ID   A0A231NZ34_9DELT        Unreviewed;       432 AA.
AC   A0A231NZ34;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   11-DEC-2019, entry version 13.
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. 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       ECO:0000256|SAAS:SAAS01076750}.
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       ECO:0000256|SAAS:SAAS00561096}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|HAMAP-
CC       Rule:MF_00175, ECO:0000256|SAAS:SAAS01090919}.
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}.
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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, ECO:0000256|SAAS:SAAS00326717};
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}; Protease {ECO:0000313|EMBL:OXS27718.1};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS00448058}.
FT   DOMAIN          12..51
FT                   /note="zf-C4_ClpX"
FT                   /evidence="ECO:0000259|SMART:SM00994"
FT   DOMAIN          111..331
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          315..409
FT                   /note="ClpB_D2-small"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   NP_BIND         120..127
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
FT   REGION          412..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..432
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   METAL           15
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
FT   METAL           18
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
FT   METAL           37
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
FT   METAL           40
FT                   /note="Zinc"
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
//