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 01-MAY-2013, entry version 84.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit 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].
RA Yoo S., Seol J., Ha D., Goldberg A., Chung C.;
RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
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 277:1453-1474(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 STRUCTURE BY NMR OF 1-61.
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).
CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease.
CC It directs the protease to specific substrates. It may bind to the
CC lambda O substrate protein and present it to the ClpP protease in
CC a form that can be recognized and readily hydrolyzed by ClpP. Can
CC perform chaperone functions in the absence of ClpP.
CC -!- SUBUNIT: Heterodimer of ClpP and ClpX.
CC -!- INDUCTION: By heat shock.
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_000913.2.
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 PDBsum; 1OVX; -.
DR PDBsum; 2DS5; -.
DR PDBsum; 2DS6; -.
DR PDBsum; 2DS7; -.
DR PDBsum; 2DS8; -.
DR PDBsum; 3HTE; -.
DR PDBsum; 3HWS; -.
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; SDLELEH; -.
DR ProtClustDB; PRK05342; -.
DR BioCyc; EcoCyc:EG10159-MONOMER; -.
DR BioCyc; ECOL316407:JW0428-MONOMER; -.
DR BioCyc; MetaCyc:EG10159-MONOMER; -.
DR EvolutionaryTrace; P0A6H1; -.
DR Genevestigator; P0A6H1; -.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:HAMAP.
DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
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; IPR010603; Znf_CppX_C4.
DR PANTHER; PTHR11262:SF4; PTHR11262:SF4; 1.
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 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 119 126 ATP (Potential).
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
//
