CLPX_THEYD
ID CLPX_THEYD Reviewed; 409 AA.
AC B5YI39;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=THEYE_A0256;
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-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; CP001147; ACI21821.1; -; Genomic_DNA.
DR RefSeq; WP_012546526.1; NC_011296.1.
DR RefSeq; YP_002248105.1; NC_011296.1.
DR AlphaFoldDB; B5YI39; -.
DR SMR; B5YI39; -.
DR STRING; 289376.THEYE_A0256; -.
DR PRIDE; B5YI39; -.
DR EnsemblBacteria; ACI21821; ACI21821; THEYE_A0256.
DR KEGG; tye:THEYE_A0256; -.
DR PATRIC; fig|289376.4.peg.253; -.
DR eggNOG; COG1219; Bacteria.
DR HOGENOM; CLU_014218_8_2_0; -.
DR InParanoid; B5YI39; -.
DR OMA; HYKRVQA; -.
DR OrthoDB; 718259at2; -.
DR Proteomes; UP000000718; Chromosome.
DR GO; GO:0009376; C:HslUV protease complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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 GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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;
KW Reference proteome; Zinc.
FT CHAIN 1..409
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT /id="PRO_1000123857"
FT DOMAIN 1..52
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 113..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
SQ SEQUENCE 409 AA; 45754 MW; 31178A28DD94B4F5 CRC64;
MAKKNEETLR CSFCGKSQKE VKKLIAGNGV YICDECVSLC NEILEEERFE HLEGIKQDLP
TPQEIHKFLN DYVIGQERAK KILSVAVYNH YKRIFKGTSS DEIQKSNIML IGPTGTGKTL
LAQTLAKFLD VPFAIADATT LTEAGYVGED VENILLKLLQ NANFDIQRAQ IGIIYIDEID
KISRKSDSPS ITRDVSGEGV QQALLKIVEG TLANIPPQGG RKHPQQEYIQ LDTTNILFIC
GGAFVGLEEI IKKRIGKRTI GFLSETKKID EENVLSQAEP EDLIKYGMIP EFVGRFPVVA
TLNQLDEDAL IEILTKPKNA LVKQYQKLFS IDGVKLTFTD DALRAIAKKA IERKTGARAL
RSILEDIMLD VMYLIPSERG INECIINEDV VNKKASPILI YKEKKVKHA