDEPLSNLDAKLRVTMRTEISKLHQRLEATIIYVTHDQTEAMTMGDRIVVMNEGEIQQVAKPHDIYHYPANLFVAGFIGSPGMNFLKGIIEQQHGELFFTNSSIRLHIPEEKAKRLKEKGYAGEQMIAGVRPEHITQMTGNDQLFDSVFQANVEVNENLGSELIVHVMAGDERLKVRLDGNTRIDAGDSIQLSVKMDHVVFFDAETEEAVY | Belongs to the ABC transporter superfamily. |
O32154 | MLPQKKTDSFRLEPVPDQHIEVKDKPRRKWYIGETSVWVFLFLYLIAIAYPLLWMVMSAFKNSDDIFEHSWSLPSSWHPENFVSAWNQGISSYFMNSVIVTALTCVITVFISAWAAYGLSRFEFKGKGFFLVLCLGGLMLTPQVSLVPLYSIIQSLGLYNTYWALILPYAAYRIPFTIILIRSYFLSISKELEEAAYLDGCTSFGVFFRIFLPMSVPILVTSGILTAYHTWNEFMFAIIFIDDENLRTIPAGLMQFRDALQTDWGVLLAGLTISAAPIIILFLLMQKYFVRGIASGSVKG | Probably part of the binding-protein-dependent transport system YurMNO. Probably responsible for the translocation of the substrate across the membrane. Belongs to the binding-protein-dependent transport system permease family. MalFG subfamily. |
O32155 | MVNQNKIIPYLFLVPALVFLLFVYIPIFENVFLSLFQWSSFSPEKTFIGLKNYVELFHDPVFYQALTNNVLYAVISIVCQVFGGLILAAVLEDKLVRKWSPFFRTVFFLPVVISMTVIALLFDFIYNPETGLLNQLLQAIGLDQLTRAWLGDDSTAMLSVIFVSQWQSVGYIAMLYIVSIQKIPDELYEAARLDGAGKIQQFFHITVPQTKEMSFVAVVMTLTGAFTVFNEPYILTGGGPGKASEVLSTFLYKSAFTKDMMGYASAIATVVLIITLALSLMQMKFFKTGKEE | Probably part of the binding-protein-dependent transport system YurMNO. Probably responsible for the translocation of the substrate across the membrane. Belongs to the binding-protein-dependent transport system permease family. MalFG subfamily. |
O32156 | MKKMLLFLIIAAVSMLTIAGCSSQSSSADGKVTLKFFHRWPKEPEKSYFEEVVKEFEKDHPDIDIQIEAVLNDSYKDKIKVMLGTTSPPDIYFSWSDEFAFKFIRGNKALDLSSYYKNDTDWSSQLVQSQITPFTYENKQYGVPWQMDAKSFFYNKDIFQKLNLDPPKTWDELIDVSKKLKEHGYTPISFGTKATWTISHYIGTLNQRMVDEKTREKDYNAKTGEFTDEGYVKALEKLQELMPYFNKHVNSVDHEYVRQQFKSGKSAMIYAETAEIKLVEPVNLGMFPFPEISGQKGSSEALTGAPEGFMISSRTKHPKEAMEFLQFLTSKRMGEKLVKDVGKYSAVQGTATEENATAIQREAVQHIVDAKSMVPWFDMDVDVEVADAYLTGVQQMLGGDMTPQQVMKAVQKAAKQVRASAE | Probably part of the binding-protein-dependent transport system YurMNO. Belongs to the bacterial solute-binding protein 1 family. |
Q795G5 | MRFSGRFKGYNLQKFQKDLIAGIVVGVVAIPLGMAFAIASGVEPEYGLYTVVIAGICISLFGGSKYQIGGPTGAFVPILFGIIMQYGLENLLIAGFMAGVMLVLFGLFKLGKIMKFVPKPVIVGFTAGIAVLIFTEQIANFLGLRNVEKHENFHHNMFEIVQQLGTFNVYAILTAVIGLVILLVSAKVMPKVPGALLALLISTVVAVVFFPDRMATIGSTYGEIPRHLPEFQFPELTLDKMVMLFPAALVIALLGGLESILSAMVADNMKGSKHDSNKELVGQGIANMAAPLFGGIPATGAIARTATNIKNGAVSPVSGVVHGVVVLLVLLVFAPYASHVPLASMAPILMVVAWNMSERKEVANMLRLKNADSFILAATFALTVLFDLIIGVATGLLLAFVFFIRRMSEATRIHNQETHPVLAKREDPSVSMYAIEGPLFFGSIDSLESSLLEHVQKKPKTLILLMNKVHYMDTSAEAVLGNIMNRIKRHNGKLMIVGLQSQPKELLHKTGLFHKIGKQHFFDHHDEITG | Belongs to the SLC26A/SulP transporter (TC 2.A.53) family. |
Q9CE03 | MFNIEKLQSLAKYRWVIVIILALLFSALSVSIFHLPFLMTALVLSIVGLIFAYHKSVWLVLFILSNLPMLATTIFAYQHHFTTLDTVIFFIIFLLTIISSYLIARKADIIPKISWKYFPPLKIIIGFALLFLVSILTGIFAQIINQSPTTSNQDSLNELQKVIPIAVFATQTLAAGFLEELVYRVGIFEVIFKNQKYFAFLTALLLFAYMHGPTDLYSWLTYGLMSLVLTSLYAKYRNFYLNMSVHLLWNLFGLVIALVLK | Belongs to the UPF0177 family. |
Q795G6 | MKTICVFAGSNPGGNEAYKRKAAELGVYMAEQGIGLVYGGSRVGLMGTIADAIMENGGTAIGVMPSGLFSGEVVHQNLTELIEVNGMHERKAKMSELADGFISMPGGFGTYEELFEVLCWAQIGIHQKPIGLYNVNGYFEPMMKMVKYSIQEGFSNESHLKLIHSSSRPDELIEQMQNYSYPILEKKWTEI | Belongs to the LOG family. |
P45862 | MERKTVLYIAVSLDGMIAKEDGSIDWLDEFEGEGDNGYSDFYQTVDTVILGRSTYEHVKVLTPVFPYQDKTCYVFTGSPDSYQDEHVTFINEGARAFTARLKQEKGSNIWIAGGAELVNDFMKEDAIDEFIITVIPVVLGSGIPLFHELTNETKLRLKGTKQFGQAVQLHYVRA | To B.subtilis YyaP. |
P06629 | MLKIFTTQLTGIFSRIQDKESDAIEDGARLLAQAVISGHSIYLYGANELQGVFYEATESKEPFPSVKAFPENAEEVTESDRVLMFCSGTGTAEEQELAKELYEKGAGVVCVSPAAKDSAGIEQYCDVHIDSKLKMPLVPDEDGTRYGFPSLMTALYVYHALSFTLKEILQEYA | Was originally thought to be the spo0F protein. |
P45869 | MSILDILILLAPIFFVIVLGWFAGHFGSYDAKSAKGVSTLVTKYALPAHFIAGILTTSRSEFLSQVPLMISLIIGIVGFYIIILLVCRFIFKYDLTNSSVFSLNSAQPTFAFMGIPVLGSLFGANEVAIPIAVTGIVVNAILDPLAIIIATVGESSKKNEESGDSFWKMTGKSILHGLCEPLAAAPLISMILVLVFNFTLPELGVKMLDQLGSTTSGVALFAVGVTVGIRKIKLSMPAIGIALLKVAVQPALMFLIALAIGLPADQTTKAILLVAFPGSAVAAMIATRFEKQEEETATAFVVSAILSLISLPIIIALTA | Belongs to the auxin efflux carrier (TC 2.A.69) family. |
P39150 | MKYNYTVLLSAFTMSVLYSVIYIHSFIIAALITMAFYFLFPYLIFALPLQIMMNKKPKRFSPLYLLYYLAAAFIANAIIFGMLQPSGQSLFQNTAFYLFAVLTALIYWIWDSVLLQKKEA | Belongs to the UPF0715 family. |
P39156 | MKVAIASDHGGVHIRNEIKELMDELQIEYIDMGCDCGSGSVDYPDYAFPVAEKVVSGEVDRGILICGTGIGMSISANKVKGIRCALAHDTFSAKATREHNDTNILAMGERVIGPGLAREIAKIWLTTEFTGGRHQTRIGKISDYEEKNL | Negatively regulated by TnrA under nitrogen-limited conditions. Belongs to the LacAB/RpiB family. |
P39157 | MNELKQTWKTMLSEFQDQAELKQDQLFVLGCSTSEVAGSRIGTSGSVDIAESIYSGLAELREKTGIHLAFQCCEHLNRALVVEAETAKLFRLPTVSAVPVPKAGGAMASYAFKQMKSPVLVETIQADAGIDIGDTFIGMHLKPVAVPVRVSQNSLGSAHVTLARTRPKLIGGVRAVYECE | Negatively regulated by TnrA under nitrogen-limited conditions. Belongs to the UPF0340 family. |
P70960 | MKKRFSLIMMTGLLFGLTSPAFAAEKTETEAKAPANVAVLLDASGSMAKRIDGVSKFNSAKKEISKFASSLPEGTQVKMSVFGSEGNNKNSGKVQSCEAIRNVYGFQSFNEQSFLNSLNTIGPTGWTPIAKALNEAKSSFDQLDAKGEKVVYLLTDGEETCGGNPIKTAKELQKDNITVNVIGFDYKEGYKGQLNAIAKVGGGEYFPAYTQKDVEKIFTQQSLMLSK | To B.subtilis YwmD. |
P70961 | MKKLLAAGIIGLLTVSIASPSFAAEKQADTNVAVLFDGSGSMVQKTGGERKIDIAKKSVKSFAELLPKDTNLMLRVFGHAGNNKLSGKALSCSTTETIYGLHPYEGSLFDNSLSELKPTGWTPIAKALADTRKEFEAFDADGKNVVYLITDGEETCGGDPAAEIEKLRASNVDTIVNIIGFNFDVKGNEEMKQAAVAGGGEYISANSADEFEQAWEKEAQKFTE | To B.subtilis YwmC. |
Q794Z8 | MKIGIIGASGKAGNEILKEAKKRGHEVTAIVRNASKVQEQDVAILEKDVFELTAEDIKPFDAVVNAFGAAPGQEHLHVEAGRALISILKDAKHTRLLVVGGAGSLFVDEAKTTRLMDTPEFPKEYLPTASNQGENLKDLQQTDSISWTFLSPAAFFDPAGKRTGSYQKGKDNVIVNAKGDSYISYADYAIAVLDELEHPEHKNERFTVVSEAE | The N-terminus share sequence similarity with the dihydrodipicolinate reductase family. It however lacks the conserved C-terminal part, suggesting it has no dihydrodipicolinate reductase activity. |
O66423 | MLEVEKKIKQKLGIDETEVLSSLTSYRKKGKTYYKIVTYDSKTKQSRRYHVPRMFEEEILALWKQRQKYIEEERELEREVKSLLKKYGDAEKIKEILEKVAGESFDKAVSSYAIKTYTNKAKELFKSFKEDLIKLYREGVLKRLSVLQVLYLLANLKEISEDTERGSYFFKKGLNTIIKVAKNERIPNPFGTLKNDFFLSGKQTPYDFLLSNFLEELIGETLGELLEKEIEKLVAEEKAKEIEGKVKKLKEIVSWFETLPYEIKQIAKEVISDNVLDIAEKFYKDMKECNYSLDEAKAFLTSSPRDNLVNYMQYLKSI | To A.aeolicus AA07 and AA11. |
Q55480 | MGHKYDVYGMGNALVDMEFEVTPEQLASLGIDKGVMTLVEEARENELIAQLAQQRGKQSSGGSAANTLVSLAQLGGTGFYACKVGKDEAGAFYLQDLNDCGLDTNPHHETAGEGITGKCLVFVTPDADRTMNAFLGISGSLSVTEMDWSALKQSQYLYLEGYLVTSPSAKAACIEAKAIAEQSGVKTCLSLSDPNMAKFFQDGLKEMLGSGVDLLFANEAEALEMAGTSDLNQAIAYCKSIAKNFALTRGGAGSLIFDGENLLTIGTPKVQPIDTVGAGDMYAGGFLYGLTHGMDYEKAGQLASETAAKVVTCYGPRLDTEILQEILQSVQAV | Belongs to the carbohydrate kinase PfkB family. |
O66426 | MTYQNGVEVLLEEFLDYLTKEETICSLEIEKLKVSIDELEKETDEPRVLQGINYFRTAKEVYQLSRKAYETKEEVVSEALILWIYENLWKGFNVPKGYRKSDMVIFGAKFSPPPPYVVPNLIRTIVNWLRNEKTIDVVKKSIIFHTLFEVIHPFPDGNGRVGRILLNAILVENGLLNVAFRNREKYISALREAEEGAIVVVEKLSRGRKIDYSSITETVEYYGNLNVFDELIRTEMMHSLKVYSNIKQVFLTPEEAAKLLGLKNKDYVRVLIHRGKLKAVKEEGKWKIPLSEVVKNFEHKLKGEEFKLANNLFKGKLSPS | Probable adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein] ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate Belongs to the fic family. |
Q19297 | MLRILTVVLALVTIATVHAELSKKKEDKTLKDLEDKIVNDVMTHKVMVYSKTYCPWSKRLKAILANYEIDDMKIVELDRSNQTEEMQEILKKYSGRTTVPQLFISGKFVGGHDETKAIEEKGELRPLLEKAHALFTNRVPVPDNGA | Belongs to the glutaredoxin family. Monothiol subfamily. |
Q19405 | MPKGNKKPNEKKEELEKFAKELQGSDSDEDAVVIEQPTVEPKLPQNDSSSSNKIVLSQAEKDLLRTELDKTEEEISTLKQVLSARQKHAAELKRKLGLTPFSELSQDINRSLKTVTDTDAYQKTAEVAAATSDTVKEKWNDMRNSSLFKSFESKLGSALNNAKMAASTSIDHLAGAARGPSQTGTPVAEEAKPIS | Belongs to the TPD52 family. |
Q79CZ1 | MQNRKWILTSLVMTFFGIPILAQFLAVVIAMLGVGLAGIIEVCNILITPTIYLLLKIFMLALGALMLFFSGRVGNVPEFCYVGYDGVGFAVIP | Missing up to 410 C-terminal residues compared to orthologs. Extended N-terminus. |
P17776 | MSRLFFVCRKVR | Could be the product of a pseudogene. |
Q9K470 | MTNSSGRRRPDVTTVEIIGGPEALEIGLSDYDARWAETYLRHRRRILDALGADVDVEHIGSTSVPGLAAKPIVDIVVAVADITSEEDYLDALLAAGYELRVREPGHRLVRTPGRDVHVHVYERGAAAVHEYLLFRDHLRADADDRALYENVKRALFEQPWNDMNDYSDAKSDVILAIKSRAGAARR | Belongs to the UPF0157 (GrpB) family. |
P0DUS2 | MKKTFLPIFLVILLASYALANPQVTFSRDWGPGKK | Potently activates insect G protein-coupled receptor. It activates the ACP receptor (ACPR) from the mosquito A.aegypti (EC(50)=0.55 nM) with a potency comparable to that of the endogenous ligand. Has no activity on receptors of the closely related neuropeptides adipokinetic hormone and corazonin. In vivo, does not reveal any observable effects when injected into crickets (A.domesticus). Does not induce increase in intracellular calcium in mouse DRG neurons, suggesting that it does not induce pain. Expressed by the spine venom secretory cell. The spine is a cuticular structure containing at its base a single large nucleated venom secretory cell, as well as a central venom reservoir extending throughout the spine. It is an independent unit capable of producing, storing, and injecting venom. Spines are grouped by 50 to 100 in each of the eight venom scoli on the back of D.vulnerans caterpillars. Only secreted by caterpillars. Adult moth do not have spines. Extremely abundant peptide in the venom (almost one-quarter of all toxin-encoding transcripts, and the highest represented peptide by proteomics methods). Belongs to the limacoditoxin-1 (ACP-like) family. |
P82292 | DSTDGLLVKDKYLCGDLYGEEYGVIFPYLGLKTECLWTIKMDPLYRILLTVRDVHENCNKESLEIIEGPPESSNSRKICDTSHAEYTSCTNTMTVKYTRKPNHPAPDFFLIFRRVL | May be involved in the fertilization process. Homodimer; disulfide-linked. Seminal plasma. Belongs to the spermadhesin family. |
P0DUS3 | MKKTFLPIFLVILLASYALGNPQITFSKDWRPGKK | Potently activates insect GPCR. More precisely, it activates the ACP receptor (ACPR) from the mosquito A.aegypti (EC(50)=3.07 nM) with a potency comparable to that of the endogenous ligand. Has no activity on receptors of the closely related neuropeptides adipokinetic hormone and corazonin. In vivo, does not reveal any observable effects when injected into crickets (A.domesticus). Does not induce increase in intracellular calcium in mouse DRG neurons, suggesting that it does not induce pain. Expressed by the spine venom secretory cell. The spine is a cuticular structure containing at its base a single large nucleated venom secretory cell, as well as a central venom reservoir extending throughout the spine. It is an independent unit capable of producing, storing, and injecting venom. Spines are grouped by 50 to 100 in each of the eight venom scoli on the back of D.vulnerans caterpillars. Only secreted by caterpillars. Adult moth do not have spines. Extremely abundant peptide in the venom (almost one-quarter of all toxin-encoding transcripts, and the highest represented peptide by proteomics methods). Belongs to the limacoditoxin-1 (ACP-like) family. |
L9V568 | MSESEQRHAHQCVSCGINIAGMSAATFKCPDCGQEISRCSKCRKQSNLYECPDCGFMGP | Zinc-binding protein. Binds 1 zinc ion. Required for swarming. Involved in biofilm formation. Monomer in solution. Cells lacking this gene grow as the wild-type in complex medium and in synthetic medium with glucose as sole carbon and energy source, but the mutant cells are not capable of swarming and have severe defects in forming biofilms. |
Q7AMB9 | MSAQPVDIQIFGRSLRVNCPPDQRDALNQAADDLNQRLQDLKVRTRVTNTEQLVFIAALNISYELTQEKAKTRDYAASMEQRIRMLQQTIEQALLDQGRITEKTGQNFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
Q7CPU9 | MSAQPVDIQIFGRSLRVNCPPDQRDALNQAADDLNQRLQDLKVRTRVTNTEQLVFIAALNISYELTQEKAKTRDYAASMEQRIRMLQQTIEQALLDQGRITEKTGQNFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
A8GIS6 | MSAQPVDIQIFGRSLRVNCPPEQQDALNMAAVDLNERLQDLKVRTRVTNTEQLVFIAALNVCHELAQERLKTRDYASNMEQRIRMLQQTIEQALLEQGRISERQDAQFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
B2U0S7 | MSAQPVDIQIFGRSLRVNCPPDQRDALNQAADDLNQRLQDLKERTRVTNTEQLVFIAALNISYELAQEKAKTRDYAASMEQRIRMLQQTIEQALLEQGRITEKTNQNFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
Q31WH1 | MSAQPVDIQIFGRSLRVNCPPDQRDALNQAADDLNQRLQDLKERTRVTNTEQLVFIAALNISYELAQEKAKTRDYAASMEQRIRMLQQTIEQALLEQGRITEKTNQNFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
Q32BX2 | MSAQPVDIQIFGRSLRVNCPPDQRDALNQAADDLNQRLQDLKERTRVTNTEQLVFIAALNISYELAQEKAKTRDYAASMEQRIRMLQQTIEQALLERGRITEKTNQNFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
Q0T0Y8 | MSAQPVDIQIFGRSLRVNCPPDQRDALNQAADDLNQRLQDLKERTRVTNTEQLVFIAALNISYELAQEKAKTRDYAASMEQRIRMLQQTIEQALLEQGRITEKTNQNFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
Q3YXW0 | MSAQPVDIQIFGRSLRVNCPPDQRDALNQAADDLNQRLQDLKERTRVTNTEQLVFIAALNISYELAQEKAKTRDYAASMEQRIRMLQQTIEQALLEQGRITEKTNQNFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
Q2NRE3 | MSAQPVDIQIFGRTLRVNCPPEQQEALNQAAEDLNQRLQNLKVRTRVTNTEQLVFIAALNVCHELAQERLKTRDYAANMEQRIRLLQQTIEQALVEQGRITERPGNQFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
A1JPP1 | MSAQPVDIQIFGRSLRVNCPPEQQDALNMAAEDLNQRLQDLKVRTRVTNTEQLVFIAALNVCHELAQERLKTRDYASNMEQRIRMLQQTIEQALLEQGRISERQDAQFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
A7FF14 | MSAQPVDIQVFGRSLRVNCPPEQQDALNMAAEDLSQRLQDLKVRTRVNNTEQLVFIAALNVCHELAQERLKTRDYASNMEQRIRMLQQTIEQALLEQGRISDRQDTQFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
Q1CB49 | MSAQPVDIQVFGRSLRVNCPPEQQDALNMAAEDLSQRLQDLKVRTRVNNTEQLVFIAALNVCHELAQERLKTRDYASNMEQRIRMLQQTIEQALLEQGRISDRQDTQFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
B2K0R1 | MSAQPVDIQVFGRSLRVNCPPEQQDALNMAAEDLSQRLQDLKVRTRVNNTEQLVFIAALNVCHELAQERLKTRDYASNMEQRIRMLQQTIEQALLEQGRISDRQDTQFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
Q8CZW1 | MSAQPVDIQVFGRSLRVNCPPEQQDALNMAAEDLSQRLQDLKVRTRVNNTEQLVFIAALNVCHELAQERLKTRDYASNMEQRIRMLQQTIEQALLEQGRISDRQDTQFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
A9R4K1 | MSAQPVDIQVFGRSLRVNCPPEQQDALNMAAEDLSQRLQDLKVRTRVNNTEQLVFIAALNVCHELAQERLKTRDYASNMEQRIRMLQQTIEQALLEQGRISDRQDTQFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
C4GXF1 | MSAQPVDIQVFGRSLRVNCPPEQQDALNMAAEDLSQRLQDLKVRTRVNNTEQLVFIAALNVCHELAQERLKTRDYASNMEQRIRMLQQTIEQALLEQGRISDRQDTQFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
Q666R0 | MSAQPVDIQVFGRSLRVNCPPEQQDALNMAAEDLSQRLQDLKVRTRVNNTEQLVFIAALNVCHELAQERLKTRDYASNMEQRIRMLQQTIEQALLEQGRISDRQDTQFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
B1JNS0 | MSAQPVDIQVFGRSLRVNCPPEQQDALNMAAEDLSQRLQDLKVRTRVNNTEQLVFIAALNVCHELAQERLKTRDYASNMEQRIRMLQQTIEQALLEQGRISDRQDTQFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. Homodimer. Interacts with FtsZ. Localizes at mid-cell. Belongs to the ZapA family. Type 1 subfamily. |
A3MZY9 | MSLPILDQLEEKIKQAVETIQLLQLEVEELKEKNTTVEQEKETLRQEYEQLKSEQQSFQDRLRSLLGQIDNV | Non-essential, abundant cell division factor that is required for proper Z-ring formation. It is recruited early to the divisome by direct interaction with FtsZ, stimulating Z-ring assembly and thereby promoting cell division earlier in the cell cycle. Its recruitment to the Z-ring requires functional FtsA or ZipA. Homodimer. The ends of the coiled-coil dimer bind to each other, forming polymers. Interacts with FtsZ. Localizes to the septum at mid-cell, in a FtsZ-like pattern. Belongs to the ZapB family. |
Q3IGZ2 | MLQASKQWQWISCAKKNRLLLDLNEDMQLCTPYKLRQLTDSTFKNPYFSLEDAAFYEQVYQYLVQFKLWNPAQLCQISLNATAVKFQLKPVLAKSWFFEQYTGSTPSTEAVINLTSKAQSGEFLIVEHSSDASVCINLSENFQLDDNLSLVQFEAIRVLNNRVHPLLNQHIHSKIA | Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ. Interacts directly with FtsZ. Belongs to the ZapC family. |
A1SX24 | MCKKTHRIIDFRPQANWYWLFDHNRAILTLNMGDRVIDIVYKPEMLILKFDQPVFFTIEDVANYMDLFEGPALGDYWPALRSQIILHALVANQFHKPIMPKNWLFESSVGEQPRVHKGDHIILKSSAIKEAKKYFVLDNDENFILCMLIEKSHGLTFNRNFVQFQIVKVTYDKIFATKADCNTLSQYV | Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ. Interacts directly with FtsZ. Belongs to the ZapC family. |
Q8ZQ75 | MRIKPDDNWRWYYDEEHDRMMLDLANGMLFRSRFSRKMLTPDAFCPTGFCVDDAALYFSFEEKCRDFELTKEQRAELVLNALVAIRYLKPQMPKSWHFVAHGEMWTPGTGDAASVWLSDTAEQVNLLVVEPGENAALCLLAQPGVVIAGRTMQLGDAIKIMNDRLKPQVHCHSFSLEQAV | Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ. Interacts directly with FtsZ. Belongs to the ZapC family. |
Q081K0 | MLLMPNKDWHWEYNETCKQLSISLGSEMEFLTPYKTKLLIPDALTATEFNLEHAKFYIKMLETLPKVLHISDAGIVQTALNATAAHFLLQSQMPKSWFFDVSDECVYCEVGKLFQLNCGYSKVLALVVDNGLQAATVMILSQYCQLSDSKSLVQFDTIKVMHNRLHPLRKARQVVAA | Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ. Interacts directly with FtsZ. Belongs to the ZapC family. |
Q8EDZ9 | MLLLPQKDWHWKYNDSYGVLSVSLGSEIEFLTAYKAKSLIPDALSSMEFNISHAKFYMSLLDKLPKTLTLTDAAVVQIALNATAAHFMLTPQMPKSWFFDTSEVCVYSDVGKVFELKCQKQRALVLVVENTLQSALVMLLSPECVLSGAKTLGQFETIKVMHNRLHPLRAQRHVVAA | Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ. Interacts directly with FtsZ. Belongs to the ZapC family. |
B1KDM9 | MVEIMLLMPKKDWQWRYSDTYGVLSVSLGSEMEFLTPYKSKSLIPDALSELEFSVEHAKFYIDFIELLSKSLTISDAMKVQLALNGTAAHFLLKPQMPKSWFFDTSSMCVYSELGKVFQLKCRGAIAQVLVVETSIQASLVMLLSNELPLNDNKSLMQFECIKVMHDRLHPLKVSRAIAAA | Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ. Interacts directly with FtsZ. Belongs to the ZapC family. |
Q32HW0 | MRIKPDDNWRWYYDKEHDRMMLDLADGMLFRSRFARKMLTPDAFSPAGFCVDDASLYFSFEEKCRDFNLSKEQKAELVLNALVAIRYLKPQMPKSWHFVSHGEMWVPMPGDAACVWLSDTNEQVNLLVVESGENAALCLLAQPCVVIAGRAMQLGDAIKIMNDRLKPQVNVDSFSLEQAV | Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ. Interacts directly with FtsZ. Belongs to the ZapC family. Extended N-terminus. |
C4LEY8 | MILLPDENWRWVFDEQRQSLLLDLSDDMQFVVSVPPKQLAQKQAFTEHFSLDDSSLYFHFLECLGEFPFTDPERVQIVLNAVAAVKYTRPLVSQSWYYRDVDMLSGEPELGEVFSVVTEFTYGDVMIISPGSNASLCIVISQAIQLDADKSLRQSSVCKLMNSKLLPYQAATQYLSKMA | Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ. Interacts directly with FtsZ. Belongs to the ZapC family. |
Q9KRZ3 | MLKPSDKWSWYFSDSEGYLMLNLGDDMLFRTNLSRNLLVDCAFIENPFTVDDASDFQLYKEHIACLPLSEPRKAELALYCVAAKRFHKPVQPKSWFFDVQGTGYTPQQGQLISLRNSLNSGIFIALEVGENATLCAYSDLVSFALNGSKTLEFGQVIKVMHDRMSDVNTLLYTPQMAMVS | Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ. Interacts directly with FtsZ. Belongs to the ZapC family. |
Q8D9G6 | MLKPSDKWSWYFDKPSGRLMLDLGDRYLFQTNLSDKLLVDCAFSYNDFTVDDASAFQTFKECLSSLDLSEYRRDELTLYCVAAKRFHKPVQPKSWFFHSTGSDYQPSEGELVQLQNGLNQGLFIVLEAGDNASLVSCVELEGFMLSGSKSLSYGEAIKVMHDRMSTAARMNTLMPMALVG | Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ. Interacts directly with FtsZ. Belongs to the ZapC family. |
D3UWU5 | MKIRPDDQWRWYFDSEHSRVMLDLANGMVFRSRFLAKMLTDYAITMEEMPFSVDDAALYYAFEEHFRCINIASELRAELALNGVVAFRFMKPQMPKSWYFSSFSVMTKPEQGEIVQVRLQDCGTEVLFMVAEVGDSASLCLLAQQKLELSDRVMNFCDPIKIMNDRLMPYVEPTRETIYGRVI | Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ. Interacts directly with FtsZ. Belongs to the ZapC family. |
Q74VU6 | MRIKPDDKWRWYFDTEHDRLMLDLANGMIFRSRFPSKMLTPDAFDESAFCVDDAALYFEFEDQCRQIKLSNEQRSELVLNALVACRFLKPLMPKSWHFVQQPKVLIPQNGELTLVTVLDNGENVRLLVVEPSCSASLCLLAQSQVVLAGRQLVLGDAIKIMNNRLLPLMVEEVNTTTAYDRAV | Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ. Interacts directly with FtsZ. Belongs to the ZapC family. |
Q5E2R1 | MNGLGMQKFEHPLNERTRIYLRIESLFRKLGHSADLTQPFEYQVFFSSLFNMLDILEQVQVKAELGKDLEKLRLQYRAWMDIEGVDQSALLSVLEQISQVHQNLMQTTRPGHSLKEDRFLSALKQRFFIPGGDCCFDLPALHHWLHLPLEVRCRNTHNWMAQLLSLSDALSLWLRLTRETARFEPQIARNGFMQSEMENANLLRLEIPIDQGVYPMISGHKSRFALRFMSFETNKNCEKDIEFTLAVC | Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. Interacts with FtsZ. Localizes to mid-cell in an FtsZ-dependent manner. Belongs to the ZapD family. |
B6ELG5 | MNGLGMQKFEHPLNERTRIYLRIESLLRKLGHSADLTQPYEYQVFFSSLFHMLDILEQVQVKADLGKDLEKLRLQYRAWMNIEGVDQSALLSVLEQISQVHQNLMQTTRPGHSLKEDRFLSALKQRFFIPGGDCCFDLPALHHWLHLPLDVRCRNTHNWMSQLLSLSDALSLWLRLTRETARYTPQIARNGFMQSEMENSNLLRLEIPIDQGVYPMISGHKSRFALRFMSFETNKNCEKDIEFTLAVC | Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. Interacts with FtsZ. Localizes to mid-cell in an FtsZ-dependent manner. Belongs to the ZapD family. |
Q5P2L5 | MRAQPVISYEYPLNERIRTLLRLEDLYAKIAHFLGGDAPQDHHVALLTLFEVLEVAGRADLKVDLVQELERQRQILISFRHNPEISEQALSGALYEIEQASSSLLAMAGKIGQYLRENEWLMAIRSRASIPGGVCQFDLPSYHYWLNRDPEQRRGDLEGWLRPMIPIREGLTIVLRLLRASAQPERQLARGGTYQLTMGGRGAQMLQLRLAPAEAVVPEISANKYAINIRFMLSETVVRPRLAERDIPFEITFCSL | Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. Interacts with FtsZ. Localizes to mid-cell in an FtsZ-dependent manner. Belongs to the ZapD family. |
A1K3E2 | MISYEYPLSERIRTLLRLEDLFRKVAHFGGSEAPLDHHVALLTIFEILEVASRADLKVDLVQELERQRQILLSFRNNPEISEEALAGALYEIEQASTALLSMAGKIGQYLRENEWLMGIRSRAAIPGGVCQFDLPSYHFWLNRDAAERRHDLDAWIMPMTPIRDGIEIVMRLLRSSGRPEQQRARAGTYQLTMAGRVAQMLRVRIPRSEAVVPEISANKYALNIRFMLPETVARPRVAEREITFELTFCTL | Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. Interacts with FtsZ. Localizes to mid-cell in an FtsZ-dependent manner. Belongs to the ZapD family. |
Q7WF47 | MASVILYEYPFNERIRAYLRLEYLFDRLFFFAREGDARLHQIAVSSLFDLLDASERTDIKGAVLQDLERQRMALVGLRDHPGVAQDALEAMLRDMERVVAALAAQGKTGQALRENEWLVSLRGRLAVPGGATQVDMPSYHAWQNKPESVRCADLQSWLAPLLPLHEGLSMALRLLRESGRRADIAAEQGGYQQMLAGKIYHLLRVWVDPSLGVFPEISANKYMVWIRFSTQDGEVKPQQVSRDVAFQMSLCSS | Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. Interacts with FtsZ. Localizes to mid-cell in an FtsZ-dependent manner. Belongs to the ZapD family. |
A9I1I9 | MILYEYPFNERVRAYLRLEYLFDRLFYFAREGDARHHQIAVATLFDILDATERTDIKTSVLQDLERQRAALQALRDHPGVAQDALESMLAEMERTVSGLAGQGRAGQPLRENEWLVSLRGRLAVPGGATQVDMPSYHAWQHRTEAVRCADLQTWTAPLRPLHDAVAMALRLLRESGRRSEIVAEQGGYQQMLAGKLFQLLRVWIDPAQGVFPEISANKYMIWIRFSAQDGDAKPQQVARNIDFQMSLCSS | Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. Interacts with FtsZ. Localizes to mid-cell in an FtsZ-dependent manner. Belongs to the ZapD family. |
P42855 | DTIFGKIISKEIPSTVVYEDDKVLAFRDITPQGPVHILLIPKVRDGLTGLFKAEERHIDILGRLLYTAKLVAKQEGLDEGFRIVINDGPQGCQSVYHIHVHLIGGRQMNWPPG | Homodimer. |
P42856 | MSSEKEAALRRLDDSPTIFDKIIKKEIPSTVVYEDEKVLAFRDINPQAPTHILIIPKVKDGLTGLAKAEERHIEILGYLLYVAKVVAKQEGLEDGYRVVINDGPSGCQSVYHIHVHLLGGRQMNWPPG | Homodimer. |
Q802Y8 | MDLTKMGMIQLQNPNHPNALLHKANQMRLAGTLCDVVIMVDSQEFHAHRTVLACTSKMFEILFHRNSQHYTLDFLSPKTFQQILEYAYTATLQAKVEDLDDLLYAAEILEIEYLEEQCLKILETIQSSDENDTEVNMNDGGTEDDEERKGRHGRNLVGSKKHSTEESGYVSAAQQALALPGMVDQSPSVSTSFGLSTMSPTKAAVDSLMSIGQSLLQSTMHPGVGAEQPLHGNSHPMMGEIKTEMMQVDESGEHESPKAMESIASSNGERSGEPDKNRDGPGTPTRSSVITSARELHYVRDEGLGDQQAEVSQMGLEAMAGMTEKHLASLYGIPSNHKNEAMLSMPASMASSLHMSPALAMSMDFSAYGGLLPQSFIQREFFSKLGELAAGIKPDGRSLNERCNVCGAELPDNEAIEQHRKLHSGMKTYGCELCGKRFLDSLRLRMHLLSHSAGEKAIVCDQCGAQFQKEDALEAHRQIHTGSDMAIFCLLCGKRFQTQTALQQHMEVHAGVRSYICSECNRTFPSHTALKRHLRSHTAGDHPFECEFCGSCFRDESTLKGHKRIHTGEKPYECNGCGKKFSLKHQLETHYRVHTGEKPFECKLCHQRSRDYSAMIKHLRTHNGASPYQCTICLEYCPSLSAMQKHMKGHKPEDIPPDWRIEKTYLYLCYV | Probable transcription factor. Probable substrate-recognition component of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Inhibits neurogenesis. Protein modification; protein ubiquitination. Interacts with btbd6a (via BTB domain). Nuclear export to the cytoplasm is promoted by btbd6a. During early stages of primary neurogenesis, expressed in the neural epithelium, with highest levels in the forebrain and midbrain. Also expressed in a posterior-to-anterior gradient in the caudal neural plate at the 3-6 somite stage. Polyubiquitinated, leading to its proteasomal degradation. Belongs to the krueppel C2H2-type zinc-finger protein family. |
Q7ZWZ4 | MEFPDHSRQLLQCLSQQRHQGFLCDCTVLVGEAQFRAHRAVLASCSMYFHLFYRDQLDKRDIVHLNSDIVTAPAFSLLLQFMYEGKLEFSNLPVEDVLAAASYLHMYDIVKVCKGKLKDKELNSGEKIIDDGEKDDKPVDSEEHHEHSFDASQQKISTLDSVKPIWKEKVSGLSGLSSDLIGVNSVPAEAVMCKRAAGKTKANDSSPSSPLSQRSANHTHPPSDRDGALDLSFKPMPGRDSFHPSYVFGQLVSDSQQQGSLPLVKHEQDLLSEQEDSQAKSPKSQQVGNPAKSLVTGLGHMFTGNGNSHTREDDLYQDRDESEDEMDSSDLSTSGVLVSPGQICICPLCSKVFPSPHILQLHLSSHFKDKDNSRIKMSPDGSVPTCTICGKTFSCMYTLKRHERTHSGEKPFTCGQCGKSFQYSHNLSRHAVVHTREKPHACKWCERRFTQSGDLYRHIRKFHCGLVKSLVV | Transcriptional repressor that plays a role in various developmental processes. Specifically binds the consensus DNA sequence 5'-[AC]ACATCTG[GT][AC]-3' which contains the E box core, and acts by recruiting chromatin remodeling multiprotein complexes (By similarity). Belongs to the krueppel C2H2-type zinc-finger protein family. ZBTB18 subfamily. Extended N-terminus. |