TASA_BACSU
ID TASA_BACSU Reviewed; 261 AA.
AC P54507;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Major biofilm matrix component {ECO:0000305};
DE AltName: Full=Spore coat-associated protein N {ECO:0000303|PubMed:9384377};
DE AltName: Full=Translocation-dependent antimicrobial spore component {ECO:0000303|PubMed:10049401};
DE Flags: Precursor;
GN Name=tasA {ECO:0000303|PubMed:10049401};
GN Synonyms=cotN {ECO:0000303|PubMed:9384377}, yqhF;
GN OrderedLocusNames=BSU24620;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 223-261.
RX PubMed=3096962; DOI=10.1128/jb.168.2.860-869.1986;
RA Gaur N.K., Dubnau E., Smith I.;
RT "Characterization of a cloned Bacillus subtilis gene that inhibits
RT sporulation in multiple copies.";
RL J. Bacteriol. 168:860-869(1986).
RN [4]
RP PROTEIN SEQUENCE OF 28-40, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10368135; DOI=10.1128/jb.181.12.3632-3643.1999;
RA Serrano M., Zilhao R., Ricca E., Ozin A.J., Moran C.P. Jr., Henriques A.O.;
RT "A Bacillus subtilis secreted protein with a role in endospore coat
RT assembly and function.";
RL J. Bacteriol. 181:3632-3643(1999).
RN [5]
RP PROTEIN SEQUENCE OF 28-39, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=10658653; DOI=10.1099/00221287-146-1-65;
RA Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.;
RT "Proteome analysis of Bacillus subtilis extracellular proteins: a two-
RT dimensional protein electrophoretic study.";
RL Microbiology 146:65-75(2000).
RN [6]
RP PROTEIN SEQUENCE OF 28-36, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RC STRAIN=168;
RX PubMed=10049401; DOI=10.1128/jb.181.5.1664-1672.1999;
RA Stoever A.G., Driks A.;
RT "Secretion, localization, and antibacterial activity of TasA, a Bacillus
RT subtilis spore-associated protein.";
RL J. Bacteriol. 181:1664-1672(1999).
RN [7]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=10464223; DOI=10.1128/jb.181.17.5476-5481.1999;
RA Stoever A.G., Driks A.;
RT "Regulation of synthesis of the Bacillus subtilis transition-phase, spore-
RT associated antibacterial protein TasA.";
RL J. Bacteriol. 181:5476-5481(1999).
RN [8]
RP POSSIBLE INTERACTION WITH OBG.
RX PubMed=12429099; DOI=10.1016/s0969-2126(02)00882-1;
RA Buglino J., Shen V., Hakimian P., Lima C.D.;
RT "Structural and biochemical analysis of the Obg GTP binding protein.";
RL Structure 10:1581-1592(2002).
RN [9]
RP REPRESSION BY SINR, AND DISRUPTION PHENOTYPE.
RX PubMed=16430695; DOI=10.1111/j.1365-2958.2005.05019.x;
RA Chu F., Kearns D.B., Branda S.S., Kolter R., Losick R.;
RT "Targets of the master regulator of biofilm formation in Bacillus
RT subtilis.";
RL Mol. Microbiol. 59:1216-1228(2006).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16430696; DOI=10.1111/j.1365-2958.2005.05020.x;
RA Branda S.S., Chu F., Kearns D.B., Losick R., Kolter R.;
RT "A major protein component of the Bacillus subtilis biofilm matrix.";
RL Mol. Microbiol. 59:1229-1238(2006).
RN [11]
RP FUNCTION, AND SUBUNIT.
RX PubMed=20080671; DOI=10.1073/pnas.0910560107;
RA Romero D., Aguilar C., Losick R., Kolter R.;
RT "Amyloid fibers provide structural integrity to Bacillus subtilis
RT biofilms.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2230-2234(2010).
RN [12]
RP INDUCTION BY REMA.
RX PubMed=23646920; DOI=10.1111/mmi.12235;
RA Winkelman J.T., Bree A.C., Bate A.R., Eichenberger P., Gourse R.L.,
RA Kearns D.B.;
RT "RemA is a DNA-binding protein that activates biofilm matrix gene
RT expression in Bacillus subtilis.";
RL Mol. Microbiol. 88:984-997(2013).
RN [13] {ECO:0007744|PDB:5OF1, ECO:0007744|PDB:5OF2}
RP X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 30-239, AND SUBUNIT.
RX PubMed=29531041; DOI=10.1073/pnas.1718102115;
RA Diehl A., Roske Y., Ball L., Chowdhury A., Hiller M., Moliere N.,
RA Kramer R., Stoppler D., Worth C.L., Schlegel B., Leidert M., Cremer N.,
RA Erdmann N., Lopez D., Stephanowitz H., Krause E., van Rossum B.J.,
RA Schmieder P., Heinemann U., Turgay K., Akbey U., Oschkinat H.;
RT "Structural changes of TasA in biofilm formation of Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:3237-3242(2018).
CC -!- FUNCTION: TasA is the major protein component of the biofilm
CC extracellular matrix (PubMed:16430696, PubMed:20080671). It forms
CC amyloid fibers that bind cells together in the biofilm
CC (PubMed:20080671). Exhibits an antibacterial activity against a variety
CC of Gram-positive and Gram-negative bacteria (PubMed:10049401). In
CC laboratory strains, is also involved in proper spore coat assembly
CC (PubMed:10368135). {ECO:0000269|PubMed:10049401,
CC ECO:0000269|PubMed:10368135, ECO:0000269|PubMed:16430696,
CC ECO:0000269|PubMed:20080671}.
CC -!- SUBUNIT: Forms fibers (PubMed:20080671, PubMed:29531041). Fibers have
CC variable length and are 10-15 nm width (PubMed:20080671). Interacts
CC with obg (AC P20964) in pull-down experiments (PubMed:12429099).
CC {ECO:0000269|PubMed:12429099, ECO:0000269|PubMed:20080671,
CC ECO:0000269|PubMed:29531041}.
CC -!- INTERACTION:
CC P54507; P54507: tasA; NbExp=6; IntAct=EBI-15827660, EBI-15827660;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10049401,
CC ECO:0000269|PubMed:10368135, ECO:0000269|PubMed:10658653,
CC ECO:0000269|PubMed:16430696}. Forespore intermembrane space
CC {ECO:0000269|PubMed:10049401, ECO:0000269|PubMed:10368135}. Note=In
CC undomesticated strains, is secreted and primarily associated with the
CC extracellular matrix (PubMed:16430696). In laboratory strains, is
CC secreted into the medium early in sporulation and is also incorporated
CC into the spore. Processing, export and incorporation into spores depend
CC on SipW (PubMed:10049401). {ECO:0000269|PubMed:10049401,
CC ECO:0000269|PubMed:16430696}.
CC -!- DEVELOPMENTAL STAGE: In laboratory strains, is a transition-phase
CC protein that is expressed early in spore formation, as cells enter
CC stationary phase (PubMed:10049401, PubMed:10368135, PubMed:10464223).
CC Expression can occur as cells enter stationary phase even under
CC sporulation-repressing conditions (PubMed:10464223).
CC {ECO:0000269|PubMed:10049401, ECO:0000269|PubMed:10368135,
CC ECO:0000269|PubMed:10464223}.
CC -!- INDUCTION: Part of the tapA-sipW-tasA operon (PubMed:10464223).
CC Expression is directly repressed by the DNA-binding protein master
CC regulator of biofilm formation SinR and activated by the extracellular
CC matrix regulatory protein RemA (PubMed:16430695, PubMed:23646920). Also
CC positively regulated by the sporulation transcription factors sigma H
CC and Spo0A and repressed by the transition phase regulatory protein
CC AbrB, probably indirectly (PubMed:10049401, PubMed:10368135,
CC PubMed:10464223). {ECO:0000269|PubMed:10049401,
CC ECO:0000269|PubMed:10368135, ECO:0000269|PubMed:10464223,
CC ECO:0000269|PubMed:16430695, ECO:0000269|PubMed:23646920}.
CC -!- DISRUPTION PHENOTYPE: Mutation impairs colony surface architecture
CC (PubMed:16430695). Mutant forms pellicles with less extracellular
CC material (PubMed:16430696). Deletion of the gene results in the
CC production of asymmetric spores that accumulate misassembled material
CC in one pole and have a greatly expanded undercoat and an altered outer
CC coat structure (PubMed:10368135). {ECO:0000269|PubMed:10368135,
CC ECO:0000269|PubMed:16430695, ECO:0000269|PubMed:16430696}.
CC -!- SIMILARITY: Belongs to the peptidase M73 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D84432; BAA12541.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14393.1; -; Genomic_DNA.
DR EMBL; M14112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; D69606; D69606.
DR RefSeq; NP_390342.1; NC_000964.3.
DR RefSeq; WP_004398632.1; NZ_JNCM01000036.1.
DR PDB; 5OF1; X-ray; 1.56 A; A/B=30-239.
DR PDB; 5OF2; X-ray; 1.86 A; A=30-239.
DR PDBsum; 5OF1; -.
DR PDBsum; 5OF2; -.
DR AlphaFoldDB; P54507; -.
DR SMR; P54507; -.
DR DIP; DIP-58529N; -.
DR STRING; 224308.BSU24620; -.
DR MEROPS; M73.A01; -.
DR PaxDb; P54507; -.
DR PRIDE; P54507; -.
DR DNASU; 938545; -.
DR EnsemblBacteria; CAB14393; CAB14393; BSU_24620.
DR GeneID; 938545; -.
DR KEGG; bsu:BSU24620; -.
DR PATRIC; fig|224308.179.peg.2680; -.
DR eggNOG; ENOG502ZBTW; Bacteria.
DR OMA; TWAAFND; -.
DR PhylomeDB; P54507; -.
DR BioCyc; BSUB:BSU24620-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR022121; Peptidase_M73_camelysin.
DR InterPro; IPR023833; Signal_peptide_camelysin.
DR Pfam; PF12389; Peptidase_M73; 1.
DR TIGRFAMs; TIGR04088; cognate_SipW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome; Secreted;
KW Signal; Sporulation.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:10049401,
FT ECO:0000269|PubMed:10368135, ECO:0000269|PubMed:10658653"
FT CHAIN 28..261
FT /note="Major biofilm matrix component"
FT /id="PRO_0000079268"
FT REGION 241..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:5OF1"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:5OF1"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:5OF1"
FT STRAND 82..93
FT /evidence="ECO:0007829|PDB:5OF1"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:5OF1"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:5OF1"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:5OF1"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:5OF1"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:5OF1"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:5OF1"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:5OF1"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:5OF1"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:5OF1"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:5OF1"
FT STRAND 221..231
FT /evidence="ECO:0007829|PDB:5OF1"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:5OF2"
SQ SEQUENCE 261 AA; 28305 MW; 08C6B75785D8E1FA CRC64;
MGMKKKLSLG VASAALGLAL VGGGTWAAFN DIKSKDATFA SGTLDLSAKE NSASVNLSNL
KPGDKLTKDF QFENNGSLAI KEVLMALNYG DFKANGGSNT SPEDFLSQFE VTLLTVGKEG
GNGYPKNIIL DDANLKDLYL MSAKNDAAAA EKIKKQIDPK FLNASGKVNV ATIDGKTAPE
YDGVPKTPTD FDQVQMEIQF KDDKTKDEKG LMVQNKYQGN SIKLQFSFEA TQWNGLTIKK
DHTDKDGYVK ENEKAHSEDK N
