CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003455
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 D-alanyl-D-alanine carboxypeptidase DacA 
Protein Synonyms/Alias
 DD-carboxypeptidase; DD-peptidase; Beta-lactamase; Penicillin-binding protein 5; PBP-5 
Gene Name
 dacA 
Gene Synonyms/Alias
 pfv; b0632; JW0627 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
121GSSLMFLKPGMQVPVacetylation[1]
215EYSIYKEKEFTFNGIacetylation[1]
302VNPLKVGKEFASEPVacetylation[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 C-terminal D-alanyl residues from sugar-peptide cell wall precursors. 
Sequence Annotation
 ACT_SITE 73 73 Acyl-ester intermediate.
 ACT_SITE 76 76 Proton acceptor.
 ACT_SITE 139 139
 BINDING 242 242 Substrate.  
Keyword
 3D-structure; Carboxypeptidase; Cell inner membrane; Cell membrane; Cell shape; Cell wall biogenesis/degradation; Complete proteome; Direct protein sequencing; Hydrolase; Membrane; Peptidoglycan synthesis; Protease; Reference proteome; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 403 AA 
Protein Sequence
MNTIFSARIM KRLALTTALC TAFISAAHAD DLNIKTMIPG VPQIDAESYI LIDYNSGKVL 60
AEQNADVRRD PASLTKMMTS YVIGQAMKAG KFKETDLVTI GNDAWATGNP VFKGSSLMFL 120
KPGMQVPVSQ LIRGINLQSG NDACVAMADF AAGSQDAFVG LMNSYVNALG LKNTHFQTVH 180
GLDADGQYSS ARDMALIGQA LIRDVPNEYS IYKEKEFTFN GIRQLNRNGL LWDNSLNVDG 240
IKTGHTDKAG YNLVASATEG QMRLISAVMG GRTFKGREAE SKKLLTWGFR FFETVNPLKV 300
GKEFASEPVW FGDSDRASLG VDKDVYLTIP RGRMKDLKAS YVLNSSELHA PLQKNQVVGT 360
INFQLDGKTI EQRPLVVLQE IPEGNFFGKI IDYIKLMFHH WFG 403 
Gene Ontology
 GO:0005887; C:integral to plasma membrane; IDA:EcoliWiki.
 GO:0008800; F:beta-lactamase activity; IEA:EC.
 GO:0008658; F:penicillin binding; IDA:EcoCyc.
 GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IDA:EcoCyc.
 GO:0051301; P:cell division; IGI:EcoCyc.
 GO:0044036; P:cell wall macromolecule metabolic process; IDA:EcoCyc.
 GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0000270; P:peptidoglycan metabolic process; IDA:EcoCyc.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0008360; P:regulation of cell shape; IGI:EcoCyc. 
Interpro
 IPR012338; Beta-lactam/transpept-like.
 IPR015956; Peniciliin-bd_prot-assoc.
 IPR018044; Peptidase_S11.
 IPR012907; Peptidase_S11_C.
 IPR001967; Peptidase_S11_N. 
Pfam
 PF07943; PBP5_C
 PF00768; Peptidase_S11 
SMART
 SM00936; PBP5_C 
PROSITE
  
PRINTS
 PR00725; DADACBPTASE1.