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 03-AUG-2022, entry version 107.
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; 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 [5]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=10559173; DOI=10.1128/jb.181.22.7065-7069.1999;
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}.
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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 PDB; 6HQC; X-ray; 1.28 A; A=75-190.
DR PDB; 6QAY; NMR; -; A=44-190.
DR PDBsum; 6HQC; -.
DR PDBsum; 6QAY; -.
DR AlphaFoldDB; P40949; -.
DR BMRB; P40949; -.
DR SMR; P40949; -.
DR STRING; 224308.BSU24640; -.
DR PaxDb; P40949; -.
DR PRIDE; P40949; -.
DR DNASU; 938532; -.
DR EnsemblBacteria; CAB14395; CAB14395; BSU_24640.
DR GeneID; 938532; -.
DR KEGG; bsu:BSU24640; -.
DR PATRIC; fig|224308.179.peg.2682; -.
DR eggNOG; ENOG5030CJ7; Bacteria.
DR OMA; WKWELHK; -.
DR BioCyc; BSUB:BSU24640-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0097311; C:bacterial biofilm matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; 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 1: Evidence at protein level;
KW 3D-structure; 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 REGION 190..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 39..51
FT /note="DDTSAAFHDIETF -> MIQALLFMILKHL (in Ref. 3;
FT AAA83374)"
FT /evidence="ECO:0000305"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:6QAY"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:6HQC"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:6HQC"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:6HQC"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:6HQC"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:6QAY"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:6HQC"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:6HQC"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:6HQC"
FT STRAND 157..165
FT /evidence="ECO:0007829|PDB:6HQC"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:6HQC"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:6HQC"
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
