(data stored in SCRATCH zone)

SWISSPROT: TAPA_BACSU

ID   TAPA_BACSU              Reviewed;         253 AA.
AC   P40949;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   11-DEC-2019, entry version 96.
DE   RecName: Full=TasA anchoring/assembly protein {ECO:0000303|PubMed:21477127};
DE   AltName: Full=Biofilm assembly accessory protein TapA {ECO:0000305};
DE   Flags: Precursor;
GN   Name=tapA {ECO:0000303|PubMed:21477127}; Synonyms=yqhD, yqxM;
GN   OrderedLocusNames=BSU24640;
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 1-51.
RX   PubMed=2507524; DOI=10.1128/jb.171.10.5386-5404.1989;
RA   Albano M., Breitling R., Dubnau D.A.;
RT   "Nucleotide sequence and genetic organization of the Bacillus subtilis comG
RT   operon.";
RL   J. Bacteriol. 171:5386-5404(1989).
RN   [4]
RP   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   [5]
RP   SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=10559173;
RA   Stoever A.G., Driks A.;
RT   "Control of synthesis and secretion of the Bacillus subtilis protein
RT   YqxM.";
RL   J. Bacteriol. 181:7065-7069(1999).
RN   [6]
RP   FUNCTION, 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   [7]
RP   FUNCTION.
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   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21477127; DOI=10.1111/j.1365-2958.2011.07653.x;
RA   Romero D., Vlamakis H., Losick R., Kolter R.;
RT   "An accessory protein required for anchoring and assembly of amyloid fibres
RT   in B. subtilis biofilms.";
RL   Mol. Microbiol. 80:1155-1168(2011).
RN   [9]
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   [10]
RP   FUNCTION.
RX   PubMed=24488317; DOI=10.1128/jb.01363-13;
RA   Romero D., Vlamakis H., Losick R., Kolter R.;
RT   "Functional analysis of the accessory protein TapA in Bacillus subtilis
RT   amyloid fiber assembly.";
RL   J. Bacteriol. 196:1505-1513(2014).
CC   -!- FUNCTION: Required for biofilm formation (PubMed:16430695,
CC       PubMed:16430696, PubMed:21477127, PubMed:24488317). Required for the
CC       proper anchoring and polymerization of TasA amyloid fibers at the cell
CC       surface (PubMed:16430696, PubMed:21477127, PubMed:24488317). Is also a
CC       minor component of TasA fibers (PubMed:21477127).
CC       {ECO:0000269|PubMed:16430695, ECO:0000269|PubMed:16430696,
CC       ECO:0000269|PubMed:21477127, ECO:0000269|PubMed:24488317}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000269|PubMed:21477127}. Secreted {ECO:0000269|PubMed:10559173,
CC       ECO:0000269|PubMed:21477127}. Note=Closely associated with the
CC       peptidoglycan in the cell wall. Is also present in the extracellular
CC       matrix (PubMed:21477127). Processing and export depend on SipW
CC       (PubMed:10559173). {ECO:0000269|PubMed:10559173,
CC       ECO:0000269|PubMed:21477127}.
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:10464223). Induced by a high
CC       concentration of salt (PubMed:10559173). During most conditions of
CC       growth, may be present at very low levels or is not synthesized at all,
CC       due, at least in part, to post-transcriptional repression
CC       (PubMed:10559173). {ECO:0000269|PubMed:10464223,
CC       ECO:0000269|PubMed:10559173, ECO:0000269|PubMed:16430695,
CC       ECO:0000269|PubMed:23646920}.
CC   -!- DISRUPTION PHENOTYPE: Mutation impairs colony surface architecture
CC       (PubMed:16430695). Mutant produces fewer and altered amyloid fibers
CC       (PubMed:21477127). {ECO:0000269|PubMed:16430695,
CC       ECO:0000269|PubMed:21477127}.
DR   EMBL; D84432; BAA12539.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14395.1; -; Genomic_DNA.
DR   EMBL; M29691; AAA83374.1; -; Genomic_DNA.
DR   PIR; G69968; G69968.
DR   RefSeq; NP_390344.1; NC_000964.3.
DR   RefSeq; WP_004399106.1; NZ_JNCM01000036.1.
DR   SMR; P40949; -.
DR   STRING; 224308.BSU24640; -.
DR   PaxDb; P40949; -.
DR   PRIDE; P40949; -.
DR   EnsemblBacteria; CAB14395; CAB14395; BSU24640.
DR   GeneID; 938532; -.
DR   KEGG; bsu:BSU24640; -.
DR   PATRIC; fig|224308.179.peg.2682; -.
DR   HOGENOM; HOG000009026; -.
DR   KO; K19433; -.
DR   OMA; WKWELHK; -.
DR   BioCyc; BSUB:BSU24640-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0097311; C:bacterial biofilm matrix; IEA:InterPro.
DR   GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
DR   InterPro; IPR023833; Signal_peptide_camelysin.
DR   InterPro; IPR023848; TasA.
DR   TIGRFAMs; TIGR04088; cognate_SipW; 1.
DR   TIGRFAMs; TIGR04087; YqxM_for_SipW; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; P40949.
DR   SWISS-2DPAGE; P40949.
KW   Cell wall; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..253
FT                   /note="TasA anchoring/assembly protein"
FT                   /id="PRO_0000049851"
FT   REGION          50..57
FT                   /note="Important for TasA fiber formation"
FT                   /evidence="ECO:0000269|PubMed:24488317"
FT   CONFLICT        39..51
FT                   /note="DDTSAAFHDIETF -> MIQALLFMILKHL (in Ref. 3;
FT                   AAA83374)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   253 AA;  29075 MW;  C94B701ADFF4E5E4 CRC64;
     MFRLFHNQQK AKTKLKVLLI FQLSVIFSLT AAICLQFSDD TSAAFHDIET FDVSLQTCKD
     FQHTDKNCHY DKRWDQSDLH ISDQTDTKGT VCSPFALFAV LENTGEKLKK SKWKWELHKL
     ENARKPLKDG NVIEKGFVSN QIGDSLYKIE TKKKMKPGIY AFKVYKPAGY PANGSTFEWS
     EPMRLAKCDE KPTVPKKETK SDVKKENETT QKDIPEKTMK EETSQEAVTK EKETQSDQKE
     SGEEDEKSNE ADQ
//

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