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P13016 (AMPD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length183 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processCell wall biogenesis/degradation
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpeptidoglycan catabolic process

Inferred from electronic annotation. Source: InterPro

peptidoglycan turnover

Inferred from mutant phenotype PubMed 7925310. Source: EcoCyc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionN-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1831831,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD
PRO_0000164413

Sites

Active site1161Proton acceptor By similarity
Metal binding341Zinc; catalytic By similarity
Metal binding1541Zinc; catalytic By similarity
Metal binding1641Zinc; catalytic By similarity
Site1621Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
P13016 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: F62910F8F889043D

FASTA18320,536
        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 

« Hide

References

« Hide '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 277:1453-1462(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.
PIRS05569.
RefSeqNP_414652.1. NC_000913.3.
YP_488413.1. NC_007779.1.

3D structure databases

ProteinModelPortalP13016.
SMRP13016. Positions 1-179.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING511145.b0110.

Proteomic databases

PRIDEP13016.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73221; AAC73221; b0110.
BAB96679; BAB96679; BAB96679.
GeneID12932901.
948877.
KEGGecj:Y75_p0107.
eco:b0110.
PATRIC32115321. VBIEscCol129921_0112.

Organism-specific databases

EchoBASEEB0039.
EcoGeneEG10041. ampD.

Phylogenomic databases

eggNOGCOG3023.
HOGENOMHOG000255963.
KOK03806.
OMACNDDSIG.
OrthoDBEOG60GRR5.
PhylomeDBP13016.
ProtClustDBPRK11789.

Enzyme and pathway databases

BioCycEcoCyc:EG10041-MONOMER.
ECOL316407:JW0106-MONOMER.
MetaCyc:EG10041-MONOMER.

Gene expression databases

GenevestigatorP13016.

Family and domain databases

Gene3D3.40.80.10. 1 hit.
InterProIPR002502. Amidase_domain.
[Graphical view]
PfamPF01510. Amidase_2. 1 hit.
[Graphical view]
SMARTSM00644. Ami_2. 1 hit.
[Graphical view]
SUPFAMSSF55846. SSF55846. 1 hit.
ProtoNetSearch...

Other

PROP13016.

Entry information

Entry nameAMPD_ECOLI
AccessionPrimary (citable) accession number: P13016
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene