ID   TIG_BRUME               Reviewed;         477 AA.
AC   Q8YGT8;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Trigger factor;
DE            Short=TF;
DE            EC=5.2.1.8;
DE   AltName: Full=PPIase;
GN   Name=tig; OrderedLocusNames=BMEI1069;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL52250.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008917; AAL52250.1; ALT_INIT; Genomic_DNA.
DR   PIR; AG3385; AG3385.
DR   AlphaFoldDB; Q8YGT8; -.
DR   SMR; Q8YGT8; -.
DR   STRING; 224914.BMEI1069; -.
DR   EnsemblBacteria; AAL52250; AAL52250; BMEI1069.
DR   KEGG; bme:BMEI1069; -.
DR   PATRIC; fig|224914.52.peg.357; -.
DR   eggNOG; COG0544; Bacteria.
DR   OMA; KGIKTQF; -.
DR   PhylomeDB; Q8YGT8; -.
DR   PRO; PR:Q8YGT8; -.
DR   Proteomes; UP000000419; Chromosome I.
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..477
FT                   /note="Trigger factor"
FT                   /id="PRO_0000179324"
FT   DOMAIN          169..254
FT                   /note="PPIase FKBP-type"
FT   REGION          435..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..457
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  53561 MW;  3EF7502661711C15 CRC64;
     MQVTETLNEG LKREIKVVVP AGDLEAKLAE RLETARGRAR INGFRPGKVP TAHLRKMYGK
     SFMAEIVNEI LNDSSRSILA ERNEKSATQP EVIMSEDEKE AEKVLDGKAD FVFSLNYEVL
     PAIEVKDFSK IAVTREVVDI SDEEVDEQVK RIASSTRTFE TKKGKAENED RVTIDYLGKL
     DGEPFEGGAD NDAQLVLGSG QFIPGFEEQL IGLKAGDEKV ITVTFPAEYG AAHLAGKEAT
     FDIKVKEVAK PNELVLDDET AKKLGIESLE RLRQVVREQI ESQYGQITRQ KVKRQILDAL
     DGDYQFETPQ KLVDAEFNNI WQQINFDLQQ AGRTFEDEET TEEAAREEYR KLAERRVRLG
     LVLSEIGEKA GVEVTEEELQ RAVYDQVRRY PGQEKEIYDF LRRTPDAVAN LRAPIFEEKV
     VDHLLANINV TDKKVSKEEL TAEDEDAASE AKPAKKAAAK KKAAPKKKAE EGKSEEA