TIG_VIBCH
ID TIG_VIBCH Reviewed; 433 AA.
AC Q9KQS5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Trigger factor;
DE Short=TF;
DE EC=5.2.1.8;
DE AltName: Full=PPIase;
GN Name=tig; OrderedLocusNames=VC_1923;
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 [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 protein export. Acts as a chaperone by
CC maintaining the newly synthesized protein in an open conformation.
CC Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=About half TF is bound to the
CC ribosome near the polypeptide exit tunnel while the other half is free
CC in the cytoplasm. {ECO:0000250}.
CC -!- DOMAIN: Consists of 3 domains; the N-terminus binds the ribosome, the
CC middle domain has PPIase activity, while the C-terminus has intrinsic
CC chaperone activity on its own. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.
CC {ECO:0000305}.
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DR EMBL; AE003852; AAF95071.1; -; Genomic_DNA.
DR PIR; H82139; H82139.
DR RefSeq; NP_231557.1; NC_002505.1.
DR RefSeq; WP_001198446.1; NZ_LT906614.1.
DR PDB; 1T11; X-ray; 2.50 A; A/B=1-389.
DR PDBsum; 1T11; -.
DR AlphaFoldDB; Q9KQS5; -.
DR SMR; Q9KQS5; -.
DR STRING; 243277.VC_1923; -.
DR DNASU; 2613552; -.
DR EnsemblBacteria; AAF95071; AAF95071; VC_1923.
DR GeneID; 57740555; -.
DR KEGG; vch:VC_1923; -.
DR PATRIC; fig|243277.26.peg.1840; -.
DR eggNOG; COG0544; Bacteria.
DR HOGENOM; CLU_033058_2_0_6; -.
DR OMA; KGIKTQF; -.
DR BioCyc; VCHO:VC1923-MON; -.
DR EvolutionaryTrace; Q9KQS5; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0043335; P:protein unfolding; IBA:GO_Central.
DR Gene3D; 1.10.3120.10; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 3.30.70.1050; -; 1.
DR HAMAP; MF_00303; Trigger_factor_Tig; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR005215; Trig_fac.
DR InterPro; IPR008880; Trigger_fac_C.
DR InterPro; IPR037041; Trigger_fac_C_sf.
DR InterPro; IPR008881; Trigger_fac_ribosome-bd_bac.
DR InterPro; IPR036611; Trigger_fac_ribosome-bd_sf.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR30560; PTHR30560; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF05698; Trigger_C; 1.
DR Pfam; PF05697; Trigger_N; 1.
DR PIRSF; PIRSF003095; Trigger_factor; 1.
DR SUPFAM; SSF102735; SSF102735; 1.
DR SUPFAM; SSF109998; SSF109998; 1.
DR TIGRFAMs; TIGR00115; tig; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chaperone; Cytoplasm; Isomerase;
KW Reference proteome; Rotamase.
FT CHAIN 1..433
FT /note="Trigger factor"
FT /id="PRO_0000179457"
FT DOMAIN 161..246
FT /note="PPIase FKBP-type"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1T11"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:1T11"
FT HELIX 21..36
FT /evidence="ECO:0007829|PDB:1T11"
FT HELIX 51..81
FT /evidence="ECO:0007829|PDB:1T11"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1T11"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1T11"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:1T11"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:1T11"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:1T11"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:1T11"
FT STRAND 163..175
FT /evidence="ECO:0007829|PDB:1T11"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:1T11"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1T11"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:1T11"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:1T11"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1T11"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:1T11"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:1T11"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:1T11"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:1T11"
FT HELIX 262..287
FT /evidence="ECO:0007829|PDB:1T11"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:1T11"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:1T11"
FT HELIX 304..321
FT /evidence="ECO:0007829|PDB:1T11"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:1T11"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:1T11"
FT HELIX 338..357
FT /evidence="ECO:0007829|PDB:1T11"
FT HELIX 364..376
FT /evidence="ECO:0007829|PDB:1T11"
SQ SEQUENCE 433 AA; 47954 MW; 23A889FA74C4510A CRC64;
MQVTVETLEG LQRRLNITVP AANIEDAVAA ELRNIAKNRR FDGFRKGKVP MKMVAKMYGK
AVRQDVLGEV MQRHFIEAIV KEKINPAGAP TFAPVEIGEG KDLVFTATFE VYPEVELKGL
ENIAVEKPAA EVTDADVAEM LETLRKQQAT WKEVDEAAEN GKRVSIDFVG SIDGVEFEGG
KAENFPLEMG AGRMIPGFED GIVGKTKGME FVIDVTFPED YHAENLKGKA AKFAIKVNKV
EARELPELND EFVARFGVAE GGVDALKAEV RKNMERELKQ AIKARIKEQA IEGLVKENEI
QVPSALIDQE INVLRQQAAQ RFGGNVEAAA QLPRELFEEQ AKRRVVVGLL LGEVIRTHEL
KADEEKVKAL ITEMATAYED PSEVVSYYEQ NQQLMNNMRN VALEEQAVDA IIAKAKVTEK
AISFSELMNP VAA
