UniProt Accession

 AMPD_ECOLI; P13016 

Genbank Protein ID

 X15237; U00096; AP009048; L28105 

Genbank Nucleotide ID

 CAA33314.1; AAC73221.1; BAB96679.1; AAC36921.1 

Protein Name

 1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD 

Protein Synonyms/Alias

 N-acetylmuramoyl-L-alanine amidase 

Gene Name

 ampD 

Gene Synonyms/Alias

 b0110; JW0106 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
92	VQYVPFDKRAWHAGV	acetylation	[1]
162	CDIAPDRKTDPGPAF	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

 Involved in both cell wall peptidoglycans recycling and beta-lactamase induction. Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha- amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety (By similarity). 

Sequence Annotation

 ACT_SITE 116 116 Proton acceptor (By similarity).
 METAL 34 34 Zinc; catalytic (By similarity).
 METAL 154 154 Zinc; catalytic (By similarity).
 METAL 164 164 Zinc; catalytic (By similarity).  

Keyword

 Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Reference proteome; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 183 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IDA:EcoCyc.
 GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
 GO:0009254; P:peptidoglycan turnover; IMP:EcoCyc. 

Interpro

 IPR002502; Amidase_domain. 

Pfam

 PF01510; Amidase_2 

SMART

 SM00644; Ami_2 

PROSITE

  

PRINTS