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Protein Overview: gi|93278469, gi|...

General Information:
Name(s) found: gi|93278469 [NCBI NR]
gi|93278468 [NCBI NR]
gi|93278467 [NCBI NR]
gi|93278466 [NCBI NR]
gi|93278465 [NCBI NR]
gi|93278464 [NCBI NR]
gi|93278463 [NCBI NR]
gi|93278462 [NCBI NR]
gi|93278461 [NCBI NR]
gi|93278460 [NCBI NR]
gi|93278459 [NCBI NR]
gi|93278458 [NCBI NR]
gi|93278457 [NCBI NR]
gi|93278456 [NCBI NR]
gi|3318866 [NCBI NR]
gi|3318865 [NCBI NR]
gi|3318864 [NCBI NR]
gi|3318863 [NCBI NR]
gi|3318862 [NCBI NR]
gi|3318861 [NCBI NR]
gi|3318860 [NCBI NR]
gi|3318859 [NCBI NR]
gi|3318858 [NCBI NR]
gi|3318857 [NCBI NR]
gi|3318856 [NCBI NR]
gi|3318855 [NCBI NR]
gi|3318854 [NCBI NR]
gi|3318853 [NCBI NR]
gi|109157743 [NCBI NR]
gi|109157742 [NCBI NR]
gi|109157741 [NCBI NR]
gi|109157740 [NCBI NR]
gi|109157739 [NCBI NR]
gi|109157738 [NCBI NR]
gi|109157737 [NCBI NR]
gi|109157736 [NCBI NR]
gi|109157735 [NCBI NR]
gi|109157734 [NCBI NR]
gi|109157733 [NCBI NR]
gi|109157732 [NCBI NR]
gi|109157731 [NCBI NR]
gi|109157730 [NCBI NR]
Description(s) found:
Found 85 descriptions.
SHOW ALL
  • gi|93278469|pdb|1YG6|N Chain N, Clpp [NCBI NR]
  • gi|93278468|pdb|1YG6|M Chain M, Clpp [NCBI NR]
  • gi|93278467|pdb|1YG6|L Chain L, Clpp [NCBI NR]
  • gi|93278466|pdb|1YG6|K Chain K, Clpp [NCBI NR]
  • gi|93278465|pdb|1YG6|J Chain J, Clpp [NCBI NR]
  • gi|93278464|pdb|1YG6|I Chain I, Clpp [NCBI NR]
  • gi|93278463|pdb|1YG6|H Chain H, Clpp [NCBI NR]
  • gi|93278462|pdb|1YG6|G Chain G, Clpp [NCBI NR]
  • gi|93278461|pdb|1YG6|F Chain F, Clpp [NCBI NR]
  • gi|93278460|pdb|1YG6|E Chain E, Clpp [NCBI NR]
  • gi|93278459|pdb|1YG6|D Chain D, Clpp [NCBI NR]
  • gi|93278458|pdb|1YG6|C Chain C, Clpp [NCBI NR]
  • gi|93278457|pdb|1YG6|B Chain B, Clpp [NCBI NR]
  • gi|93278456|pdb|1YG6|A Chain A, Clpp [NCBI NR]
  • gi|3318866|pdb|1TYF|N Chain N, The Structure Of Clpp At 2.3 Angstrom Resolution Suggests A Model For Atp-Dependent Proteolysis [NCBI NR]
  • gi|3318865|pdb|1TYF|M Chain M, The Structure Of Clpp At 2.3 Angstrom Resolution Suggests A Model For Atp-Dependent Proteolysis [NCBI NR]
  • gi|3318864|pdb|1TYF|L Chain L, The Structure Of Clpp At 2.3 Angstrom Resolution Suggests A Model For Atp-Dependent Proteolysis [NCBI NR]
  • gi|3318863|pdb|1TYF|K Chain K, The Structure Of Clpp At 2.3 Angstrom Resolution Suggests A Model For Atp-Dependent Proteolysis [NCBI NR]
  • gi|3318862|pdb|1TYF|J Chain J, The Structure Of Clpp At 2.3 Angstrom Resolution Suggests A Model For Atp-Dependent Proteolysis [NCBI NR]
  • gi|3318861|pdb|1TYF|I Chain I, The Structure Of Clpp At 2.3 Angstrom Resolution Suggests A Model For Atp-Dependent Proteolysis [NCBI NR]
  • gi|3318860|pdb|1TYF|H Chain H, The Structure Of Clpp At 2.3 Angstrom Resolution Suggests A Model For Atp-Dependent Proteolysis [NCBI NR]
  • gi|3318859|pdb|1TYF|G Chain G, The Structure Of Clpp At 2.3 Angstrom Resolution Suggests A Model For Atp-Dependent Proteolysis [NCBI NR]
  • gi|3318858|pdb|1TYF|F Chain F, The Structure Of Clpp At 2.3 Angstrom Resolution Suggests A Model For Atp-Dependent Proteolysis [NCBI NR]
  • gi|3318857|pdb|1TYF|E Chain E, The Structure Of Clpp At 2.3 Angstrom Resolution Suggests A Model For Atp-Dependent Proteolysis [NCBI NR]
  • gi|3318856|pdb|1TYF|D Chain D, The Structure Of Clpp At 2.3 Angstrom Resolution Suggests A Model For Atp-Dependent Proteolysis [NCBI NR]
  • gi|3318855|pdb|1TYF|C Chain C, The Structure Of Clpp At 2.3 Angstrom Resolution Suggests A Model For Atp-Dependent Proteolysis [NCBI NR]
  • gi|3318854|pdb|1TYF|B Chain B, The Structure Of Clpp At 2.3 Angstrom Resolution Suggests A Model For Atp-Dependent Proteolysis [NCBI NR]
  • gi|3318853|pdb|1TYF|A Chain A, The Structure Of Clpp At 2.3 Angstrom Resolution Suggests A Model For Atp-Dependent Proteolysis [NCBI NR]
  • gi|109157743|pdb|2FZS|N Chain N, Crystal Structure Of E. Coli Clpp With A Peptide Chloromethyl Ketone Covalently Bound At The Active Site [NCBI NR]
  • gi|109157742|pdb|2FZS|M Chain M, Crystal Structure Of E. Coli Clpp With A Peptide Chloromethyl Ketone Covalently Bound At The Active Site [NCBI NR]
  • gi|109157741|pdb|2FZS|L Chain L, Crystal Structure Of E. Coli Clpp With A Peptide Chloromethyl Ketone Covalently Bound At The Active Site [NCBI NR]
  • gi|109157740|pdb|2FZS|K Chain K, Crystal Structure Of E. Coli Clpp With A Peptide Chloromethyl Ketone Covalently Bound At The Active Site [NCBI NR]
  • gi|109157739|pdb|2FZS|J Chain J, Crystal Structure Of E. Coli Clpp With A Peptide Chloromethyl Ketone Covalently Bound At The Active Site [NCBI NR]
  • gi|109157738|pdb|2FZS|I Chain I, Crystal Structure Of E. Coli Clpp With A Peptide Chloromethyl Ketone Covalently Bound At The Active Site [NCBI NR]
  • gi|109157737|pdb|2FZS|H Chain H, Crystal Structure Of E. Coli Clpp With A Peptide Chloromethyl Ketone Covalently Bound At The Active Site [NCBI NR]
  • gi|109157736|pdb|2FZS|G Chain G, Crystal Structure Of E. Coli Clpp With A Peptide Chloromethyl Ketone Covalently Bound At The Active Site [NCBI NR]
  • gi|109157735|pdb|2FZS|F Chain F, Crystal Structure Of E. Coli Clpp With A Peptide Chloromethyl Ketone Covalently Bound At The Active Site [NCBI NR]
  • gi|109157734|pdb|2FZS|E Chain E, Crystal Structure Of E. Coli Clpp With A Peptide Chloromethyl Ketone Covalently Bound At The Active Site [NCBI NR]
  • gi|109157733|pdb|2FZS|D Chain D, Crystal Structure Of E. Coli Clpp With A Peptide Chloromethyl Ketone Covalently Bound At The Active Site [NCBI NR]
  • gi|109157732|pdb|2FZS|C Chain C, Crystal Structure Of E. Coli Clpp With A Peptide Chloromethyl Ketone Covalently Bound At The Active Site [NCBI NR]
  • gi|109157731|pdb|2FZS|B Chain B, Crystal Structure Of E. Coli Clpp With A Peptide Chloromethyl Ketone Covalently Bound At The Active Site [NCBI NR]
  • gi|109157730|pdb|2FZS|A Chain A, Crystal Structure Of E. Coli Clpp With A Peptide Chloromethyl Ketone Covalently Bound At The Active Site [NCBI NR]
    • Organism: Escherichia coli
    Length: 193 amino acids

    Gene Ontology:
    Cellular Component: NONE FOUND
    Biological Process: NONE FOUND
    Molecular Function: NONE FOUND


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 ALVPMVIEQT SRGERSFDIY SRLLKERVIF LTGQVEDHMA NLIVAQMLFL EAENPEKDIY  60
   61 LYINSPGGVI TAGMSIYDTM QFIKPDVSTI CMGQAASMGA FLLTAGAKGK RFCLPNSRVM 120
  121 IHQPLGGYQG QATDIEIHAR EILKVKGRMN ELMALHTGQS LEQIERDTER DRFLSAPEAV 180
  181 EYGLVDSILT HRN

    Protein Complex Data

      PUBLICATION TOPOLOGY COCOMPLEXED PROTEINS
    View Details Noble WS, et al. (2009) Manuscript in preparation. gi|134105085, gi... gi|189095939, gi... gi|60594470, gi|... gi|93278469, gi|...

    Mass Spectrometry Data

    No mass spectrometry results found for this protein.

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    SHOWING SINGLE HITS. [ Hide 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..193] PSI-BLAST 74.522879 Clp protease, ClpP subunit

    Functions predicted (by domain):

    # Gene Ontology predictions
    1
    Term Confidence Notes
  • catalytic activity
    		•  1.46154163027498 bayes_pls_golite062009
  • CoA carboxylase activity
    		•  0.939626895227199 bayes_pls_golite062009
  • acetyl-CoA carboxylase activity
    		•  0.764444938444292 bayes_pls_golite062009
  • ligase activity, forming carbon-carbon bonds
    		•  0.621229080200493 bayes_pls_golite062009
  • enoyl-CoA hydratase activity
    		•  0.620657548610719 bayes_pls_golite062009
  • hydrolase activity
    		•  0.534319520590169 bayes_pls_golite062009
  • binding
    		•  0.367666848528835 bayes_pls_golite062009
  • ligase activity
    		•  0.32092496884003 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:

    Protein predicted to be: GLOBULAR (No transmembrane regions or signal peptide)
    Confidence of classification: 0.72

    Source: Reynolds et al. (2008)

    YRC Informatics Platform - Version 3.0
    Created and Maintained by: Michael Riffle