ID A0A0G0KTR3_9BACT Unreviewed; 871 AA.
AC A0A0G0KTR3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=US70_C0008G0031 {ECO:0000313|EMBL:KKQ52544.1};
OS Parcubacteria group bacterium GW2011_GWD2_38_11.
OC Bacteria.
OX NCBI_TaxID=1618941 {ECO:0000313|EMBL:KKQ52544.1, ECO:0000313|Proteomes:UP000034843};
RN [1] {ECO:0000313|EMBL:KKQ52544.1, ECO:0000313|Proteomes:UP000034843}
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 -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
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:KKQ52544.1}.
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DR EMBL; LBTZ01000008; KKQ52544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0KTR3; -.
DR STRING; 1618941.US70_C0008G0031; -.
DR PATRIC; fig|1618941.3.peg.360; -.
DR Proteomes; UP000034843; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
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; IPR017730; Chaperonin_ClpB.
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 NCBIfam; TIGR03346; chaperone_ClpB; 1.
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; 2.
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|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 413..534
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 871 AA; 98376 MW; D9BA1A819009A7CA CRC64;
MDINKLTIKS QELLRKSQEY ALSFGQQQID VFHLLFSLIS QEGSIVPVIF KKIGVDTEKI
KSEAVQEVKK YPKTEIGTLG QVFITPALVQ VLEQAEKEMG HIGDDFVSTE HLLLAFLSIN
SPAKKILEGN GVFYDIVLQI LSQIRGAQRV DTPEPEGKFQ VVEKYTINLT ELARQDKLDP
VIGRDEEIRR VMQVLSRRRK NNPVLIGEAG TGKTAIAEGL AQRIASGDVP ETLKDKELIS
LDLGSLLAGA KFRGEFEDRL KAILKETEHA DGKYIMFIDE LHTLVGAGAT EGSLDASNML
KPALARGKLK TIGATTTKEY QKYIEKDAAL ERRFQPVLVS EPSALDSLAI LRGIKEKYEL
HHGIKITDGA LSAAVKLSSR YISDRFLPDK AVDLIDEAAS ALRMEIDSMP IEIDQMQRKI
RQFEIEKKAI QRDNAKDSRG KILQINKQLA ELKEKSNSLT LQWKTEKDLI TATRQHKKDI
DKLKSEAEIA ERNGELDKVA EIRYGKIPFL EKKIKDEERK LGKIQKEDSI LKEEITEEEI
ARVVSRWTGI PVSKMLEGEL EKLAYMEKEL SQRVIGQDEA IKAVSNAIRR SRAGISEENR
PIGSFIFLGP TGVGKTELAK TLAEFLFNDP KSMVRLDMSE YMESHSTAKM IGSPPGYVGY
DEGGQLTEIV RKRPYSVILF DEIEKAHPQV FNILLQILDD GRLTDSKGRI VNFKNTVIVM
TSNVGSEIIY KMESFGFQSE RKEDVVGENE MRAKVQASLR EQFKPEFLNR IDELIIFHPL
NKKVLLQITN LQLALVQKRL DEKNIKLKVS NDVKVYLTQK GFDPVYGARP LKRIIQNEIL
DELALEIIEK KIVDGDTVKV LLEKEKIVFQ K
//
