| IED ID | IndEnz0002019149 |
| Enzyme Type ID | protease019149 |
| Protein Name |
Archaeosortase A EC 3.4.22.- |
| Gene Name | artA cyo HVO_0915 C498_14173 |
| Organism | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Stenosarchaea group Halobacteria Haloferacales Haloferacaceae Haloferax Haloferax volcanii (Halobacterium volcanii) Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
| Enzyme Sequence | MPGLLSDILAWVVIGTFVAGAVANGRDRELGRRVMTAAWVLFALFWLQLIPHFTLVHKSYIEGLLTIAAVPASLYAGWLLYNGRDTLFVLSRAVAAMGVVYLPFETIPAFTLLGATVPAPRGVLMETVAAQTRFLIESLGYTPQMIVGDQGYLNTFLWMQGSHRLEISVVLACTGLGSIAIFAGLIAAVDAPMGRKLRGLAIAVPIIYALNLLRTTFIAISVGKQYFHLFVDEVLFLFGSSDPYMVSFFISDRIISQALAVVALVGVTYLVVHEVPELLTVIEDVLYMVTGDEYDLRNELGLD |
| Enzyme Length | 303 |
| Uniprot Accession Number | D4GUZ4 |
| Absorption | |
| Active Site | ACT_SITE 173; /note=Acyl-thioester intermediate; /evidence=ECO:0000305|PubMed:29465796; ACT_SITE 214; /note=Proton donor; /evidence=ECO:0000305|PubMed:29465796 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Transpeptidase that recognizes and modifies its substrate by proteolytic cleavage of a sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the archaeosortase and its substrate, which is then transferred and covalently attached to the cell membrane (Probable). This sortase recognizes a tripartite structure consisting of a conserved Pro-Gly-Phe (PGF) motif, followed by a transmembrane alpha helix domain and a cluster of basic residues, usually at the C-terminus of target proteins (Probable). Confirmed substrates include the cell surface S-layer glycoprotein Csg and HVO_0405 (PubMed:23651326, PubMed:26712937, PubMed:28069824). ArtA is required for the C-terminal processing of Csg and for its lipidation and attachment to the archaeal plasma membrane (PubMed:23651326, PubMed:26712937). It is also required for the processing of HVO_0405, which contains an atypical central tripartite structure (PubMed:28069824). {ECO:0000269|PubMed:23651326, ECO:0000269|PubMed:26712937, ECO:0000269|PubMed:28069824, ECO:0000305|PubMed:23651326, ECO:0000305|PubMed:26712937}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Mutagenesis (3); Site (1); Transmembrane (7) |
| Keywords | Cell membrane;Hydrolase;Membrane;Protease;Reference proteome;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 33,092 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |