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Reviewed, UniProtKB/Swiss-Prot P26365 (AMIB_ECOLI)

Last modified February 9, 2010. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Cell-wall hydrolase probably involved in cell-wall hydrolysis, septation or recycling.

Catalytic activity

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

Subcellular location

Secreted Potential.

Sequence similarities

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

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Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcellular cell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

peptidoglycan biosynthetic process

Inferred from genetic interaction. Source: UniProtKB

peptidoglycan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionN-acetylmuramoyl-L-alanine amidase activity

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

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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

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Sequences

Sequence LengthMass (Da)Tools
P26365-1 [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

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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: 7511774] [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: 7610040] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 1594459] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-445.
Strain: K12.

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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.
RefSeqAP_004669.1.
NP_418590.1.

3D structure databases

SMRP26365. Positions 193-417.
ModBaseSearch...

Protein-protein interaction databases

STRINGP26365.

Genome annotation databases

GeneID948683.
GenomeReviewsGene locus JW4127 in contig AP009048_GR.
Gene locus b4169 in contig U00096_GR.
KEGGecj:JW4127.
eco:b4169.

Organism-specific databases

EchoBASEEB1338.
EcoGeneEG11363. amiB.
CMRSearch...

Phylogenomic databases

eggNOGCOG0860.
HOGENOMHBG656726.
OMAANSQADP.

Enzyme and pathway databases

BioCycEcoCyc:NACMURLALAAMI2-MONOMER.
ECOL168927:B4169-MONOMER.

Gene expression databases

GenevestigatorP26365.

Family and domain databases

InterProIPR002508. CW_Hdrlase/autolysin_cat.
[Graphical view]
Gene3DG3DSA:3.40.630.40. Cell_wall_OHase/autolysin_cat. 1 hit.
PfamPF01520. Amidase_3. 1 hit.
[Graphical view]
SMARTSM00646. Ami_3. 1 hit.
[Graphical view]
ProtoNetSearch...

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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: February 9, 2010
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents