ID A0A0G0QE17_9BACT Unreviewed; 855 AA.
AC A0A0G0QE17;
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=UT36_C0005G0011 {ECO:0000313|EMBL:KKR08640.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWF2_39_17.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619067 {ECO:0000313|EMBL:KKR08640.1, ECO:0000313|Proteomes:UP000034818};
RN [1] {ECO:0000313|EMBL:KKR08640.1, ECO:0000313|Proteomes:UP000034818}
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:KKR08640.1}.
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DR EMBL; LBWM01000005; KKR08640.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0QE17; -.
DR STRING; 1619067.UT36_C0005G0011; -.
DR PATRIC; fig|1619067.4.peg.565; -.
DR Proteomes; UP000034818; 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:KKR08640.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KKR08640.1};
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 400..487
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 855 AA; 96058 MW; DB9FB04DB0318BD0 CRC64;
MDFNHFTTKA AEAVQGTMQL AGQLFHQSLG PLHLLFVLVT QSEGLVPTIL EKLEKRPKEL
AEHIRLELGK YPKIEGAAQT YLAPSLKKVF DQAESFAAQL KDEYISTEHL FLALLGQPDI
SSILNLSKEE VLRELATLRG SQRVTDAEPE SKYQVLGKYT MDFTQLAATG KIDPVIGRDE
EIRRVLQILS RRTKNNPVLV GEPGTGKTAI VEGLAKKIVD GDVPDSIKNK RLLALDLGAM
IAGTKYRGEF EDRLKALIKE IESSDGQIIL FIDELHTIVG AGASEGAMDA SNLLKPALAR
GKLRTIGATT LKEYRKYVEK DAALERRFQP VMVEEPALKD AISILRGIKE KYEVHHGVKI
RDNALVAAVN LSSRYITDRF LPDKAIDLMD EACSVLRIEN DSLPTEIDRL NRQIRQFEIE
REALKKEKDE VSKNRLKEIE RELAELNENH KRFELQWRKE KEIIDQVKGS DKEIDRLKGE
AAQAERAGNL QRVAEINYGE IPGFEKKQKE ARAQLVKSQE GGHSLLKDEI TEEDIAAVVS
RWTGVPISKM LTEETHKLAQ MEAMIKKQVI GQKKAIKAVS NAIRRSRAGI QEEGRPIGSF
MFLGPTGVGK TELTKALARF LFNDEKSMTR IDMSEYMEKH SVARLIGSPP GYVGYEEGGQ
LTEAVRRHPY NVVLFDEIEK AHPDVFNVLL QVLDDGRLTD SKGRTVDFKN TVIIMTSNLG
SDVIEKYSTD AKKQYDAVLK VLQMQFRPEF LNRVDDIIIF QYLIEEEISE IVGIQIAKVA
ERLAKKGITL EITKMARMWL ASAGFDQAFG ARPLKRVIQN KILDELALQI VEGKIMAGDK
VVVDFKGDEV VIEKK
//
