AC MF_00303; DC Protein; auto TR HAMAP; MF_00303; -; 1; level=0 XX Names: Trigger_factor_Tig XX ID TIG DE RecName: Full=Trigger factor; DE Short=TF; DE EC=5.2.1.8; DE AltName: Full=PPIase; GN Name=tig; XX 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. 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; case or CC -!- SUBUNIT: Homodimer and monomer. In vivo most of the ribosomes are in CC complex with monomeric TF. Uncomplexed TF, however, is in a monomer- CC dimer equilibrium with approximately two thirds of TF existing in a CC dimeric state. end case 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. 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. CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily. XX DR Pfam; PF00254; FKBP_C; 1; trigger=no DR Pfam; PF05698; Trigger_C; 1; trigger=no DR Pfam; PF05697; Trigger_N; 1; trigger=no DR PIRSF; PIRSF003095; Trigger_factor; 1; trigger=no DR NCBIfam; TIGR00115; Tig; 1; trigger=no DR PROSITE; PS50059; FKBP_PPIASE; 1; trigger=yes XX KW Cell cycle KW Cell division KW Chaperone KW Cytoplasm KW Isomerase KW Rotamase XX GO GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity GO GO:0006457; P:protein folding GO GO:0015031; P:protein transport XX FT None XX Size: 404-557; Related: None; Template: P0A850; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: Possible wrong start in AQUAE XX # Revision 1.27 2023/06/01 //