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Protein

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

Gene

ampD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.

Cofactori

Zn2+By similarityNote: Zn2+ is required for amidase activity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341Zinc; catalyticBy similarity
Active sitei116 – 1161Proton acceptorBy similarity
Metal bindingi154 – 1541Zinc; catalyticBy similarity
Sitei162 – 1621Transition state stabilizerBy similarity
Metal bindingi164 – 1641Zinc; catalyticBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. N-acetylmuramoyl-L-alanine amidase activity Source: EcoCyc

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. peptidoglycan catabolic process Source: InterPro
  3. peptidoglycan turnover Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
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 namesi
Name:ampD
Ordered Locus Names:b0110, JW0106
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10041. ampD.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1831831,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpDPRO_0000164413Add
BLAST

Proteomic databases

PRIDEiP13016.

Expressioni

Inductioni

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.

Gene expression databases

GenevestigatoriP13016.

Interactioni

Protein-protein interaction databases

STRINGi511145.b0110.

Structurei

3D structure databases

ProteinModelPortaliP13016.
SMRiP13016. Positions 1-179.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3023.
HOGENOMiHOG000255963.
InParanoidiP13016.
KOiK03806.
OMAiCNDDSIG.
OrthoDBiEOG60GRR5.
PhylomeDBiP13016.

Family and domain databases

Gene3Di3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
[Graphical view]
PfamiPF01510. Amidase_2. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.

Sequencei

Sequence statusi: Complete.

P13016-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLEQGWLVG ARRVPSPHYD CRPDDETPTL LVVHNISLPP GEFGGPWIDA
60 70 80 90 100
LFTGTIDPQA HPFFAEIAHL RVSAHCLIRR DGEIVQYVPF DKRAWHAGVS
110 120 130 140 150
QYQGRERCND FSIGIELEGT DTLAYTDAQY QQLAAVTRAL IDCYPDIAKN
160 170 180
MTGHCDIAPD RKTDPGPAFD WARFRVLVSK ETT
Length:183
Mass (Da):20,536
Last modified:January 1, 1990 - v1
Checksum:iF62910F8F889043D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15237 Genomic DNA. Translation: CAA33314.1.
U00096 Genomic DNA. Translation: AAC73221.1.
AP009048 Genomic DNA. Translation: BAB96679.1.
L28105 Genomic DNA. Translation: AAC36921.1.
PIRiS05569.
RefSeqiNP_414652.1. NC_000913.3.
YP_488413.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73221; AAC73221; b0110.
BAB96679; BAB96679; BAB96679.
GeneIDi12932901.
948877.
KEGGiecj:Y75_p0107.
eco:b0110.
PATRICi32115321. VBIEscCol129921_0112.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15237 Genomic DNA. Translation: CAA33314.1.
U00096 Genomic DNA. Translation: AAC73221.1.
AP009048 Genomic DNA. Translation: BAB96679.1.
L28105 Genomic DNA. Translation: AAC36921.1.
PIRiS05569.
RefSeqiNP_414652.1. NC_000913.3.
YP_488413.1. NC_007779.1.

3D structure databases

ProteinModelPortaliP13016.
SMRiP13016. Positions 1-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi511145.b0110.

Proteomic databases

PRIDEiP13016.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73221; AAC73221; b0110.
BAB96679; BAB96679; BAB96679.
GeneIDi12932901.
948877.
KEGGiecj:Y75_p0107.
eco:b0110.
PATRICi32115321. VBIEscCol129921_0112.

Organism-specific databases

EchoBASEiEB0039.
EcoGeneiEG10041. ampD.

Phylogenomic databases

eggNOGiCOG3023.
HOGENOMiHOG000255963.
InParanoidiP13016.
KOiK03806.
OMAiCNDDSIG.
OrthoDBiEOG60GRR5.
PhylomeDBiP13016.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP13016.

Gene expression databases

GenevestigatoriP13016.

Family and domain databases

Gene3Di3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
[Graphical view]
PfamiPF01510. Amidase_2. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiAMPD_ECOLI
AccessioniPrimary (citable) accession number: P13016
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: January 7, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.