ID A0A285CRH6_9BACI Unreviewed; 866 AA.
AC A0A285CRH6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN05877753_103477 {ECO:0000313|EMBL:SNX70094.1};
OS Bacillus oleivorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1448271 {ECO:0000313|EMBL:SNX70094.1, ECO:0000313|Proteomes:UP000219546};
RN [1] {ECO:0000313|EMBL:SNX70094.1, ECO:0000313|Proteomes:UP000219546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC228 {ECO:0000313|EMBL:SNX70094.1,
RC ECO:0000313|Proteomes:UP000219546};
RA de Groot N.N.;
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; OAOP01000003; SNX70094.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285CRH6; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000219546; 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 104; 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:SNX70094.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SNX70094.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000219546};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..152
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 418..539
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 866 AA; 98808 MW; 754693938279B7E8 CRC64;
MMFNKMTYKL QDAIREAADV AKEKKHPAIE PEHIFYALCQ DPFGLFTEIL KQNNVSVQSA
QIGMQKALEK FPEVTGTNID QDDNQLSISY PANTLLKEGE KLQLKWDDQY LSVEHICLAI
YSLTNSRVKE ILEKAGLTAQ KTEYTIQRIR GNHKVMSQSP EDQYQALKKY GRDLVEEVKE
GRLDPVIGRD EEIRNVIRIL SRKTKNNPVL IGEPGVGKTA IVEGLAQRIV KKDVPEALKN
KTIFSLDMSS LIAGAKFRGE FEERLKAVLQ EIKKSDGQIL LFIDELHTIV GAGKTEGAMD
AGNMLKPMLA RGELHCIGAT TLDEYRKYIE KDPALERRFQ QVLVQQPDVE DTISILRGLK
ERYEVHHGVK IHDRALVSAA TLSNRYITDR FLPDKAIDLV DEACAMIRTE IDSMPSELDQ
VTRKVMQLEI EEAALLKEKD EVSQKRLEEL RNELEEYRKT AASMKEKWEI EKKQLQNIRD
KRKELEELRR ELEDAEDRYD LNRAAELRHG KIPALEKELE QLETEQTQAG SDKKLLREEV
TEEEIAQIIS RWTGIPITKL VEGEREKLLR LQDTLKQRVI GQNHAIEFVA NAILRSRSGL
KDPKRPIGSF LFLGPTGVGK TELAKALAEA LFDSEEQMIR IDMSEYMEKH AVSRLIGAPP
GYVGYEEGGQ LTEALRRQPY TVILLDEVEK AHPEVFNILL QLLDDGRITD SQGRTVDGRN
AILIMTSNIG SDIILEQQKS DHPSETDLLP ILQSFFRPEF LNRVDEIVYF NALDETVLKQ
IVEKFISDLE TRLKEREVSL TVEEEAKLFI ARNGWDPKFG ARPLKRFIQR EVENRLAKEL
IAGNIREGDQ AIVSLRSGEI TIGTEK
//