Reviewed, UniProtKB/Swiss-Prot P13016 (AMPD_ECOLI)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	183 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
Gene Ontology (GO)
Biological process	cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N-acetylmuramoyl-L-alanine amidase activity Inferred from electronic annotation. Source: EC zinc 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
	Metal binding	34	1	Zinc; catalytic By similarity
	Metal binding	154	1	Zinc; catalytic By similarity
	Metal binding	164	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	P13016-1 [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: 2691840] [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: 2607970] [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: 9278503] [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: 16738553] [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: 7959070] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-92. Strain: K12.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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	AP_000771.1. NP_414652.1.
3D structure databases
HSSP	HSSP built from PDB template 1J3G based on UniProtKB P82974.
SMR	P13016. Positions 1-182.
ModBase	Search...
Genome annotation databases
GeneID	948877.
GenomeReviews	Gene locus JW0106 in contig AP009048_GR. Gene locus b0110 in contig U00096_GR.
KEGG	ecj:JW0106. eco:b0110.
Organism-specific databases
EchoBASE	EB0039.
EcoGene	EG10041. ampD.
CMR	Search...
Phylogenomic databases
HOGENOM	P13016.
OMA	P13016. VQFVSCD.
Enzyme and pathway databases
BioCyc	EcoCyc:EG10041-MON.
Family and domain databases
InterPro	IPR002502. Amidase_2. [Graphical view]
Gene3D	G3DSA:3.40.80.10. Amidase_2. 1 hit.
Pfam	PF01510. Amidase_2. 1 hit. [Graphical view]
SMART	SM00644. Ami_2. 1 hit. [Graphical view]
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:	June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)