## Supplementary materials

Supplementary material associated with this article can be found, in the online version, at doi:10.1016/j.crmicr.2025.100387.

## Data availability

The authors are unable or have chosen not to specify which data has been used.

## References

Arbour, C.A., Nagar, R., Bernstein, H.M., Ghosh, S., Al-Sammarraie, Y., Dorfmueller, H. C., Ferguson, M.A.J., Stanley-Wall, N.R., Imperiali, B., 2023. Defining early steps in Bacillus subtilis biofilm biosynthesis. mBio 14. https://doi.org/10.1128/MBIO.00948-23/SUPPL_FILE/MBIO.00948-23-S0008.DOCX.

Arnaouteli, S., Bamford, N.C., Stanley-Wall, N.R., Kovács, Á.T., 2021. Bacillus subtilis biofilm formation and social interactions. Nat. Rev. Microbiol. 9, 600–614. https://doi.org/10.1038/s41579-021-00540-9.

Arnaouteli, S., MacPhee, C.E., Stanley-Wall, N.R., 2016. Just in case it rains: building a hydrophobic biofilm the Bacillus subtilis way. Curr. Opin. Microbiol. 34, 7–12. https://doi.org/10.1016/j.mib.2016.07.012.

Azrin, N.A.M., Ali, M.S.M., Rahman, R.N.Z.R.A., Oslan, S.N., Noor, N.D.M., 2022. Versatility of subtilisin: a review on structure, characteristics, and applications. Biotechnol. Appl. Biochem. 69, 2599–2616. https://doi.org/10.1002/BAB.2309.

Azulay, D.N., Späker, O., Ghrayeb, M., Wilsch-Bräuninger, M., Scoppola, E., Burghammer, M., Zizak, I., Bertinetti, L., Politi, Y., Chai, L., 2021. Spores and extracellular matrix components impart molecular order in Bacillus subtilis biofilms. bioRxiv 2021.07.2453653. 10.1101/2021.07.2453653.

Benigar, E., Dogsa, I., Stopar, D., Jamnik, A., Gigić, I.K., Tomšić, M., 2014. Structure and dynamics of a polysaccharide matrix: aqueous solutions of bacterial levan. Langmuir 30, 4172–4182. https://doi.org/10.1021/LA500830J.

Bhoopalan, S.V., Piekarowicz, A., Lenz, J.D., Dillard, J.P., Stein, D.C., 2016. nagZ triggers gonococcal biofilm disassembly. Sci. Rep. 61 (6), 1–10. https://doi.org/10.1038/srep22372, 2016.

Böhning, J., Ghrayeb, M., Pedebos, C., Abbas, D.K., Khalid, S., Chai, L., Bharat, T.A.M., 2022. Donor-strand exchange drives assembly of the TasA scaffold in Bacillus subtilis biofilms. Nat. Commun. 13, 7082. https://doi.org/10.1038/s41467-022-34700-z.

Bou-Sarkis, A., Paul, E., Bessiere, Y., Derlon, N., Girbal-Neuhauser, E., 2024. Impact of biochemical properties on the gelation of EPS extracted from aerobic granules. J. Environ. Chem. Eng. 12, 113648. https://doi.org/10.1016/J.JECE.2024.113648.

Branda, S.S., Chu, F., Kearns, D.B., Losick, R., Kolter, R., 2006. A major protein component of the Bacillus subtilis biofilm matrix. Mol. Microbiol. 59, 1229–1238. https://doi.org/10.1111/j.1365-2958.2005.05020.x.

Branda, S.S., González-Pastor, J.E., Ben-Yehuda, S., Losick, R., Kolter, R., 2001. Fruiting body formation by Bacillus subtilis. Proc. Natl. Acad. Sci. U. S. A. 98, 11621–11626. https://doi.org/10.1073/pnas.191384198.

Cairns, L.S., Hobley, L., Stanley-Wall, N.R., 2014. Biofilm formation by Bacillus subtilis: new insights into regulatory strategies and assembly mechanisms. Mol. Microbiol. 93, 587–598. https://doi.org/10.1111/mmi.12697.

Cámara-Almirón, J., Navarro, Y., Díaz-Martínez, L., Magno-Pérez-Bryan, M.C., Molina-Santiago, C., Pearson, J.R., de Vicente, A., Pérez-García, A., Romero, D., 2020. Dual functionality of the amyloid protein TasA in Bacillus physiology and fitness on the phylloplane. Nat. Commun. 111 (11), 1–21. https://doi.org/10.1038/s41467-020-15758-z, 2020.

Caudan, C., Filali, A., Lefebvre, D., Spérandio, M., Girbal-Neuhauser, E., 2012. Extracellular polymeric substances (EPS) from aerobic granular sludges: extraction, fractionation, and anionic properties. Appl. Biochem. Biotechnol. 166, 1685–1702. https://doi.org/10.1007/s12102-012-9569-z.

Chambert, R., Pereira, Y., Petit-Glatron, M.F., 2003. Purification and characterization of YfkN, a trifunctional nucleotide phosphoesterase secreted by Bacillus subtilis. J. Biochem. 134, 655–660. https://doi.org/10.1093/JB/MVG189.

Costerton, J.W., Lewandowski, Z., Caldwell, D.E., Korber, D.R., Lappin-Scott, H.M., 1995. Microbial biofilms. Annu. Rev. Microbiol. 49, 711–745. https://doi.org/10.1146/ANNUREV.MI.49.100195.003431.

Deka, P., Goswami, G., Das, P., Gautom, T., Chowdhury, N., Boro, R.C., Barooah, M., 2019. Bacterial exopolysaccharide promotes acid tolerance in (Bacillus) amyloliquefaciens and improves soil aggregation. Mol. Biol. Rep. 46, 1079–1091. https://doi.org/10.1007/s11033-018-4566-0.

Devi, S., Sharma, P., Sharma, N., Chauhan, S., Sharma, A., Thakur, M., 2023. Microbial biofilms: beneficial and detrimental impacts. J. Microbiol. Biotechnol. Food Sci. 12. https://doi.org/10.55251/jmbfs.5211.

Dogsa, I., Brloznik, M., Stopar, D., Mandic-Mulec, I., 2013. Exopolymer diversity and the role of levan in Bacillus subtilis biofilms. PLoS One 8. https://doi.org/10.1371/JOURNAL.PONE.0062044.

Duong, V.A., Lee, H., 2023. Bottom-up proteomics: advancements in sample preparation. Int. J. Mol. Sci. 24. https://doi.org/10.3390/ijms24065350.

El-Khoury, N., Bennaceur, I., Verplaatse, E., Aymerich, S., Lereclus, D., Kallassy, M., Gohar, M., 2021. Massive integration of plantonic cells within a developing biofilm. Microorganisms 9, 1–10. https://doi.org/10.3390/MICROORGANISMS9020298.

Faille, C., Bénézech, T., Midelet-Bourdin, G., Lequette, Y., Clarisse, M., Ronse, G., Ronse, A., Slomianny, C., 2014. Sporulation of Bacillus spp. Within biofilms: a

potential source of contamination in food processing environments. Food Microbiol. 40, 64–74. https://doi.org/10.1016/j.FM.2013.12.004.

Farhat-Khemakhem, A., Blibech, M., Boukhris, I., Makni, M., Chouaykh, H., 2018. Assessment of the potential of the multi-enzyme producer Bacillus amyloliquefaciens US573 as alternative feed additive. J. Sci. Food Agric. 98, 1208–1215. https://doi.org/10.1002/JSFA.8574.

Flemming, H.C., Wuertz, S., 2019. Bacteria and archaea on Earth and their abundance in biofilms. Nat. Rev. Microbiol. 17 (1). https://doi.org/10.1038/s41579-019-0158-9.

Fong, J.N.C., Yildiz, F.H., 2015. Biofilm matrix proteins. Microbiol. Spectr. 3. https://doi.org/10.1128/MICROBIOOLSPEC.MB-0004-2014.

Galperin, M.Y., Wolf, Y.I., Makarova, K.S., Alvarez, R.V., Landsman, D., Koonin, E.V., 2021. COG database update: focus on microbial diversity, model organisms, and widespread pathogens. Nucleic Acids Res. 49, D274–D281. https://doi.org/10.1093/NAR/GKAA1018.

Gao, X.A., Ju, W.T., Jung, W.J., Park, R.D., 2008. Purification and characterization of chitosanase from Bacillus cereus D-11. Carbohydr. Polym. 72, 513–520. https://doi.org/10.1016/j.CARBPOL.2007.09.025.

Gao, X.Y., Liu, Y., Miao, L.L., Li, E.W., Sun, G., Liu, Y., Liu, Z.P., 2017. Characterization and mechanism of anti-Aeromonas salmonicida activity of a marine probiotic strain, Bacillus velezensis V4. Appl. Microbiol. Biotechnol. 101, 3759–3768. https://doi.org/10.1007/S00253-017-8095-X.

Gerwig, J., Stülke, J., 2014. Far from being well understood: multiple protein phosphorylation events control cell differentiation in Bacillus subtilis at different levels. Front. Microbiol. 5. https://doi.org/10.3389/FMICB.2014.00704.

Hamza, F., Kumar, A.R., Zinjarde, S., 2018. Efficacy of cell free supernatant from Bacillus licheniformis in protecting Artemia salina against Vibrio alginolyticus and Pseudomonas gessardii. Microb. Pathog. 116, 335–344. https://doi.org/10.1016/J.MICPATH.2018.02.003.

Harwood, C.R., Kikuchi, Y., 2022. The ins and outs of Bacillus proteases: activities, functions and commercial significance. FEMS Microbiol. Rev. 46. https://doi.org/10.1093/FEMSRE/FUA046.

Hilbert, D.W., Piggot, P.J., 2004. Compartmentalization of gene expression during Bacillus subtilis spore formation. Microbiol. Mol. Biol. Rev. 68, 234–262. https://doi.org/10.1128/MMBR.68.2.234-262.2004.

Houry, A., Gohar, M., Deschamps, J., Tischenko, E., Aymerich, S., Gruss, A., Briandet, R., 2012. Bacterial swimmers that infiltrate and take over the biofilm matrix. Proc. Natl. Acad. Sci. U. S. A. 109, 13088–13093. https://doi.org/10.1073/PNAS.1200791109/SUPPL_FILE/SM07.MOV.

Islam, C.R., Mahmud, M.L., Almalki, W.H., Biswas, S., Islam, M.A., Mortuza, M.G., Hossain, M.A., Ekram, M.A.E., Uddin, M.S., Zaman, S., Saleh, M.A., 2022. Cell-free supernatants (CFSs) from the culture of Bacillus subtilis inhibit Pseudomonas sp. Biofilm formation. Microorganisms 10. https://doi.org/10.3390/MICROORGANISMS10112105/S1.

Jacques, P., 2011. Surfactin and other lipopeptides from Bacillus spp. 57–91. 10.1007/978-3-642-14490-5-3.

Jiao, R., Cai, Y., He, P., Munir, S., Li, X., Wu, Y., Wang, J., Xia, M., He, P., Wang, G., Yang, H., Karunaratna, S.C., Xie, Y., He, Y., 2021. Bacillus amyloliquefaciens YN201732 produces lipopeptides with promising biocontrol activity against fungal pathogen erysiphe cichoracearum. Front. Cell Infect. Microbiol. 11, 598999. https://doi.org/10.3389/FCIMB.2021.598999/BIBTEX.

Kalamara, M., Abbott, J.C., Macphee, C.E., Stanley-Wall, N.R., 2021. Biofilm hydrophobicity in environmental isolates of Bacillus subtilis. Microbiology 167. https://doi.org/10.1099/mic.0001082 (United Kingdom).

Karygianni, L., Ren, Z., Koo, H., Thurnheer, T., 2020. Biofilm matrix: extracellular components in structured microbial communities. Trends Microbiol. 28, 668–681. https://doi.org/10.1016/j.tim.2020.03.016.

Khamhati, K., Patel, J., Saxena, V., Parvathy, A., Jain, N., 2021. Gene regulation of biofilm-associated functional amyloids. Pathogens 10. https://doi.org/10.3390/PATHOGENS10040490 (Basel, Switzerland).

Kimani, V.N., Chen, L., Liu, Y., Raza, W., Zhang, N., Mungai, L.K., Shen, Q., Zhang, R., 2016. Characterization of extracellular polymeric substances of Bacillus amyloliquefaciens SQR9 induced by root exudates of cucumber. J. Basic Microbiol. 56, 1183–1193. https://doi.org/10.1002/JOBM.2016000104.

Latorre, J.D., Hernández-Velasco, X., Wolfenden, R.E., Vicente, J.L., Wolfenden, A.D., Menconi, A., Bielke, L.R., Hargis, B.M., Tellez, G., 2016. Evaluation and selection of Bacillus species based on enzyme production, antimicrobial activity, and biofilm synthesis as direct-fed microbial candidates for poultry. Front. Vet. Sci. 3. https://doi.org/10.3389/FVETS.2016.00095.

Lin, H., Zhang, M., Wang, F., Meng, F., Liao, B.Q., Hong, H., Chen, J., Gao, W., 2014. A critical review of extracellular polymeric substances (EPSs) in membrane bioreactors: characteristics, roles in membrane fouling and control strategies. J. Memb. Sci. 460, 110–125. https://doi.org/10.1016/J.MEMSCI.2014.02.034.

López, D., Vlamakis, H., Losick, R., Kolter, R., 2009. Paracrine signaling in a bacterium. Genes Dev. 23, 1631–1638. https://doi.org/10.1101/gad.1813709.

Lundgren, D.H., Hwang, S.II, Wu, L., Han, D.K., 2010. Role of spectral counting in quantitative proteomics. Expert Rev. Proteom. 7, 39–53. https://doi.org/10.1586/ERP.09.69.

Mahto, K.U., Vandana, Priyadarshanee, M., Samantaray, D.P., Das, S., 2022. Bacterial biofilm and extracellular polymeric substances in the treatment of environmental pollutants: beyond the protective role in survivability. J. Clean. Prod. 379, 134759. https://doi.org/10.1016/j.jclepro.2022.134759.

McBride, S., Haldenwang, W.G., 2004. Sporulation phenotype of a Bacillus subtilis mutant expressing an unprocessable but active σe transcription factor. J. Bacteriol. 186, 1999–2005. https://doi.org/10.1128/JB.186.7.1999-2005.2004.
Mckenney, P.T., Driks, A., Eichenberger, P., 2013. The Bacillus subtilis endos pore: assembly and functions of the multilayered coat. Nat. Rev. Microbiol. 11, 33–44. https://doi.org/10.1038/NRMICRO2921.

Milton, M.E., Cavanagh, J., 2023. The biofilm regulatory network from Bacillus subtilis: a structure-function analysis. J. Mol. Biol. 435. https://doi.org/j.jmb.2022.167923.

Moore-Ott, J.A., Chiu, S., Amchin, D.B., Battacharjee, T., Datta, S.S., 2022. A biophysical threshold for biofilm formation. Elife 11. https://doi.org/10.7554/ELIFE.76380.

Morikawa, M., 2006. Beneficial biofilm formation by industrial bacteria Bacillus subtilis and related species. J. Biosci. Bioeng. 101, 1–8. https://doi.org/10.1263/JBB.101.1.

Morris, R.J., Schor, M., Gillespie, R.M.C., Ferreira, A.S., Baldauf, L., Earl, C., Ostrowski, A., Hobley, L., Bromley, K.M., Sukhodub, T., Arnaouteli, S., Stanley-Wall, N.R., MacPhee, C.E., 2017. Natural variations in the biofilm-associated protein BslA from the genus Bacillus. Sci. Rep. 7, 6730. https://doi.org/10.1038/s41598-017-06786-9.

Mukhi, M., Vishwanathan, A.S., 2022. Beneficial biofilms: a minireview of strategies to enhance biofilm formation for biotechnological applications. Appl. Environ. Microbiol. 88. https://doi.org/10.1128/AEM.019941-21.

Muslim, S.N., AL-Kadmy, I.M.S., Hussein, N.H., Mohammed Ali, A.N., Taha, B.M., Aziz, S.N., Kheraif, A.A.AI, Divakar, D.D., Ramakrishnaiah, R., 2016. Chitosanase purified from bacterial isolate Bacillus licheniformis of strained vegetables displays broad spectrum biofilm inhibition. Microb. Pathog. 100, 257–262. https://doi.org/10.1016/j.MICPATH.2016.10.001.

Naamala, J., Misimbira, L.A., Antar, M., Subramanian, S., Smith, D.L., 2022. Cell-free supernatant obtained from a salt tolerant Bacillus amyloliquefaciens strain enhances germination and radicle length under NaCl stressed and optimal conditions. Front. Sustain. Food Syst. 6, 788939. https://doi.org/10.3389/FSUFS.2022.788939/BIBTEX.

Naclerio, G., Baccigalupi, L., Caruso, C., De Felice, M., Ricca, E., 1995. Bacillus subtilis vegetative catalase is an extracellular enzyme. Appl. Environ. Microbiol. 61, 4471. https://doi.org/10.1128/AEM.61.12.4471-4473.1995.

Ngalimat, M.S., Yahaya, R.S.R., Baharudin, M.M.A.A., Yaminudin, S.M., Karim, M., Ahmad, S.A., Sabri, S., 2021. A review on the biotechnological applications of the operational group Bacillus amyloliquefaciens. Microorganisms 9. https://doi.org/10.3390/MICROORGANISMS9030614. Page 614 9, 614.

Ning, K., Fermin, D., Nesvizhskii, A.I., 2012. Comparative analysis of different label-free mass spectrometry based protein abundance estimates and their correlation with RNA-seq gene expression data. J. Proteome Res. 11, 2261. https://doi.org/10.1021/PR201052X.

Ostrowski, A., Mehert, A., Prescott, A., Kiley, T.B., Stanley-Wall, N.R., 2011. YuaB functions synergistically with the exopolysaccharide and TasA amyloid fibers to allow biofilm formation by Bacillus subtilis. J. Bacteriol. 193, 4821–4831. https://doi.org/10.1128/JB.00223-11.

Ouidir, T., Gabriel, B., Nait Chabane, Y., 2022. Overview of multi-species biofilms in different ecosystems: wastewater treatment, soil and oral cavity. J. Biotechnol. 350, 67–74. https://doi.org/10.1016/j.jbiotec.2022.03.014.

Park, S., Wolanin, P.M., Yuzbashyan, E.A., Lin, H., Darnton, N.C., Stock, J.B., Silberzan, P., Austin, R., 2003. Influence of topology on bacterial social interaction. Proc. Natl. Acad. Sci. U. S. A. 100, 13910–13915. https://doi.org/10.1073/pnas.1935975100.

Park, Y.J., Kim, Y.J., Yu, H.H., Lee, N.K., Paik, H.D., 2023. Cell-free supernatants of Bacillus subtilis and Bacillus polyfermenticus inhibit Listeria monocytogenes biofilm formation. Food Control 144. https://doi.org/10.1016/j.FOODCONT.2022.109387.

Parrilli, E., Tutino, M.L., Marino, G., 2022. Biofilm as an adaptation strategy to extreme conditions. Rend. Lincei 33, 527–536. https://doi.org/10.1007/S12210-022-01083-8/FIGURES/2.

Pedretti, N., Iseppi, R., Condò, C., Spaggiari, L., Messi, P., Pericolini, E., Di Cerbo, A., Ardizzoni, A., Sabia, C., 2024. Cell-free supernatant from a strain of Bacillus siamensis isolated from the skin showed a broad spectrum of antimicrobial activity. Microorganisms 12. https://doi.org/10.3390/MICROORGANISMS12040718.

Philipp, L.A., Bühler, K., Ulber, R., Gescher, J., 2024. Beneficial applications of biofilms. Nat. Rev. Microbiol. 22, 276–290. https://doi.org/10.1038/s41579-023-00985-0.

Pradeep, S., Arratia, P.E., 2022. To biofilm or not to biofilm. Elife 11, e80891. https://doi.org/10.7554/ELIFE.80891.

Puan, S.L., Erriah, P., Baharudin, M.M.A., Yahaya, N.M., Kamil, W.N.I.W.A., Ali, M.S.M., Ahmad, S.A., Oslan, S.N., Lim, S., Sabri, S., 2023. Antimicrobial peptides from Bacillus spp. And strategies to enhance their yield. Appl. Microbiol. Biotechnol. 107, 5569–5593. https://doi.org/10.1007/S00253-023-12651-9.

Qiu, M., Xu, Z., Li, X., Li, Q., Zhang, N., Shen, Q., Zhang, R., 2014. Comparative proteomics analysis of Bacillus amyloliquefaciens SQR9 revealed the key proteins involved in *in situ* root colonization. J. Proteome Res. 13, 5581–5591. https://doi.org/10.1021/PR500565M.

Ranjan, A., Rajput, V.D., Prazdnova, E.V., Gurnani, M., Bhardwaj, P., Sharma, S., Sushkova, S., Mandzhieva, S.S., Minkina, T., Sudan, J., Zargar, S.M., Chauhan, A., Jindal, T., 2023. Nature's antimicrobial arsenal: non-ribosomal peptides from PGPB for plant pathogen biocontrol. Fermentation 9. https://doi.org/10.3390/FERMENTATION9070597. Page 597, 597.

Riley, E.P., Schwarz, C., Derman, A.I., Lopez-Garrido, J., 2020. Milestones in Bacillus subtilis sporulation research. Microb. Cell 8. https://doi.org/10.15698/MIC2021.01.739 (Graz, Austria).

Romero, D., Aguilar, C., Losick, R., Kolter, R., 2010. Amyloid fibers provide structural integrity to Bacillus subtilis biofilms. Proc. Natl. Acad. Sci. U. S. A. 107, 2230–2234. https://doi.org/10.1073/PNAS.0910560107.

Romero, D., Vlamakis, H., Losick, R., Kolter, R., 2011. An accessory protein required for anchoring and assembly of amyloid fibres in B. subtilis biofilms. Mol. Microbiol. 80, 1155–1168. https://doi.org/10.1111/j.1365-2958.2011.07653.x.

Rosazza, T., Earl, C., Eigentler, L., Davidson, F.A., Stanley-Wall, N.R., 2024. Reciprocal sharing of extracellular proteases and extracellular matrix molecules facilitates Bacillus subtilis biofilm formation. Mol. Microbiol. 122. https://doi.org/10.1111/ MML1.15288.

Schmiedeknecht, G.B.H.J.H., Schmiedeknecht, G., Bochow, H., Junge, H., 1998. Use of Bacillus subtilis as biocontrol agent. II. Biological control of potato diseases. Z. Pflanzenkrankh. Pflanzenschutz 105, 376–386, 10.0/FONT/BOOTSTRAP-ICONS. MIN.CSS.

Srinivasan, S., Vladescu, I.D., Koehler, S.A., Wang, X., Mani, M., Rubinstein, S.M., 2018. Matrix production and sporulation in Bacillus subtilis biofilms localize to propagating wave fronts. Biophys. J. 114, 1490–1498. https://doi.org/10.1016/j.bpj.2018.02.002.

St. John, F.J., Rice, J.D., Preston, J.F., 2006. Characterization of XynC from Bacillus subtilis subsp. Subtilis strain 168 and analysis of its role in depolymerization of glucuronoxylan. J. Bacteriol. 188, 8617–8626. https://doi.org/10.1128/JB.01283-06.

Steinberg, N., Keren-Paz, A., Hou, Q., Doron, S., Yanuka-Golub, K., Olender, T., Hadar, R., Rosenberg, G., Jain, R., Cámara-Almirón, J., Romero, D., van Teeffelen, S., Kolodkin-Gal, I., 2020. The extracellular matrix protein TasA is a developmental cue that maintains a motile subpopulation within Bacillus subtilis biofilms. Sci. Signal. 13. https://doi.org/10.1126/SCISIGNAL.AAW8905.

Stöver, A.G., Driks, A., 1999. Regulation of synthesis of the Bacillus subtilis transition-phase, spore-associated antibacterial protein TasA. J. Bacteriol. 181, 5476–5481. https://doi.org/10.1128/JB.181.17.5476-5481.1999.

Szklarczyk, D., Kirsch, R., Koutrouli, M., Nastou, K., Mehryary, F., Hachilif, R., Gable, A. L., Fang, T., Doncheva, N.T., Pyysalo, S., Bork, P., Jensen, L.J., Von Mering, C., 2023. The STRING database in 2023: protein-protein association networks and functional enrichment analyses for any sequenced genome of interest. Nucleic Acids Res. 51, D638–D646. https://doi.org/10.1093/NAR/GKAC1000.

Tallawi, M., Opitz, M., Lieleg, O., 2017. Modulation of the mechanical properties of bacterial biofilms in response to environmental challenges. Biomater. Sci. 5, 887–900. https://doi.org/10.1039/C6BM00832A.

Teng, J., Wu, M., Chen, J., Lin, H., He, Y., 2020. Different fouling propensities of loosely and tightly bound extracellular polymeric substances (EPSs) and the related fouling mechanisms in a membrane bioreactor. Chemosphere 255, 126953. https://doi.org/10.1016/j.CHEMOSPHERE.2020.126953.

Tjalsma, H., Antelmann, H., Jongbloed, J.D.H., Braun, P.G., Darmon, E., Dorenbos, R., Dubois, J.Y.F., Westers, H., Zanen, G., Quax, W.J., Kuipers, O.P., Bron, S., Hecker, M., van Dijl, J.M., 2004. Proteomics of protein secretion by Bacillus subtilis: separating the “secrets” of the secretome. Microbiol. Mol. Biol. Rev. 68, 207–233. https://doi.org/10.1128/MMBR.68.2.207-233.2004.

Tran, C., Cock, I.E., Chen, X., Feng, Y., 2022. Antimicrobial Bacillus: metabolites and their mode of action. Antibiotics 11. https://doi.org/10.3390/ANTIBIOTICS11010088.

Vaccari, L., Molaei, M., Niepa, T.H.R., Lee, D., Leheny, R.L., Stebe, K.J., 2017. Films of bacteria at interfaces. Adv. Colloid Interface Sci. 247, 561–572. https://doi.org/10.1016/j.cis.2017.07.016.

Vlamakis, H., Aguilar, C., Losick, R., Kolter, R., 2008. Control of cell fate by the formation of an architecturally complex bacterial community. Genes Dev. 22, 945–953. https://doi.org/10.1101/gad.1645008.

Vlamakis, H., Chai, Y., Beauregard, P., Losick, R., Kolter, R., 2013. Sticking together: building a biofilm the Bacillus subtilis way. Nat. Rev. Microbiol. 1, 157–168. https://doi.org/10.1038/NRMICRO2960.

Wang, X., Chen, Z., Feng, H., Chen, X., Wei, L., 2019. Genetic variants of the oppA gene are involved in metabolic regulation of surfactin in Bacillus subtilis. Microb. Cell Factories 18, 1–12. https://doi.org/10.1186/S12934-019-1176-Z/TABLES/4.

Wang, X., Yang, T., Lin, B., Tang, Y., 2017. Effects of salinity on the performance, microbial community, and functional proteins in an aerobic granular sludge system. Chemosphere 184, 1241–1249. https://doi.org/10.1016/j.chemosphere.2017.06.047.

Welker, N.E., Campbell, L.L., 1967. Unrelatedness of Bacillus amyloliquefaciens and Bacillus subtilis. J. Bacteriol. 94, 1124. https://doi.org/10.1128/JB.94.4.1124-1130.1967.

Xu, Z., Mandic-Mulec, I., Zhang, H., Liu, Y., Sun, X., Feng, H., Xun, W., Zhang, N., Shen, Q., Zhang, R., 2019. Antibiotic bacillicomycin D affects iron acquisition and biofilm formation in Bacillus velezensis through a btr-mediated FeuABC-dependent pathway. Cell Rep. 29, 1192–1202. https://doi.org/10.1016/j.CELREP.2019.09.061 e5.

Yu, G.H., He, P.J., Shao, L.M., Lee, D.J., Mujumdar, A.S., 2010. Extracellular polymeric substances (EPS) and Extracellular enzymes in aerobic granules. Dry. Technol. 28, 910–915. https://doi.org/10.1080/07373937.2010.490766.

Zaidi-Ait Salem, M., Girbal-Neuhauser, E., Nait Chabane, Y., 2021a. Genome sequence data of Bacillus amyloliquefaciens L-17. Data Brief 39, 107505. https://doi.org/10.1016/j.dib.2021.107505.

Zaidi-Ait Salem, M., Nait Chabane, Y., Girbal-Neuhauser, E., 2021b. Architecture and physico-chemical properties of Bacillus amyloliquefaciens L-17 pellicule formed at the air-liquid interface. J. Biosci. Bioeng. 132, 560–568. https://doi.org/10.1016/J.JBIOSC.2021.07.010.

Zhang, N., Yang, D., Kendall, J.R.A., Borriss, R., Druzhinina, I.S., Kubicek, C.P., Shen, Q., Zhang, R., 2016. Comparative genomic analysis of Bacillus amyloliquefaciens and
Bacillus subtilis reveals evolutional traits for adaptation to plant-associated habitats.
Front. Microbiol. 7. https://doi.org/10.3389/FMICB.2016.02039.

Zhao, H., Liu, K., Fan, Y., Cao, J., Li, H., Song, W., Liu, Y., Miao, M., 2022. Cell-free supernatant of Bacillus velezensis suppresses mycelial growth and reduces virulence of botrytis cinerea by inducing oxidative stress. Front. Microbiol. 13. https://doi.org/10.3389/FMICB.2022.980022.

Zhao, X., Wang, R., Shang, Q., Hao, H., Li, Y., Zhang, Y., Guo, Z., Wang, Y., Xie, Z., 2016.
The new flagella-associated collagen-like proteins ClpB and ClpC of Bacillus
amyloliquefaciens FZB42 are involved in bacterial motility. Microbiol. Res. 184,
25-31. https://doi.org/10.1016/J.MICRES.2015.12.004.