Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0A7C0

- HSLV_ECO57

UniProt

P0A7C0 - HSLV_ECO57

Protein

ATP-dependent protease subunit HslV

Gene

hslV

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.UniRule annotation

    Catalytic activityi

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

    Enzyme regulationi

    Allosterically activated by HslU binding.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei2 – 21UniRule annotation
    Metal bindingi157 – 1571Sodium; via carbonyl oxygenUniRule annotation
    Metal bindingi160 – 1601Sodium; via carbonyl oxygenUniRule annotation
    Metal bindingi163 – 1631Sodium; via carbonyl oxygenUniRule annotation

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. threonine-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. proteolysis involved in cellular protein catabolic process Source: InterPro
    2. response to stress Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    Metal-binding, Sodium

    Enzyme and pathway databases

    BioCyciECOL386585:GJFA-4849-MONOMER.
    ECOO157:HSLV-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent protease subunit HslVUniRule annotation (EC:3.4.25.2UniRule annotation)
    Alternative name(s):
    Heat shock protein HslVUniRule annotation
    Gene namesi
    Name:hslVUniRule annotation
    Ordered Locus Names:Z5479, ECs4859
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. HslUV protease complex Source: UniProtKB-HAMAP
    2. proteasome core complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 176175ATP-dependent protease subunit HslVPRO_0000148106Add
    BLAST

    Expressioni

    Inductioni

    By heat shock.UniRule annotation

    Interactioni

    Subunit structurei

    A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP.UniRule annotation

    Protein-protein interaction databases

    MINTiMINT-1218920.
    STRINGi155864.Z5479.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A7C0.
    SMRiP0A7C0. Positions 2-175.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family. HslV subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG5405.
    HOGENOMiHOG000064533.
    KOiK01419.
    OMAiRLYHGKV.
    OrthoDBiEOG6ND0PJ.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    HAMAPiMF_00248. HslV.
    InterProiIPR022281. ATP-dep_Prtase_HsIV_su.
    IPR029055. Ntn_hydrolases_N.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.
    TIGRFAMsiTIGR03692. ATP_dep_HslV. 1 hit.
    PROSITEiPS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A7C0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTIVSVRRN GHVVIAGDGQ ATLGNTVMKG NVKKVRRLYN DKVIAGFAGG    50
    TADAFTLFEL FERKLEMHQG HLVKAAVELA KDWRTDRMLR KLEALLAVAD 100
    ETASLIITGN GDVVQPENDL IAIGSGGPYA QAAARALLEN TELSAREIAE 150
    KALDIAGDIC IYTNHFHTIE ELSYKA 176
    Length:176
    Mass (Da):19,093
    Last modified:January 23, 2007 - v2
    Checksum:i3B35E01F51486965
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG59127.1.
    BA000007 Genomic DNA. Translation: BAB38282.1.
    PIRiC86083.
    C91236.
    RefSeqiNP_290563.1. NC_002655.2.
    NP_312886.1. NC_002695.1.

    Genome annotation databases

    EnsemblBacteriaiAAG59127; AAG59127; Z5479.
    BAB38282; BAB38282; BAB38282.
    GeneIDi915032.
    960205.
    KEGGiece:Z5479.
    ecs:ECs4859.
    PATRICi18359379. VBIEscCol44059_4839.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG59127.1 .
    BA000007 Genomic DNA. Translation: BAB38282.1 .
    PIRi C86083.
    C91236.
    RefSeqi NP_290563.1. NC_002655.2.
    NP_312886.1. NC_002695.1.

    3D structure databases

    ProteinModelPortali P0A7C0.
    SMRi P0A7C0. Positions 2-175.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1218920.
    STRINGi 155864.Z5479.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG59127 ; AAG59127 ; Z5479 .
    BAB38282 ; BAB38282 ; BAB38282 .
    GeneIDi 915032.
    960205.
    KEGGi ece:Z5479.
    ecs:ECs4859.
    PATRICi 18359379. VBIEscCol44059_4839.

    Phylogenomic databases

    eggNOGi COG5405.
    HOGENOMi HOG000064533.
    KOi K01419.
    OMAi RLYHGKV.
    OrthoDBi EOG6ND0PJ.

    Enzyme and pathway databases

    BioCyci ECOL386585:GJFA-4849-MONOMER.
    ECOO157:HSLV-MONOMER.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    HAMAPi MF_00248. HslV.
    InterProi IPR022281. ATP-dep_Prtase_HsIV_su.
    IPR029055. Ntn_hydrolases_N.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    TIGRFAMsi TIGR03692. ATP_dep_HslV. 1 hit.
    PROSITEi PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

    Entry informationi

    Entry nameiHSLV_ECO57
    AccessioniPrimary (citable) accession number: P0A7C0
    Secondary accession number(s): P31059, P97542
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 64 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3