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P26365

- AMIB_ECOLI

UniProt

P26365 - AMIB_ECOLI

Protein

N-acetylmuramoyl-L-alanine amidase AmiB

Gene

amiB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Cell-wall hydrolase involved in septum cleavage during cell division. Can also act as powerful autolysin in the presence of murein synthesis inhibitors.2 Publications

    Catalytic activityi

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

    GO - Molecular functioni

    1. N-acetylmuramoyl-L-alanine amidase activity Source: EcoliWiki

    GO - Biological processi

    1. peptidoglycan catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acetylmuramoyl-L-alanine amidase AmiB (EC:3.5.1.28)
    Gene namesi
    Name:amiB
    Synonyms:yjeD
    Ordered Locus Names:b4169, JW4127
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11363. amiB.

    Subcellular locationi

    Periplasm By similarity

    GO - Cellular componenti

    1. periplasmic space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 445423N-acetylmuramoyl-L-alanine amidase AmiBPRO_0000006462Add
    BLAST

    Proteomic databases

    PaxDbiP26365.

    Expressioni

    Gene expression databases

    GenevestigatoriP26365.

    Interactioni

    Protein-protein interaction databases

    STRINGi511145.b4169.

    Structurei

    3D structure databases

    ProteinModelPortaliP26365.
    SMRiP26365. Positions 192-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi130 – 1378Poly-Pro

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0860.
    HOGENOMiHOG000263828.
    KOiK01448.
    OMAiLNADPMF.
    OrthoDBiEOG6CP3X3.
    PhylomeDBiP26365.

    Family and domain databases

    Gene3Di3.40.630.40. 2 hits.
    InterProiIPR002508. CW_Hdrlase/autolysin_cat.
    [Graphical view]
    PfamiPF01520. Amidase_3. 1 hit.
    [Graphical view]
    SMARTiSM00646. Ami_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P26365-1 [UniParc]FASTAAdd to Basket

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    MMYRIRNWLV ATLLLLCTPV GAATLSDIQV SNGNQQARIT LSFIGDPDYA    50
    FSHQSKRTVA LDIKQTGVIQ GLPLLFSGNN LVKAIRSGTP KDAQTLRLVV 100
    DLTENGKTEA VKRQNGSNYT VVFTINADVP PPPPPPPVVA KRVETPAVVA 150
    PRVSEPARNP FKTESNRTTG VISSNTVTRP AARATANTGD KIIIAIDAGH 200
    GGQDPGAIGP GGTREKNVTI AIARKLRTLL NDDPMFKGVL TRDGDYFISV 250
    MGRSDVARKQ NANFLVSIHA DAAPNRSATG ASVWVLSNRR ANSEMASWLE 300
    QHEKQSELLG GAGDVLANSQ SDPYLSQAVL DLQFGHSQRV GYDVATSMIS 350
    QLQRIGEIHK RRPEHASLGV LRSPDIPSVL VETGFISNNS EERLLASDDY 400
    QQQLAEAIYK GLRNYFLAHP MQSAPQGATA QTASTVTTPD RTLPN 445
    Length:445
    Mass (Da):47,985
    Last modified:July 1, 1993 - v2
    Checksum:iC79CC9FD77BFCD38
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiS41741.
    RefSeqiNP_418590.1. NC_000913.3.
    YP_492311.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77126; AAC77126; b4169.
    BAE78170; BAE78170; BAE78170.
    GeneIDi12934195.
    948683.
    KEGGiecj:Y75_p4055.
    eco:b4169.
    PATRICi32123911. VBIEscCol129921_4300.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi S41741.
    RefSeqi NP_418590.1. NC_000913.3.
    YP_492311.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P26365.
    SMRi P26365. Positions 192-416.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 511145.b4169.

    Proteomic databases

    PaxDbi P26365.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77126 ; AAC77126 ; b4169 .
    BAE78170 ; BAE78170 ; BAE78170 .
    GeneIDi 12934195.
    948683.
    KEGGi ecj:Y75_p4055.
    eco:b4169.
    PATRICi 32123911. VBIEscCol129921_4300.

    Organism-specific databases

    EchoBASEi EB1338.
    EcoGenei EG11363. amiB.

    Phylogenomic databases

    eggNOGi COG0860.
    HOGENOMi HOG000263828.
    KOi K01448.
    OMAi LNADPMF.
    OrthoDBi EOG6CP3X3.
    PhylomeDBi P26365.

    Enzyme and pathway databases

    BioCyci EcoCyc:NACMURLALAAMI2-MONOMER.
    ECOL316407:JW4127-MONOMER.
    MetaCyc:NACMURLALAAMI2-MONOMER.

    Miscellaneous databases

    PROi P26365.

    Gene expression databases

    Genevestigatori P26365.

    Family and domain databases

    Gene3Di 3.40.630.40. 2 hits.
    InterProi IPR002508. CW_Hdrlase/autolysin_cat.
    [Graphical view ]
    Pfami PF01520. Amidase_3. 1 hit.
    [Graphical view ]
    SMARTi SM00646. Ami_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiAMIB_ECOLI
    AccessioniPrimary (citable) accession number: P26365
    Secondary accession number(s): Q2M6D6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3