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P63883

- AMIC_ECOLI

UniProt

P63883 - AMIC_ECOLI

Protein

N-acetylmuramoyl-L-alanine amidase AmiC

Gene

amiC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      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: EcoCyc

    GO - Biological processi

    1. FtsZ-dependent cytokinesis Source: EcoCyc
    2. peptidoglycan catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Enzyme and pathway databases

    BioCyciEcoCyc:G7458-MONOMER.
    ECOL316407:JW5449-MONOMER.
    MetaCyc:G7458-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acetylmuramoyl-L-alanine amidase AmiC (EC:3.5.1.28)
    Gene namesi
    Name:amiC
    Synonyms:ygdN
    Ordered Locus Names:b2817, JW5449
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG13086. amiC.

    Subcellular locationi

    Periplasm 1 Publication
    Note: Present throughout the periplasm in non-dividing cells, but localizes almost exclusively to a ring at the site of constriction in dividing cells.

    GO - Cellular componenti

    1. outer membrane-bounded periplasmic space Source: EcoCyc
    2. periplasmic space Source: EcoliWiki

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    Disruption phenotypei

    Mutants are growing in chains of 3 to 6 cells.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Tat-type signalPROSITE-ProRule annotationAdd
    BLAST
    Chaini32 – 417386N-acetylmuramoyl-L-alanine amidase AmiCPRO_0000006465Add
    BLAST

    Post-translational modificationi

    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.

    Proteomic databases

    PRIDEiP63883.

    Expressioni

    Gene expression databases

    GenevestigatoriP63883.

    Interactioni

    Protein-protein interaction databases

    IntActiP63883. 2 interactions.
    STRINGi511145.b2817.

    Structurei

    Secondary structure

    1
    417
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 428
    Beta strandi48 – 569
    Beta strandi59 – 657
    Turni66 – 694
    Beta strandi70 – 778
    Helixi82 – 854
    Helixi86 – 905
    Beta strandi96 – 10712
    Beta strandi110 – 11910
    Beta strandi121 – 1288
    Beta strandi136 – 1449
    Helixi155 – 1595
    Turni182 – 1843
    Beta strandi188 – 1947
    Helixi211 – 22616
    Beta strandi232 – 2376
    Beta strandi239 – 2413
    Helixi246 – 25510
    Beta strandi259 – 2657
    Beta strandi270 – 2723
    Beta strandi276 – 2827
    Helixi290 – 30011
    Helixi302 – 3065
    Helixi324 – 34320
    Turni344 – 3463
    Beta strandi349 – 3535
    Beta strandi355 – 3573
    Helixi360 – 3623
    Beta strandi369 – 3735
    Helixi380 – 3867
    Helixi389 – 40618

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4BINX-ray2.49A35-417[»]
    ProteinModelPortaliP63883.
    SMRiP63883. Positions 35-408.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    N-terminal domain is required and sufficient for targeting to the septal ring.1 Publication

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0860.
    HOGENOMiHOG000263827.
    KOiK01448.
    OMAiHKNKVDQ.
    OrthoDBiEOG6CP3X3.
    PhylomeDBiP63883.

    Family and domain databases

    Gene3Di3.40.630.40. 2 hits.
    InterProiIPR021731. AMIN_dom.
    IPR002508. CW_Hdrlase/autolysin_cat.
    IPR006311. TAT_signal.
    [Graphical view]
    PfamiPF01520. Amidase_3. 1 hit.
    PF11741. AMIN. 1 hit.
    [Graphical view]
    SMARTiSM00646. Ami_3. 1 hit.
    [Graphical view]
    PROSITEiPS51318. TAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P63883-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGSNTAISR RRLLQGAGAM WLLSVSQVSL AAVSQVVAVR VWPASSYTRV    50
    TVESNRQLKY KQFALSNPER VVVDIEDVNL NSVLKGMAAQ IRADDPFIKS 100
    ARVGQFDPQT VRMVFELKQN VKPQLFALAP VAGFKERLVM DLYPANAQDM 150
    QDPLLALLED YNKGDLEKQV PPAQSGPQPG KAGRDRPIVI MLDPGHGGED 200
    SGAVGKYKTR EKDVVLQIAR RLRSLIEKEG NMKVYMTRNE DIFIPLQVRV 250
    AKAQKQRADL FVSIHADAFT SRQPSGSSVF ALSTKGATST AAKYLAQTQN 300
    ASDLIGGVSK SGDRYVDHTM FDMVQSLTIA DSLKFGKAVL NKLGKINKLH 350
    KNQVEQAGFA VLKAPDIPSI LVETAFISNV EEERKLKTAT FQQEVAESIL 400
    AGIKAYFADG ATLARRG 417
    Length:417
    Mass (Da):45,634
    Last modified:October 11, 2004 - v1
    Checksum:i76F8F733DCCC36D7
    GO

    Sequence cautioni

    The sequence AAB40464.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29581 Genomic DNA. Translation: AAB40464.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC75856.2.
    AP009048 Genomic DNA. Translation: BAE76886.1.
    RefSeqiNP_417294.4. NC_000913.3.
    YP_491022.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75856; AAC75856; b2817.
    BAE76886; BAE76886; BAE76886.
    GeneIDi12932175.
    947293.
    KEGGiecj:Y75_p2751.
    eco:b2817.
    PATRICi32121052. VBIEscCol129921_2915.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29581 Genomic DNA. Translation: AAB40464.1 . Different initiation.
    U00096 Genomic DNA. Translation: AAC75856.2 .
    AP009048 Genomic DNA. Translation: BAE76886.1 .
    RefSeqi NP_417294.4. NC_000913.3.
    YP_491022.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4BIN X-ray 2.49 A 35-417 [» ]
    ProteinModelPortali P63883.
    SMRi P63883. Positions 35-408.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P63883. 2 interactions.
    STRINGi 511145.b2817.

    Proteomic databases

    PRIDEi P63883.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75856 ; AAC75856 ; b2817 .
    BAE76886 ; BAE76886 ; BAE76886 .
    GeneIDi 12932175.
    947293.
    KEGGi ecj:Y75_p2751.
    eco:b2817.
    PATRICi 32121052. VBIEscCol129921_2915.

    Organism-specific databases

    EchoBASEi EB2895.
    EcoGenei EG13086. amiC.

    Phylogenomic databases

    eggNOGi COG0860.
    HOGENOMi HOG000263827.
    KOi K01448.
    OMAi HKNKVDQ.
    OrthoDBi EOG6CP3X3.
    PhylomeDBi P63883.

    Enzyme and pathway databases

    BioCyci EcoCyc:G7458-MONOMER.
    ECOL316407:JW5449-MONOMER.
    MetaCyc:G7458-MONOMER.

    Miscellaneous databases

    PROi P63883.

    Gene expression databases

    Genevestigatori P63883.

    Family and domain databases

    Gene3Di 3.40.630.40. 2 hits.
    InterProi IPR021731. AMIN_dom.
    IPR002508. CW_Hdrlase/autolysin_cat.
    IPR006311. TAT_signal.
    [Graphical view ]
    Pfami PF01520. Amidase_3. 1 hit.
    PF11741. AMIN. 1 hit.
    [Graphical view ]
    SMARTi SM00646. Ami_3. 1 hit.
    [Graphical view ]
    PROSITEi PS51318. TAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. "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.
    3. "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.
    4. "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.
    5. "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, DOMAIN.
      Strain: K12.
    6. "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 nameiAMIC_ECOLI
    AccessioniPrimary (citable) accession number: P63883
    Secondary accession number(s): Q2MA20, Q46929
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3