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Protein

ATP-dependent protease subunit HslV

Gene

hslV

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins.UniRule annotation7 Publications

Catalytic activityi

ATP-dependent cleavage of peptide bonds with broad specificity.UniRule annotation5 Publications

Enzyme regulationi

Allosterically activated by HslU binding.Curated

Kineticsi

Arc is a repressor protein, Arc-MYL-st11 is a hyperstable variant of Arc.

  1. KM=5.2 µM for Arc-MYL-st11 (at 37 degrees Celsius)1 Publication

    Temperature dependencei

    Optimum temperature is 55 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei2UniRule annotation1 Publication1
    Metal bindingi157Sodium; via carbonyl oxygen1
    Metal bindingi160Sodium; via carbonyl oxygen1
    Metal bindingi163Sodium; via carbonyl oxygen1

    GO - Molecular functioni

    • metal ion binding Source: UniProtKB-KW
    • threonine-type endopeptidase activity Source: EcoCyc

    GO - Biological processi

    • proteolysis involved in cellular protein catabolic process Source: EcoCyc
    • response to heat Source: EcoliWiki
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    Metal-binding, Sodium

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11676-MONOMER.
    ECOL316407:JW3903-MONOMER.
    MetaCyc:EG11676-MONOMER.
    BRENDAi3.4.25.2. 2026.

    Protein family/group databases

    MEROPSiT01.006.

    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
    Synonyms:htpO, yiiC
    Ordered Locus Names:b3932, JW3903
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11676. hslV.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • HslUV protease complex Source: UniProtKB-HAMAP
    • proteasome core complex Source: InterPro
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi2T → S: 80% reduced protease activity in the absence of HslU. Almost no effect in the presence of HslU. 1 Publication1
    Mutagenesisi2T → V: No protease activity. 1 Publication1
    Mutagenesisi3T → S or V: 80% reduced protease activity. 1 Publication1
    Mutagenesisi6S → A: No effect. 1 Publication1
    Mutagenesisi104S → A: 50% reduced protease activity. 1 Publication1
    Mutagenesisi125S → A: Almost no protease activity. 1 Publication1
    Mutagenesisi144S → A: No effect. 1 Publication1
    Mutagenesisi160C → A or S: No protease activity. Cannot form complexes with HslU. 1 Publication1
    Mutagenesisi173S → A: Almost no protease activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved
    ChainiPRO_00001481052 – 176ATP-dependent protease subunit HslVAdd BLAST175

    Proteomic databases

    EPDiP0A7B8.
    PaxDbiP0A7B8.
    PRIDEiP0A7B8.

    2D gel databases

    SWISS-2DPAGEP0A7B8.

    Expressioni

    Inductioni

    By heat shock.UniRule annotation1 Publication

    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 annotation1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-552265,EBI-552265
    hslUP0A6H56EBI-552265,EBI-369317

    Protein-protein interaction databases

    BioGridi4261781. 262 interactors.
    DIPiDIP-35866N.
    IntActiP0A7B8. 32 interactors.
    MINTiMINT-1218940.
    STRINGi511145.b3932.

    Structurei

    Secondary structure

    1176
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 8Combined sources6
    Beta strandi10 – 17Combined sources8
    Beta strandi21 – 23Combined sources3
    Beta strandi26 – 30Combined sources5
    Beta strandi35 – 38Combined sources4
    Turni39 – 42Combined sources4
    Beta strandi43 – 49Combined sources7
    Helixi51 – 66Combined sources16
    Turni67 – 70Combined sources4
    Helixi72 – 85Combined sources14
    Helixi89 – 91Combined sources3
    Beta strandi94 – 99Combined sources6
    Beta strandi104 – 108Combined sources5
    Turni109 – 111Combined sources3
    Beta strandi112 – 114Combined sources3
    Turni117 – 119Combined sources3
    Beta strandi121 – 124Combined sources4
    Helixi127 – 138Combined sources12
    Helixi145 – 159Combined sources15
    Beta strandi168 – 173Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1E94X-ray2.80A/B/C/D2-176[»]
    1G4AX-ray3.00A/B/C/D2-176[»]
    1G4BX-ray7.00M/N/O/P2-176[»]
    1HQYX-ray2.80A/B/C/D2-176[»]
    1HT1X-ray2.80A/B/C/D/V/X/Y/Z2-176[»]
    1HT2X-ray2.80A/B/C/D/I/J/K/L2-176[»]
    1NEDX-ray3.80A/B/C2-176[»]
    4G4EX-ray2.89A/B/C/D/E/F/G/H/I/J/K/L2-175[»]
    ProteinModelPortaliP0A7B8.
    SMRiP0A7B8.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7B8.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiENOG4108R5P. Bacteria.
    COG5405. LUCA.
    HOGENOMiHOG000064533.
    InParanoidiP0A7B8.
    KOiK01419.
    OMAiIMKGNAR.
    PhylomeDBiP0A7B8.

    Family and domain databases

    CDDicd01913. protease_HslV. 1 hit.
    Gene3Di3.60.20.10. 1 hit.
    HAMAPiMF_00248. HslV. 1 hit.
    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]
    PIRSFiPIRSF039093. HslV. 1 hit.
    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.

    P0A7B8-1 [UniParc]FASTAAdd to basket

    « Hide

            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
    Length:176
    Mass (Da):19,093
    Last modified:January 23, 2007 - v2
    Checksum:i3B35E01F51486965
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L19201 Genomic DNA. Translation: AAB03064.1.
    U00096 Genomic DNA. Translation: AAC76914.1.
    AP009048 Genomic DNA. Translation: BAE77378.1.
    D89965 mRNA. Translation: BAA14040.1. Sequence problems.
    L14281 Genomic DNA. No translation available.
    PIRiJT0760.
    RefSeqiNP_418367.1. NC_000913.3.
    WP_000208242.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76914; AAC76914; b3932.
    BAE77378; BAE77378; BAE77378.
    GeneIDi948429.
    KEGGiecj:JW3903.
    eco:b3932.
    PATRICi32123379. VBIEscCol129921_4050.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L19201 Genomic DNA. Translation: AAB03064.1.
    U00096 Genomic DNA. Translation: AAC76914.1.
    AP009048 Genomic DNA. Translation: BAE77378.1.
    D89965 mRNA. Translation: BAA14040.1. Sequence problems.
    L14281 Genomic DNA. No translation available.
    PIRiJT0760.
    RefSeqiNP_418367.1. NC_000913.3.
    WP_000208242.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1E94X-ray2.80A/B/C/D2-176[»]
    1G4AX-ray3.00A/B/C/D2-176[»]
    1G4BX-ray7.00M/N/O/P2-176[»]
    1HQYX-ray2.80A/B/C/D2-176[»]
    1HT1X-ray2.80A/B/C/D/V/X/Y/Z2-176[»]
    1HT2X-ray2.80A/B/C/D/I/J/K/L2-176[»]
    1NEDX-ray3.80A/B/C2-176[»]
    4G4EX-ray2.89A/B/C/D/E/F/G/H/I/J/K/L2-175[»]
    ProteinModelPortaliP0A7B8.
    SMRiP0A7B8.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261781. 262 interactors.
    DIPiDIP-35866N.
    IntActiP0A7B8. 32 interactors.
    MINTiMINT-1218940.
    STRINGi511145.b3932.

    Protein family/group databases

    MEROPSiT01.006.

    2D gel databases

    SWISS-2DPAGEP0A7B8.

    Proteomic databases

    EPDiP0A7B8.
    PaxDbiP0A7B8.
    PRIDEiP0A7B8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76914; AAC76914; b3932.
    BAE77378; BAE77378; BAE77378.
    GeneIDi948429.
    KEGGiecj:JW3903.
    eco:b3932.
    PATRICi32123379. VBIEscCol129921_4050.

    Organism-specific databases

    EchoBASEiEB1627.
    EcoGeneiEG11676. hslV.

    Phylogenomic databases

    eggNOGiENOG4108R5P. Bacteria.
    COG5405. LUCA.
    HOGENOMiHOG000064533.
    InParanoidiP0A7B8.
    KOiK01419.
    OMAiIMKGNAR.
    PhylomeDBiP0A7B8.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11676-MONOMER.
    ECOL316407:JW3903-MONOMER.
    MetaCyc:EG11676-MONOMER.
    BRENDAi3.4.25.2. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP0A7B8.
    PROiP0A7B8.

    Family and domain databases

    CDDicd01913. protease_HslV. 1 hit.
    Gene3Di3.60.20.10. 1 hit.
    HAMAPiMF_00248. HslV. 1 hit.
    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]
    PIRSFiPIRSF039093. HslV. 1 hit.
    SUPFAMiSSF56235. SSF56235. 1 hit.
    TIGRFAMsiTIGR03692. ATP_dep_HslV. 1 hit.
    PROSITEiPS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiHSLV_ECOLI
    AccessioniPrimary (citable) accession number: P0A7B8
    Secondary accession number(s): P31059, P97542, Q2M8M8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: January 23, 2007
    Last modified: November 2, 2016
    This is version 108 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    PubMed:9013898 sequence is supposed to originate from rat but, based on sequence similarity, it seems that this is a case of bacterial contamination from E.coli.Curated

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.