| IED ID | IndEnz0002008512 |
| Enzyme Type ID | protease008512 |
| Protein Name |
PII-type proteinase EC 3.4.21.96 Cell wall-associated serine proteinase LP151 Lactocepin |
| Gene Name | prtP |
| Organism | Lacticaseibacillus paracasei (Lactobacillus paracasei) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Lactobacillaceae Lacticaseibacillus Lacticaseibacillus paracasei (Lactobacillus paracasei) |
| Enzyme Sequence | MQRKKKGLSILLAGTVALGALAVLPVGEIQAKAAISQQTKVSSLANTVKAATAKQAATDTTAATTNQAIATQLAAKGIDYNKLNKVQQQDTYVDVIVQMSAAPASENGTLRTDYSSTAEIQQETNKVIAAQASVKAAVEQVTQQTAGESYGYVVNGFSTKVRVVDIPKLKQIAGVKTVTLAKVYYPTDAKANSMANVQAVWSNYKYKGEGTVVSVIDTGIDPTHKDMRLSDDKDVKLTKYDVEKFTDTAKHGRYFTSKVPYGFNYADNNDTITDDTVDEQHGMHVAGIIGANGTGDDPTKSVVGVAPEAQLLAMKVFTNSDTSATTGSATLVSAIEDSAKIGADVLNMSLGSDSGNQTLEDPEIAAVQNANESGTAAVISAGNSGTSGSATQGVNKDYYGLQDNEMVGTPGTSRGATTVASAENTDVISQAVTITDGKDLQLGPETIQLSSNDFTGSFDQKKFYVVKDASGDLSKGAAADYTADAKGKIAIVKRGELNFADKQKYAQAAGAAGLIIVNNDGTATPLTSIRLTTTFPTFGLSSKTGQKLVDWVTAHPDDSLGVKIALTLLPNQKYTEDKMSDFTSYGPVSNLSFKPDITAPGGNIWSTQNNNGYTNMSGTSMASPFIAGSQALLKQALNNKNNPFYADYKQLKGTALTDFLKTVEMNTAQPINDINYNNVIVSPRRQGAGLVDVKAAIDALEKNPSTVVAENGYPAVELKDFTSTDKTFKLTFTNRTTHELTYQMDSNTDTNAVYTSATDPNSGVLYDKKIDGAAIKAGSDITVPAGKTAQIEFTLSLPKSFDQQQFVEGFLNFKGSDGSRLNLPYMGFFGDWNDGKIVDSLNGITYSPAGGNYGTVPLLTNKNTGHQYYGGMVTDADGKQTVDDQAIAFSSDKNALYNDISMQYYLLRNISNVQVDILDGQGNKVTTLSSSTNQTKTYYDAHSQKYIYYNAPAWDGTYYDQRDGNIKTADDGSYTYRISGVPEGGDKRQVFDVPFKLDSKAPTVRHVALSAKTENGKTQYYLTAEAKDDLSGLDATKSVKTAINEVTNLDATFTDAGTTADGYTKIETPLSDEQAQALGNGDNSAELYLTDNASNATNQDASVQKPGSTSFDLIVNGGGIPDKISSTTTGYEANTQGGGTYTFSGTYPAAVDGTYTDAQGKKHDLNTTYDAATNSFTASMAVTNADYAAQVDLYADKAHTQLLKHFDTKVRLTAPTFTDLKFNNGSDQTSEATIKVTGTVSSDTKTVNVGDTVAALDAQHHFSVDVPVNYGDNTIKVTATDEDGNTTTEQKTITSSYDPDVLKNAVTFDQGVKFGANEFNATSAKFYDPKTGIATITGKVKHPTTTLQVDGKQISIKNDLTFSFTLDLGTLGQKPFGVVVGDTTQNKTFQEALTFILDAVAPTLSLDSSTDAPVYTNDPNFQITGTATDNAQYLSLAINGSHVASQYADININSGKPGHMAIDQPVKLLEGKNVLTVAVTDSENNTTTKKITVYYEPKKTLAAPTVTPSTTEPAKTVTLTANAAATGETVQYSADGGKTYQDVPAAGVTVTANGTFKFKSTDLYGNESPAVDYVVTNIKADDPAQLQTAKQALTNLIASAKTLSASGKYDDATTTALAAATQKAQTALDQTDASVDSLTGANRDLQTAINQLAAKLPADKKTSLLNQLQSVKAALGTDLGNQTDPSTGKTFTAALDDLVAQAQAGTQTADQLQASLAKVLDAVLAKLAEGIKAATPAEVGNAKDAATGKTWYADIADTLTSGQASADASDKLAHLQALQSLKTKVAAAVEAAKTAGKGDDTTGTSDKGGGQGTPAPAPGDTGKDKGDEGSQPSSGGNIPTKPATTTSTSTDDTTDRNGQHTSGKGALPKTAETTERPAFGFLGVIVVSLMGVLGLKRKQREE |
| Enzyme Length | 1902 |
| Uniprot Accession Number | Q02470 |
| Absorption | |
| Active Site | ACT_SITE 217; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 281; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 620; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endopeptidase activity with very broad specificity, although some subsite preference have been noted, e.g. large hydrophobic residues in the P1 and P4 positions, and Pro in the P2 position. Best known for its action on caseins, although it has been shown to hydrolyze hemoglobin and oxidized insulin B-chain.; EC=3.4.21.96; |
| DNA Binding | |
| EC Number | 3.4.21.96 |
| Enzyme Function | FUNCTION: Protease which breaks down milk proteins during the growth of the bacteria on milk. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Motif (1); Propeptide (2); Region (1); Signal peptide (1) |
| Keywords | Cell wall;Direct protein sequencing;Hydrolase;Peptidoglycan-anchor;Protease;Repeat;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. |
| Modified Residue | MOD_RES 1870; /note=Pentaglycyl murein peptidoglycan amidated threonine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00477 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..33; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 1867..1871; /note=LPXTG sorting signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00477 |
| Gene Encoded By | |
| Mass | 200,253 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |