| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | D-alanyl-D-alanine carboxypeptidase DacC |
Protein Synonyms/Alias | DD-carboxypeptidase; DD-peptidase; PBP-6 |
Gene Name | dacC |
Gene Synonyms/Alias | b0839, JW0823 |
Created Date | 3-June-2014 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Phosphorylation | Position | Peptide | Code | Type | References | | 108 | GNPALRGSSVMFLKP | S | HTP | [1] | | 109 | NPALRGSSVMFLKPG | S | HTP | [1] | |
Reference | [1]Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Macek B,Gnad F,Soufi B,Kumar C,Olsen JV,Mijakovic I,Mann M Mol. Cell Proteomics 2008, Feb;7(2):299-307. [ PMID:17938405] |
Functional Description From UniProt | FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors |
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| 3D-structure; Carboxypeptidase; Cellinnermembrane; Cellmembrane; Cellshape; Cellwallbiogenesis/degradation; Completeproteome; Directproteinsequencing; Hydrolase; Membrane; Peptidoglycansynthesis; Protease; Referenceproteome; Signal |
Protein Sequence | MTQYSSLLRG LAAGSAFLFL FAPTAFAAEQ TVEAPSVDAR AWILMDYASG KVLAEGNADE 60
KLDPASLTKI MTSYVVGQAL KADKIKLTDM VTVGKDAWAT GNPALRGSSV MFLKPGDQVS 120
VADLNKGVII QSGNDACIAL ADYVAGSQES FIGLMNGYAK KLGLTNTTFQ TVHGLDAPGQ 180
FSTARDMALL GKALIHDVPE EYAIHKEKEF TFNKIRQPNR NRLLWSSNLN VDGMKTGTTA 240
GAGYNLVASA TQGDMRLISV VLGAKTDRIR FNESEKLLTW GFRFFETVTP IKPDATFVTQ 300
RVWFGDKSEV NLGAGEAGSV TIPRGQLKNL KASYTLTEPQ LTAPLKKGQV VGTIDFQLNG 360
KSIEQRPLIV MENVEEGGFF GRVWDFVMMK FHQWFGSWFS 400 |
| GO:0005887 C:integral component of plasma membrane IDA:EcoliWiki GO:0004180 F:carboxypeptidase activity IDA:EcoCyc GO:0008658 F:penicillin binding IDA:EcoCyc GO:0009002 F:serine-type D-Ala-D-Ala carboxypeptidase activity IEA:UniProtKB-EC GO:0009252 P:peptidoglycan biosynthetic process IDA:EcoCyc GO:0008360 P:regulation of cell shape IGI:EcoCyc GO:0042493 P:response to drug IMP:EcoCyc |
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