ID A0A231NZ34_9BACT Unreviewed; 432 AA. AC A0A231NZ34; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 28-JUN-2023, entry version 25. 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 ORFNames=BCS36_12950 {ECO:0000313|EMBL:OXS27718.1}; OS Desulfovibrio sp. MES5. OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=1899016 {ECO:0000313|EMBL:OXS27718.1, ECO:0000313|Proteomes:UP000215488}; RN [1] {ECO:0000313|EMBL:OXS27718.1, ECO:0000313|Proteomes:UP000215488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MES5 {ECO:0000313|EMBL:OXS27718.1}; RA Marshall C., Ross D.E., Handley K., Weisenhorn P., Edirisinghe J., RA Henry C., Gilbert J., May H., Norman R.S.; RT "Metabolic Reconstruction and Modeling Microbial Electrosynthesis."; RL Submitted (SEP-2016) 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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OXS27718.1}. 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; MJUZ01000051; OXS27718.1; -; Genomic_DNA. DR AlphaFoldDB; A0A231NZ34; -. DR EnsemblBacteria; OXS27718; OXS27718; BCS36_12950. DR Proteomes; UP000215488; Unassembled WGS sequence. 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 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 TIGRFAMs; TIGR00382; clpX; 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:OXS27718.1}; 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:OXS27718.1}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}. FT DOMAIN 1..56 FT /note="ClpX-type ZB" FT /evidence="ECO:0000259|PROSITE:PS51902" FT REGION 412..432 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 417..432 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 432 AA; 47192 MW; 13D1B3A7C1559AC6 CRC64; MAKNDKPTVS EPLTCSFCGR SELEVRNLIV QDGASICDKC VKACNDIIAR DQVESTEGDE RLLSPQEIKD RLDQYVIGQH EAKKILSVAV HNHYKRVFYA DAMGDDGVEL EKSNILLVGP SGSGKTLLAK TLARVLRVPF AIADATTLTE AGYVGEDVEN ILVQLLQNAD YDLEAASKGI IYVDEIDKIS RKGDGPSITR DVSGEGVQQA LLKIIEGTEA NIPPKGGRKH PQQEFIRMNT SNILFIVGGA FVGLDKIVES RMSGGAMGFG AKVRASKDMP LSELLDRIHP QDLVKFGLIP EFVGRIPIIT HVDELDEADL VRILTEPKNA LVRQYQKLFG FEHVTLRFTP NALKAIAAKA IERKTGARGL RNVMERTMLD IMFKLPSMPN VRECLINQAV IDKGKEPVLL FGETGESPVS KSGQAQASGD SA //