Detail Information for IndEnz0002012344
IED ID IndEnz0002012344
Enzyme Type ID protease012344
Protein Name Ancillary SecYEG translocon subunit
Periplasmic chaperone YfgM
Gene Name yfgM b2513 JW2497
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MEIYENENDQVEAVKRFFAENGKALAVGVILGVGALIGWRYWNSHQVDSARSASLAYQNAVTAVSEGKPDSIPAAEKFAAENKNTYGALASLELAQQFVDKNELEKAAAQLQQGLADTSDENLKAVINLRLARVQVQLKQADAALKTLDTIKGEGWAAIVADLRGEALLSKGDKQGARSAWEAGVKSDVTPALSEMMQMKINNLSI
Enzyme Length 206
Uniprot Accession Number P76576
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Is stable during exponential growth and degraded in stationary phase by the essential FtsH protease. Degradation is influenced by the alarmone (p)ppGpp, but not by inorganic polyphosphate (polyP), RpoS, RcsB or PpiD. {ECO:0000269|PubMed:26092727}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: May mediate protein transfer from the SecYEG translocon to the periplasmic chaperone network via its periplasmic C-terminal region (PubMed:24855643). In addition, at the cytosolic site, acts as a negative regulator of RcsB (PubMed:26092727). In stationary phase, the FtsH-dependent degradation of YfgM ensures the release of RcsB from YfgM and thereby permits cellular protection by the Rcs phosphorelay system (PubMed:26092727). May coordinate stress responses across the inner membrane via a dynamic protein-protein interaction network inside and outside of the membrane (PubMed:26092727). {ECO:0000269|PubMed:24855643, ECO:0000269|PubMed:26092727}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Mutagenesis (19); Topological domain (2); Transmembrane (1)
Keywords Cell inner membrane;Cell membrane;Chaperone;Membrane;Reference proteome;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:21210718}; Single-pass type II membrane protein {ECO:0000269|PubMed:21210718}; Periplasmic side {ECO:0000269|PubMed:21210718}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 16606699; 16858726; 22885295; 24561554;
Motif
Gene Encoded By
Mass 22,176
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda