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Database: UniProt
Entry: A0A0G1DTX3_9BACT
LinkDB: A0A0G1DTX3_9BACT
Original site: A0A0G1DTX3_9BACT 
ID   A0A0G1DTX3_9BACT        Unreviewed;       854 AA.
AC   A0A0G1DTX3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Chaperone ClpB {ECO:0000313|EMBL:KKT01085.1};
GN   ORFNames=UV79_C0020G0005 {ECO:0000313|EMBL:KKT01085.1};
OS   candidate division TM6 bacterium GW2011_GWF2_43_17.
OC   Bacteria; Candidatus Dependentiae.
OX   NCBI_TaxID=1619085 {ECO:0000313|EMBL:KKT01085.1, ECO:0000313|Proteomes:UP000034620};
RN   [1] {ECO:0000313|EMBL:KKT01085.1, ECO:0000313|Proteomes:UP000034620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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:KKT01085.1}.
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DR   EMBL; LCFV01000020; KKT01085.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1DTX3; -.
DR   STRING; 1619085.UV79_C0020G0005; -.
DR   PATRIC; fig|1619085.3.peg.378; -.
DR   Proteomes; UP000034620; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          3..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          406..493
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   854 AA;  96303 MW;  616DE5EE48D26011 CRC64;
     MDLQQKLTDA AYELLSSAAQ DAKNRNNQFV TALHLFSQTL TTPFCQSLYQ FTPQELGNIR
     RETERELAHL PRVQGSQELH ADQTLEQILL KAQNEAHSLN DSYISLEHLL LAFSQTTVLP
     QALAALLSQT KFSRTSLLDH MRILRKGKTV NEKNAEQQYE ILKKYCQNIT EQARQGKLDP
     VIGRHEEIRR VIQILSRRTK NNPVLIGEPG VGKTAIVEGI AQRIINNDVP ESLKKSTLYS
     LDLGLLIAGA KYQGEFEERL KGVLKAIEES DEHIILFIDE LHMLVGTGAT GGGMDASNLL
     KPALARGILH CIGATTIQEY KKYIEKDAAL ERRFQKVLVE EPSVEDALSI LRGLKERYEL
     HHGIQIKDQA LVAAVTLSAQ NIPDRFLPDK AIDLIDEAAS MVKMSIDSQP EQIDKLARKI
     RQLEIEKIAL SKEQDDASKK RLEELEKELA NLKEEHKILI QQWQAERAPL EKIKMLKEQI
     EQAQIQFQQA ERRGDYSKAS EIKYGKLMQL EKDLATETGK LNNGNKQLIK DVVDEHDVAK
     VLARWTGIPV EKLQTNETEK LLQIEPILKK RVIGQSAAIT KVAHAIQMHR AGLADPNRPI
     GSFLFLGPTG VGKTEVARTL ADYLFNDEHK LVRIDMSEYM EKHAVARLIG APPGYVGYEE
     GGQLTEAVRR HPFSVVLFDE IEKAHPDVFN IFLQILDEGT LTDGQGRHIS FKNTIIIMTS
     NIGSEIILEA PTITSEIESS VTNLLNKQFR PEFLNRIDAI VFFNRLSQKD LVQIATIQAN
     KIIKQLAQQH ITLQVEESVV KKLADLGYQP EFGARPLKRI VQSHITVPLA QEILKNPDKK
     TFTTQLKEDL ITTT
//
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