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P75820 (AMID_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
N-acetylmuramoyl-L-alanine amidase AmiD

EC=3.5.1.28
Gene names
Name:amiD
Synonyms:ybjR
Ordered Locus Names:b0867, JW0851
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length276 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit. Ref.4

Subcellular location

Cell outer membrane; Lipid-anchor Probable.

Sequence similarities

Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 By similarity
Chain17 – 276260N-acetylmuramoyl-L-alanine amidase AmiD
PRO_0000164417

Regions

Region51 – 522Substrate binding

Sites

Active site1191Proton acceptor Ref.4
Metal binding501Zinc; catalytic
Metal binding1661Zinc; catalytic
Metal binding1761Zinc; catalytic
Site1741Transition state stabilizer

Amino acid modifications

Lipidation171N-palmitoyl cysteine By similarity
Lipidation171S-diacylglycerol cysteine By similarity

Secondary structure

...................................... 276
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P75820 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: E6E4F642AFF548CD

FASTA27631,072
        10         20         30         40         50         60 
MRRFFWLVAA ALLLAGCAGE KGIVEKEGYQ LDTRRQAQAA YPRIKVLVIH YTADDFDSSL 

        70         80         90        100        110        120 
ATLTDKQVSS HYLVPAVPPR YNGKPRIWQL VPEQELAWHA GISAWRGATR LNDTSIGIEL 

       130        140        150        160        170        180 
ENRGWQKSAG VKYFAPFEPA QIQALIPLAK DIIARYHIKP ENVVAHADIA PQRKDDPGPL 

       190        200        210        220        230        240 
FPWQQLAQQG IGAWPDAQRV NFYLAGRAPH TPVDTASLLE LLARYGYDVK PDMTPREQRR 

       250        260        270 
VIMAFQMHFR PTLYNGEADA ETQAIAEALL EKYGQD 

« Hide

References

« Hide 'large scale' references
[1]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"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.
[3]"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.
[4]"Specific structural features of the N-acetylmuramoyl-L-alanine amidase AmiD from Escherichia coli and mechanistic implications for enzymes of this family."
Kerff F., Petrella S., Mercier F., Sauvage E., Herman R., Pennartz A., Zervosen A., Luxen A., Frere J.M., Joris B., Charlier P.
J. Mol. Biol. 397:249-259(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 18-276 IN COMPLEX WITH ZINC AND N-ACETYLMURAMOYL-TRIPEPTIDE, COFACTOR, ACTIVE SITE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC73954.1.
AP009048 Genomic DNA. Translation: BAA35581.1.
PIRC64825.
RefSeqNP_415388.1. NC_000913.3.
YP_489140.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BH7X-ray2.20A18-276[»]
2WKXX-ray1.80A18-276[»]
3D2YX-ray1.75A18-276[»]
3D2ZX-ray2.80A18-276[»]
ProteinModelPortalP75820.
SMRP75820. Positions 20-276.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING511145.b0867.

Proteomic databases

PRIDEP75820.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73954; AAC73954; b0867.
BAA35581; BAA35581; BAA35581.
GeneID12931004.
945494.
KEGGecj:Y75_p0840.
eco:b0867.
PATRIC32116941. VBIEscCol129921_0896.

Organism-specific databases

EchoBASEEB3451.
EcoGeneEG13687. amiD.

Phylogenomic databases

eggNOGCOG3023.
HOGENOMHOG000255964.
KOK11066.
OMAIGAWPDE.
OrthoDBEOG60GRR5.
PhylomeDBP75820.
ProtClustDBCLSK879798.

Enzyme and pathway databases

BioCycEcoCyc:G6452-MONOMER.
ECOL316407:JW0851-MONOMER.
MetaCyc:G6452-MONOMER.

Gene expression databases

GenevestigatorP75820.

Family and domain databases

Gene3D3.40.80.10. 1 hit.
InterProIPR002502. Amidase_domain.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamPF01510. Amidase_2. 1 hit.
[Graphical view]
SMARTSM00644. Ami_2. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF55846. SSF55846. 1 hit.
PROSITEPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP75820.
PROP75820.

Entry information

Entry nameAMID_ECOLI
AccessionPrimary (citable) accession number: P75820
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 111 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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