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Protein Overview: HSLU_ECOLI

General Information:
Name(s) found: HSLU_ECOLI [Swiss-Prot]
Description(s) found:
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  • gi|73535733|pdb|1YYF|B Chain B, Correction Of X-Ray Intensities From An Hslv-Hslu Co- Crystal Containing Lattice Translocation Defects [NCBI NR]
  • gi|73535732|pdb|1YYF|A Chain A, Correction Of X-Ray Intensities From An Hslv-Hslu Co- Crystal Containing Lattice Translocation Defects [NCBI NR]
  • gi|62288339|sp|P0A6H5.1|HSLU_ECOLI RecName: Full=ATP-dependent hsl protease ATP-binding subunit hslU; AltName: Full=Heat shock protein hslU [NCBI NR]
  • pir||JT0761 heat shock protein hslU - Escherichia coli (strain K-12) [NCBI NR]
  • gi|305034|gb|AAB03063.1| matches PS00017: ATP_GTP_A; similar to Pasteurella haemolytica hypoth. protein ORF1; heat shock induced [Escherichia coli] [NCBI NR]
  • pir||B86083 heat shock protein HslU [imported] - Escherichia coli (strain O157:H7, substrain EDL933) [NCBI NR]
  • pir||B91236 heat shock protein HslU [imported] - Escherichia coli (strain O157:H7, substrain RIMD 0509952) [NCBI NR]
  • gi|209752256|gb|ACI74435.1| heat shock protein HslV [Escherichia coli] [NCBI NR]
  • gi|209752254|gb|ACI74434.1| heat shock protein HslV [Escherichia coli] [NCBI NR]
  • gi|209752252|gb|ACI74433.1| heat shock protein HslV [Escherichia coli] [NCBI NR]
  • gi|209752250|gb|ACI74432.1| heat shock protein HslV [Escherichia coli] [NCBI NR]
  • gi|209752248|gb|ACI74431.1| heat shock protein HslV [Escherichia coli] [NCBI NR]
  • gi|13399760|pdb|1G4B|L Chain L, Crystal Structures Of The Hslvu Peptidase-Atpase Complex Reveal An Atp-Dependent Proteolysis Mechanism [NCBI NR]
  • gi|13399759|pdb|1G4B|K Chain K, Crystal Structures Of The Hslvu Peptidase-Atpase Complex Reveal An Atp-Dependent Proteolysis Mechanism [NCBI NR]
  • gi|13399758|pdb|1G4B|F Chain F, Crystal Structures Of The Hslvu Peptidase-Atpase Complex Reveal An Atp-Dependent Proteolysis Mechanism [NCBI NR]
  • gi|13399757|pdb|1G4B|E Chain E, Crystal Structures Of The Hslvu Peptidase-Atpase Complex Reveal An Atp-Dependent Proteolysis Mechanism [NCBI NR]
  • gi|13399752|pdb|1G4A|F Chain F, Crystal Structures Of The Hslvu Peptidase-Atpase Complex Reveal An Atp-Dependent Proteolysis Mechanism [NCBI NR]
  • gi|13399751|pdb|1G4A|E Chain E, Crystal Structures Of The Hslvu Peptidase-Atpase Complex Reveal An Atp-Dependent Proteolysis Mechanism [NCBI NR]
  • ATP-dependent hsl protease ATP-binding subunit hslU (Heat shock protein hslU) - Escherichia coli [Swiss-Prot]
  • ATPase component of the HslUV protease, also functions as molecular chaperone; heat shock protein hslVU, ATPase subunit, homologous to chaperones [Escherichia coli K12]gi|15834112|ref|NP_312885.1| HslU [Escherichia coli O157:H7]gi|30064776|ref|NP_838947 [nrdb_11152004_Chlamydomonas]
  • ATP-dependent hsl protease ATP-binding subunit hslU (Heat shock protein hslU) [NCBI-RefSeq_human_na_08-09-2006_reversed.fasta]
  • matches PS00017: ATP_GTP_A; similar to Pasteurella haemolytica hypoth. protein ORF1; heat shock induced [Escherichia coli] [NCBI-RefSeq_human_na_08-09-2006_reversed.fasta]
  • Chain F, Crystal Structures Of The Hslvu Peptidase-Atpase Complex Reveal An Atp-Dependent Proteolysis Mechanism [nr-271106-contam.fasta]
  • Chain L, Crystal Structures Of The Hslvu Peptidase-Atpase Complex Reveal An Atp-Dependent Proteolysis Mechanism [nr-271106-contam.fasta]
  • Chain E, Crystal Structures Of The Hslvu Peptidase-Atpase Complex Reveal An Atp-Dependent Proteolysis Mechanism [nr-271106-contam.fasta]
  • Chain A, Correction Of X-Ray Intensities From An Hslv-Hslu Co- Crystal Containing Lattice Translocation Defects [nr-271106-contam.fasta]
  • Chain K, Crystal Structures Of The Hslvu Peptidase-Atpase Complex Reveal An Atp-Dependent Proteolysis Mechanism [nr-271106-contam.fasta]
  • Chain B, Correction Of X-Ray Intensities From An Hslv-Hslu Co- Crystal Containing Lattice Translocation Defects [nr-271106-contam.fasta]
  • ATP-dependent protease ATPase subunit HslU OS=Escherichia coli (strain K12) GN=hslU PE=1 SV=1 [uniprot-Ecoli-reviewed-110511.fasta]
    • Organism: Escherichia coli
    Length: 443 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 MSEMTPREIV SELDKHIIGQ DNAKRSVAIA LRNRWRRMQL NEELRHEVTP KNILMIGPTG  60
   61 VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII RDLTDAAVKM VRVQAIEKNR 120
  121 YRAEELAEER ILDVLIPPAK NNWGQTEQQQ EPSAARQAFR KKLREGQLDD KEIEIDLAAA 180
  181 PMGVEIMAPP GMEEMTSQLQ SMFQNLGGQK QKARKLKIKD AMKLLIEEEA AKLVNPEELK 240
  241 QDAIDAVEQH GIVFIDEIDK ICKRGESSGP DVSREGVQRD LLPLVEGCTV STKHGMVKTD 300
  301 HILFIASGAF QIAKPSDLIP ELQGRLPIRV ELQALTTSDF ERILTEPNAS ITVQYKALMA 360
  361 TEGVNIEFTD SGIKRIAEAA WQVNESTENI GARRLHTVLE RLMEEISYDA SDLSGQNITI 420
  421 DADYVSKHLD ALVADEDLSR FIL

    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:

    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..443] PSI-BLAST 102.0 HslU

    Functions predicted (by domain):

    # Gene Ontology predictions
    1
    Term Confidence Notes
  • hydrolase activity
    		•  2.55157966585974 bayes_pls_golite062009
  • binding
    		•  1.31163400557981 bayes_pls_golite062009
  • catalytic activity
    		•  1.00104173493322 bayes_pls_golite062009
  • hydrolase activity, acting on acid anhydrides
    		•  0.546796591575762 bayes_pls_golite062009
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
    		•  0.543610140926125 bayes_pls_golite062009
  • pyrophosphatase activity
    		•  0.540750418412449 bayes_pls_golite062009
  • nucleoside-triphosphatase activity
    		•  0.517457589081898 bayes_pls_golite062009
  • purine nucleotide binding
    		•  0.428373955572763 bayes_pls_golite062009
  • purine ribonucleotide binding
    		•  0.424644011903671 bayes_pls_golite062009
  • ribonucleotide binding
    		•  0.424583288440993 bayes_pls_golite062009
  • nucleotide binding
    		•  0.422354428195324 bayes_pls_golite062009
  • ATP binding
    		•  0.04834397972685 bayes_pls_golite062009
  • adenyl ribonucleotide binding
    		•  0.0149501427627318 bayes_pls_golite062009
  • adenyl nucleotide binding
    		•  0.00365326483311895 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: 0.99

    Source: Reynolds et al. (2008)

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