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P0A6H1

- CLPX_ECOLI

UniProt

P0A6H1 - CLPX_ECOLI

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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

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
Complete GO annotation...

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.
SMRiP0A6H1. Positions 9-52, 63-413.
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.
InParanoidiP0A6H1.
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

        10         20         30         40         50
MTDKRKDGSG KLLYCSFCGK SQHEVRKLIA GPSVYICDEC VDLCNDIIRE
60 70 80 90 100
EIKEVAPHRE RSALPTPHEI RNHLDDYVIG QEQAKKVLAV AVYNHYKRLR
110 120 130 140 150
NGDTSNGVEL GKSNILLIGP TGSGKTLLAE TLARLLDVPF TMADATTLTE
160 170 180 190 200
AGYVGEDVEN IIQKLLQKCD YDVQKAQRGI VYIDEIDKIS RKSDNPSITR
210 220 230 240 250
DVSGEGVQQA LLKLIEGTVA AVPPQGGRKH PQQEFLQVDT SKILFICGGA
260 270 280 290 300
FAGLDKVISH RVETGSGIGF GATVKAKSDK ASEGELLAQV EPEDLIKFGL
310 320 330 340 350
IPEFIGRLPV VATLNELSEE ALIQILKEPK NALTKQYQAL FNLEGVDLEF
360 370 380 390 400
RDEALDAIAK KAMARKTGAR GLRSIVEAAL LDTMYDLPSM EDVEKVVIDE
410 420
SVIDGQSKPL LIYGKPEAQQ ASGE
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.
SMRi P0A6H1. Positions 9-52, 63-413.
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.
InParanoidi P0A6H1.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 97 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