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P0A6H1 (CLPX_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent Clp protease ATP-binding subunit ClpX
Alternative name(s):
ATP-dependent unfoldase ClpX
Gene names
Name:clpX
Synonyms:lopC
Ordered Locus Names:b0438, JW0428
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9

Cofactor

Binds 1 Zn2+ per subunit.

Subunit structure

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. Ref.11 Ref.13 Ref.14

Induction

By heat shock. Part of the clpP-clpX operon, clpX can be expressed individually from its own promoter. Ref.2

Disruption phenotype

Delayed and decreased induction of the extracytoplasmic-stress response. Ref.9 Ref.10

Sequence similarities

Belongs to the ClpX chaperone family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself6EBI-547386,EBI-547386

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 424423ATP-dependent Clp protease ATP-binding subunit ClpX HAMAP-Rule MF_00175
PRO_0000160352

Regions

Zinc finger15 – 4026C4-type HAMAP-Rule MF_00175
Nucleotide binding120 – 1278ATP HAMAP-Rule MF_00175

Sites

Metal binding151Zinc
Metal binding181Zinc
Metal binding371Zinc
Metal binding401Zinc

Experimental info

Mutagenesis1851E → Q: No ATP hydrolyis. Ref.15
Mutagenesis3701R → K: No ATP hydrolyis. Ref.15
Sequence conflict268 – 2747IGFGATV → HWCWRSG in CAA80816. Ref.2

Secondary structure

.................................................................... 424
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6H1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 9DEF1B0786E42B6F

FASTA42446,356
        10         20         30         40         50         60 
MTDKRKDGSG KLLYCSFCGK SQHEVRKLIA GPSVYICDEC VDLCNDIIRE EIKEVAPHRE 

        70         80         90        100        110        120 
RSALPTPHEI RNHLDDYVIG QEQAKKVLAV AVYNHYKRLR NGDTSNGVEL GKSNILLIGP 

       130        140        150        160        170        180 
TGSGKTLLAE TLARLLDVPF TMADATTLTE AGYVGEDVEN IIQKLLQKCD YDVQKAQRGI 

       190        200        210        220        230        240 
VYIDEIDKIS RKSDNPSITR DVSGEGVQQA LLKLIEGTVA AVPPQGGRKH PQQEFLQVDT 

       250        260        270        280        290        300 
SKILFICGGA FAGLDKVISH RVETGSGIGF GATVKAKSDK ASEGELLAQV EPEDLIKFGL 

       310        320        330        340        350        360 
IPEFIGRLPV VATLNELSEE ALIQILKEPK NALTKQYQAL FNLEGVDLEF RDEALDAIAK 

       370        380        390        400        410        420 
KAMARKTGAR GLRSIVEAAL LDTMYDLPSM EDVEKVVIDE SVIDGQSKPL LIYGKPEAQQ 


ASGE 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA48709.
RefSeqNP_414972.1. NC_000913.3.
YP_488730.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP0A6H1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35907N.
IntActP0A6H1. 32 interactions.
STRING511145.b0438.

Proteomic databases

PaxDbP0A6H1.
PRIDEP0A6H1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73541; AAC73541; b0438.
BAE76218; BAE76218; BAE76218.
GeneID12931741.
945083.
KEGGecj:Y75_p0426.
eco:b0438.
PATRIC32116029. VBIEscCol129921_0456.

Organism-specific databases

EchoBASEEB0157.
EcoGeneEG10159. clpX.

Phylogenomic databases

eggNOGCOG1219.
HOGENOMHOG000010093.
KOK03544.
OMAILLDIMY.
OrthoDBEOG625JZK.
PhylomeDBP0A6H1.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP0A6H1.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
HAMAPMF_00175. ClpX.
InterProIPR003593. 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]
PfamPF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
PF06689. zf-C4_ClpX. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
SM01086. ClpB_D2-small. 1 hit.
SM00994. zf-C4_ClpX. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00382. clpX. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A6H1.
PROP0A6H1.

Entry information

Entry nameCLPX_ECOLI
AccessionPrimary (citable) accession number: P0A6H1
Secondary accession number(s): P33138, Q2MBY8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene