Detail Information for IndEnz0002004305
IED ID IndEnz0002004305
Enzyme Type ID protease004305
Protein Name Oligopeptide-binding protein OppA
Stage 0 sporulation protein KA
Gene Name oppA spo0KA BSU11430
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 MKKRWSIVTLMLIFTLVLSACGFGGTGSNGEGKKDSKGKTTLNINIKTEPFSLHPGLANDSVSGGVIRQTFEGLTRINADGEPEEGMASKIETSKDGKTYTFTIRDGVKWSNGDPVTAQDFEYAWKWALDPNNESQYAYQLYYIKGAEAANTGKGSLDDVAVKAVNDKTLKVELNNPTPYFTELTAFYTYMPINEKIAEKNKKWNTNAGDDYVSNGPFKMTAWKHSGSITLEKNDQYWDKDKVKLKKIDMVMINNNNTELKKFQAGELDWAGMPLGQLPTESLPTLKKDGSLHVEPIAGVYWYKFNTEAKPLDNVNIRKALTYSLDRQSIVKNVTQGEQMPAMAAVPPTMKGFEDNKEGYFKDNDVKTAKEYLEKGLKEMGLSKASDLPKIKLSYNTDDAHAKIAQAVQEMWKKNLGVDVELDNSEWNVYIDKLHSQDYQIGRMGWLGDFNDPINFLELFRDKNGGNNDTGWENPEFKKLLNQSQTETDKTKRAELLKKAEGIFIDEMPVAPIYFYTDTWVQDENLKGVIMPGTGEVYFRNAYFK
Enzyme Length 545
Uniprot Accession Number P24141
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: This protein is a component of the oligopeptide permease, a binding protein-dependent transport system, It binds peptides up to five amino acids long with high affinity. Also required for sporulation and competence.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Lipidation (2); Modified residue (1); Sequence conflict (6); Signal peptide (1)
Keywords Cell membrane;Competence;Lipoprotein;Membrane;Palmitate;Peptide transport;Phosphoprotein;Protein transport;Reference proteome;Signal;Sporulation;Transport
Interact With
Induction INDUCTION: Positively regulated by TnrA under nitrogen-limited conditions. {ECO:0000269|PubMed:12823818}.
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456, ECO:0000305|PubMed:27362352}; Lipid-anchor {ECO:0000305}. Membrane raft {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456, ECO:0000305|PubMed:27362352}; Lipid-anchor {ECO:0000305}. Note=Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion. {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456}.
Modified Residue MOD_RES 470; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:17218307
Post Translational Modification
Signal Peptide SIGNAL 1..20
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 61,525
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda