| IED ID | IndEnz0002012095 |
| Enzyme Type ID | protease012095 |
| Protein Name |
Zinc metalloprotease ZmpB EC 3.4.24.- |
| Gene Name | zmpB SP_0664 |
| 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 | MFKKDRFSIRKIKGVVGSVFLGSLLMAPSVVDAATYHYVNKEIISQEAKDLIQTGKPDRNEVVYGLVYQKDQLPQTGTEASVLTAFGLLTVGSLLLIYKRKKIASVFLVGAMGLVVLPSAGAVDPVATLALASREGVVEMEGYRYVGYLSGDILKTLGLDTVLEETSAKPGEVTVVEVETPQSITNQEQARTENQVVETEEAPKEEAPKTEESPKEEPKSEVKPTDDTLPKVEEGKEDSAEPAPVEEVGGEVESKPEEKVAVKPESQPSDKPAEESKVEQAGEPVAPREDEKAPVEPEKQPEAPEEEKAVEETPKQEESTPDTKAEETVEPKEETVNQSIEQPKVETPAVEKQTEPTEEPKVEQAGEPVAPREDEQAPTAPVEPEKQPEVPEEEKAVEETPKPEDKIKGIGTKEPVDKSELNNQIDKASSVSPTDYSTASYNALGPVLETAKGVYASEPVKQPEVNSETNKLKTAIDALNVDKTELNNTIADAKTKVKEHYSDRSWQNLQTEVTKAEKVAANTDAKQSEVNEAVEKLTATIEKLVELSEKPILTLTSTDKKILEREAVAKYTLENQNKTKIKSITAELKKGEEVINTVVLTDDKVTTETISAAFKNLEYYKEYTLSTTMIYDRGNGEETETLENQNIQLDLKKVELKNIKRTDLIKYENGKETNESLITTIPDDKSNYYLKITSNNQKTTLLAVKNIEETTVNGTPVYKVTAIADNLVSRTADNKFEEEYVHYIEKPKVHEDNVYYNFKELVEAIQNDPSKEYRLGQSMSARNVVPNGKSYITKEFTGKLLSSEGKQFAITELEHPLFNVITNATINNVNFENVEIERSGQDNIASLANTMKGSSVITNVKITGTLSGRNNVAGFVNNMNDGTRIENVAFFGKLHSTSGNGSHTGGIAGTNYRGIVRKAYVDATITGNKTRASLLVPKVDYGLTLDHLIGTKALLTESVVKGKIDVSNPVEVGAIASKTWPVGTVSNSVSYAKIIRGEELFGSNDVDDSDYASAHIKDLYAVEGYSSGNRSFRKSKTFTKLTKEQADAKVTTFNITADKLESDLSPLAKLNEEKAYSSIQDYNAEYNQAYKNLEKLIPFYNKDYIVYQGNKLNKEHHLNTKEVLSVTAMNNNEFITNLDEANKIIVHYADGTKDYFNLSSSSEGLSNVKEYTITDLGIKYTPNIVQKDNTTLVNDIKSILESVELQSQTMYQHLNRLGDYRVNAIKDLYLEESFTDVKENLTNLITKLVQNEEHQLNDSPAARQMIRDKVEKNKAALLLGLTYLNRYYGVKFGDVNIKELMLFKPDFYGEKVSVLDRLIEIGSKENNIKGSRTFDAFGQVLAKYTKSGNLDAFLNYNRQLFTNIDNMNDWFIDATEDHVYIAERASEVEEIKNSKHRAFDNLKRSHLRNTILPLLNIDKAHLYLISNYNAIAFGSAERLGKKSLEDIKDIVNKAADGYRNYYDFWYRLASDNVKQRLLRDAVIPIWEGYNAPGGWVEKYGRYNTDKVYTPLREFFGPMDKYYNYNGTGAYAAIYPNSDDIRTDVKYVHLEMVGEYGISVYTHETTHVNDRAIYLGGFGHREGTDAEAYAQGMLQTPVTGSGFDEFGSLGINMVFKRKNDGNQWYITDPKTLKTREDINRYMKGYNDTLTLLDEIEAESVISQQNKDLNSAWFKKIDREYRDNNKLNQWDKIRNLSQEEKNELNIQSVNDLVDQQLMTNRNPGNGIYKPEAISYNDQSPYVGVRMMTGIYGGNTSKGAPGAVSFKHNAFRLWGYYGYENGFLGYASNKYKQQSKTDGESVLSDEYIIKKISNNTFNTIEEFKKAYFKEVKDKATKGLTTFEVNGSSVSSYDDLLTLFKEAVKKDAETLKQEANGNKTVSMNNTVKLKEAVYKKLLQQTNSFKTSIFK |
| Enzyme Length | 1906 |
| Uniprot Accession Number | Q9L7Q2 |
| Absorption | |
| Active Site | ACT_SITE 1563; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Is a virulence factor capable of inducing inflammation in the lower respiratory tract, by increasing tumor necrosis factor alpha (TNF-alpha) concentration in the lungs. Also appears to have other functions important in virulence in models of pneumonia and septicemia. {ECO:0000269|PubMed:12841855, ECO:0000269|PubMed:12933834}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (5); Erroneous initiation (2); Metal binding (3); Modified residue (1); Motif (1); Propeptide (1); Region (3); Repeat (4); Signal peptide (1); Topological domain (1); Transmembrane (2) |
| Keywords | Cell wall;Hydrolase;Membrane;Metal-binding;Metalloprotease;Peptidoglycan-anchor;Protease;Repeat;Secreted;Signal;Transmembrane;Transmembrane helix;Virulence;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Multi-pass membrane protein. Secreted, cell wall; Peptidoglycan-anchor. |
| Modified Residue | MOD_RES 76; /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. |
| Signal Peptide | SIGNAL 1..33; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 73..77; /note=LPXTG sorting signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00477 |
| Gene Encoded By | |
| Mass | 213,535 |
| Kinetics | |
| Metal Binding | METAL 1562; /note=Zinc; /evidence=ECO:0000250; METAL 1566; /note=Zinc; /evidence=ECO:0000250; METAL 1586; /note=Zinc; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |