ID K0AXH1_GOTA9 Unreviewed; 423 AA.
AC K0AXH1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 63.
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:AFS77420.1};
GN OrderedLocusNames=Curi_c03450 {ECO:0000313|EMBL:AFS77420.1};
OS Gottschalkia acidurici (strain ATCC 7906 / DSM 604 / BCRC 14475 / CIP
OS 104303 / KCTC 5404 / NCIMB 10678 / 9a) (Clostridium acidurici).
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Gottschalkiaceae;
OC Gottschalkia.
OX NCBI_TaxID=1128398 {ECO:0000313|EMBL:AFS77420.1, ECO:0000313|Proteomes:UP000006094};
RN [1] {ECO:0000313|EMBL:AFS77420.1, ECO:0000313|Proteomes:UP000006094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7906 / DSM 604 / BCRC 14475 / CIP 104303 / KCTC 5404 /
RC NCIMB 10678 / 9a {ECO:0000313|Proteomes:UP000006094};
RX PubMed=23240052; DOI=10.1371/journal.pone.0051662;
RA Hartwich K., Poehlein A., Daniel R.;
RT "The purine-utilizing bacterium Clostridium acidurici 9a: a genome-guided
RT metabolic reconsideration.";
RL PLoS ONE 7:E51662-E51662(2012).
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; CP003326; AFS77420.1; -; Genomic_DNA.
DR RefSeq; WP_014966557.1; NC_018664.1.
DR AlphaFoldDB; K0AXH1; -.
DR STRING; 1128398.Curi_c03450; -.
DR KEGG; cad:Curi_c03450; -.
DR PATRIC; fig|1128398.3.peg.353; -.
DR eggNOG; COG1219; Bacteria.
DR HOGENOM; CLU_014218_8_2_9; -.
DR OMA; HYKRVQA; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000006094; 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:AFS77420.1};
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:AFS77420.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006094};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT DOMAIN 1..52
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT REGION 402..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 11
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 14
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 33
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 36
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 115..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
SQ SEQUENCE 423 AA; 47407 MW; C0683508C848AF85 CRC64;
MAKIEEKQLK CSFCGKTQEQ VRRLVAGPNV FICDECIDLC QEIIEEEFEV DFEVDFTELP
KPSEIKETLD EYVIQQEKAK RALAVAVYNH YKRINKKSSN NDIELQKSNI VMIGPTGSGK
TLLAQTLAKI LNVPFAIADA TSLTEAGYVG EDVENIILKL IQAADYDVER AEKGIIYIDE
IDKIARKSEN PSITRDVSGE GVQQALLKIL EGTVASVPPQ GGRKHPHQEF IQIDTTNILF
IVGGAFDGIQ DVVQQRIGKK SMGFGAEIQS KNDKDTSELL KNLQPEDLLK FGLIPEFVGR
LPIMVTLEQL DRDALVDILT KPKNALTKQY KELLAMDGVE LEIEKEALEL VAEKAIERKT
GARGLRGIIE EIMLDIMYEI PSREDIEKCI ITKDTIKENK EPTLVLSEKR KNKSTEETDE
ETA
//