ID   CLPX_RHIE6              Reviewed;         425 AA.
AC   B3PVY5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 87.
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};
GN   OrderedLocusNames=RHECIAT_CH0001660;
OS   Rhizobium etli (strain CIAT 652).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=491916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIAT 652;
RA   Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA   Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA   Palacios R., Davila G.;
RT   "Genome diversity and DNA divergence of Rhizobium etli.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000255|HAMAP-
CC       Rule:MF_00175}.
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DR   EMBL; CP001074; ACE90637.1; -; Genomic_DNA.
DR   RefSeq; WP_004680013.1; NC_010994.1.
DR   AlphaFoldDB; B3PVY5; -.
DR   SMR; B3PVY5; -.
DR   EnsemblBacteria; ACE90637; ACE90637; RHECIAT_CH0001660.
DR   GeneID; 45956984; -.
DR   GeneID; 58689080; -.
DR   GeneID; 61480048; -.
DR   GeneID; 66145766; -.
DR   KEGG; rec:RHECIAT_CH0001660; -.
DR   eggNOG; COG1219; Bacteria.
DR   HOGENOM; CLU_014218_8_2_5; -.
DR   OMA; HYKRVQA; -.
DR   Proteomes; UP000008817; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 6.20.220.10; -; 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   InterPro; IPR038366; Znf_CppX_C4_sf.
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.
DR   PROSITE; PS51902; CLPX_ZB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Metal-binding; Nucleotide-binding; Zinc.
FT   CHAIN           1..425
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT                   /id="PRO_1000097988"
FT   DOMAIN          6..59
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         21
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         43
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         122..129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   425 AA;  46937 MW;  2CA7E1B3C5037D6D CRC64;
     MSKVSGSNGG DSKNTLYCSF CGKSQHEVRK LIAGPTVFIC DECVELCMDI IREENKSSMV
     KSRDGVPTPQ DIIKVLDEYV IGQRQAKKIL SVAVHNHYKR LAHASKNGEV ELAKSNIMLV
     GPTGCGKTYL AQTLARIIDV PFTMADATTL TEAGYVGEDV ENIILKLLQA ADYNVERAQR
     GIVYIDEVDK ISRKSDNPSI TRDVSGEGVQ QALLKIMEGT VASVPPQGGR KHPQQEFLQV
     DTTNILFICG GAFAGLDKII SARGEKTSIG FGATVKAQDD RRVGEVLREL EPEDLVKFGL
     IPEFIGRLPV LATLEDLDED ALIQILSEPK NALIKQYQRL FEMEDVELTF HEDALREIAR
     KAIVRKTGAR GLRSIMEKIL LDTMFELPTL EGVREVVISE EVVRGSARPL YIYADRQEEK
     ANASA