ID   TIG_RICPR               Reviewed;         445 AA.
AC   Q9ZCB7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Trigger factor;
DE            Short=TF;
DE            EC=5.2.1.8;
DE   AltName: Full=PPIase;
GN   Name=tig; OrderedLocusNames=RP842;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235273; CAA15266.1; -; Genomic_DNA.
DR   PIR; B71646; B71646.
DR   RefSeq; NP_221190.1; NC_000963.1.
DR   RefSeq; WP_004599675.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZCB7; -.
DR   SMR; Q9ZCB7; -.
DR   STRING; 272947.RP842; -.
DR   EnsemblBacteria; CAA15266; CAA15266; CAA15266.
DR   GeneID; 57569965; -.
DR   KEGG; rpr:RP842; -.
DR   PATRIC; fig|272947.5.peg.880; -.
DR   eggNOG; COG0544; Bacteria.
DR   HOGENOM; CLU_033058_3_2_5; -.
DR   OMA; KGIKTQF; -.
DR   Proteomes; UP000002480; 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; 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;
KW   Reference proteome; Rotamase.
FT   CHAIN           1..445
FT                   /note="Trigger factor"
FT                   /id="PRO_0000179417"
FT   DOMAIN          162..247
FT                   /note="PPIase FKBP-type"
SQ   SEQUENCE   445 AA;  51135 MW;  86676A8A1BA56A08 CRC64;
     MGIIVLKNEG LNFHARISTP LSEIDDDIQK ELLDLTKKVK VAGFRAGKVP VSIVKKKYGT
     SVRHDIIEKR INNLVNHIIK EYNLNIIGRP KIEELQNEPD KDLEFTVKIE LLPKITIPDL
     KKISLDRPKL AVNSQDVEIQ LEKLAALTKC YTKESKTKIK DGDQVTIDAI GYIKDRAFDG
     GKLNDFKVVI GSNTLIQGFE QQLIGSKTGN EVDVNVTFPE NYHDKNLSGK DAHFVVQIKA
     VHTAEPTIID EEFAKKFQSN SLEELRTHFA KQIENESEEA INTIMKMNLF DKLEKLLDFD
     VPESLLEQEK NILKSETDKN KHDGSLLNGK SSKEITEYYN KLALRRVRIG LLLAEYAKFK
     NLQLEPDDFK KIIMQQARNF PGQENMIFDF YKNNPRAIEG LKGPALEDKT VQYIFNNEIQ
     LKEKRYTKEE LEKYLETEEQ RISLI