ID   A0A1V4MYY6_9BACT        Unreviewed;       415 AA.
AC   A0A1V4MYY6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   28-MAR-2018, entry version 6.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS01014625};
GN   Name=clpX {ECO:0000256|HAMAP-Rule:MF_00175};
GN   ORFNames=AVO35_00545 {ECO:0000313|EMBL:OPL19979.1};
OS   Candidatus Aegiribacteria bacterium MLS_C.
OC   Bacteria; Candidatus Aegiribacteria.
OX   NCBI_TaxID=1775674 {ECO:0000313|EMBL:OPL19979.1, ECO:0000313|Proteomes:UP000190202};
RN   [1] {ECO:0000313|EMBL:OPL19979.1, ECO:0000313|Proteomes:UP000190202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MLS_C {ECO:0000313|EMBL:OPL19979.1};
RA   Hamilton T.L., Pearson A., Macalady J.;
RT   "Carbon and sulfur cycling below the chemocline in a meromictic
RT   lake.";
RL   Submitted (DEC-2015) 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:SAAS01014585}.
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:SAAS00645732}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family.
CC       {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS00701777}.
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:OPL19979.1}.
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DR   EMBL; LQBI01000001; OPL19979.1; -; Genomic_DNA.
DR   Proteomes; UP000190202; 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; IPR001270; ClpA/B.
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   PRINTS; PR00300; CLPPROTEASEA.
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:SAAS00701780, ECO:0000313|EMBL:OPL19979.1};
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_00175,
KW   ECO:0000256|SAAS:SAAS00645733};
KW   Complete proteome {ECO:0000313|Proteomes:UP000190202};
KW   Hydrolase {ECO:0000313|EMBL:OPL19979.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00175,
KW   ECO:0000256|SAAS:SAAS00645729};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00175,
KW   ECO:0000256|SAAS:SAAS00701776};
KW   Protease {ECO:0000313|EMBL:OPL19979.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190202};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS00645735};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00175,
KW   ECO:0000256|SAAS:SAAS00645738}.
FT   DOMAIN        4     43       zf-C4_ClpX. {ECO:0000259|SMART:SM00994}.
FT   DOMAIN      105    258       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      308    402       ClpB_D2-small. {ECO:0000259|SMART:
FT                                SM01086}.
FT   ZN_FING       7     32       C4-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00175}.
FT   NP_BIND     114    121       ATP. {ECO:0000256|HAMAP-Rule:MF_00175}.
SQ   SEQUENCE   415 AA;  45541 MW;  7C1033F783363A19 CRC64;
     MAKDKKCSFC GRPIGEVNQL IQGPGVHICD ECIRYCSELV DLESEQMTRV PEILNDKLPA
     PAEIKALLDD YVVGQEQAKK VLSVAVYNHY KRLRSSREIG DVELEKSNIL LLGPTGVGKT
     LLARTLARIL DVPFAIADAT TLTEAGYVGE DVENILLRLL QVTDMDVPAA QQGIIYIDEI
     DKISRKSENP SITRDVSGEG VQQALLKIIE GTVASVPPQG GRKHPYQDNI LVDTSNILFI
     CGGAFNGLDK IIERRLRRNA MGFSAAVENG GENRRNMLSI VESHDLVKYG LVPELVGRLP
     VLVALDDLDT DDLVRVLTEP RNALVRQYQY LFELEDVRLE FADGALEEIA RRAQKAGSGA
     RGLRSVIESI LLEPMYELPG LKGIVKIVIS PEVVRGEAGP VLVKAEKKKQ SGRAG
//