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Database: UniProt
Entry: P0A6H1
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Original site: P0A6H1 
ID   CLPX_ECOLI              Reviewed;         424 AA.
AC   P0A6H1; P33138; Q2MBY8;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-APR-2014, entry version 92.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX;
DE   AltName: Full=ATP-dependent unfoldase ClpX;
GN   Name=clpX; Synonyms=lopC; OrderedLocusNames=b0438, JW0428;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=8226770;
RA   Gottesman S., Clark W.P., de Crecy-Lagard V., Maurizi M.R.;
RT   "ClpX, an alternative subunit for the ATP-dependent Clp protease of
RT   Escherichia coli. Sequence and in vivo activities.";
RL   J. Biol. Chem. 268:22618-22626(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, OPERON, AND ATP-BINDING.
RX   PubMed=8093059; DOI=10.1006/bbrc.1994.2253;
RA   Yoo S.J., Seol J.H., Kang M.S., Ha D.B., Chung C.H.;
RT   "clpX encoding an alternative ATP-binding subunit of protease Ti (Clp)
RT   can be expressed independently from clpP in Escherichia coli.";
RL   Biochem. Biophys. Res. Commun. 203:798-804(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-25, AND CHARACTERIZATION.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8226769;
RA   Wojtkowiak D., Georgopoulos C., Zylicz M.;
RT   "Isolation and characterization of ClpX, a new ATP-dependent
RT   specificity component of the Clp protease of Escherichia coli.";
RL   J. Biol. Chem. 268:22609-22617(1993).
RN   [7]
RP   CHARACTERIZATION.
RX   PubMed=7743994;
RA   Wawrzynow A., Wojtkowiak D., Marszalek J., Banecki B., Jonsen M.,
RA   Graves B., Georgopoulos C., Zylicz M.;
RT   "The ClpX heat-shock protein of Escherichia coli, the ATP-dependent
RT   substrate specificity component of the ClpP-ClpX protease, is a novel
RT   molecular chaperone.";
RL   EMBO J. 14:1867-1877(1995).
RN   [8]
RP   FUNCTION.
RX   PubMed=12941278; DOI=10.1016/S0092-8674(03)00612-3;
RA   Kenniston J.A., Baker T.A., Fernandez J.M., Sauer R.T.;
RT   "Linkage between ATP consumption and mechanical unfolding during the
RT   protein processing reactions of an AAA+ degradation machine.";
RL   Cell 114:511-520(2003).
RN   [9]
RP   FUNCTION, SUBSTRATE, AND DISRUPTION PHENOTYPE.
RX   PubMed=15371343; DOI=10.1101/gad.1240104;
RA   Flynn J.M., Levchenko I., Sauer R.T., Baker T.A.;
RT   "Modulating substrate choice: the SspB adaptor delivers a regulator of
RT   the extracytoplasmic-stress response to the AAA+ protease ClpXP for
RT   degradation.";
RL   Genes Dev. 18:2292-2301(2004).
RN   [10]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17210793; DOI=10.1101/gad.1496707;
RA   Chaba R., Grigorova I.L., Flynn J.M., Baker T.A., Gross C.A.;
RT   "Design principles of the proteolytic cascade governing the sigmaE-
RT   mediated envelope stress response in Escherichia coli: keys to graded,
RT   buffered, and rapid signal transduction.";
RL   Genes Dev. 21:124-136(2007).
RN   [11]
RP   STRUCTURE BY NMR OF 2-61 IN COMPLEX WITH ZINC.
RX   PubMed=14525985; DOI=10.1074/jbc.M307826200;
RA   Donaldson L.W., Wojtyra U., Houry W.A.;
RT   "Solution structure of the dimeric zinc binding domain of the
RT   chaperone ClpX.";
RL   J. Biol. Chem. 278:48991-48996(2003).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 2-52 IN COMPLEX WITH ZINC
RP   AND IN COMPLEX WITH SSPB, AND SUBUNIT.
RX   PubMed=17258768; DOI=10.1016/j.jmb.2007.01.003;
RA   Park E.Y., Lee B.G., Hong S.B., Kim H.W., Jeon H., Song H.K.;
RT   "Structural basis of SspB-tail recognition by the zinc binding domain
RT   of ClpX.";
RL   J. Mol. Biol. 367:514-526(2007).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 62-424 IN COMPLEX WITH ATP,
RP   AND SUBUNIT.
RX   PubMed=19914167; DOI=10.1016/j.cell.2009.09.034;
RA   Glynn S.E., Martin A., Nager A.R., Baker T.A., Sauer R.T.;
RT   "Structures of asymmetric ClpX hexamers reveal nucleotide-dependent
RT   motions in a AAA+ protein-unfolding machine.";
RL   Cell 139:744-756(2009).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 62-424 IN COMPLEX WITH ATP,
RP   AND MUTAGENESIS OF GLU-185 AND ARG-370.
RX   PubMed=23622246; DOI=10.1016/j.cell.2013.03.029;
RA   Stinson B.M., Nager A.R., Glynn S.E., Schmitz K.R., Baker T.A.,
RA   Sauer R.T.;
RT   "Nucleotide binding and conformational switching in the hexameric ring
RT   of a AAA+ machine.";
RL   Cell 153:628-639(2013).
CC   -!- FUNCTION: ATP-dependent specificity component of the Clp protease.
CC       Uses cycles of ATP binding and hydrolysis to unfold proteins and
CC       translocate them to the ClpP protease. It directs the protease to
CC       specific substrates both with and without the help of adapter
CC       proteins such as SspB. Participates in the final steps of RseA-
CC       sigma-E degradation, liberating sigma-E to induce the
CC       extracytoplasmic-stress response. It may bind to the lambda O
CC       substrate protein and present it to the ClpP protease in a form
CC       that can be recognized and readily hydrolyzed by ClpP. Can perform
CC       chaperone functions in the absence of ClpP.
CC   -!- COFACTOR: Binds 1 Zn(2+) per subunit.
CC   -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric
CC       ring that, in the presence of ATP, binds to fourteen ClpP subunits
CC       assembled into a disk-like structure with a central cavity,
CC       resembling the structure of eukaryotic proteasomes.
CC   -!- INTERACTION:
CC       Self; NbExp=6; IntAct=EBI-547386, EBI-547386;
CC   -!- INDUCTION: By heat shock. Part of the clpP-clpX operon, clpX can
CC       be expressed individually from its own promoter.
CC   -!- DISRUPTION PHENOTYPE: Delayed and decreased induction of the
CC       extracytoplasmic-stress response.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family.
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DR   EMBL; L18867; AAA16116.1; -; Unassigned_DNA.
DR   EMBL; Z23278; CAA80816.1; -; Genomic_DNA.
DR   EMBL; U82664; AAB40194.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73541.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76218.1; -; Genomic_DNA.
DR   PIR; A48709; A48709.
DR   RefSeq; NP_414972.1; NC_000913.3.
DR   RefSeq; YP_488730.1; NC_007779.1.
DR   PDB; 1OVX; NMR; -; A/B=2-61.
DR   PDB; 2DS5; X-ray; 1.50 A; A/B=2-51.
DR   PDB; 2DS6; X-ray; 2.00 A; A/B=2-51.
DR   PDB; 2DS7; X-ray; 2.50 A; A=2-51.
DR   PDB; 2DS8; X-ray; 1.60 A; A/B=2-51.
DR   PDB; 3HTE; X-ray; 4.03 A; A/B/C/D/E/F=62-424.
DR   PDB; 3HWS; X-ray; 3.25 A; A/B/C/D/E/F=62-424.
DR   PDB; 4I34; X-ray; 4.12 A; A/B/C/D/E/F=62-424.
DR   PDB; 4I4L; X-ray; 3.70 A; A/B/C/D/E/F=62-424.
DR   PDB; 4I5O; X-ray; 4.48 A; A/B/C/D/E/F=62-424.
DR   PDB; 4I63; X-ray; 5.71 A; A/B/C/D/E/F=62-424.
DR   PDB; 4I81; X-ray; 3.82 A; A/B/C/D/E/F=62-424.
DR   PDB; 4I9K; X-ray; 5.00 A; A/B=62-424.
DR   PDBsum; 1OVX; -.
DR   PDBsum; 2DS5; -.
DR   PDBsum; 2DS6; -.
DR   PDBsum; 2DS7; -.
DR   PDBsum; 2DS8; -.
DR   PDBsum; 3HTE; -.
DR   PDBsum; 3HWS; -.
DR   PDBsum; 4I34; -.
DR   PDBsum; 4I4L; -.
DR   PDBsum; 4I5O; -.
DR   PDBsum; 4I63; -.
DR   PDBsum; 4I81; -.
DR   PDBsum; 4I9K; -.
DR   ProteinModelPortal; P0A6H1; -.
DR   SMR; P0A6H1; 9-52, 63-413.
DR   DIP; DIP-35907N; -.
DR   IntAct; P0A6H1; 31.
DR   STRING; 511145.b0438; -.
DR   PaxDb; P0A6H1; -.
DR   PRIDE; P0A6H1; -.
DR   EnsemblBacteria; AAC73541; AAC73541; b0438.
DR   EnsemblBacteria; BAE76218; BAE76218; BAE76218.
DR   GeneID; 12931741; -.
DR   GeneID; 945083; -.
DR   KEGG; ecj:Y75_p0426; -.
DR   KEGG; eco:b0438; -.
DR   PATRIC; 32116029; VBIEscCol129921_0456.
DR   EchoBASE; EB0157; -.
DR   EcoGene; EG10159; clpX.
DR   eggNOG; COG1219; -.
DR   HOGENOM; HOG000010093; -.
DR   KO; K03544; -.
DR   OMA; LDTMFDL; -.
DR   OrthoDB; EOG625JZK; -.
DR   PhylomeDB; P0A6H1; -.
DR   ProtClustDB; PRK05342; -.
DR   BioCyc; EcoCyc:EG10159-MONOMER; -.
DR   BioCyc; ECOL316407:JW0428-MONOMER; -.
DR   BioCyc; MetaCyc:EG10159-MONOMER; -.
DR   EvolutionaryTrace; P0A6H1; -.
DR   PRO; PR:P0A6H1; -.
DR   Genevestigator; P0A6H1; -.
DR   GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:CACAO.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006200; P:ATP catabolic process; IDA:GOC.
DR   GO; GO:0051301; P:cell division; IGI:CACAO.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_00175; ClpX; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013093; ATPase_AAA-2.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010603; Znf_CppX_C4.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   Pfam; PF06689; zf-C4_ClpX; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SMART; SM00994; zf-C4_ClpX; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00382; clpX; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Chaperone; Complete proteome;
KW   Direct protein sequencing; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Stress response; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    424       ATP-dependent Clp protease ATP-binding
FT                                subunit ClpX.
FT                                /FTId=PRO_0000160352.
FT   ZN_FING      15     40       C4-type.
FT   NP_BIND     120    127       ATP.
FT   METAL        15     15       Zinc.
FT   METAL        18     18       Zinc.
FT   METAL        37     37       Zinc.
FT   METAL        40     40       Zinc.
FT   MUTAGEN     185    185       E->Q: No ATP hydrolyis.
FT   MUTAGEN     370    370       R->K: No ATP hydrolyis.
FT   CONFLICT    268    274       IGFGATV -> HWCWRSG (in Ref. 2; CAA80816).
FT   TURN         16     18
FT   TURN         22     24
FT   STRAND       28     30
FT   STRAND       35     37
FT   HELIX        38     49
FT   HELIX        67     77
FT   HELIX        82    100
FT   STRAND      105    107
FT   STRAND      115    118
FT   HELIX       125    135
FT   STRAND      140    144
FT   HELIX       145    148
FT   HELIX       152    158
FT   HELIX       160    168
FT   TURN        169    171
FT   HELIX       173    178
FT   STRAND      180    184
FT   HELIX       186    189
FT   HELIX       201    216
FT   STRAND      242    249
FT   HELIX       254    262
FT   HELIX       283    288
FT   HELIX       292    298
FT   HELIX       302    305
FT   STRAND      310    313
FT   HELIX       319    327
FT   HELIX       333    342
FT   TURN        343    345
FT   STRAND      347    350
FT   HELIX       352    364
FT   TURN        368    371
FT   HELIX       372    385
FT   TURN        387    389
FT   STRAND      393    397
FT   HELIX       399    402
FT   STRAND      410    412
SQ   SEQUENCE   424 AA;  46356 MW;  9DEF1B0786E42B6F CRC64;
     MTDKRKDGSG KLLYCSFCGK SQHEVRKLIA GPSVYICDEC VDLCNDIIRE EIKEVAPHRE
     RSALPTPHEI RNHLDDYVIG QEQAKKVLAV AVYNHYKRLR NGDTSNGVEL GKSNILLIGP
     TGSGKTLLAE TLARLLDVPF TMADATTLTE AGYVGEDVEN IIQKLLQKCD YDVQKAQRGI
     VYIDEIDKIS RKSDNPSITR DVSGEGVQQA LLKLIEGTVA AVPPQGGRKH PQQEFLQVDT
     SKILFICGGA FAGLDKVISH RVETGSGIGF GATVKAKSDK ASEGELLAQV EPEDLIKFGL
     IPEFIGRLPV VATLNELSEE ALIQILKEPK NALTKQYQAL FNLEGVDLEF RDEALDAIAK
     KAMARKTGAR GLRSIVEAAL LDTMYDLPSM EDVEKVVIDE SVIDGQSKPL LIYGKPEAQQ
     ASGE
//
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