| Tag | Content |
|---|
| CPLM ID | CPLM-005272 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Peptidyl-dipeptidase dcp |
Protein Synonyms/Alias | Dipeptidyl carboxypeptidase |
Gene Name | dcp |
Gene Synonyms/Alias | b1538; JW1531 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 149 | RFVLAGAKLAQADKA | acetylation | [1] | | 216 | REKGLDNKWLIPLLN | acetylation | [1] | | 241 | RDRATREKLFIAGWT | acetylation | [1] | | 285 | FPHYAAWKIADQMAK | acetylation | [1] | | 348 | AEQVRREKFDLDEAQ | acetylation | [1] | | 535 | MPDELQQKMRNASLF | acetylation | [1] | | 669 | QWRGKAPKIMPMLQH | 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 | Removes dipeptides from the C-termini of N-blocked tripeptides, tetrapeptides and larger peptides. |
Sequence Annotation | ACT_SITE 471 471 By similarity.
METAL 470 470 Zinc; catalytic (By similarity).
METAL 474 474 Zinc; catalytic (By similarity).
METAL 477 477 Zinc; catalytic (By similarity). |
Keyword | 3D-structure; Calcium; Carboxypeptidase; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 681 AA |
Protein Sequence | MTTMNPFLVQ STLPYLAPHF DQIANHHYRP AFDEGMQQKR AEIAAIALNP QMPDFNNTIL 60
ALEQSGELLT RVTSVFFAMT AAHTNDELQR LDEQFSAELA ELANDIYLNG ELFARVDAVW 120
QRRESLGLDS ESIRLVEVIH QRFVLAGAKL AQADKAKLKV LNTEAATLTS QFNQRLLAAN 180
KSGGLVVNDI AQLAGMSEQE IALAAEAARE KGLDNKWLIP LLNTTQQPAL AEMRDRATRE 240
KLFIAGWTRA EKNDANDTRA IIQRLVEIRA QQATLLGFPH YAAWKIADQM AKTPEAALNF 300
MREIVPAARQ RASDELASIQ AVIDKQQGGF SAQPWDWAFY AEQVRREKFD LDEAQLKPYF 360
ELNTVLNEGV FWTANQLFGI KFVERFDIPV YHPDVRVWEI FDHNGVGLAL FYGDFFARDS 420
KSGGAWMGNF VEQSTLNKTH PVIYNVCNYQ KPAAGEPALL LWDDVITLFH EFGHTLHGLF 480
ARQRYATLSG TNTPRDFVEF PSQINEHWAT HPQVFARYAR HYQSGAAMPD ELQQKMRNAS 540
LFNKGYEMSE LLSAALLDMR WHCLEENEAM QDVDDFELRA LVAENMDLPA IPPRYRSSYF 600
AHIFGGGYAA GYYAYLWTQM LADDGYQWFV EQGGLTRENG LRFREAILSR GNSEDLERLY 660
RQWRGKAPKI MPMLQHRGLN I 681 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:EcoCyc. GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc. GO:0004180; F:carboxypeptidase activity; IDA:EcoCyc. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |