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TIG_SHEON
ID   TIG_SHEON               Reviewed;         434 AA.
AC   Q8EG20;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Trigger factor {ECO:0000255|HAMAP-Rule:MF_00303};
DE            Short=TF {ECO:0000255|HAMAP-Rule:MF_00303};
DE            EC=5.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00303};
DE   AltName: Full=PPIase {ECO:0000255|HAMAP-Rule:MF_00303};
GN   Name=tig {ECO:0000255|HAMAP-Rule:MF_00303}; OrderedLocusNames=SO_1793;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(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. {ECO:0000255|HAMAP-
CC       Rule:MF_00303}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00303};
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:0000255|HAMAP-Rule:MF_00303}.
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:0000255|HAMAP-Rule:MF_00303}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00303}.
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DR   EMBL; AE014299; AAN54846.1; -; Genomic_DNA.
DR   RefSeq; NP_717402.1; NC_004347.2.
DR   RefSeq; WP_011071915.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EG20; -.
DR   SMR; Q8EG20; -.
DR   STRING; 211586.SO_1793; -.
DR   PaxDb; Q8EG20; -.
DR   KEGG; son:SO_1793; -.
DR   PATRIC; fig|211586.12.peg.1723; -.
DR   eggNOG; COG0544; Bacteria.
DR   HOGENOM; CLU_033058_2_0_6; -.
DR   OMA; KGIKTQF; -.
DR   OrthoDB; 932993at2; -.
DR   PhylomeDB; Q8EG20; -.
DR   BioCyc; SONE211586:G1GMP-1644-MON; -.
DR   Proteomes; UP000008186; 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; 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..434
FT                   /note="Trigger factor"
FT                   /id="PRO_0000179422"
FT   DOMAIN          160..245
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
SQ   SEQUENCE   434 AA;  47596 MW;  96613EE7648BC203 CRC64;
     MQVSVEATQG LERRLTISVP AEQIEKLVKD SLQREAKRAR IPGFRPGKVP VTVINKRYGA
     AIRQDITGEV MQRNFIEAII AEKLNPAGAP TFVPGATDGE KFEFVATFEI YPEVELKGLD
     AIVVEQPKAS VTDADVDSMI ETLRKQHATF AAVEREAVDG DKVKMNFVGS VDGVEFEGGK
     AEDFELQLGS GRMIPGFEAG ILGHKAGEEF VIDVTFPEEY HAENLKGKAA KFAITLTEVL
     AANLPEVNDE FAALFGITEG GLEALKTEIR KNMNRELEQA LKANVKEQVI AGLLANNDIE
     LPKALIDGEV NVLRQQAMQR FGGQTANMPE LPAELFTEQA ARRVKIGLLL GEVIKTNELK
     AEDERVQGLI ASMASAYEDP SEVIAYYNSN KELMQNMRNV ALEEQAVEAL LKTAKVTEKT
     VAFEEFMNKA TGRA
 
 
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