| Tag | Content |
|---|
| CPLM ID | CPLM-004926 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Xaa-Pro dipeptidase |
Protein Synonyms/Alias | X-Pro dipeptidase; Imidodipeptidase; Proline dipeptidase; Prolidase |
Gene Name | pepQ |
Gene Synonyms/Alias | b3847; JW3823 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 231 | AAVLHYTKLDHQAPE | acetylation | [1] | | 265 | LTRTWSAKSDNDYAQ | acetylation | [1] | | 275 | NDYAQLVKDVNDEQL | acetylation | [1] | | 404 | WREGQFSKHFNWQKI | acetylation | [1] | | 410 | SKHFNWQKIEALKPF | acetylation | [1] | | 415 | WQKIEALKPFGGIRI | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Splits dipeptides with a prolyl residue in the C- terminal position and a polar or nonpolar amino acid at the N- terminal position. With much lower efficiency, also catalyzes the stereoselective hydrolysis of a wide variety of organophosphate triesters and organophosphonate diesters. Is able to hydrolyze the organophosphorus insecticide paraoxon and the p-nitrophenyl analogs of the nerve agents GB (sarin), GD (soman), GF, Vx and rVX. |
Sequence Annotation | METAL 246 246 Manganese 2 (By similarity).
METAL 257 257 Manganese 1 (By similarity).
METAL 257 257 Manganese 2 (By similarity).
METAL 339 339 Manganese 1 (By similarity).
METAL 384 384 Manganese 1 (By similarity).
METAL 423 423 Manganese 1 (By similarity).
METAL 423 423 Manganese 2 (By similarity). |
Keyword | Complete proteome; Dipeptidase; Direct protein sequencing; Hydrolase; Manganese; Metal-binding; Metalloprotease; Protease; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 443 AA |
Protein Sequence | MESLASLYKN HIATLQERTR DALARFKLDA LLIHSGELFN VFLDDHPYPF KVNPQFKAWV 60
PVTQVPNCWL LVDGVNKPKL WFYLPVDYWH NVEPLPTSFW TEDVEVIALP KADGIGSLLP 120
AARGNIGYIG PVPERALQLG IEASNINPKG VIDYLHYYRS FKTEYELACM REAQKMAVNG 180
HRAAEEAFRS GMSEFDINIA YLTATGHRDT DVPYSNIVAL NEHAAVLHYT KLDHQAPEEM 240
RSFLLDAGAE YNGYAADLTR TWSAKSDNDY AQLVKDVNDE QLALIATMKA GVSYVDYHIQ 300
FHQRIAKLLR KHQIITDMSE EAMVENDLTG PFMPHGIGHP LGLQVHDVAG FMQDDSGTHL 360
AAPAKYPYLR CTRILQPGMV LTIEPGIYFI ESLLAPWREG QFSKHFNWQK IEALKPFGGI 420
RIEDNVVIHE NNVENMTRDL KLA 443 |
Gene Ontology | GO:0016805; F:dipeptidase activity; IEA:HAMAP. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0008235; F:metalloexopeptidase activity; IEA:HAMAP. GO:0016795; F:phosphoric triester hydrolase activity; IEA:InterPro. GO:0043171; P:peptide catabolic process; IGI:EcoliWiki. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |