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P0A6H1

- CLPX_ECOLI

UniProt

P0A6H1 - CLPX_ECOLI

Protein

ATP-dependent Clp protease ATP-binding subunit ClpX

Gene

clpX

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    ATP-dependent specificity component of the Clp protease. Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized and readily hydrolyzed by ClpP. Can perform chaperone functions in the absence of ClpP.2 Publications

    Cofactori

    Binds 1 Zn2+ per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi15 – 151Zinc1 Publication
    Metal bindingi18 – 181Zinc1 Publication
    Metal bindingi37 – 371Zinc1 Publication
    Metal bindingi40 – 401Zinc1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri15 – 4026C4-typeUniRule annotationAdd
    BLAST
    Nucleotide bindingi120 – 1278ATP2 PublicationsUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: EcoCyc
    2. ATP-dependent peptidase activity Source: CACAO
    3. identical protein binding Source: IntAct
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cell division Source: CACAO
    3. protein folding Source: UniProtKB-HAMAP
    4. proteolysis Source: GOC
    5. response to stress Source: UniProtKB-KW
    6. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Host-virus interaction, Stress response

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10159-MONOMER.
    ECOL316407:JW0428-MONOMER.
    MetaCyc:EG10159-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent Clp protease ATP-binding subunit ClpXUniRule annotation
    Alternative name(s):
    ATP-dependent unfoldase ClpX
    Gene namesi
    Name:clpXUniRule annotation
    Synonyms:lopC
    Ordered Locus Names:b0438, JW0428
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10159. clpX.

    Pathology & Biotechi

    Disruption phenotypei

    Delayed and decreased induction of the extracytoplasmic-stress response.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi185 – 1851E → Q: No ATP hydrolyis. 1 Publication
    Mutagenesisi370 – 3701R → K: No ATP hydrolyis. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 424423ATP-dependent Clp protease ATP-binding subunit ClpXPRO_0000160352Add
    BLAST

    Proteomic databases

    PaxDbiP0A6H1.
    PRIDEiP0A6H1.

    Expressioni

    Inductioni

    By heat shock. Part of the clpP-clpX operon, clpX can be expressed individually from its own promoter.1 Publication

    Gene expression databases

    GenevestigatoriP0A6H1.

    Interactioni

    Subunit structurei

    Component of the ClpX-ClpP complex. Forms a hexameric ring that, in the presence of ATP, binds to fourteen ClpP subunits assembled into a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes. Interacts with Mu phage DDE-recombinase A; this interaction remodels the viral transpososome for replication.5 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself6EBI-547386,EBI-547386

    Protein-protein interaction databases

    DIPiDIP-35907N.
    IntActiP0A6H1. 32 interactions.
    STRINGi511145.b0438.

    Structurei

    Secondary structure

    1
    424
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni16 – 183
    Turni22 – 243
    Beta strandi28 – 303
    Beta strandi35 – 373
    Helixi38 – 4912
    Helixi67 – 7711
    Helixi82 – 10019
    Beta strandi105 – 1073
    Beta strandi115 – 1184
    Helixi125 – 13511
    Beta strandi140 – 1445
    Helixi145 – 1484
    Helixi152 – 1587
    Helixi160 – 1689
    Turni169 – 1713
    Helixi173 – 1786
    Beta strandi180 – 1845
    Helixi186 – 1894
    Helixi201 – 21616
    Beta strandi242 – 2498
    Helixi254 – 2629
    Helixi283 – 2886
    Helixi292 – 2987
    Helixi302 – 3054
    Beta strandi310 – 3134
    Helixi319 – 3279
    Helixi333 – 34210
    Turni343 – 3453
    Beta strandi347 – 3504
    Helixi352 – 36413
    Turni368 – 3714
    Helixi372 – 38514
    Turni387 – 3893
    Beta strandi393 – 3975
    Helixi399 – 4024
    Beta strandi410 – 4123

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OVXNMR-A/B2-61[»]
    2DS5X-ray1.50A/B2-52[»]
    2DS6X-ray2.00A/B2-52[»]
    2DS7X-ray2.50A2-52[»]
    2DS8X-ray1.60A/B2-52[»]
    3HTEX-ray4.03A/B/C/D/E/F62-424[»]
    3HWSX-ray3.25A/B/C/D/E/F62-424[»]
    4I34X-ray4.12A/B/C/D/E/F62-424[»]
    4I4LX-ray3.70A/B/C/D/E/F62-424[»]
    4I5OX-ray4.48A/B/C/D/E/F62-424[»]
    4I63X-ray5.71A/B/C/D/E/F62-424[»]
    4I81X-ray3.82A/B/C/D/E/F62-424[»]
    4I9KX-ray5.00A/B62-424[»]
    ProteinModelPortaliP0A6H1.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6H1.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ClpX chaperone family.UniRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri15 – 4026C4-typeUniRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG1219.
    HOGENOMiHOG000010093.
    KOiK03544.
    OMAiILLDIMY.
    OrthoDBiEOG625JZK.
    PhylomeDBiP0A6H1.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    HAMAPiMF_00175. ClpX.
    InterProiIPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR019489. Clp_ATPase_C.
    IPR004487. Clp_protease_ATP-bd_su_ClpX.
    IPR027417. P-loop_NTPase.
    IPR010603. Znf_CppX_C4.
    [Graphical view]
    PfamiPF07724. AAA_2. 1 hit.
    PF10431. ClpB_D2-small. 1 hit.
    PF06689. zf-C4_ClpX. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    SM01086. ClpB_D2-small. 1 hit.
    SM00994. zf-C4_ClpX. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00382. clpX. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P0A6H1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDKRKDGSG KLLYCSFCGK SQHEVRKLIA GPSVYICDEC VDLCNDIIRE    50
    EIKEVAPHRE RSALPTPHEI RNHLDDYVIG QEQAKKVLAV AVYNHYKRLR 100
    NGDTSNGVEL GKSNILLIGP TGSGKTLLAE TLARLLDVPF TMADATTLTE 150
    AGYVGEDVEN IIQKLLQKCD YDVQKAQRGI VYIDEIDKIS RKSDNPSITR 200
    DVSGEGVQQA LLKLIEGTVA AVPPQGGRKH PQQEFLQVDT SKILFICGGA 250
    FAGLDKVISH RVETGSGIGF GATVKAKSDK ASEGELLAQV EPEDLIKFGL 300
    IPEFIGRLPV VATLNELSEE ALIQILKEPK NALTKQYQAL FNLEGVDLEF 350
    RDEALDAIAK KAMARKTGAR GLRSIVEAAL LDTMYDLPSM EDVEKVVIDE 400
    SVIDGQSKPL LIYGKPEAQQ ASGE 424
    Length:424
    Mass (Da):46,356
    Last modified:January 23, 2007 - v2
    Checksum:i9DEF1B0786E42B6F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti268 – 2747IGFGATV → HWCWRSG in CAA80816. (PubMed:8093059)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18867 Unassigned DNA. Translation: AAA16116.1.
    Z23278 Genomic DNA. Translation: CAA80816.1.
    U82664 Genomic DNA. Translation: AAB40194.1.
    U00096 Genomic DNA. Translation: AAC73541.1.
    AP009048 Genomic DNA. Translation: BAE76218.1.
    PIRiA48709.
    RefSeqiNP_414972.1. NC_000913.3.
    YP_488730.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73541; AAC73541; b0438.
    BAE76218; BAE76218; BAE76218.
    GeneIDi12931741.
    945083.
    KEGGiecj:Y75_p0426.
    eco:b0438.
    PATRICi32116029. VBIEscCol129921_0456.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18867 Unassigned DNA. Translation: AAA16116.1 .
    Z23278 Genomic DNA. Translation: CAA80816.1 .
    U82664 Genomic DNA. Translation: AAB40194.1 .
    U00096 Genomic DNA. Translation: AAC73541.1 .
    AP009048 Genomic DNA. Translation: BAE76218.1 .
    PIRi A48709.
    RefSeqi NP_414972.1. NC_000913.3.
    YP_488730.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OVX NMR - A/B 2-61 [» ]
    2DS5 X-ray 1.50 A/B 2-52 [» ]
    2DS6 X-ray 2.00 A/B 2-52 [» ]
    2DS7 X-ray 2.50 A 2-52 [» ]
    2DS8 X-ray 1.60 A/B 2-52 [» ]
    3HTE X-ray 4.03 A/B/C/D/E/F 62-424 [» ]
    3HWS X-ray 3.25 A/B/C/D/E/F 62-424 [» ]
    4I34 X-ray 4.12 A/B/C/D/E/F 62-424 [» ]
    4I4L X-ray 3.70 A/B/C/D/E/F 62-424 [» ]
    4I5O X-ray 4.48 A/B/C/D/E/F 62-424 [» ]
    4I63 X-ray 5.71 A/B/C/D/E/F 62-424 [» ]
    4I81 X-ray 3.82 A/B/C/D/E/F 62-424 [» ]
    4I9K X-ray 5.00 A/B 62-424 [» ]
    ProteinModelPortali P0A6H1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35907N.
    IntActi P0A6H1. 32 interactions.
    STRINGi 511145.b0438.

    Proteomic databases

    PaxDbi P0A6H1.
    PRIDEi P0A6H1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73541 ; AAC73541 ; b0438 .
    BAE76218 ; BAE76218 ; BAE76218 .
    GeneIDi 12931741.
    945083.
    KEGGi ecj:Y75_p0426.
    eco:b0438.
    PATRICi 32116029. VBIEscCol129921_0456.

    Organism-specific databases

    EchoBASEi EB0157.
    EcoGenei EG10159. clpX.

    Phylogenomic databases

    eggNOGi COG1219.
    HOGENOMi HOG000010093.
    KOi K03544.
    OMAi ILLDIMY.
    OrthoDBi EOG625JZK.
    PhylomeDBi P0A6H1.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10159-MONOMER.
    ECOL316407:JW0428-MONOMER.
    MetaCyc:EG10159-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A6H1.
    PROi P0A6H1.

    Gene expression databases

    Genevestigatori P0A6H1.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    HAMAPi MF_00175. ClpX.
    InterProi IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR019489. Clp_ATPase_C.
    IPR004487. Clp_protease_ATP-bd_su_ClpX.
    IPR027417. P-loop_NTPase.
    IPR010603. Znf_CppX_C4.
    [Graphical view ]
    Pfami PF07724. AAA_2. 1 hit.
    PF10431. ClpB_D2-small. 1 hit.
    PF06689. zf-C4_ClpX. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    SM01086. ClpB_D2-small. 1 hit.
    SM00994. zf-C4_ClpX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00382. clpX. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities."
      Gottesman S., Clark W.P., de Crecy-Lagard V., Maurizi M.R.
      J. Biol. Chem. 268:22618-22626(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "clpX encoding an alternative ATP-binding subunit of protease Ti (Clp) can be expressed independently from clpP in Escherichia coli."
      Yoo S.J., Seol J.H., Kang M.S., Ha D.B., Chung C.H.
      Biochem. Biophys. Res. Commun. 203:798-804(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, OPERON, ATP-BINDING.
    3. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli."
      Wojtkowiak D., Georgopoulos C., Zylicz M.
      J. Biol. Chem. 268:22609-22617(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-25, CHARACTERIZATION.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    7. "The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone."
      Wawrzynow A., Wojtkowiak D., Marszalek J., Banecki B., Jonsen M., Graves B., Georgopoulos C., Zylicz M.
      EMBO J. 14:1867-1877(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    8. "Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine."
      Kenniston J.A., Baker T.A., Fernandez J.M., Sauer R.T.
      Cell 114:511-520(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Modulating substrate choice: the SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation."
      Flynn J.M., Levchenko I., Sauer R.T., Baker T.A.
      Genes Dev. 18:2292-2301(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBSTRATE, DISRUPTION PHENOTYPE.
    10. "Design principles of the proteolytic cascade governing the sigmaE-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transduction."
      Chaba R., Grigorova I.L., Flynn J.M., Baker T.A., Gross C.A.
      Genes Dev. 21:124-136(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    11. "Unique contacts direct high-priority recognition of the tetrameric Mu transposase-DNA complex by the AAA+ unfoldase ClpX."
      Abdelhakim A.H., Oakes E.C., Sauer R.T., Baker T.A.
      Mol. Cell 30:39-50(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MU DDE-RECOMBINASE A.
    12. "Solution structure of the dimeric zinc binding domain of the chaperone ClpX."
      Donaldson L.W., Wojtyra U., Houry W.A.
      J. Biol. Chem. 278:48991-48996(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2-61 IN COMPLEX WITH ZINC.
    13. "Structural basis of SspB-tail recognition by the zinc binding domain of ClpX."
      Park E.Y., Lee B.G., Hong S.B., Kim H.W., Jeon H., Song H.K.
      J. Mol. Biol. 367:514-526(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 2-52 IN COMPLEX WITH ZINC AND IN COMPLEX WITH SSPB, SUBUNIT.
    14. "Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine."
      Glynn S.E., Martin A., Nager A.R., Baker T.A., Sauer R.T.
      Cell 139:744-756(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 62-424 IN COMPLEX WITH ATP, SUBUNIT.
    15. "Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine."
      Stinson B.M., Nager A.R., Glynn S.E., Schmitz K.R., Baker T.A., Sauer R.T.
      Cell 153:628-639(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 62-424 IN COMPLEX WITH ATP, MUTAGENESIS OF GLU-185 AND ARG-370.

    Entry informationi

    Entry nameiCLPX_ECOLI
    AccessioniPrimary (citable) accession number: P0A6H1
    Secondary accession number(s): P33138, Q2MBY8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 96 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

    3D-structure, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3