TIG_THEMA
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 25-MAY-2022, entry version 132.
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; Thermotogae; Thermotogales; Thermotogaceae; 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}.
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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 SMR; Q9WZF8; -.
DR IntAct; Q9WZF8; 1.
DR STRING; 243274.THEMA_01195; -.
DR DNASU; 898361; -.
DR EnsemblBacteria; AAD35776; AAD35776; TM_0694.
DR KEGG; tma:TM0694; -.
DR eggNOG; COG0544; Bacteria.
DR InParanoid; Q9WZF8; -.
DR OMA; KGIKTQF; -.
DR OrthoDB; 932993at2; -.
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; 1.10.3120.10; -; 1.
DR Gene3D; 3.10.50.30; -; 1.
DR Gene3D; 3.30.70.1050; -; 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 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 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
