| IED ID | IndEnz0002006502 |
| Enzyme Type ID | protease006502 |
| Protein Name |
Iron-regulated surface determinant protein C Staphylococcal iron-regulated protein D |
| Gene Name | isdC sirD SAOUHSC_01082 |
| Organism | Staphylococcus aureus (strain NCTC 8325 / PS 47) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus aureus Staphylococcus aureus (strain NCTC 8325 / PS 47) |
| Enzyme Sequence | MKNILKVFNTTILALIIIIATFSNSANAADSGTLNYEVYKYNTNDTSIANDYFNKPAKYIKKNGKLYVQITVNHSHWITGMSIEGHKENIISKNTAKDERTSEFEVSKLNGKIDGKIDVYIDEKVNGKPFKYDHHYNITYKFNGPTDVAGANAPGKDDKNSASGSDKGSDGTTTGQSESNSSNKDKVENPQTNAGTPAYIYAIPVASLALLIAITLFVRKKSKGNVE |
| Enzyme Length | 227 |
| Uniprot Accession Number | Q8KQR1 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 47; /note=Heme; /evidence=ECO:0000269|PubMed:17287214; BINDING 48; /note=Heme; via amide nitrogen; /evidence=ECO:0000269|PubMed:17287214; BINDING 136; /note=Heme; /evidence=ECO:0000269|PubMed:17287214 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Involved in heme (porphyrin) scavenging. Binds hemoglobin and almost exclusively free-base protoporphyrin IX. Probably has a role as the central conduit of the isd heme uptake system, i.e. mediates the transfer of the iron-containing nutrient from IsdABH to the membrane translocation system IsdDEF. Hemin-free IsdC (apo-IsdC) acquires hemin from hemin-containing IsdA (holo-IsdA) probably through the activated holo-IsdA-apo-IsdC complex and due to the higher affinity of apo-IsdC for the cofactor. The reaction is reversible (By similarity). {ECO:0000250, ECO:0000269|PubMed:15240116, ECO:0000269|PubMed:17287214}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (9); Binding site (3); Chain (1); Compositional bias (1); Domain (1); Helix (2); Metal binding (1); Modified residue (1); Motif (1); Mutagenesis (5); Propeptide (1); Region (1); Sequence conflict (5); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Cell wall;Heme;Iron;Metal-binding;Peptidoglycan-anchor;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Repressed by fur in the presence of iron. {ECO:0000305|PubMed:11830639}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:11830639, ECO:0000269|PubMed:15718231}; Peptidoglycan-anchor {ECO:0000269|PubMed:11830639, ECO:0000269|PubMed:15718231}. Note=Partially protected from extracellular protease in situ (PubMed:15718231). Anchored to the cell wall by sortase B (PubMed:11830639, PubMed:15718231) (Probable). {ECO:0000269|PubMed:11830639, ECO:0000269|PubMed:15718231, ECO:0000305|PubMed:24519933}. |
| Modified Residue | MOD_RES 192; /note="Pentaglycyl murein peptidoglycan amidated threonine"; /evidence="ECO:0000305|PubMed:11830639, ECO:0000305|PubMed:15718231" |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2O6P; |
| Mapped Pubmed ID | - |
| Motif | MOTIF 189..193; /note=NPQTN sorting signal; /evidence=ECO:0000305|PubMed:11830639 |
| Gene Encoded By | |
| Mass | 24,855 |
| Kinetics | |
| Metal Binding | METAL 132; /note=Iron (heme axial ligand) |
| Rhea ID | |
| Cross Reference Brenda |