Detail Information for IndEnz0002009388
IED ID IndEnz0002009388
Enzyme Type ID protease009388
Protein Name Sporulation sigma-E factor-processing peptidase
EC 3.4.23.-
Membrane-associated aspartic protease
Stage II sporulation protein GA
Gene Name spoIIGA BMQ_4271
Organism Priestia megaterium (strain ATCC 12872 / QMB1551) (Bacillus megaterium)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Priestia Priestia megaterium (Bacillus megaterium) Priestia megaterium (strain ATCC 12872 / QMB1551) (Bacillus megaterium)
Enzyme Sequence MPIYLDLIWMLNFGLDTILLMLCAVVLKRNYKWWRLLLGGFIGSLIVLLMFTPFSHLMVHPAIKILFSFFMVLMTFGYKRLRFFFENLLTFYFATFVVGGGLMGVHFLFQDQFLVLNQMVDTKSPQFGDPISWIFVLIGFPLLSYFSKTRVDDLRIKNITFDQLVDVEIILNEQTLSMKGLIDSGNQLVDPLTKTPVMIVTADSLKEILPEGLMELSKNVQSFSHSEDIDQEWYSKVRFVPYRSVGQANQLLLALKPDMVRLVHQSNTIEVTKVLVGISHTTLSVEKQYECIVHPKLIVIGEVSSAS
Enzyme Length 307
Uniprot Accession Number D5DQW6
Absorption
Active Site ACT_SITE 183; /evidence=ECO:0000250|UniProtKB:P13801
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.23.-
Enzyme Function FUNCTION: Probable aspartic protease that is responsible for the proteolytic cleavage of the RNA polymerase sigma E factor (SigE/spoIIGB) to yield the active peptide in the mother cell during sporulation. Responds to a signal from the forespore that is triggered by the extracellular signal protein SpoIIR (By similarity). {ECO:0000250|UniProtKB:P13801}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Erroneous initiation (1); Sequence conflict (1); Transmembrane (5)
Keywords Aspartyl protease;Cell membrane;Hydrolase;Membrane;Protease;Reference proteome;Sporulation;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9663680}; Multi-pass membrane protein {ECO:0000269|PubMed:9663680}. Note=Localized to the sporulation septum. Early in sporulating cells localized in an annulus at the septal periphery and later localized uniformly throughout the septa. {ECO:0000269|PubMed:9663680}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 35,146
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda