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}.
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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
//