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E1W818 (AMPD_SALTS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:SL1344_0146
OrganismSalmonella typhimurium (strain SL1344) [Complete proteome] [HAMAP]
Taxonomic identifier216597 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length187 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

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
Gene Ontology (GO)
   Biological_processpeptidoglycan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionN-acetylmuramoyl-L-alanine amidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

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 – 1871871,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD
PRO_0000405414

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
E1W818 [UniParc].

Last modified November 30, 2010. Version 1.
Checksum: 9E7EBAC553AEDFE1

FASTA18720,913
        10         20         30         40         50         60 
MLPDKGWLVE ARRVPSPHYD CRPDDEKPSL LVVHNISLPP GEFGGPWIDA LFTGTIDPDA 

        70         80         90        100        110        120 
HPFFAEIAHL RVSAHCLIRR DGEIVQYVPF DKRAWHAGVS NYQGRERCND FSIGIELEGT 

       130        140        150        160        170        180 
DTLAYTDAQY QQLAAVTRTL IASYPAIADN MTGHCNIAPD RKTDPGPAFD WPRFRALVAL 


SSHKEMT 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a Salmonella-specific region located between ampE and aroP genes."
Cano D., Casadesus J., Garcia-del Portillo F.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SL1344.
[2]"The transcriptional landscape and small RNAs of Salmonella enterica serovar Typhimurium."
Kroger C., Dillon S.C., Cameron A.D., Papenfort K., Sivasankaran S.K., Hokamp K., Chao Y., Sittka A., Hebrard M., Handler K., Colgan A., Leekitcharoenphon P., Langridge G.C., Lohan A.J., Loftus B., Lucchini S., Ussery D.W., Dorman C.J. expand/collapse author list , Thomson N.R., Vogel J., Hinton J.C.
Proc. Natl. Acad. Sci. U.S.A. 109:E1277-E1286(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SL1344.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ242516 Genomic DNA. Translation: CAB89835.1.
FQ312003 Genomic DNA. Translation: CBW16249.1.
RefSeqYP_005180083.1. NC_016810.1.

3D structure databases

ProteinModelPortalE1W818.
SMRE1W818. Positions 1-187.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCBW16249; CBW16249; SL1344_0146.
PATRIC43185606. VBISalEnt88447_0162.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMARCNDYSI.

Enzyme and pathway databases

BioCycSENT216597:GJB7-148-MONOMER.

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...

Entry information

Entry nameAMPD_SALTS
AccessionPrimary (citable) accession number: E1W818
Secondary accession number(s): P30013, Q9L4I4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: November 30, 2010
Last modified: February 19, 2014
This is version 24 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