ID   TIG_OENOE               Reviewed;         438 AA.
AC   Q9RLJ3;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Trigger factor;
DE            Short=TF;
DE            EC=5.2.1.8;
DE   AltName: Full=PPIase;
GN   Name=tig;
OS   Oenococcus oeni (Leuconostoc oenos).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Oenococcus.
OX   NCBI_TaxID=1247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=8413;
RX   PubMed=10542163; DOI=10.1128/jb.181.21.6634-6641.1999;
RA   Jobin M.P., Garmyn D., Divies C., Guzzo J.;
RT   "The Oenococcus oeni clpx homologue is a heat shock gene preferentially
RT   expressed in exponential growth phase.";
RL   J. Bacteriol. 181:6634-6641(1999).
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; Y15953; CAB60144.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RLJ3; -.
DR   SMR; Q9RLJ3; -.
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; 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   3: Inferred from homology;
KW   Cell cycle; Cell division; Chaperone; Cytoplasm; Isomerase; Rotamase.
FT   CHAIN           1..438
FT                   /note="Trigger factor"
FT                   /id="PRO_0000179398"
FT   DOMAIN          170..255
FT                   /note="PPIase FKBP-type"
SQ   SEQUENCE   438 AA;  48176 MW;  9EF11F9E1879F77B CRC64;
     MVDIIKTNAT FKAGKGNKGT LSFEIPAKQI SSGIDQAFNK QKDKINIPGF RKGHVSKELF
     LARFGEEALY EDALNAILPD IYDQAVNEAD ITVVGQPQII PDDLKHGGPS KIHAEVTLAP
     TVELGDYKGV EVEKESDEVS DKELNAELER LQKGEAELVP AKEDQVSEKG DTVVIDFDGS
     VDGKQFDGGK AQNFSLSLGS GQFIPGFEDQ LVGHKAGDDV DVKVTFPKDY QAKNLAGKEA
     VFAVTIHELK KLETPALDNE FAKDVDDSVL VLEELKAKTK EKLAKDKAEK NKDAFEDAAI
     QKVVDGAKIN PEKLPEEMIN DDVSRQMQTF FNNLAGQGVK PEMYFQIPNQ PGAVKATNDR
     RRTNRVKTNL VLEEIARVEK INPSNEEIDK EIKSLASEYN IKESEVEKSV SAGMLSHDLK
     VQQAVELIVN SAQAVEKK