Reviewed,
UniProtKB/Swiss-Prot P26365 (AMIB_ECOLI)
Last modified
February 9, 2010.
Version 74.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: N-acetylmuramoyl-L-alanine amidase amiB EC=3.5.1.28 | ||||||
| Gene names |
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| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 445 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell wall biogenesis/degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic processInferred from genetic interaction. Source: UniProtKB peptidoglycan catabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | N-acetylmuramoyl-L-alanine amidase activity Inferred from direct assay. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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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. |
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. |
| PIR | S41741. |
| RefSeq | AP_004669.1. NP_418590.1. |
3D structure databases | |
| SMR | P26365. Positions 193-417. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P26365. |
Genome annotation databases | |
| GeneID | 948683. |
| GenomeReviews | Gene locus JW4127 in contig AP009048_GR. Gene locus b4169 in contig U00096_GR. |
| KEGG | ecj:JW4127. eco:b4169. |
Organism-specific databases | |
| EchoBASE | EB1338. |
| EcoGene | EG11363. amiB. |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0860. |
| HOGENOM | HBG656726. |
| OMA | ANSQADP. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:NACMURLALAAMI2-MONOMER. ECOL168927:B4169-MONOMER. |
Gene expression databases | |
| Genevestigator | P26365. |
Family and domain databases | |
| InterPro | IPR002508. CW_Hdrlase/autolysin_cat. [Graphical view] |
| Gene3D | G3DSA:3.40.630.40. Cell_wall_OHase/autolysin_cat. 1 hit. |
| Pfam | PF01520. Amidase_3. 1 hit. [Graphical view] |
| SMART | SM00646. Ami_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMIB_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P26365 Secondary accession number(s): Q2M6D6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| SIMILARITY comments Index of protein domains and families |

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