Detail Information for IndEnz0002013297
IED ID IndEnz0002013297
Enzyme Type ID protease013297
Protein Name Zinc metalloprotease ZmpB
EC 3.4.24.-
Gene Name zmpB spr0581
Organism Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus pneumoniae Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Enzyme Sequence MFKKDRFSIRKIKGVVGSVFLGSLLMAPSVVDAATYHYVNKEIISQEAKDLIQTGKPDRNEVVYGLVYQKDQLPQTGTEASVLTAFGLLTVGSLLLIYKRKKIASVFLVGTMGLVVLPSAGAVDPVATLALASREGVVEMEGYRYVGYLSGDILKTLGLDTVLEETSAKPGEVTVVEVETPQSTTNQEQARTENQVVETEEAPKEEAPKTEESPKEEPKSEVKPTDDTLPKVEEGKEDSAEPAPVEEVGGEVESKPEEKVAVKPESQPSDKPAEESKVEQAGEPVAPRKDEQAPVEPENQPEAPEEEKAVEETPKQEESTPDTKAEETVEPKEETKTAKGTQEEGKEGQAPVQEVNPEYKVTTGTVEKSTESELDFTTEVVPDDTKYVDEEVVERQGSKGVQVTKTTYETVEVVETDKVLSTTTEVKTPVVPKVVKKGTKPVETREEVIPFATKEQEDDTLKRGTRQVAQEGVNGKKQITETYKTIRGEKTNEAPTVEETVLQAPQDEIIKKGTKGLEKPTLQWANTEKDVLKKSATASYTLTKPAGVEIKSIKLALKDKDGQLVKEVTVAENNLNATLDKLKYYQGYTLSTTMVYDRGEGEETEKLEDKQIQLDLKKVEIKNIKETSLMNVDAEGNETDKSLLSEKPTDVSQLYLRVTTHDNKVTRLAVSSVEEVVVDGKTLYKVVAKAPDLVQRRADDTLSEEYVHYFEKQLPKVNNVYYNFNELVKDMQANPMGEFKLGADLNAVNVKPAGKAYVMAKFRGTLSSVENHQYTIHNLERPLFNEAEGATLKNFNLGNVNINMPWADKVAPIGNMFKKSTLENIKVVGSVTGNNDVTGAVNKLDEANMRNVAFIGKINSLGDKGWWSGGLVSESWRSNTDSVYFDGDIVGNNSKFGGLVAKVNHGSNQWDVKQKGRLTNSVVKGTMTLKNHGQSGGLVHENYDWGWVENNISMMKVNNGEIMYGSGSIDGDPYFGFDYFKNNYYVKDVATGESTYKRSKQIQSISQAEADAKIANMGITANTFAIQDPVVNKLNRIIDRDSEYKAIQDYQETRNLAYRNLEKLQPFYNKEWIVNQGNKLTDESNLVKKTVLSVTGMKSGQFVTDLSSVDKIMIHYADGTKEEFGVSAISDSRVKQVKEYNVDDLGVVYTPNMVDKNRDSLITKVKEKLSSVALDSAEVKSITNNPASLYLEESFAEVRETLDKLVKSLLENEDHQLNSDEVAEKALLKKVEDNKAKIILALTYLNRYYGIDYDGLNFKHLMMFKPDFYGKTPSILDFLIRIGSAEKNLKGDRSLEAYREVIGGTIGKGELNGLLGYNMRLFTKYTDLNDWFIHAAKNVYVSEPETTTEDFKDKRHRIYDGLNNDVHGRMILPLLNLKKAHIFVISTYNTIAFSSFEKYGKNTEEERNAYKAEIDRVAKAQQRYLDFWSRLALPKVRNQLLKSQNSVPTPVWDNQVYVGLGGANRMGYGDGGRVVTPVRELFGPTDRWHQINWNMGAMAKIYERPWKDDQVYFMVTNMMEPFGISAFTHETTHVNDRMAYYGGDWHREGTDLEAFAQGMLQTPDKSTTNGEYGALGINMAYERKNDGEQLYNYDPEKLDSREKIDSYMKNYNESMMMLDYLEASAVIRQNLSDNSKWFKKMDKEWRTNADRNRLIGEPHQWDKLRDLTEEEKKLPIDSIDKLVENNFVTLHGMPKNGRYRTEGFDSSYQPVNMMAGVFGGNTSKSTVGSISFKHNAFRMWGYYGYENGFIPYVSNKLKGAANKENKGLLGDDFIIKKVSKNQFQNLEEWKKHWYHEVYDKAQKGFVEIEVDGVKISTYAQLQSLFEEAVSKDLAGMDDKNIKNHYQYTENLKWKIYKQLLKNTDGFSSDLFTAPQA
Enzyme Length 1876
Uniprot Accession Number Q8DQN5
Absorption
Active Site ACT_SITE 1530; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Compositional bias (3); Domain (2); 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;Reference proteome;Repeat;Secreted;Signal;Transmembrane;Transmembrane helix;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 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 (By similarity). {ECO:0000250}.
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 211,058
Kinetics
Metal Binding METAL 1529; /note=Zinc; /evidence=ECO:0000250; METAL 1533; /note=Zinc; /evidence=ECO:0000250; METAL 1553; /note=Zinc; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda