| IED ID | IndEnz0002012471 |
| Enzyme Type ID | protease012471 |
| Protein Name |
Zinc metalloprotease ZmpC EC 3.4.24.- MMP-9 protease |
| Gene Name | zmpC SP_0071 |
| Organism | Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus pneumoniae Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) |
| Enzyme Sequence | MSRKSIGEKRHSFSMRKLSVGLVSVTVSSFFLMSQGIQSVSADNMESPIHYKYMTEGKLTDEEKSLLVEALPQLAEESDDTYYLVYRSQQFLPNTGFNPTVGTFLFTAGLSLLVLLVSKRENGKKRLVHFLLLTSMGVQLLPASAFGLTSQILSAYNSQLSIGVGEHLPEPLKIEGYQYIGYIKTKKQDNTELSRTVDGKYSAQRDSQPNSTKTSDVVHSADLEWNQGQGKVSLQGEASGDDGLSEKSSIAADNLSSNDSFASQVEQNPDHKGESVVRPTVPEQGNPVSATTVQSAEEEVLATTNDRPEYKLPLETKGTQEPGHEGEAAVREDLPVYTKPLETKGTQGPGHEGEAAVREEEPAYTEPLATKGTQEPGHEGKATVREETLEYTEPVATKGTQEPEHEGEAAVEEELPALEVTTRNRTEIQNIPYTTEEIQDPTLLKNRRKIERQGQAGTRTIQYEDYIVNGNVVETKEVSRTEVAPVNEVVKVGTLVKVKPTVEITNLTKVENKKSITVSYNLIDTTSAYVSAKTQVFHGDKLVKEVDIENPAKEQVISGLDYYTPYTVKTHLTYNLGENNEENTETSTQDFQLEYKKIEIKDIDSVELYGKENDRYRRYLSLSEAPTDTAKYFVKVKSDRFKEMYLPVKSITENTDGTYKVTVAVDQLVEEGTDGYKDDYTFTVAKSKAEQPGVYTSFKQLVTAMQSNLSGVYTLASDMTADEVSLGDKQTSYLTGAFTGSLIGSDGTKSYAIYDLKKPLFDTLNGATVRDLDIKTVSADSKENVAALAKAANSANINNVAVEGKISGAKSVAGLVASATNTVIENSSFTGKLIANHQDSNKNDTGGIVGNITGNSSRVNKVRVDALISTNARNNNQTAGGIVGRLENGALISNSVATGEIRNGQGYSRVGGIVGSTWQNGRVNNVVSNVDVGDGYVITGDQYAAADVKNASTSVDNRKADRFATKLSKDQIDAKVADYGITVTLDDTGQDLKRNLREVDYTRLNKAEAERKVAYSNIEKLMPFYNKDLVVHYGNKVATTDKLYTTELLDVVPMKDDEVVTDINNKKNSINKVMLHFKDNTVEYLDVTFKENFINSQVIEYNVTGKEYIFTPEAFVSDYTAITNNVLSDLQNVTLNSEATKKVLGAANDAALDNLYLDRQFEEVKANIAEHLRKVLAMDKSINTTGDGVVEYVSEKIKNNKEAFMLGLTYMNRWYDINYGKMNTKDLSTYKFDFNGNNETSTLDTIVALGNSGLDNLRASNTVGLYANKLASVKGEDSVFDFVEAYRKLFLPNKTNNEWFKENTKAYIVEMKSDIAEVREKQESPTADRKYSLGVYDRISAPSWGHKSMLLPLLTLPEESVYISSNMSTLAFGSYERYRDSVDGVILSGDALRTYVRNRVDIAAKRHRDHYDIWYNLLDSASKEKLFRSVIVYDGFNVKDETGRTYWARLTDKNIGSIKEFFGPVGKWYEYNSSAGAYANGSLTHFVLDRLLDAYGTSVYTHEMVHNSDSAIYFEGNGRREGLGAELYALGLLQSVDSVNSHILALNTLYKAEKDDLNRLHTYNPVERFDSDEALQSYMHGSYDVMYTLDAMEAKAILAQNNDVKKKWFRKIENYYVRDTRHNKDTHAGNKVRPLTDEEVANLTSLNSLIDNDIINRRSYDDSREYKRNGYYTISMFSPVYAALSNSKGAPGDIMFRKIAYELLAEKGYHKGFLPYVSNQYGAEAFASGSKTFSSWHGRDVALVTDDLVFKKVFNGEYSSWADFKKAMFKQRIDKQDNLKPITIQYELGNPNSTKEVTITTAAQMQQLINEAAAKDITNIDRATSHTPASWVHLLKQKIYNAYLRTTDDFRNSIYK |
| Enzyme Length | 1856 |
| Uniprot Accession Number | Q97T80 |
| Absorption | |
| Active Site | ACT_SITE 1503; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Zinc metalloproteinase that specifically cleaves human matrix metalloproteinase 9 (MMP-9), leading to its activation. May play a role in pneumococcal virulence and pathogenicity in the lung. {ECO:0000269|PubMed:12841855, ECO:0000269|PubMed:12864860}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (3); Domain (1); Metal binding (3); Modified residue (1); Motif (1); Propeptide (1); Region (1); Signal peptide (1); Topological domain (1); Transmembrane (2) |
| Keywords | Cell wall;Hydrolase;Membrane;Metal-binding;Metalloprotease;Peptidoglycan-anchor;Protease;Secreted;Signal;Transmembrane;Transmembrane helix;Virulence;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}. Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Secreted, cell wall {ECO:0000250}; Peptidoglycan-anchor {ECO:0000250}. |
| Modified Residue | MOD_RES 95; /note=Pentaglycyl murein peptidoglycan amidated threonine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00477 |
| Post Translational Modification | PTM: The Gram-positive cell-wall anchor motif LPXTG is located in the N-terminal part, in contrast to such motifs in other known streptococcal and staphylococcal proteins. The protease could be cleaved by the sortase and anchored in the membrane via the two potential N-terminal transmembrane domains, whereas the propeptide located prior to the LPXTG motif would remain attached to the cell wall peptidoglycan by an amide bond (By similarity). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..42; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 92..96; /note=LPXTG sorting signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00477 |
| Gene Encoded By | |
| Mass | 206,737 |
| Kinetics | |
| Metal Binding | METAL 1502; /note=Zinc; /evidence=ECO:0000250; METAL 1506; /note=Zinc; /evidence=ECO:0000250; METAL 1526; /note=Zinc; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |