ID A0A231NZ34_9DELT Unreviewed; 432 AA. AC A0A231NZ34; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 13-NOV-2019, entry version 12. DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS01076755}; GN Name=clpX {ECO:0000256|HAMAP-Rule:MF_00175}; GN ORFNames=BCS36_12950 {ECO:0000313|EMBL:OXS27718.1}; OS Desulfovibrio sp. MES5. OC Bacteria; Proteobacteria; Deltaproteobacteria; 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. CC It directs the protease to specific substrates. Can perform CC chaperone functions in the absence of ClpP. {ECO:0000256|HAMAP- CC Rule:MF_00175, ECO:0000256|SAAS:SAAS01076750}. CC -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric CC ring that, in the presence of ATP, binds to fourteen ClpP subunits CC assembled into a disk-like structure with a central cavity, CC resembling the structure of eukaryotic proteasomes. CC {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS00561096}. CC -!- SIMILARITY: Belongs to the ClpX chaperone family. CC {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS01090919}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 Proteomes; UP000215488; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. 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:0006457; P:protein folding; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.50.30; -; 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; IPR027417; P-loop_NTPase. DR InterPro; IPR010603; Znf_CppX_C4. DR InterPro; IPR038366; Znf_CppX_C4_sf. DR PANTHER; PTHR11262; PTHR11262; 2. 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. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00175, KW ECO:0000256|SAAS:SAAS00089772, ECO:0000313|EMBL:OXS27718.1}; KW Chaperone {ECO:0000256|HAMAP-Rule:MF_00175, KW ECO:0000256|SAAS:SAAS00326717}; KW Complete proteome {ECO:0000313|Proteomes:UP000215488}; KW Hydrolase {ECO:0000313|EMBL:OXS27718.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00175, KW ECO:0000256|SAAS:SAAS00448062}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00175, KW ECO:0000256|SAAS:SAAS00089789}; KW Protease {ECO:0000313|EMBL:OXS27718.1}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS00448058}. FT DOMAIN 12 51 zf-C4_ClpX. {ECO:0000259|SMART:SM00994}. FT DOMAIN 111 331 AAA. {ECO:0000259|SMART:SM00382}. FT DOMAIN 315 409 ClpB_D2-small. {ECO:0000259|SMART: FT SM01086}. FT NP_BIND 120 127 ATP. {ECO:0000256|HAMAP-Rule:MF_00175}. FT REGION 412 432 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 417 432 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT METAL 15 15 Zinc. {ECO:0000256|HAMAP-Rule:MF_00175}. FT METAL 18 18 Zinc. {ECO:0000256|HAMAP-Rule:MF_00175}. FT METAL 37 37 Zinc. {ECO:0000256|HAMAP-Rule:MF_00175}. FT METAL 40 40 Zinc. {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 //