| IED ID |
IndEnz0002008073 |
| Enzyme Type ID |
protease008073 |
| Protein Name |
Regulatory protein BlaR1
|
| Gene Name |
blaR1 |
| Organism |
Staphylococcus aureus |
| Taxonomic Lineage |
cellular organisms
Bacteria
Terrabacteria group
Firmicutes
Bacilli
Bacillales
Staphylococcaceae
Staphylococcus
Staphylococcus aureus
|
| Enzyme Sequence |
MAKLLIMSIVSFCFIFLLLLFFRYILKRYFNYMLNYKVWYLTLLAGLIPFIPIKFSLFKFNNVNNQAPTVESKSHDLNHNINTTKPIQEFATDIHKFNWDSIDNISTVIWIVLVIILSFKFLKALLYLKYLKKQSLYLNENEKNKIDTILFNHQYKKNIVIRKAETIQSPITFWYGKYIILIPSSYFKSVIDKRLKYIILHEYAHAKNRDTLHLIIFNIFSIIMSYNPLVHIVKRKIIHDNEVEADRFVLNNINKNEFKTYAESIMDSVLNVPFFNKNILSHSFNGKKSLLKRRLINIKEANLKKQSKLILIFICIFTFLLMVIQSQFLMGQSITDYNYKKPLHNDYQILDKSKIFGSNSGSFVMYSMKKDKYYIYNEKESRKRYSPNSTYKIYLAMFGLDRHIINDENSRMSWNHKHYPFDAWNKEQDLNTAMQNSVNWYFERISDQIPKNYTATQLKQLNYGNKNLGSYKSYWMEDSLKISNLEQVIVFKNMMEQNNHFSKKAKNQLSSSLLIKKNEKYELYGKTGTGIVNGKYNNGWFVGYVITNHDKYYFATHLSDGKPSGKNAELISEKILKEMGVLNGQ |
| Enzyme Length |
585 |
| Uniprot Accession Number |
P18357 |
| Absorption |
|
| Active Site |
ACT_SITE 389; /note="Acyl-ester intermediate"; /evidence="ECO:0000269|PubMed:15506754, ECO:0000269|PubMed:21775440" |
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
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| Enzyme Function |
FUNCTION: Integral membrane protein involved in sensing of the presence of beta-lactam antibiotics and transduction of the information to the cytoplasm. Mechanistically, activation of the signal transducer involves acylation of a serine in the C-terminal sensor domain upon binding of the beta-lactam antibiotic (PubMed:12591921, PubMed:15506754). In turn, a conformational change occurs and the signal is transmitted from the cell surface to the cytoplasm. There, the zinc protease domain is activated and initiates autoproteolysis as well as cleavage of the transcriptional repressor BlaI leading to derepression of antibiotic resistance genes (PubMed:11239156). {ECO:0000269|PubMed:11239156, ECO:0000269|PubMed:12591921, ECO:0000269|PubMed:15506754}. |
| Temperature Dependency |
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| PH Dependency |
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| Pathway |
|
| nucleotide Binding |
|
| Features |
Active site (1); Beta strand (10); Chain (1); Helix (11); Modified residue (1); Mutagenesis (5); Region (1); Topological domain (5); Transmembrane (4); Turn (4) |
| Keywords |
3D-structure;Cell membrane;Membrane;Transmembrane;Transmembrane helix;Transposable element |
| Interact With |
|
| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P12287}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P12287}. |
| Modified Residue |
MOD_RES 392; /note=N6-carboxylysine; /evidence=ECO:0000269|PubMed:12591921 |
| Post Translational Modification |
PTM: Carboxylation occurs on two lysine residues. Carboxylation at 'Lys-392' activates the active site serine residue for acylation (PubMed:12591921). On acylation, the lysine side chain experiences a spontaneous decarboxylation that entraps the sensor in its activated state (PubMed:15506754, PubMed:21775440). {ECO:0000269|PubMed:12591921, ECO:0000269|PubMed:15506754, ECO:0000269|PubMed:21775440}. |
| Signal Peptide |
|
| Structure 3D |
X-ray crystallography (7) |
| Cross Reference PDB |
1XA1;
1XA7;
1XKZ;
3Q81;
3Q82;
3UY6;
6O9W;
|
| Mapped Pubmed ID |
32518158;
|
| Motif |
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| Gene Encoded By |
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| Mass |
69,246 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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