ID A0A0G0C9R9_9BACT Unreviewed; 876 AA.
AC A0A0G0C9R9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=UR28_C0002G0024 {ECO:0000313|EMBL:KKP40167.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWF2_33_10.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619065 {ECO:0000313|EMBL:KKP40167.1, ECO:0000313|Proteomes:UP000034183};
RN [1] {ECO:0000313|EMBL:KKP40167.1, ECO:0000313|Proteomes:UP000034183}
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:KKP40167.1}.
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DR EMBL; LBOP01000002; KKP40167.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0C9R9; -.
DR PATRIC; fig|1619065.3.peg.131; -.
DR Proteomes; UP000034183; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:KKP40167.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KKP40167.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..141
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 407..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 876 AA; 99109 MW; 21AFC29C7B86EC8A CRC64;
MDFNNFTTKA AEAVQGMISF ASKMSHQTLM PLHLLLVLLE QKDSIIPTLL QKLELKPEEI
SRQTQDIIKT YPQVSGASGP YISAEMKKVF DEAESAAGKL RDEYISTEHL FLALLDQSEV
KKILNISKDE VLKVLATVRG NQRVTDQEPE GKYQALEKYT QDFTALARQG KIDPVIGRDD
EIRRVIQILS RRTKNNPVLV GEPGTGKTAI VEGLAKKIID NDVPDVIANK KLLSLDLGAM
IAGTKYRGEF EDRLKAVLKE IEASKGDIIL FIDELHTIVG AGASEGAMDA GNLLKPALAR
GKIRTIGATT LKEYRKYIEK DAALERRFQP VNVEEPSIED AVSILRGIKE KYEVHHGVKI
RDNAVIAAVT LSDRYITDRF LPDKAIDLMD EACSVIRIEN ESKPTEIDKL HRRIRQLEIE
REALKKEKDE QSMKRLKELE KELADLKEEN SKIEMHWKNE KTFIDQIKNL SKEIDTLKEE
SIKVERMGDL QKVAEINYGK IPENEKKIKD LKSKLDDIQK DQKILREEVN EDDIAKIVAK
WTGVPVTKMM SSEITKLANM EQEIAKRVIG QKEAIKAVSN AIRRSRAGIQ EENKPIGSFI
FLGPTGVGKT ELAKALAEFM FNDDNAMIRI DMSEYGEKHS IARLIGSPPG YVGYEEGGQL
TEAVRRRPYS VVLFDEIEKA HPEVFNTFLQ VLDDGRLTDS KGRTVDFKNT IIIMTSNLGS
SEIAKNMKDS SFASNFAKAS LDKKALKDRQ EKQKNEVMQV LHKFFRPEFL NRIDDIIVFQ
HLNEDEIAQI VKLQMDKVAK RLNKKSIQIQ ISDFALKYLA SAGFDELFGA RPLKRLIQNK
ILDELALQIV EGKIKEGDKV KIDFVADEVV VRKLKM
//
