ID A0A0G3CLD5_9GAMM Unreviewed; 423 AA.
AC A0A0G3CLD5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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:AKJ42764.1};
GN ORFNames=QQ39_12280 {ECO:0000313|EMBL:AKJ42764.1};
OS Pragia fontium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Pragia.
OX NCBI_TaxID=82985 {ECO:0000313|EMBL:AKJ42764.1, ECO:0000313|Proteomes:UP000068021};
RN [1] {ECO:0000313|EMBL:AKJ42764.1, ECO:0000313|Proteomes:UP000068021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24613 {ECO:0000313|EMBL:AKJ42764.1,
RC ECO:0000313|Proteomes:UP000068021};
RX PubMed=26159528;
RA Snopkova K., Sedlar K., Bosak J., Chaloupkova E., Provaznik I., Smajs D.;
RT "Complete Genome Sequence of Pragia fontium 24613, an Environmental
RT Bacterium from the Family Enterobacteriaceae.";
RL Genome Announc. 3:e00740-15(2015).
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; CP010423; AKJ42764.1; -; Genomic_DNA.
DR RefSeq; WP_047781497.1; NZ_UGTK01000001.1.
DR STRING; 82985.QQ39_12280; -.
DR KEGG; pfq:QQ39_12280; -.
DR PATRIC; fig|82985.3.peg.2571; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000068021; 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|HAMAP-Rule:MF_00175};
KW Chaperone {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|PROSITE-
KW ProRule:PRU01250}; Hydrolase {ECO:0000313|EMBL:AKJ42764.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|PROSITE-
KW ProRule:PRU01250}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00175};
KW Protease {ECO:0000313|EMBL:AKJ42764.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000068021};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|PROSITE-
KW ProRule:PRU01250}.
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 120..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ SEQUENCE 423 AA; 46445 MW; 08FCD37501DDA30F CRC64;
MTDKGKDGSG KLLYCTFCGK SQHEVRKLIA GPSVYICDEC VDLCNDIIRE EIKELIPHRE
RNALPTPHEI RQHLDDYVIG QDQAKKVLAV AVYNHYKRLR NGDGNSDIEL GKSNILLIGP
TGSGKTLLAE TLARLLDVPF TMADATTLTE AGYVGEDVEN IIQKLLQKCD YDVEKAQRGI
VYIDEIDKIS RKSDNPSITR DVSGEGVQQA LLKLIEGTVA AVPPQGGRKH PQQEFLQVDT
SKILFICGGA FAGLDKVIGQ RVDTGSGIGF GAKVKKESDK ASTGELFRQV EPEDLIKFGL
IPEFIGRLPV VATLGELDEA ALIQILKEPK NALTKQYQAL FHIENVELEF RDEALNAIAK
KAMSRKTGAR GLRSIVEAAL LNTMYDIPSM ENVEKVVIDA SVIDNNSEPL LIYSKQEAQA
SGE
//
