ID   TIG_AQUAE               Reviewed;         478 AA.
AC   O67358;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Trigger factor;
DE            Short=TF;
DE            EC=5.2.1.8;
DE   AltName: Full=PPIase;
GN   Name=tig; OrderedLocusNames=aq_1340;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(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   -!- MISCELLANEOUS: The N-terminus of this protein overlaps with a tRNA(Leu)
CC       encoded in another frame on the same strand. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000657; AAC07311.1; -; Genomic_DNA.
DR   PIR; C70416; C70416.
DR   RefSeq; NP_213922.1; NC_000918.1.
DR   AlphaFoldDB; O67358; -.
DR   SMR; O67358; -.
DR   STRING; 224324.aq_1340; -.
DR   EnsemblBacteria; AAC07311; AAC07311; aq_1340.
DR   KEGG; aae:aq_1340; -.
DR   PATRIC; fig|224324.8.peg.1047; -.
DR   eggNOG; COG0544; Bacteria.
DR   HOGENOM; CLU_033058_3_1_0; -.
DR   InParanoid; O67358; -.
DR   OMA; YTIEGFR; -.
DR   OrthoDB; 932993at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0051083; P:'de novo' cotranslational protein folding; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0043335; P:protein unfolding; IBA:GO_Central.
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; 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..478
FT                   /note="Trigger factor"
FT                   /id="PRO_0000179302"
FT   DOMAIN          197..279
FT                   /note="PPIase FKBP-type"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   478 AA;  54896 MW;  6868FD51F2A5BAD0 CRC64;
     MAELADAPDL GSGARKGVRV RLPPPAPHKN GGKNESRGSG QGSLFKALTV EIQGDSVKEK
     IDEMYKQLQK TVQIQGFRKG KAPLWIVRAK YKDYVEEEVG KKIADETLQK ALEEANLKPV
     ADVFLEKVEV DEKEGKVKYV VSFEVAPEFE LKDVENLEVE VPKIEFKEDY VKEELERLRE
     ANAVWEPKDE NEPAQEGDML VVEYEVEEIG GEGEKVKQET SVILGQGMLR PEVEEALKGK
     KVGEEVELKE LPLYDQEGKE VGKVNIKIKI KEIKKKVLPE LNDEFAKELG YASLKDLEEK
     IREDIKQKLE KLKEQVIEER VADKLVEIHD IPVPQTLLRR ELSFLVDRRL RELQALGIDT
     RYVDIKKIVE EVQPIAEANI KLRFILDKYA QEKGIEPTGE DIEAQYKELA EQYGTTVDEI
     KKYFKENNLE QVVYEDARRK KALKEIISKV KIKEVEQKQE EEKKEEKEEV KNESQGNT