ID   TIG_CAMJE               Reviewed;         444 AA.
AC   Q46108; Q0PBU6; Q46109; Q9PIT6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Trigger factor;
DE            Short=TF;
DE            EC=5.2.1.8;
DE   AltName: Full=PPIase;
GN   Name=tig; OrderedLocusNames=Cj0193c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=7670637; DOI=10.1099/13500872-141-6-1359;
RA   Griffiths P.L., Park R.W.A., Connerton I.F.;
RT   "The gene for Campylobacter trigger factor: evidence for multiple
RT   transcription start sites and protein products.";
RL   Microbiology 141:1359-1367(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Long; Synonyms=P2;
CC         IsoId=Q46108-1; Sequence=Displayed;
CC       Name=Short; Synonyms=P3;
CC         IsoId=Q46108-2; Sequence=VSP_018899;
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; X85954; CAA59930.1; -; Genomic_DNA.
DR   EMBL; X85954; CAA59931.1; -; Genomic_DNA.
DR   EMBL; AL111168; CAL34362.1; -; Genomic_DNA.
DR   PIR; H81437; H81437.
DR   PIR; I40755; I40755.
DR   RefSeq; WP_002851938.1; NC_002163.1.
DR   RefSeq; YP_002343651.1; NC_002163.1. [Q46108-1]
DR   AlphaFoldDB; Q46108; -.
DR   SMR; Q46108; -.
DR   IntAct; Q46108; 2.
DR   STRING; 192222.Cj0193c; -.
DR   PaxDb; Q46108; -.
DR   PRIDE; Q46108; -.
DR   DNASU; 904535; -.
DR   EnsemblBacteria; CAL34362; CAL34362; Cj0193c.
DR   GeneID; 904535; -.
DR   KEGG; cje:Cj0193c; -.
DR   PATRIC; fig|192222.6.peg.190; -.
DR   eggNOG; COG0544; Bacteria.
DR   HOGENOM; CLU_033058_2_2_7; -.
DR   OMA; KGIKTQF; -.
DR   Proteomes; UP000000799; 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   Alternative initiation; Cell cycle; Cell division; Chaperone; Cytoplasm;
KW   Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..444
FT                   /note="Trigger factor"
FT                   /id="PRO_0000034304"
FT   DOMAIN          165..250
FT                   /note="PPIase FKBP-type"
FT   VAR_SEQ         1..22
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018899"
FT   CONFLICT        63
FT                   /note="T -> S (in Ref. 1; CAA59930/CAA59931)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        228
FT                   /note="A -> R (in Ref. 1; CAA59930/CAA59931)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        330
FT                   /note="S -> C (in Ref. 1; CAA59930/CAA59931)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        395..401
FT                   /note="NPKEHLE -> IQRAFR (in Ref. 1; CAA59930)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        405..444
FT                   /note="KQGALPAVKMALIEEKLFNDIFIPKTEKSEKVSKKEKEDK -> NKELCLL
FT                   (in Ref. 1; CAA59930/CAA59931)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   444 AA;  50968 MW;  004EDE28043D9113 CRC64;
     MEVKAKQLDS VNATASVKIP SGMIKSEVEN LAKKASKSVK MDGFRPGKVP VSAVLKRYER
     ELTQDAEQNL FKSAVNSALQ ELKKENKELV GEPYFEKFDR KDGEIIAELI LSFKPEIKLE
     GYEKLIPEYQ TPKVSKKEID EKKDELLKRF ATPEAIKTKR ALKEGDFAKF DFEGFVDDKA
     FEGGKAENYV LEIGSKQFIP GFEDGMVGMK IGEEKDIKVT FPKEYGAAHL AGKDAVFKVK
     LHEIQELKIP ELDDEMLKKL LPGEEKASVE VLDEKLKEQI KNEKLFKLVN DELKGKFADA
     LIEKYNFDLP KGIVEQETDM QMRAAFNTFS EKEIEELKAS KEKYQEKRDS FKEEAQKSVK
     LTFIIDELAK LRKIEVNDQE LIQAIYFEAY RYGMNPKEHL ENYKKQGALP AVKMALIEEK
     LFNDIFIPKT EKSEKVSKKE KEDK