P13016 (AMPD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD
EC=3.5.1.28

Alternative name(s):
N-acetylmuramoyl-L-alanine amidase

Gene names

Name:	ampD
Ordered Locus Names:	b0110, JW0106

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	183 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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.
Catalytic activity	Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Cofactor	Zinc; required for amidase activity By similarity.
Subcellular location	Cytoplasm.
Induction	Inactivation of AmpD results in AmpR-dependent hyperinduction and AmpD affects beta-lactam susceptibility in the absence of cloned C.freundii amp genes suggesting a linkage between AmpD and peptidoglycan synthesis.
Sequence similarities	Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro peptidoglycan turnover Inferred from mutant phenotype PubMed 7925310. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	N-acetylmuramoyl-L-alanine amidase activity Inferred from direct assay PubMed 7958768. Source: EcoCyc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 183	183	1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD		PRO_0000164413
Sites
	Active site	116	1	Proton acceptor By similarity
	Metal binding	34	1	Zinc; catalytic By similarity
	Metal binding	154	1	Zinc; catalytic By similarity
	Metal binding	164	1	Zinc; catalytic By similarity
	Site	162	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	P13016 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: F62910F8F889043D	FASTA	183	20,536
	10 20 30 40 50 60 MLLEQGWLVG ARRVPSPHYD CRPDDETPTL LVVHNISLPP GEFGGPWIDA LFTGTIDPQA 70 80 90 100 110 120 HPFFAEIAHL RVSAHCLIRR DGEIVQYVPF DKRAWHAGVS QYQGRERCND FSIGIELEGT 130 140 150 160 170 180 DTLAYTDAQY QQLAAVTRAL IDCYPDIAKN MTGHCDIAPD RKTDPGPAFD WARFRVLVSK ETT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Signalling proteins in enterobacterial AmpC beta-lactamase regulation." Lindquist S., Galleni M., Lindberg F., Normark S. Mol. Microbiol. 3:1091-1102(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Regulation of enterobacterial cephalosporinase production: the role of a membrane-bound sensory transducer." Honore N., Nicolas M.H., Cole S.T. Mol. Microbiol. 3:1121-1130(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Escherichia coli contains a set of genes homologous to those involved in protein secretion, DNA uptake and the assembly of type-4 fimbriae in other bacteria." Whitchurch C.B., Mattick J.S. Gene 150:9-15(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-92. Strain: K12.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X15237 Genomic DNA. Translation: CAA33314.1. U00096 Genomic DNA. Translation: AAC73221.1. AP009048 Genomic DNA. Translation: BAB96679.1. L28105 Genomic DNA. Translation: AAC36921.1.
PIR	S05569.
RefSeq	NP_414652.1. NC_000913.2. YP_488413.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P13016.
SMR	P13016. Positions 1-179.
ModBase	Search...
Protein-protein interaction databases
STRING	511145.b0110.
Proteomic databases
PRIDE	P13016.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73221; AAC73221; b0110. BAB96679; BAB96679; BAB96679.
GeneID	12932901. 948877.
KEGG	ecj:Y75_p0107. eco:b0110.
PATRIC	32115321. VBIEscCol129921_0112.
Organism-specific databases
EchoBASE	EB0039.
EcoGene	EG10041. ampD.
Phylogenomic databases
eggNOG	COG3023.
HOGENOM	HOG000255963.
KO	K03806.
OMA	CNDDSIG.
ProtClustDB	PRK11789.
Enzyme and pathway databases
BioCyc	EcoCyc:EG10041-MONOMER. ECOL316407:JW0106-MONOMER. MetaCyc:EG10041-MONOMER.
Gene expression databases
Genevestigator	P13016.
Family and domain databases
Gene3D	3.40.80.10. 1 hit.
InterPro	IPR002502. Amidase_domain. [Graphical view]
Pfam	PF01510. Amidase_2. 1 hit. [Graphical view]
SMART	SM00644. Ami_2. 1 hit. [Graphical view]
SUPFAM	SSF55846. Amidase_2. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AMPD_ECOLI

Accession

Primary (citable) accession number: P13016

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program