ATP-dependent protease subunit HslV

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Caution

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• ATP-dependent cleavage of peptide bonds with broad specificity.UniRule annotation

  Manual assertion according to rulesⁱ

  • HAMAP-Rule:MF_00248

  5 Publications

  Manual assertion based on experiment inⁱ

  • Ref.8

    "HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome."
    Rohrwild M., Coux O., Huang H.-C., Moerschell R.P., Yoo S.J., Seol J.H., Chung C.H., Goldberg A.L.
    Proc. Natl. Acad. Sci. U.S.A. 93:5808-5813(1996) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, PROTEIN SEQUENCE OF N-TERMINUS.
  • Ref.11

    "The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase."
    Seol J.H., Yoo S.J., Shin D.H., Shim Y.K., Kang M.-S., Goldberg A.L., Chung C.H.
    Eur. J. Biochem. 247:1143-1150(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
  • Ref.12

    "Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli."
    Kanemori M., Nishihara K., Yanagi H., Yura T.
    J. Bacteriol. 179:7219-7225(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  • Ref.15

    "ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli."
    Seong I.S., Oh J.Y., Yoo S.J., Seol J.H., Chung C.H.
    FEBS Lett. 456:211-214(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  • Ref.16

    "Marked instability of the sigma(32) heat shock transcription factor at high temperature. Implications for heat shock regulation."
    Kanemori M., Yanagi H., Yura T.
    J. Biol. Chem. 274:22002-22007(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION.

  EC:3.4.25.2

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationⁱ

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsⁱ

Temperature dependenceⁱ

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• ATP binding Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.20

    "The structures of HslU and the ATP-dependent protease HslU-HslV."
    Bochtler M., Hartmann C., Song H.K., Bourenkov G.P., Bartunik H.D., Huber R.
    Nature 403:800-805(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF COMPLEXES WITH HSLU AND ATP ANALOG.
• identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Subunit oligomerization and substrate recognition of the Escherichia coli ClpYQ (HslUV) protease implicated by in vivo protein-protein interactions in the yeast two-hybrid system."
    Lee Y.Y., Chang C.F., Kuo C.L., Chen M.C., Yu C.H., Lin P.I., Wu W.F.
    J. Bacteriol. 185:2393-2401(2003) [PubMed] [Europe PMC] [Abstract]
  • "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis."
    Lasserre J.P., Beyne E., Pyndiah S., Lapaillerie D., Claverol S., Bonneu M.
    Electrophoresis 27:3306-3321(2006) [PubMed] [Europe PMC] [Abstract]
  • "A second-generation protein-protein interaction network of Helicobacter pylori."
    Hauser R., Ceol A., Rajagopala S.V., Mosca R., Siszler G., Wermke N., Sikorski P., Schwarz F., Schick M., Wuchty S., Aloy P., Uetz P.
    Mol. Cell Proteomics 13:1318-1329(2014) [PubMed] [Europe PMC] [Abstract]
  • "The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome."
    Rohrwild M., Pfeifer G., Santarius U., Muller S.A., Huang H.C., Engel A., Baumeister W., Goldberg A.L.
    Nat. Struct. Biol. 4:133-139(1997) [PubMed] [Europe PMC] [Abstract]
• magnesium ion binding Source: CAFAInferred from direct assayⁱ
  • Ref.20

    "The structures of HslU and the ATP-dependent protease HslU-HslV."
    Bochtler M., Hartmann C., Song H.K., Bourenkov G.P., Bartunik H.D., Huber R.
    Nature 403:800-805(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF COMPLEXES WITH HSLU AND ATP ANALOG.
• protein domain specific binding Source: CAFAInferred from physical interactionⁱ
  • Ref.20

    "The structures of HslU and the ATP-dependent protease HslU-HslV."
    Bochtler M., Hartmann C., Song H.K., Bourenkov G.P., Bartunik H.D., Huber R.
    Nature 403:800-805(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF COMPLEXES WITH HSLU AND ATP ANALOG.
• threonine-type endopeptidase activity Source: EcoCyc <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.13

    "Mutagenesis of two N-terminal Thr and five Ser residues in HslV, the proteolytic component of the ATP-dependent HslVU protease."
    Yoo S.J., Shim Y.K., Seong I.S., Seol J.H., Kang M.-S., Chung C.H.
    FEBS Lett. 412:57-60(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: MUTAGENESIS OF THR-2; THR-3; SER-6; SER-104; SER-125; SER-144 AND SER-173, ACTIVE SITE.

GO - Biological processⁱ

• protein hexamerization Source: CAFAInferred from direct assayⁱ
  • Ref.20

    "The structures of HslU and the ATP-dependent protease HslU-HslV."
    Bochtler M., Hartmann C., Song H.K., Bourenkov G.P., Bartunik H.D., Huber R.
    Nature 403:800-805(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF COMPLEXES WITH HSLU AND ATP ANALOG.
• proteolysis Source: CAFAInferred from direct assayⁱ
  • Ref.20

    "The structures of HslU and the ATP-dependent protease HslU-HslV."
    Bochtler M., Hartmann C., Song H.K., Bourenkov G.P., Bartunik H.D., Huber R.
    Nature 403:800-805(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF COMPLEXES WITH HSLU AND ATP ANALOG.
• proteolysis involved in cellular protein catabolic process Source: EcoCycInferred from mutant phenotypeⁱ
  • "Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli."
    Missiakas D., Schwager F., Betton J.M., Georgopoulos C., Raina S.
    EMBO J. 15:6899-6909(1996) [PubMed] [Europe PMC] [Abstract]
• response to heat Source: EcoliWiki <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • "Characterization of twenty-six new heat shock genes of Escherichia coli."
    Chuang S.E., Blattner F.R.
    J. Bacteriol. 175:5242-5252(1993) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

GO - Cellular componentⁱ

• cytosol Source: EcoCycInferred from direct assayⁱ
  • "Protein abundance profiling of the Escherichia coli cytosol."
    Ishihama Y., Schmidt T., Rappsilber J., Mann M., Hartl F.U., Kerner M.J., Frishman D.
    BMC Genomics 9:102-102(2008) [PubMed] [Europe PMC] [Abstract]
• HslUV protease complex Source: CAFAInferred from direct assayⁱ
  • Ref.20

    "The structures of HslU and the ATP-dependent protease HslU-HslV."
    Bochtler M., Hartmann C., Song H.K., Bourenkov G.P., Bartunik H.D., Huber R.
    Nature 403:800-805(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF COMPLEXES WITH HSLU AND ATP ANALOG.
• proteasome core complex Source: InterPro

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Proteomic databases

2D gel databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductionⁱ

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "Subunit oligomerization and substrate recognition of the Escherichia coli ClpYQ (HslUV) protease implicated by in vivo protein-protein interactions in the yeast two-hybrid system."
    Lee Y.Y., Chang C.F., Kuo C.L., Chen M.C., Yu C.H., Lin P.I., Wu W.F.
    J. Bacteriol. 185:2393-2401(2003) [PubMed] [Europe PMC] [Abstract]
  • "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis."
    Lasserre J.P., Beyne E., Pyndiah S., Lapaillerie D., Claverol S., Bonneu M.
    Electrophoresis 27:3306-3321(2006) [PubMed] [Europe PMC] [Abstract]
  • "A second-generation protein-protein interaction network of Helicobacter pylori."
    Hauser R., Ceol A., Rajagopala S.V., Mosca R., Siszler G., Wermke N., Sikorski P., Schwarz F., Schick M., Wuchty S., Aloy P., Uetz P.
    Mol. Cell Proteomics 13:1318-1329(2014) [PubMed] [Europe PMC] [Abstract]
  • "The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome."
    Rohrwild M., Pfeifer G., Santarius U., Muller S.A., Huang H.C., Engel A., Baumeister W., Goldberg A.L.
    Nat. Struct. Biol. 4:133-139(1997) [PubMed] [Europe PMC] [Abstract]
• protein domain specific binding Source: CAFAInferred from physical interactionⁱ
  • Ref.20

    "The structures of HslU and the ATP-dependent protease HslU-HslV."
    Bochtler M., Hartmann C., Song H.K., Bourenkov G.P., Bartunik H.D., Huber R.
    Nature 403:800-805(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF COMPLEXES WITH HSLU AND ATP ANALOG.

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

        10         20         30         40         50
MTTIVSVRRN GHVVIAGDGQ ATLGNTVMKG NVKKVRRLYN DKVIAGFAGG 
        60         70         80         90        100
TADAFTLFEL FERKLEMHQG HLVKAAVELA KDWRTDRMLR KLEALLAVAD 
       110        120        130        140        150
ETASLIITGN GDVVQPENDL IAIGSGGPYA QAAARALLEN TELSAREIAE 
       160        170 
KALDIAGDIC IYTNHFHTIE ELSYKA                           

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families
3. Peptidase families
   Classification of peptidase families and list of entries