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P36548 (AMIA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. 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:
N-acetylmuramoyl-L-alanine amidase AmiA

EC=3.5.1.28
Gene names
Name:amiA
Synonyms:yfeE
Ordered Locus Names:b2435, JW2428
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell-wall hydrolase involved in septum cleavage during cell division. Can also act as powerful autolysin in the presence of murein synthesis inhibitors. Ref.6 Ref.9

Catalytic activity

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

Subcellular location

Periplasm. Note: Distributed throughout the periplasm in all cells. Ref.7

Post-translational modification

Exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. Can also be exported by the Sec system.

Disruption phenotype

Mutants are growing in chains of 3 to 6 cells. Ref.6

Sequence similarities

Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentPeriplasm
   DomainSignal
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpeptidoglycan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentperiplasmic space

Inferred from direct assay Ref.7. Source: EcoliWiki

   Molecular_functionN-acetylmuramoyl-L-alanine amidase activity

Inferred from direct assay Ref.6. Source: EcoliWiki

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434Tat-type signal Potential
Chain35 – 289255N-acetylmuramoyl-L-alanine amidase AmiA
PRO_0000006460

Sequences

Sequence LengthMass (Da)Tools
P36548 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 614D1E526D9FEFC5

FASTA28931,412
        10         20         30         40         50         60 
MSTFKPLKTL TSRRQVLKAG LAALTLSGMS QAIAKDELLK TSNGHSKPKA KKSGGKRVVV 

        70         80         90        100        110        120 
LDPGHGGIDT GAIGRNGSKE KHVVLAIAKN VRSILRNHGI DARLTRSGDT FIPLYDRVEI 

       130        140        150        160        170        180 
AHKHGADLFM SIHADGFTNP KAAGASVFAL SNRGASSAMA KYLSERENRA DEVAGKKATD 

       190        200        210        220        230        240 
KDHLLQQVLF DLVQTDTIKN SLTLGSHILK KIKPVHKLHS RNTEQAAFVV LKSPSVPSVL 

       250        260        270        280 
VETSFITNPE EERLLGTAAF RQKIATAIAE GVISYFHWFD NQKAHSKKR 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of the hemF operon containing the gene for the Escherichia coli aerobic coproporphyrinogen III oxidase by in vivo complementation of a yeast HEM13 mutant."
Troup B., Jahn M., Hungerer C., Jahn D.
J. Bacteriol. 176:673-680(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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]"Systematic characterization of curved DNA segments randomly cloned from Escherichia coli and their functional significance."
Tanaka K., Muramatsu S., Yamada H., Mizuno T.
Mol. Gen. Genet. 226:367-376(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
[6]"Involvement of N-acetylmuramyl-L-alanine amidases in cell separation and antibiotic-induced autolysis of Escherichia coli."
Heidrich C., Templin M.F., Ursinus A., Merdanovic M., Berger J., Schwarz H., de Pedro M.A., Holtje J.V.
Mol. Microbiol. 41:167-178(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS AN AMIDASE, DISRUPTION PHENOTYPE.
Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
[7]"The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway."
Bernhardt T.G., de Boer P.A.
Mol. Microbiol. 48:1171-1182(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, EXPORT VIA THE TAT-SYSTEM.
Strain: K12.
[8]"Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides."
Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B., Palmer T., Georgiou G.
J. Biol. Chem. 282:8309-8316(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: EXPORT VIA THE TAT-SYSTEM AND THE SEC-SYSTEM.
[9]"Growth of Escherichia coli: significance of peptidoglycan degradation during elongation and septation."
Uehara T., Park J.T.
J. Bacteriol. 190:3914-3922(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: K12.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75413 Genomic DNA. Translation: CAA53166.1.
U00096 Genomic DNA. Translation: AAC75488.1.
AP009048 Genomic DNA. Translation: BAA16318.1.
X63986 Genomic DNA. Translation: CAB57860.1.
PIRA36964.
RefSeqNP_416930.1. NC_000913.3.
YP_490671.1. NC_007779.1.

3D structure databases

ProteinModelPortalP36548.
SMRP36548. Positions 59-272.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9098N.
IntActP36548. 9 interactions.
STRING511145.b2435.

Proteomic databases

PaxDbP36548.
PRIDEP36548.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75488; AAC75488; b2435.
BAA16318; BAA16318; BAA16318.
GeneID12930623.
946916.
KEGGecj:Y75_p2396.
eco:b2435.
PATRIC32120255. VBIEscCol129921_2530.

Organism-specific databases

EchoBASEEB1770.
EcoGeneEG11823. amiA.

Phylogenomic databases

eggNOGCOG0860.
HOGENOMHOG000263827.
KOK01448.
OMASYFNWFD.
OrthoDBEOG6CP3X3.
PhylomeDBP36548.

Enzyme and pathway databases

BioCycEcoCyc:NACMURLALAAMI1-MONOMER.
ECOL316407:JW2428-MONOMER.
MetaCyc:NACMURLALAAMI1-MONOMER.

Gene expression databases

GenevestigatorP36548.

Family and domain databases

Gene3D3.40.630.40. 2 hits.
InterProIPR002508. CW_Hdrlase/autolysin_cat.
IPR006311. TAT_signal.
[Graphical view]
PfamPF01520. Amidase_3. 1 hit.
[Graphical view]
SMARTSM00646. Ami_3. 1 hit.
[Graphical view]
PROSITEPS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP36548.

Entry information

Entry nameAMIA_ECOLI
AccessionPrimary (citable) accession number: P36548
Secondary accession number(s): P78199
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 109 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