(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 96.
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;
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;
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;
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:0000244|PDB:5OF1, ECO:0000244|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       Self; 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}.
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   SMR; P54507; -.
DR   DIP; DIP-58529N; -.
DR   STRING; 224308.BSU24620; -.
DR   MEROPS; M73.A01; -.
DR   PaxDb; P54507; -.
DR   PRIDE; P54507; -.
DR   EnsemblBacteria; CAB14393; CAB14393; BSU24620.
DR   GeneID; 938545; -.
DR   KEGG; bsu:BSU24620; -.
DR   PATRIC; fig|224308.179.peg.2680; -.
DR   HOGENOM; HOG000083455; -.
DR   KO; K06336; -.
DR   OMA; TWAAFND; -.
DR   PhylomeDB; P54507; -.
DR   BioCyc; BSUB:BSU24620-MONOMER; -.
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;
DR   PRODOM; P54507.
DR   SWISS-2DPAGE; P54507.
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   STRAND          42..45
FT                   /evidence="ECO:0000244|PDB:5OF1"
FT   STRAND          52..57
FT                   /evidence="ECO:0000244|PDB:5OF1"
FT   STRAND          65..73
FT                   /evidence="ECO:0000244|PDB:5OF1"
FT   STRAND          82..93
FT                   /evidence="ECO:0000244|PDB:5OF1"
FT   HELIX           102..106
FT                   /evidence="ECO:0000244|PDB:5OF1"
FT   STRAND          109..115
FT                   /evidence="ECO:0000244|PDB:5OF1"
FT   STRAND          127..134
FT                   /evidence="ECO:0000244|PDB:5OF1"
FT   HELIX           135..144
FT                   /evidence="ECO:0000244|PDB:5OF1"
FT   HELIX           147..154
FT                   /evidence="ECO:0000244|PDB:5OF1"
FT   HELIX           159..161
FT                   /evidence="ECO:0000244|PDB:5OF1"
FT   HELIX           178..180
FT                   /evidence="ECO:0000244|PDB:5OF1"
FT   STRAND          181..183
FT                   /evidence="ECO:0000244|PDB:5OF1"
FT   STRAND          194..200
FT                   /evidence="ECO:0000244|PDB:5OF1"
FT   HELIX           213..217
FT                   /evidence="ECO:0000244|PDB:5OF1"
FT   STRAND          221..231
FT                   /evidence="ECO:0000244|PDB:5OF1"
FT   STRAND          235..237
FT                   /evidence="ECO:0000244|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
//

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