ID   TIG_SALPK               Reviewed;         432 AA.
AC   B5BD84;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Trigger factor {ECO:0000255|HAMAP-Rule:MF_00303};
DE            Short=TF {ECO:0000255|HAMAP-Rule:MF_00303};
DE            EC=5.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00303};
DE   AltName: Full=PPIase {ECO:0000255|HAMAP-Rule:MF_00303};
GN   Name=tig {ECO:0000255|HAMAP-Rule:MF_00303};
GN   OrderedLocusNames=SSPA2117;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(2009).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00303}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00303};
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:0000255|HAMAP-Rule:MF_00303}.
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:0000255|HAMAP-Rule:MF_00303}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00303}.
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DR   EMBL; FM200053; CAR60327.1; -; Genomic_DNA.
DR   RefSeq; WP_001198403.1; NC_011147.1.
DR   AlphaFoldDB; B5BD84; -.
DR   SMR; B5BD84; -.
DR   KEGG; sek:SSPA2117; -.
DR   HOGENOM; CLU_033058_2_0_6; -.
DR   Proteomes; UP000001869; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.50.40; -; 1.
DR   Gene3D; 3.30.70.1050; Trigger factor ribosome-binding domain; 1.
DR   Gene3D; 1.10.3120.10; Trigger factor, C-terminal domain; 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   NCBIfam; TIGR00115; tig; 1.
DR   PANTHER; PTHR30560; TRIGGER FACTOR CHAPERONE AND PEPTIDYL-PROLYL CIS/TRANS ISOMERASE; 1.
DR   PANTHER; PTHR30560:SF3; TRIGGER FACTOR-LIKE PROTEIN TIG, CHLOROPLASTIC; 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; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR   SUPFAM; SSF102735; Trigger factor ribosome-binding domain; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Chaperone; Cytoplasm; Isomerase; Rotamase.
FT   CHAIN           1..432
FT                   /note="Trigger factor"
FT                   /id="PRO_1000115579"
FT   DOMAIN          161..246
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
SQ   SEQUENCE   432 AA;  48050 MW;  B8D973998EE7D21C CRC64;
     MQVSVETTQG LGRRVTITIA ADSIETAVKS ELVNVAKKVR IDGFRKGKVP MNIVAQRYGA
     SVRQDVLGDL MSRNFVDAII KEKINPAGAP NYVPGEYKVG EDFTYSVEFE VYPEVELTGL
     ESIEVEKPVV EVTDADVDVM LDTLRKQQAT WKEKDGAADA EDRVTIDFTG SVDGEEFEGG
     KATDFVLAMG QGRMIPGFED GVKGHKAGEE FTIDVTFPEE YHAENLKGKA AKFVINLKKV
     EERELPELTE EFIKRFGVED GSVAGLRAEV RKNMERELKG AVRNRVKSQA IEGLVKANDI
     DVPAALIDSE IDVLRRQAAQ RFGGNEKQAL ELPRELFEEQ AKRRVVVGLL LGEVIRTNEL
     KADEERVKGL IEEMASAYED PKEVIEFYSK NKELMDNMRN VALEEQAVEA VLAKAKVSEK
     ATSFNELMNQ QA
//