HAMAP rule MF_00303

General rule information [?]

PURL	https://purl.expasy.org/hamap/rule/MF_00303
Accession	MF_00303
Dates	28-FEB-2005 (Created) 01-JUN-2023 (Last updated, Version 18)
Name	Trigger_factor_Tig
Scope(s)	Bacteria
Template(s)	P0A850; [ Recover all ]
Triggered by	HAMAP; MF_00303 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier	TIG
Protein name	RecName: Full=Trigger factor; Short=TF; EC=5.2.1.8; AltName: Full=PPIase;
Gene name	Name=tig;

Comments [?]

FUNCTION	Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
CATALYTIC ACTIVITY	Reaction=[protein]-peptidylproline (omega=180) = [protein]- peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8;
case <OC:Escherichia> or <OC:Shigella>
SUBUNIT	Homodimer and monomer. In vivo most of the ribosomes are in complex with monomeric TF. Uncomplexed TF, however, is in a monomer- dimer equilibrium with approximately two thirds of TF existing in a dimeric state.
end case
SUBCELLULAR LOCATION	Cytoplasm. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm.
DOMAIN	Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
SIMILARITY	Belongs to the FKBP-type PPIase family. Tig subfamily.

Keywords [?]

Gene Ontology [?]

GO:0003755; Molecular function:peptidyl-prolyl cis-trans isomerase activity

GO:0006457; Biological process:protein folding

GO:0015031; Biological process:protein transport

Cross-references [?]

Features [?]

Additional information [?]

Size range	404-557 amino acids
Related rules	None
Fusion	Nter: None Cter: None
Comments	Possible wrong start in AQUAE