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Protein Overview: EG11823

General Information:
Name(s) found: amiA / EG11823 [EcoGene]
Description(s) found:
Found 4 descriptions.
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  • N-acetylmuramoyl-l-alanine amidase I / N-acetylmuramyl-L-alanine amidase, periplasmic; role in septal cleavage during cell division; activated by EnvC [EcoGene]
    • Organism: Escherichia coli str. K-12 substr. MG1655
    Length: 289 amino acids

    Gene Ontology:
    Cellular Component: periplasmic space [IDALink to PubMed article]
    extracellular region [IEA]
    Biological Process: peptidoglycan catabolic process [IEA]
    peptidoglycan biosynthetic process [IGILink to PubMed article]
    Molecular Function: N-acetylmuramoyl-L-alanine amidase activity [IDALink to PubMed article][IEA]


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MSTFKPLKTL TSRRQVLKAG LAALTLSGMS QAIAKDELLK TSNGHSKPKA KKSGGKRVVV  60
   61 LDPGHGGIDT GAIGRNGSKE KHVVLAIAKN VRSILRNHGI DARLTRSGDT FIPLYDRVEI 120
  121 AHKHGADLFM SIHADGFTNP KAAGASVFAL SNRGASSAMA KYLSERENRA DEVAGKKATD 180
  181 KDHLLQQVLF DLVQTDTIKN SLTLGSHILK KIKPVHKLHS RNTEQAAFVV LKSPSVPSVL 240
  241 VETSFITNPE EERLLGTAAF RQKIATAIAE GVISYFHWFD NQKAHSKKR

    Protein Complex Data

    No complex found for this protein.

    Mass Spectrometry Data

    No mass spectrometry results found for this protein.

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    NOT SHOWING SINGLE HITS. [ Show Single Hits ]

    [View our yeast two-hybrid interpretation guidelines.]

    No yeast two-hybrid interactions found for this protein.

    Microscopy / Localization Data

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    No microscopy data found in the PDR for this protein.

    Protein Structure Data


    [What does the above image mean?]
    [View Top Sequence Alignments] [Show Ginzu Version Information]

    Domains predicted:

    #   Region(s) Method Confidence Match Description
    1 View Details [1..289] PSI-BLAST 42.221849 Structure of the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus

    Functions predicted (by domain):

    # Gene Ontology predictions
    1
    Term Confidence Notes
  • hydrolase activity
    		•  3.67722840912402 bayes_pls_golite062009
  • N-acetylmuramoyl-L-alanine amidase activity
    		•  3.0995594592309 bayes_pls_golite062009
  • peptidase activity
    		•  2.70319066310115 bayes_pls_golite062009
  • peptidase activity, acting on L-amino acid peptides
    		•  2.44249748878472 bayes_pls_golite062009
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
    		•  2.07011073073947 bayes_pls_golite062009
  • carboxypeptidase activity
    		•  1.95498314957158 bayes_pls_golite062009
  • catalytic activity
    		•  1.3989281287879 bayes_pls_golite062009
  • exopeptidase activity
    		•  0.606503700246216 bayes_pls_golite062009
  • binding
    		•  0.252136075715404 bayes_pls_golite062009
  • metallopeptidase activity
    		•  0.117214777864168 bayes_pls_golite062009
  • protein binding
    		•  0.0314733407355351 bayes_pls_golite062009


    Reference: Drew K, et al. (2011) The proteome folding project: Proteome-scale prediction of structure and function. Genome Res. 2011 Sep 16


    Philius Transmembrane Prediction:

    [View Details]
    Source: Reynolds et al. 2008. Manuscript submitted Philius confidence legend
    YRC Informatics Platform - Version 3.0
    Created and Maintained by: Michael Riffle