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Database: UniProt
Entry: A0A0G3BGG0_9BURK
LinkDB: A0A0G3BGG0_9BURK
Original site: A0A0G3BGG0_9BURK 
ID   A0A0G3BGG0_9BURK        Unreviewed;       424 AA.
AC   A0A0G3BGG0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000256|HAMAP-Rule:MF_00175};
GN   Name=clpX {ECO:0000256|HAMAP-Rule:MF_00175,
GN   ECO:0000313|EMBL:AKJ28519.1};
GN   ORFNames=AAW51_1828 {ECO:0000313|EMBL:AKJ28519.1};
OS   Caldimonas brevitalea.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Caldimonas.
OX   NCBI_TaxID=413882 {ECO:0000313|EMBL:AKJ28519.1, ECO:0000313|Proteomes:UP000035352};
RN   [1] {ECO:0000313|EMBL:AKJ28519.1, ECO:0000313|Proteomes:UP000035352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7029 {ECO:0000313|EMBL:AKJ28519.1,
RC   ECO:0000313|Proteomes:UP000035352};
RA   Tang B., Yu Y.;
RL   Submitted (MAY-2015) 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:0000256|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:0000256|HAMAP-Rule:MF_00175}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|HAMAP-
CC       Rule:MF_00175, ECO:0000256|PROSITE-ProRule:PRU01250}.
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DR   EMBL; CP011371; AKJ28519.1; -; Genomic_DNA.
DR   RefSeq; WP_047194371.1; NZ_CP011371.1.
DR   AlphaFoldDB; A0A0G3BGG0; -.
DR   STRING; 413882.AAW51_1828; -.
DR   KEGG; pbh:AAW51_1828; -.
DR   PATRIC; fig|413882.6.peg.1924; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000035352; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00175};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00175};
KW   Hydrolase {ECO:0000313|EMBL:AKJ28519.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00175};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00175}; Protease {ECO:0000313|EMBL:AKJ28519.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035352};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT   DOMAIN          3..56
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   BINDING         15
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT                   ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT                   ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT                   ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT                   ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         125..132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ   SEQUENCE   424 AA;  46087 MW;  301F5DB9EC2680A7 CRC64;
     MPEKKGSSSE KVLYCSFCGK SQHEVKKLIA GPSVFICDEC IDLCNDIIRD EVPADGADAK
     AARGDLPVPS EIKSILDQYV IGQDAAKRTL SVAVYNHYKR LKHMGGGGKK DEVELAKSNI
     LLIGPTGSGK TLLAQTLARL LNVPFVIADA TTLTEAGYVG EDVENIIQKL LQNCNYDVEK
     AQRGIVYIDE IDKISRKADN PSITRDVSGE GVQQALLKLV EGTMASVPPQ GGRKHPNQDF
     LQIDTTNILF ICGGAFDGLE KVIQNRSEKS GIGFGANVKT KAERSISEVF REVEPEDLIK
     FGLIPELVGR LPVVATLGEL TEDALIQILT EPKNALVKQY QKLFSMDGVE LEIRPSALAS
     ISRKALARKT GARGLRSIME QALIDTMFDL PALDGVAKVV VDEHTIEEST KPLLVYREQA
     KASA
//
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