|
|
||
|
|
|
|
|
UniProt functional annotation for B2RID1 | ||
|
|
|
|
|
|
||
| UniProt code: B2RID1. |
|
||
| Organism: | |
Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561). |
| Taxonomy: | |
Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae; Porphyromonas. |
|
||
|
||
| Function: | |
Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Shows a strict specificity for acidic residues (Asp or Glu) in the P1 position, and has a hydrophobic residue preference at the P2 position. Preferentially cleaves the synthetic substrate Leu- Asp-methylcoumaryl-7-amide (Leu-Asp-MCA) as compared to Leu-Glu-MCA. Is involved in amino acid metabolism and bacterial growth of asaccharolytic P.gingivalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources. {ECO:0000269|PubMed:21896480, ECO:0000269|PubMed:23246913}. |
|
||
| Activity regulation: | |
Enzyme activity is completely blocked by diisopropyl-fluorophosphates, moderately by phenylmethylsulfonyl fluoride (PMSF) and 4-(2-methyl)benzenesulfonyl fluoride, and slightly by pepstatin in vitro. {ECO:0000269|PubMed:21896480}. |
| Biophysicochemical properties: | |
pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:21896480}; |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:26057589}. |
| Subcellular location: | |
Cell surface {ECO:0000269|PubMed:21896480}. Note=Is exclusively cell-associated. {ECO:0000269|PubMed:21896480}. |
| Disruption phenotype: | |
Cell growth is retarded. Complete loss of hydrolysis for ac-DNLD- and LE-MCA. The efficiency of peptide utilization of proteinaceous nutrients is reduced in mutant cells. {ECO:0000269|PubMed:21896480}. |
| Similarity: | |
Belongs to the peptidase S46 family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.