TCPT_VIBCH
ID TCPT_VIBCH Reviewed; 503 AA.
AC P29480; Q9KTR0;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Toxin coregulated pilus biosynthesis protein T;
DE AltName: Full=TCP pilus biosynthesis protein TcpT;
GN Name=tcpT; OrderedLocusNames=VC_0835;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Classical Inaba Z17561 / Serotype O1;
RX PubMed=8097178; DOI=10.1016/0378-1119(93)90589-u;
RA Ogierman M.A., Zabihi S., Mourtzios L., Manning P.A.;
RT "Genetic organization and sequence of the promoter-distal region of the tcp
RT gene cluster of Vibrio cholerae.";
RL Gene 126:51-60(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Involved in the translocation of the TcpA pilin.
CC -!- INTERACTION:
CC P29480; P0C6D5: tcpR; NbExp=2; IntAct=EBI-6399865, EBI-6399872;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}.
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DR EMBL; X64098; CAA45462.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF93998.1; -; Genomic_DNA.
DR PIR; F82275; F82275.
DR RefSeq; NP_230483.1; NC_002505.1.
DR RefSeq; WP_000020697.1; NZ_LT906614.1.
DR AlphaFoldDB; P29480; -.
DR SMR; P29480; -.
DR IntAct; P29480; 1.
DR STRING; 243277.VC_0835; -.
DR DNASU; 2614502; -.
DR EnsemblBacteria; AAF93998; AAF93998; VC_0835.
DR KEGG; vch:VC_0835; -.
DR PATRIC; fig|243277.26.peg.796; -.
DR eggNOG; COG2804; Bacteria.
DR HOGENOM; CLU_013446_12_0_6; -.
DR OMA; TVHAGNI; -.
DR BioCyc; VCHO:VC0835-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001482; T2SS/T4SS.
DR Pfam; PF00437; T2SSE; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00662; T2SP_E; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..503
FT /note="Toxin coregulated pilus biosynthesis protein T"
FT /id="PRO_0000207299"
FT BINDING 236..243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 137
FT /note="A -> S (in Ref. 1; CAA45462)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 57277 MW; ED3FD8FFD579F918 CRC64;
MSIDIKYLSR IDIDREEFFF KDSRLMCKKF DEEREVLTLL EFDTKFRVNL LKKDKVYKYF
LVSDANHKLL IANLVTEQQA KDLSFIEKDI MKIASSATAY GASDIHFIRE DRICKIKFRV
NGTMIDYREI LSSEADALMF VLYNVMATTK ETTWNRKLPQ DANIILVINE KAYRFRYAHM
PLFGEGGKNY HAVVRIIYPS NNFVCTNYQD IGYNEADTDA IARILNTSYG LFIVSGTTGS
GKSTSLKKYI ELLFFNKYKG KGCFVTVEDP VEYLISGAQQ SSIVADNDDK TKNPFADAVR
SAMRRDPDVI MIGEIRDKPT VEALSSAVES GHYCLTTIHA GSVVSVLQRL SGLGMKADKI
ASPGFLAGIT SQKLIPELCP SCKVSFVDER YQRAVFSANE NGCEACNHSG FKGRLLLLET
LVPTVEDLEL VASENWVSLY RKYRERRFIK TGKKGLGEGF SIKDKAYYNV LKGKVCHEYF
MLHFGQLDHE DENIIYENYL QEV