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Database: UniProt
Entry: A0A285CRH6_9BACI
LinkDB: A0A285CRH6_9BACI
Original site: A0A285CRH6_9BACI 
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}.
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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
//
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