ID   TIG_KOSOT               Reviewed;         439 AA.
AC   C5CGV0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
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}; OrderedLocusNames=Kole_1938;
OS   Kosmotoga olearia (strain ATCC BAA-1733 / DSM 21960 / TBF 19.5.1).
OC   Bacteria; Thermotogae; Kosmotogales; Kosmotogaceae; Kosmotoga.
OX   NCBI_TaxID=521045;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1733 / DSM 21960 / TBF 19.5.1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Noll K.;
RT   "Complete sequence of Thermotogales bacterium TBF 19.5.1.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001634; ACR80619.1; -; Genomic_DNA.
DR   RefSeq; WP_015869262.1; NC_012785.1.
DR   AlphaFoldDB; C5CGV0; -.
DR   SMR; C5CGV0; -.
DR   STRING; 521045.Kole_1938; -.
DR   EnsemblBacteria; ACR80619; ACR80619; Kole_1938.
DR   KEGG; kol:Kole_1938; -.
DR   eggNOG; COG0544; Bacteria.
DR   HOGENOM; CLU_033058_3_1_0; -.
DR   OMA; YTIEGFR; -.
DR   OrthoDB; 932993at2; -.
DR   Proteomes; UP000002382; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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   GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:InterPro.
DR   Gene3D; 1.10.3120.10; -; 1.
DR   Gene3D; 3.10.50.30; -; 1.
DR   Gene3D; 3.30.70.1050; -; 1.
DR   HAMAP; MF_00303; Trigger_factor_Tig; 1.
DR   InterPro; IPR036953; GreA/GreB_C_sf.
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; 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.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Chaperone; Cytoplasm; Isomerase;
KW   Reference proteome; Rotamase.
FT   CHAIN           1..439
FT                   /note="Trigger factor"
FT                   /id="PRO_1000204993"
FT   DOMAIN          158..233
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
FT   REGION          410..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   439 AA;  50877 MW;  7F88600A787C8021 CRC64;
     MEKNVVKAEK NVEIVEFTFG PDEIAEAENE IVRYVNKNYT IPGFRKGKAP KRIIETFFGE
     NFRDMVLEEL SRKIEDTLKD EELFIPAVIA DRKIEGDVAV FVVELHREPK VELKDYTGLE
     LSVPKQEEVL ANYVDNKLEE LRNEAAIVEP KDGPAEIGDV INIEYTIEKD GKIIADHKTQ
     EILIVEDDDR PIVTNVIGKK KGDIVEFDRT FENSNNKYHY KIEIKEVLKR TLMELNDEFA
     KSVASEVNTL EELKKKLEEE GLEAFESWKK DFLRQQVQDK LAELVELEIS EKTLDYFVNR
     AIENAKKENT YDSYLKQAGS EEKLYEEFKT GILNELKKNT AIEKIAEKEQ IEVTDEEVMK
     TAEELSTYWG ISPERAKEIV KTREDIRNDI VENIRRTKVQ DLIVEKATIK EISADEPVEE
     QKEEEEKEEA GSENSENKE