BSLA_BACSU
ID BSLA_BACSU Reviewed; 181 AA.
AC P71014;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Biofilm-surface layer protein A {ECO:0000303|PubMed:22571672};
DE AltName: Full=ORF-1;
DE Flags: Precursor;
GN Name=bslA {ECO:0000303|PubMed:22571672}; Synonyms=yuaB;
GN OrderedLocusNames=BSU31080;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-108.
RC STRAIN=168 / JH642;
RX PubMed=8752328; DOI=10.1128/jb.178.17.5121-5129.1996;
RA Boch J., Kempf B., Schmid R., Bremer E.;
RT "Synthesis of the osmoprotectant glycine betaine in Bacillus subtilis:
RT characterization of the gbsAB genes.";
RL J. Bacteriol. 178:5121-5129(1996).
RN [3]
RP FUNCTION, TRANSCRIPTION REGULATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18978066; DOI=10.1128/jb.01236-08;
RA Verhamme D.T., Murray E.J., Stanley-Wall N.R.;
RT "DegU and Spo0A jointly control transcription of two loci required for
RT complex colony development by Bacillus subtilis.";
RL J. Bacteriol. 191:100-108(2009).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21742882; DOI=10.1128/jb.00223-11;
RA Ostrowski A., Mehert A., Prescott A., Kiley T.B., Stanley-Wall N.R.;
RT "YuaB functions synergistically with the exopolysaccharide and TasA amyloid
RT fibers to allow biofilm formation by Bacillus subtilis.";
RL J. Bacteriol. 193:4821-4831(2011).
RN [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22571672; DOI=10.1111/j.1365-2958.2012.08094.x;
RA Kobayashi K., Iwano M.;
RT "BslA(YuaB) forms a hydrophobic layer on the surface of Bacillus subtilis
RT biofilms.";
RL Mol. Microbiol. 85:51-66(2012).
RN [6]
RP FUNCTION.
RX PubMed=28701036; DOI=10.1021/acs.langmuir.7b01739;
RA Liu W., Li S., Wang Z., Yan E.C.Y., Leblanc R.M.;
RT "Characterization of surface-active biofilm protein BslA in self-assembling
RT Langmuir monolayer at the air-water interface.";
RL Langmuir 33:7548-7555(2017).
RN [7] {ECO:0007744|PDB:4BHU}
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 48-172, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-76; LEU-77 AND LEU-79.
RX PubMed=23904481; DOI=10.1073/pnas.1306390110;
RA Hobley L., Ostrowski A., Rao F.V., Bromley K.M., Porter M., Prescott A.R.,
RA MacPhee C.E., van Aalten D.M., Stanley-Wall N.R.;
RT "BslA is a self-assembling bacterial hydrophobin that coats the Bacillus
RT subtilis biofilm.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:13600-13605(2013).
RN [8]
RP ERRATUM OF PUBMED:23904481.
RX PubMed=26324938; DOI=10.1073/pnas.1516042112;
RA Hobley L., Ostrowski A., Rao F.V., Bromley K.M., Porter M., Prescott A.R.,
RA MacPhee C.E., van Aalten D.M., Stanley-Wall N.R.;
RT "Correction for Hobley et al., BslA is a self-assembling bacterial
RT hydrophobin that coats the Bacillus subtilis biofilm.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E5371-E5375(2015).
CC -!- FUNCTION: Involved in biofilm formation (PubMed:18978066,
CC PubMed:21742882). Self-polymerizes and forms a layer on the surface of
CC biofilms that confers hydrophobicity to the biofilm (PubMed:22571672,
CC PubMed:23904481). The layer is stable and capable of resistance to high
CC mechanical force compression (PubMed:28701036). Required for complex
CC colony architecture (PubMed:18978066). May function synergistically
CC with exopolysaccharides and TasA amyloid fibers to facilitate the
CC assembly of the biofilm matrix (PubMed:21742882).
CC {ECO:0000269|PubMed:18978066, ECO:0000269|PubMed:21742882,
CC ECO:0000269|PubMed:22571672, ECO:0000269|PubMed:23904481,
CC ECO:0000269|PubMed:28701036}.
CC -!- SUBUNIT: Forms polymers. {ECO:0000269|PubMed:22571672,
CC ECO:0000269|PubMed:23904481}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22571672,
CC ECO:0000269|PubMed:23904481}. Secreted, cell wall
CC {ECO:0000269|PubMed:21742882}. Note=Localizes to the biofilm matrix
CC (PubMed:22571672, PubMed:23904481). Forms a distinct layer at biofilm
CC surfaces (PubMed:23904481). Localization to the matrix is
CC exopolysaccharide-dependent (PubMed:22571672).
CC {ECO:0000269|PubMed:22571672, ECO:0000269|PubMed:23904481}.
CC -!- INDUCTION: Up-regulated by DegU and Spo0A. Repressed by AbrB.
CC {ECO:0000269|PubMed:18978066}.
CC -!- DISRUPTION PHENOTYPE: Overall loss in complex colony architecture and
CC lack of fruiting body-like structures (PubMed:18978066). Disruption of
CC the gene results in the loss of surface repellency and alters the
CC biofilm surface microstructure (PubMed:22571672).
CC {ECO:0000269|PubMed:18978066, ECO:0000269|PubMed:22571672}.
CC -!- SIMILARITY: Belongs to the BslA/BslB family. {ECO:0000305}.
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DR EMBL; AL009126; CAB15086.1; -; Genomic_DNA.
DR EMBL; U47861; AAC44367.1; -; Genomic_DNA.
DR PIR; D70005; D70005.
DR RefSeq; NP_390986.1; NC_000964.3.
DR RefSeq; WP_003243556.1; NZ_JNCM01000033.1.
DR PDB; 4BHU; X-ray; 1.91 A; A/B/C/D/E/F/G/H/I/J=48-172.
DR PDBsum; 4BHU; -.
DR AlphaFoldDB; P71014; -.
DR SMR; P71014; -.
DR IntAct; P71014; 3.
DR STRING; 224308.BSU31080; -.
DR PaxDb; P71014; -.
DR DNASU; 938831; -.
DR EnsemblBacteria; CAB15086; CAB15086; BSU_31080.
DR GeneID; 938831; -.
DR KEGG; bsu:BSU31080; -.
DR PATRIC; fig|224308.179.peg.3368; -.
DR eggNOG; ENOG502ZUCW; Bacteria.
DR OMA; VHEPEMS; -.
DR BioCyc; BSUB:BSU31080-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR CDD; cd14670; BslA_like; 1.
DR Gene3D; 2.60.40.3490; -; 1.
DR InterPro; IPR034650; YuaB-like.
DR InterPro; IPR038480; YuaB-like_sf.
DR Pfam; PF17735; BslA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..181
FT /note="Biofilm-surface layer protein A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000049911"
FT MUTAGEN 76
FT /note="L->D: Partial loss of morphological complexity.
FT Biofilm retains nonwetting, hydrophobic nature."
FT /evidence="ECO:0000269|PubMed:23904481"
FT MUTAGEN 76
FT /note="L->K: Forms flat, unwrinkled biofilm. Biofilm
FT retains nonwetting, hydrophobic nature."
FT /evidence="ECO:0000269|PubMed:23904481"
FT MUTAGEN 77
FT /note="L->D,K: Forms flat, unwrinkled biofilm. Loss of
FT colony hydrophobicity."
FT /evidence="ECO:0000269|PubMed:23904481"
FT MUTAGEN 79
FT /note="L->D,K: Forms flat, unwrinkled biofilm. Loss of
FT colony hydrophobicity."
FT /evidence="ECO:0000269|PubMed:23904481"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:4BHU"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:4BHU"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:4BHU"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:4BHU"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:4BHU"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:4BHU"
FT STRAND 114..123
FT /evidence="ECO:0007829|PDB:4BHU"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:4BHU"
FT STRAND 140..150
FT /evidence="ECO:0007829|PDB:4BHU"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:4BHU"
FT STRAND 160..168
FT /evidence="ECO:0007829|PDB:4BHU"
SQ SEQUENCE 181 AA; 19257 MW; 2903AF2E5CAAFF1B CRC64;
MKRKLLSSLA ISALSLGLLV SAPTASFAAE STSTKAHTES TMRTQSTASL FATITGASKT
EWSFSDIELT YRPNTLLSLG VMEFTLPSGF TANTKDTLNG NALRTTQILN NGKTVRVPLA
LDLLGAGEFK LKLNNKTLPA AGTYTFRAEN KSLSIGNKFY AEASIDVAKR STPPTQPCGC
N
