Detail Information for IndEnz0002013795
IED ID IndEnz0002013795
Enzyme Type ID protease013795
Protein Name Regulator of sigma-W protease RasP
EC 3.4.24.-
Regulating anti-sigma-W factor activity protease
S2P endopeptidase
Site-2 protease RseP
S2P protease RseP
Site-2-type intramembrane protease
Zinc metalloprotease RasP
Gene Name rasP yluC BSU16560
Organism Bacillus subtilis (strain 168)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168)
Enzyme Sequence MFVNTVIAFIIIFGTLVFFHELGHLLLAQRAGILCREFAIGFGPKIFSFKKNETVYTIRLLPVGGFVRMAGEDPEMIEVKPGYTVGLLFNKEDQVEKVIINQKEKYPDALVIEVETADLEHDMKITGYEQGKEDELSSFTVSETSFFIVDGEEVQIAPYNRQFGSKPVWQRIKAIAAGPIMNFILAYVILVMLGLIQGVPSNEPMLGQLTDNGRAAEAGLKEGDYIQSINGEKMRSWTDIVSAVKENPEKEMDVAVKRDNKTLHISVTPEAVKDENKKTIGRFGSYAPTEKGVLSAVAYGATSTVDVTKAILTNLSKLVTGQFKLDMLSGPVGIYDMTDQVAKTGIVNLFQFAAFLSINLGIVNLLPIPALDGGRLLFLFIEAIRGKPINREKEAFVVFIGVAFLMLLMLVVTWNDIQRLFL
Enzyme Length 422
Uniprot Accession Number O31754
Absorption
Active Site ACT_SITE 21; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Is responsible for site-2 cleavage of the RsiW anti-sigma factor (PubMed:15130127). This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (PubMed:16899079). Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane (PubMed:21810987). {ECO:0000269|PubMed:15130127, ECO:0000269|PubMed:21810987}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Domain (1); Metal binding (2); Mutagenesis (1); Transmembrane (4)
Keywords Cell membrane;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Transmembrane;Transmembrane helix;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 46,744
Kinetics
Metal Binding METAL 20; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 24; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Rhea ID
Cross Reference Brenda