ID CLPX_BRUAB Reviewed; 424 AA.
AC Q9L7X5; Q57D29;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 27-MAR-2024, entry version 123.
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=BruAb1_1114;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Robertson G.T., Roop R.M. II;
RT "The Brucella abortus clpP and clpX are not subject to classical heat shock
RT regulation and are critical for cell viability.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF218420; AAF32319.1; -; Genomic_DNA.
DR EMBL; AE017223; AAX74455.1; -; Genomic_DNA.
DR RefSeq; WP_002964236.1; NC_006932.1.
DR AlphaFoldDB; Q9L7X5; -.
DR SMR; Q9L7X5; -.
DR EnsemblBacteria; AAX74455; AAX74455; BruAb1_1114.
DR GeneID; 3787779; -.
DR KEGG; bmb:BruAb1_1114; -.
DR HOGENOM; CLU_014218_8_2_5; -.
DR Proteomes; UP000000540; Chromosome I.
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 CDD; cd19497; RecA-like_ClpX; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 6.20.220.10; ClpX chaperone, C4-type zinc finger domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00382; clpX; 1.
DR PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 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 SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Metal-binding; Nucleotide-binding; Zinc.
FT CHAIN 1..424
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT /id="PRO_0000160325"
FT DOMAIN 5..58
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 20
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 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 121..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
FT CONFLICT 68..70
FT /note="PQE -> RRQ (in Ref. 1; AAF32319)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="G -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 46656 MW; 6A68089A37209608 CRC64;
MSKVSNGGGD SKNTLYCSFC GKSQHEVRKL IAGPTVFICD ECVELCMDII REENKSSMVK
SREGVPTPQE IMAVLDDYVI GQKDAKRVLS VAVHNHYKRL AHQSKNSDIE LAKSNILLVG
PTGCGKTYLA QTLARIIDVP FIMADATTLT EAGYVGEDVE NIILKLLQAA DYNVERAQRG
IVYIDEVDKI SRKSDNPSIT RDVSGEGVQQ ALLKIMEGTV ASVPPQGGRK HPQQEFLQVD
TTNILFICGG AFAGLDRIIS ARGEKTSIGF GATVKSVDER RIGEVFKELE PEDLLKFGLI
PEFVGRLPVI ATLEDLDVDA LVQILTEPKN ALVKQYQRLF DMENVELVFH DDALRAIANK
AVERKTGARG LRSIMEKILL DTMFELPTLE GVREVVISGD VVDGSARPLY IYAERQDEKG
NVSA
//
