CLPX_HELPY
ID CLPX_HELPY Reviewed; 446 AA.
AC O25926;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000255|HAMAP-Rule:MF_00175};
GN Name=clpX {ECO:0000255|HAMAP-Rule:MF_00175}; OrderedLocusNames=HP_1374;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 431-446.
RC STRAIN=ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487;
RA Perez-Casal J.F., O'Toole P.W., Trust T.J.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 71-446 IN COMPLEX WITH ADP, AND
RP SUBUNIT.
RX PubMed=14514695; DOI=10.1074/jbc.m305882200;
RA Kim D.Y., Kim K.K.;
RT "Crystal structure of ClpX molecular chaperone from Helicobacter pylori.";
RL J. Biol. Chem. 278:50664-50670(2003).
CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease. It
CC directs the protease to specific substrates. Can perform chaperone
CC functions in the absence of ClpP. {ECO:0000255|HAMAP-Rule:MF_00175}.
CC -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric ring
CC that, in the presence of ATP, binds to fourteen ClpP subunits assembled
CC into a disk-like structure with a central cavity, resembling the
CC structure of eukaryotic proteasomes. {ECO:0000255|HAMAP-Rule:MF_00175,
CC ECO:0000269|PubMed:14514695}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000255|HAMAP-
CC Rule:MF_00175}.
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DR EMBL; AE000511; AAD08417.1; -; Genomic_DNA.
DR EMBL; U95641; AAC04557.1; -; Genomic_DNA.
DR PIR; F64691; F64691.
DR RefSeq; NP_208165.1; NC_000915.1.
DR RefSeq; WP_001006287.1; NC_018939.1.
DR PDB; 1UM8; X-ray; 2.60 A; A=71-446.
DR PDBsum; 1UM8; -.
DR AlphaFoldDB; O25926; -.
DR SMR; O25926; -.
DR DIP; DIP-3286N; -.
DR IntAct; O25926; 4.
DR MINT; O25926; -.
DR STRING; 85962.C694_07090; -.
DR DrugBank; DB09275; Bismuth subcitrate potassium.
DR PaxDb; O25926; -.
DR EnsemblBacteria; AAD08417; AAD08417; HP_1374.
DR KEGG; hpy:HP_1374; -.
DR PATRIC; fig|85962.47.peg.1471; -.
DR eggNOG; COG1219; Bacteria.
DR OMA; HYKRVQA; -.
DR PhylomeDB; O25926; -.
DR EvolutionaryTrace; O25926; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0009376; C:HslUV protease complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00175; ClpX; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR InterPro; IPR046425; ClpX_bact.
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 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.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Metal-binding; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..446
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT /id="PRO_0000160365"
FT DOMAIN 1..55
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 150..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 97..123
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:1UM8"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:1UM8"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:1UM8"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:1UM8"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:1UM8"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:1UM8"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:1UM8"
FT TURN 306..311
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:1UM8"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 345..353
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 359..368
FT /evidence="ECO:0007829|PDB:1UM8"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:1UM8"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 378..390
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 398..411
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 413..416
FT /evidence="ECO:0007829|PDB:1UM8"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:1UM8"
FT HELIX 425..428
FT /evidence="ECO:0007829|PDB:1UM8"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:1UM8"
SQ SEQUENCE 446 AA; 50353 MW; F0C6E623F6A17633 CRC64;
MNETLYCSFC KKPESRDPKK RRIIFASNLN KDVCVCEYCI DVMHGELHKY DNSLLALKRD
RLRRMESSAY EEEFLLSYIP APKELKAVLD NYVIGQEQAK KVFSVAVYNH YKRLSFKEKL
KKQDNQDSNV ELEHLEEVEL SKSNILLIGP TGSGKTLMAQ TLAKHLDIPI AISDATSLTE
AGYVGEDVEN ILTRLLQASD WNVQKAQKGI VFIDEIDKIS RLSENRSITR DVSGEGVQQA
LLKIVEGSLV NIPPKGGRKH PEGNFIQIDT SDILFICAGA FDGLAEIIKK RTTQNVLGFT
QEKMSKKEQE AILHLVQTHD LVTYGLIPEL IGRLPVLSTL DSISLEAMVD ILQKPKNALI
KQYQQLFKMD EVDLIFEEEA IKEIAQLALE RKTGARGLRA IIEDFCLDIM FDLPKLKGSE
VRITKDCVLK QAEPLIIAKT HSKILP
