ID TIG_THEMA Reviewed; 425 AA. AC Q9WZF8; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 140. DE RecName: Full=Trigger factor; DE Short=TF; DE EC=5.2.1.8; DE AltName: Full=PPIase; GN Name=tig; OrderedLocusNames=TM_0694; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F., RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). 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 -!- INTERACTION: CC Q9WZF8; P38526: rpsG; NbExp=5; IntAct=EBI-2463534, EBI-2463521; 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE000512; AAD35776.1; -; Genomic_DNA. DR PIR; D72345; D72345. DR RefSeq; NP_228503.1; NC_000853.1. DR RefSeq; WP_004081061.1; NZ_CP011107.1. DR PDB; 2NSA; X-ray; 1.70 A; A=244-405. DR PDB; 2NSB; X-ray; 3.20 A; A=1-109. DR PDB; 2NSC; X-ray; 2.20 A; A=1-109. DR PDB; 3GTY; X-ray; 3.40 A; X=1-425. DR PDB; 3GU0; X-ray; 3.50 A; A=1-405. DR PDB; 6J0A; EM; 14.20 A; Q=1-405. DR PDBsum; 2NSA; -. DR PDBsum; 2NSB; -. DR PDBsum; 2NSC; -. DR PDBsum; 3GTY; -. DR PDBsum; 3GU0; -. DR PDBsum; 6J0A; -. DR AlphaFoldDB; Q9WZF8; -. DR EMDB; EMD-9759; -. DR SMR; Q9WZF8; -. DR IntAct; Q9WZF8; 1. DR STRING; 243274.TM_0694; -. DR PaxDb; 243274-THEMA_01195; -. DR DNASU; 898361; -. DR EnsemblBacteria; AAD35776; AAD35776; TM_0694. DR KEGG; tma:TM0694; -. DR eggNOG; COG0544; Bacteria. DR InParanoid; Q9WZF8; -. DR OrthoDB; 9767721at2; -. DR EvolutionaryTrace; Q9WZF8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. 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 GO; GO:0032784; P:regulation of DNA-templated transcription elongation; IEA:InterPro. DR Gene3D; 3.10.50.30; Transcription elongation factor, GreA/GreB, C-terminal domain; 1. DR Gene3D; 3.30.70.1050; Trigger factor ribosome-binding domain; 1. DR Gene3D; 1.10.3120.10; Trigger factor, C-terminal domain; 1. DR HAMAP; MF_00303; Trigger_factor_Tig; 1. DR InterPro; IPR036953; GreA/GreB_C_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 NCBIfam; TIGR00115; tig; 1. DR PANTHER; PTHR30560; TRIGGER FACTOR CHAPERONE AND PEPTIDYL-PROLYL CIS/TRANS ISOMERASE; 1. DR PANTHER; PTHR30560:SF3; TRIGGER FACTOR-LIKE PROTEIN TIG, CHLOROPLASTIC; 1. DR Pfam; PF05698; Trigger_C; 1. DR Pfam; PF05697; Trigger_N; 1. DR PIRSF; PIRSF003095; Trigger_factor; 1. DR SUPFAM; SSF54534; FKBP-like; 1. DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1. DR SUPFAM; SSF102735; Trigger factor ribosome-binding domain; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cell division; Chaperone; Cytoplasm; Isomerase; KW Reference proteome; Rotamase. FT CHAIN 1..425 FT /note="Trigger factor" FT /id="PRO_0000179452" FT DOMAIN 158..231 FT /note="PPIase FKBP-type" FT STRAND 2..9 FT /evidence="ECO:0007829|PDB:2NSC" FT STRAND 12..18 FT /evidence="ECO:0007829|PDB:2NSC" FT HELIX 21..36 FT /evidence="ECO:0007829|PDB:2NSC" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:3GU0" FT HELIX 51..58 FT /evidence="ECO:0007829|PDB:2NSC" FT HELIX 59..61 FT /evidence="ECO:0007829|PDB:2NSC" FT HELIX 62..71 FT /evidence="ECO:0007829|PDB:2NSC" FT HELIX 74..77 FT /evidence="ECO:0007829|PDB:2NSC" FT TURN 78..80 FT /evidence="ECO:0007829|PDB:2NSC" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:3GTY" FT STRAND 88..94 FT /evidence="ECO:0007829|PDB:3GTY" FT STRAND 99..107 FT /evidence="ECO:0007829|PDB:3GTY" FT STRAND 110..112 FT /evidence="ECO:0007829|PDB:3GTY" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:3GTY" FT STRAND 119..124 FT /evidence="ECO:0007829|PDB:3GTY" FT HELIX 126..144 FT /evidence="ECO:0007829|PDB:3GTY" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:3GTY" FT STRAND 159..168 FT /evidence="ECO:0007829|PDB:3GTY" FT STRAND 174..183 FT /evidence="ECO:0007829|PDB:3GTY" FT HELIX 193..196 FT /evidence="ECO:0007829|PDB:3GTY" FT STRAND 204..211 FT /evidence="ECO:0007829|PDB:3GTY" FT STRAND 214..228 FT /evidence="ECO:0007829|PDB:3GTY" FT HELIX 235..239 FT /evidence="ECO:0007829|PDB:3GTY" FT STRAND 241..244 FT /evidence="ECO:0007829|PDB:3GU0" FT HELIX 248..254 FT /evidence="ECO:0007829|PDB:2NSA" FT HELIX 259..262 FT /evidence="ECO:0007829|PDB:2NSA" FT HELIX 267..278 FT /evidence="ECO:0007829|PDB:2NSA" FT HELIX 279..282 FT /evidence="ECO:0007829|PDB:2NSA" FT STRAND 284..286 FT /evidence="ECO:0007829|PDB:3GTY" FT HELIX 289..305 FT /evidence="ECO:0007829|PDB:2NSA" FT HELIX 309..314 FT /evidence="ECO:0007829|PDB:2NSA" FT HELIX 319..347 FT /evidence="ECO:0007829|PDB:2NSA" FT HELIX 353..367 FT /evidence="ECO:0007829|PDB:2NSA" FT HELIX 371..380 FT /evidence="ECO:0007829|PDB:2NSA" FT HELIX 382..402 FT /evidence="ECO:0007829|PDB:2NSA" FT STRAND 405..410 FT /evidence="ECO:0007829|PDB:3GTY" SQ SEQUENCE 425 AA; 49898 MW; BEC16F20ACFDD922 CRC64; MEVKELERDK NRVVLEYVFG AEEIAQAEDK AVRYLNQRVE IPGFRKGRIP KNVLKMKLGE EFQEYTLDFL MDLIPDTLKD RKLILSPIVT ERELKDVTAR VVVEVHEEPE VRIGDISKIE VEKVDEEKVL EKYVERRIED LRESHALLEP KEGPAEAGDL VRVNMEVYNE EGKKLTSREY EYVISEDEDR PFVKDLVGKK KGDVVEIERE YEGKKYTYKL EVEEVYKRTL PEIGDELAKS VNNEFETLEQ LKESLKKEGK EIYDVEMKES MREQLLEKLP EIVEIEISDR TLEILVNEAI NRLKREGRYE QIVSSYESEE KFREELKERI LDDIKRDRVI EVLAQEKGIS VNDEELEKEA EELAPFWGIS PDRAKSLVKA RQDLREELRW AILKRKVLDL LLQEVKVKVV EPKGEGDDSE GKEDN //