Detail Information for IndEnz0002019040
IED ID IndEnz0002019040
Enzyme Type ID protease019040
Protein Name Disulfide bond formation protein D
Disulfide oxidoreductase D
Thiol-disulfide oxidoreductase D
Gene Name bdbD yvgV BSU33480
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 MKKKQQSSAKFAVILTVVVVVLLAAIVIINNKTEQGNDAVSGQPSIKGQPVLGKDDAPVTVVEFGDYKCPSCKVFNSDIFPKIQKDFIDKGDVKFSFVNVMFHGKGSRLAALASEEVWKEDPDSFWDFHEKLFEKQPDTEQEWVTPGLLGDLAKSTTKIKPETLKENLDKETFASQVEKDSDLNQKMNIQATPTIYVNDKVIKNFADYDEIKETIEKELKGK
Enzyme Length 222
Uniprot Accession Number O32218
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. May be required for the stability of secreted proteins with disulfide bonds. Not required for sporulation. {ECO:0000269|PubMed:11744713}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (6); Chain (1); Disulfide bond (1); Domain (1); Helix (9); Mutagenesis (1); Signal peptide (1); Turn (2)
Keywords 3D-structure;Cell membrane;Competence;Disulfide bond;Membrane;Oxidoreductase;Redox-active center;Reference proteome;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}. Membrane raft {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}. 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}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..36; /evidence=ECO:0000255
Structure 3D X-ray crystallography (4)
Cross Reference PDB 3EU3; 3EU4; 3GH9; 3GHA;
Mapped Pubmed ID 19535335;
Motif
Gene Encoded By
Mass 24,905
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda