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P26365 (AMIB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. 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 AmiB

EC=3.5.1.28
Gene names
Name:amiB
Synonyms:yjeD
Ordered Locus Names:b4169, JW4127
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length445 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.7

Catalytic activity

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

Subcellular location

Periplasm By similarity.

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 electronic annotation. Source: UniProtKB-SubCell

   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 – 2222 Potential
Chain23 – 445423N-acetylmuramoyl-L-alanine amidase AmiB
PRO_0000006462

Regions

Compositional bias130 – 1378Poly-Pro

Sequences

Sequence LengthMass (Da)Tools
P26365 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: C79CC9FD77BFCD38

FASTA44547,985
        10         20         30         40         50         60 
MMYRIRNWLV ATLLLLCTPV GAATLSDIQV SNGNQQARIT LSFIGDPDYA FSHQSKRTVA 

        70         80         90        100        110        120 
LDIKQTGVIQ GLPLLFSGNN LVKAIRSGTP KDAQTLRLVV DLTENGKTEA VKRQNGSNYT 

       130        140        150        160        170        180 
VVFTINADVP PPPPPPPVVA KRVETPAVVA PRVSEPARNP FKTESNRTTG VISSNTVTRP 

       190        200        210        220        230        240 
AARATANTGD KIIIAIDAGH GGQDPGAIGP GGTREKNVTI AIARKLRTLL NDDPMFKGVL 

       250        260        270        280        290        300 
TRDGDYFISV MGRSDVARKQ NANFLVSIHA DAAPNRSATG ASVWVLSNRR ANSEMASWLE 

       310        320        330        340        350        360 
QHEKQSELLG GAGDVLANSQ SDPYLSQAVL DLQFGHSQRV GYDVATSMIS QLQRIGEIHK 

       370        380        390        400        410        420 
RRPEHASLGV LRSPDIPSVL VETGFISNNS EERLLASDDY QQQLAEAIYK GLRNYFLAHP 

       430        440 
MQSAPQGATA QTASTVTTPD RTLPN 

« Hide

References

« Hide 'large scale' references
[1]"The mutL repair gene of Escherichia coli K-12 forms a superoperon with a gene encoding a new cell-wall amidase."
Tsui H.-C.T., Zhao G., Feng G., Leung H.-C.E., Winkler M.E.
Mol. Microbiol. 11:189-202(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[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]"Nonconserved segment of the MutL protein from Escherichia coli K-12 and Salmonella typhimurium."
Tsui H.-C.T., Mandavilli B.S., Winkler M.E.
Nucleic Acids Res. 20:2379-2379(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-445.
Strain: K12.
[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.
Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
[7]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19346 Unassigned DNA. Translation: AAA20097.1.
U14003 Genomic DNA. Translation: AAA97065.1.
U00096 Genomic DNA. Translation: AAC77126.1.
AP009048 Genomic DNA. Translation: BAE78170.1.
Z11831 Genomic DNA. Translation: CAA77851.1.
PIRS41741.
RefSeqNP_418590.1. NC_000913.3.
YP_492311.1. NC_007779.1.

3D structure databases

ProteinModelPortalP26365.
SMRP26365. Positions 192-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING511145.b4169.

Proteomic databases

PaxDbP26365.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77126; AAC77126; b4169.
BAE78170; BAE78170; BAE78170.
GeneID12934195.
948683.
KEGGecj:Y75_p4055.
eco:b4169.
PATRIC32123911. VBIEscCol129921_4300.

Organism-specific databases

EchoBASEEB1338.
EcoGeneEG11363. amiB.

Phylogenomic databases

eggNOGCOG0860.
HOGENOMHOG000263828.
KOK01448.
OMAQPVYAFF.
OrthoDBEOG6CP3X3.
PhylomeDBP26365.
ProtClustDBPRK10431.

Enzyme and pathway databases

BioCycEcoCyc:NACMURLALAAMI2-MONOMER.
ECOL316407:JW4127-MONOMER.
MetaCyc:NACMURLALAAMI2-MONOMER.

Gene expression databases

GenevestigatorP26365.

Family and domain databases

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

Other

PROP26365.

Entry information

Entry nameAMIB_ECOLI
AccessionPrimary (citable) accession number: P26365
Secondary accession number(s): Q2M6D6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 105 of the entry and version 2 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