| IED ID | IndEnz0002015358 |
| Enzyme Type ID | protease015358 |
| Protein Name |
Immunoglobulin A1 protease IgA1 protease EC 3.4.24.13 IgA-specific zinc metalloproteinase |
| Gene Name | iga |
| Organism | Streptococcus pneumoniae |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus pneumoniae |
| Enzyme Sequence | MEKYFGEKQERFSFRKLSVGLVSATISSLFFMSVLASSSVDAQETAGVHYKYVADSELSSEEKKQLVYDIPTYVENDDETYYLVYKLNSQNQLAELPNTGSKNERQALVAGASLAALGILIFAVSKKKVKNKTVLHLVLVAGIGNGVLVSVHALENHLLLNYNTDYELTSGEKLPLPKEISGYTYIGYIKEGKTTSDFEVSNQEKSAATPTKQQKVDYNVTPNFVDHPSTVQAIQEQTPVSSTKPTEVQVVEKPFSTELINPRKEEKQSSDSQEQLAEHKNLETKKEEKISPKEKTGVNTLNPQDEVLSGQLNKPELLYREETIETKIDFQEEIQENPDLAEGTVRVKQEGKLGKKVEIVRIFSVNKEEVSREIVSTSTTAPSPRIVEKGTKKTQVIKEQPETGVEHKDVQSGAIVEPAIQPELPEAVVSDKGEPEVQPTLPEAVVTDKGEPAVQPELPEAVVSDKGEPEQVAPLPEYKGNIEQVKPETPVEKTKEQGPEKTEEVPVKPTEETPVNPNEGTTEGTSIQGAENPVQPAEDTQTNSGKIANENTGEVSNKPSDSKPPVEESNQPEKNGTATKPENSGNTTSENGQTEPEPSNGNSTEDVSTKSNTSNSNGNEEIKQENELDPDKKVEDPEKTLELRNVSDLELYSLSNGTYKQHISLEQVPSNPNSYFVKVKSSSFKDVYLPVASISEGRKNDKILYKITAKVEKLQQEIESRYKDNFTFYLAKKGTEETTNFTSFSNLVKAINQNLSGTYHLGASLNANEVELSTDDKSYIKGTFTGQLIGEKDGKHYAIYNLKKPLFENLSGATVEKLSLKNVAISGKNDIGSLANEATNGTKIKQVHVDGVLAGERGVGGLLAKADQSSIAESSFKGRIVNTYETTDSYNIGGLVGHLTGKNASIAKSKATVTISSNTNRSDQTVGGLAGLVDRDAQIQDSYAEGDINNVKHFGRVAGVAGNLWDRTSGDVRHAGSLTNVLSDVNVTNGNAITGYHYTGMKVANTFSSKANRVFNVTLEKNEVVSKESFEERGTMLDASQIASKKAEINLITPPIVEPLSTSGKKDSDFSKIAHYQANRALVYKNIEKLLPFYNKATIVKYGNLVKENSILYQKELLSAVMMKDDQVITDIISNKQTANKLLLHYKDHSSEKFDLRYQADFANLAEYSIGDSGLLYTPNQFLYHQDSIINQVLPELNRVNYQSDAVRNTLGISPEVKLTELYLEEQFTKTKEHLAENLKKLLSSDAGLVTDNEVMTGYIIDKIKRNKEALLLGMSYLERWYNFSYGQVNVKDLVMYHPDFFGKGNTSPLDTLIELGKSGFNNLLAKNNVDTYAISLASHHGTTDLFSTLENYRKVFLPDKTNNDWFKSQTKAYIVEEKSNIEEVKTKQGLVGTKYSIGVYDRITSATWKYRNMVLPLLTLPERSVFVISTISSLGFGAYDRYRNKEHQANGDLNSFVEKSAHETAERQRDHYDYWYRILDEKGREKLYRNILLYDAYKFGTNHTEGKATEVADFDSPNPAMKHFFGPVGNKVGHNGHGAYATGDAVYYMGYRMLDKDGAITYTHEMTHNSDQDIYLGGYGRRSGLGPEFFAKGLLQAPDQPSDATITINSILKHSKSDSKEGERLQVLDPTTRFKDATDLQKYVHNMFDVVYMLEYLEGKSIVKKLNVYQKIEALRKIENQYLTDPADGNDVYATNVVKNLTEDEAKKLTSFDSLIDNNILSAREYKAGTYERNGYFTIKLFAPIFSALSGEKGTPGDLMGRRIAFELLAAKGFKDGMVPYISNQYEEDAKQQGQTINLYGKERGLVTDELVLKKVFDGKYKTWAEFKTAMYQERVDQFGNLKQVTFKDPTKPWPRYGTKTINNVDELQKLMDEAVLQDAKERNYYYWNNYNPETDSAVHKLKRAIFKAYLDQTNDFRRSIFENKK |
| Enzyme Length | 1927 |
| Uniprot Accession Number | Q54875 |
| Absorption | |
| Active Site | ACT_SITE 1566; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of Pro-|-Thr bond in the hinge region of the heavy chain of human IgA.; EC=3.4.24.13; |
| DNA Binding | |
| EC Number | 3.4.24.13 |
| Enzyme Function | FUNCTION: Zinc metalloproteinase which cleaves human immunoglobulin A1 (IgA1) in the hinge region, rendering it less efficient in coating the surface of colonizing or invading pneumococci. May be responsible for pneumococcal infection and is potentially involved in distinct stages of pneumococcal disease. {ECO:0000269|PubMed:8926055}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (6); Chain (1); Compositional bias (6); Domain (1); Metal binding (3); Modified residue (1); Motif (1); Propeptide (1); Region (4); Repeat (3); Signal peptide (1); Topological domain (1); Transmembrane (2) |
| Keywords | 3D-structure;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 {ECO:0000255|PROSITE-ProRule:PRU00477}. Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. |
| Modified Residue | MOD_RES 99; /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 | NMR spectroscopy (1) |
| Cross Reference PDB | 6OH1; |
| Mapped Pubmed ID | 31390088; |
| Motif | MOTIF 96..100; /note=LPXTG sorting signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00477 |
| Gene Encoded By | |
| Mass | 215,172 |
| Kinetics | |
| Metal Binding | METAL 1565; /note=Zinc; /evidence=ECO:0000250; METAL 1569; /note=Zinc; /evidence=ECO:0000250; METAL 1589; /note=Zinc; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.13; |