ID A0A0G1J6T1_9BACT Unreviewed; 710 AA.
AC A0A0G1J6T1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=ATP-dependent chaperone ClpB {ECO:0000313|EMBL:KKT67351.1};
GN ORFNames=UW60_C0008G0013 {ECO:0000313|EMBL:KKT67351.1};
OS Candidatus Woesebacteria bacterium GW2011_GWA2_44_33.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618564 {ECO:0000313|EMBL:KKT67351.1, ECO:0000313|Proteomes:UP000034826};
RN [1] {ECO:0000313|EMBL:KKT67351.1, ECO:0000313|Proteomes:UP000034826}
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:KKT67351.1}.
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DR EMBL; LCIY01000008; KKT67351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1J6T1; -.
DR PATRIC; fig|1618564.3.peg.276; -.
DR Proteomes; UP000034826; 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; 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; 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; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}.
FT DOMAIN 51..196
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 453..602
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 620..709
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 710 AA; 79315 MW; 2E5499AF11747D43 CRC64;
MNNTSPSEEK GSVLEKYTVN LTIKAKSHQL DPVIGRDMEI RRVMQVLSRR TKNNPVLIGD
PGVGKTALVE GLANRIADGD VPDSIKDKDL LVLDMASVLA GASYRGEFEQ RMKGLVDEVK
KGSGKYILFI DELHTLVGAG AAEGAVDAAN ILKPALARGE LHLIGATTID EYRKYIEKDA
ALERRFQPIL VEEPGQEDTI AILRGIKEKY EIHHKLRISD DALIAAVNLS VRYLPDRFLP
DKAIDLIDEA ASSLKIEIES MPAELDLLKR KIIQIEIELA ALKKENSDSA KARRQILEKD
REDKKLQAGK VEIAWKQQKG IIEEINKIQF EIDQTKVKLD TAEKEVRLEV AAELKYGTLP
KLQTKLVEKQ KEWGSIKPED RVLQLEVDTE DIAKVISRWA GIPVTRLLDT ESSKLIHLEE
ELTKRVVGQD NAIKAVANAI RRSRAGISDE DRPIVSFLFL GPTGVGKTET AKALAEELFG
DERALIRIDM TEYTESHSIA RLIGAPPGYV GYEEGGQLTE SVRRKPYSVI LFDEIEKAHP
QIFSAFLQIL DDGRLTDGKG HTVNFKNTVI IMTSNLGGSF VTDDNLDEAD REAKMFEILR
ASFRPEFLNR IDQIITFKRL GKEEVAKIVE IQLGELSNRL ASKGFQITFD KSVSDYVALF
GFDKIYGARP VKRVLQNKIE DELALQIIEG KLQIGRNISV GIKDGRLSVK
//
