ID L7ZW10_9BACI Unreviewed; 864 AA.
AC L7ZW10;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:AGE21284.1};
GN ORFNames=GHH_c07440 {ECO:0000313|EMBL:AGE21284.1};
OS Geobacillus sp. GHH01.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1233873 {ECO:0000313|EMBL:AGE21284.1, ECO:0000313|Proteomes:UP000011251};
RN [1] {ECO:0000313|EMBL:AGE21284.1, ECO:0000313|Proteomes:UP000011251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GHH01 {ECO:0000313|EMBL:AGE21284.1};
RX PubMed=23618712;
RA Wiegand S., Rabausch U., Chow J., Daniel R., Streit W.R., Liesegang H.;
RT "Complete Genome Sequence of Geobacillus sp. Strain GHH01, a Thermophilic
RT Lipase-Secreting Bacterium.";
RL Genome Announc. 1:E0009213-E0009213(2013).
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; CP004008; AGE21284.1; -; Genomic_DNA.
DR RefSeq; WP_015374145.1; NC_020210.1.
DR AlphaFoldDB; L7ZW10; -.
DR KEGG; ggh:GHH_c07440; -.
DR PATRIC; fig|1233873.3.peg.763; -.
DR HOGENOM; CLU_005070_4_0_9; -.
DR Proteomes; UP000011251; Chromosome.
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..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 84..111
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 412..526
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 864 AA; 97338 MW; 2840387FC50F553B CRC64;
MDASRLTEKL QEALMAAQSL AKERHHQQLD VEHLLIALLE QEGGLAPRLF ALCGADRAQA
IRWLQDRLRQ KPEVHGADGQ LYVAPALARL LEEAENEAKR MQDEYISVEH VLLALSHGAE
PVARQLASFG LTEEALVEAV RKVRGNQRVT SPHPEATYEA LAKYGRDLVA EAKAGKIDPV
IGRDSEIRRI IRILSRKTKN NPVLIGEPGV GKTAIVEGLA QRIVRKDVPE GLKDKTIFAL
DMSALVAGAK FRGEFEERLK AVLNEIKKSD GRIILFIDEL HTIVGAGRAE GAIDAGNMLK
PMLARGELRC IGATTLDEYR QYIEKDPALE RRFQQVLVQE PSVEDTISIL RGLKERYEVH
HGVKIHDRAL VAAAVLSDRY ISDRFLPDKA IDLVDEACAT IRTEMESMPS ELDEVMRRVM
QLEIEEAALS KETDEASRER LAALQKELAD LREKANAMKA QWQKEKEALD RVRRLREALE
RAKRELEEAE NEYDLNKAAE LRHGRIPQLE KQLKQLEQEI SEQSEGKLLR EEVTEEEIAE
IVSRWTGIPL TRLVEGEREK LLRLHELLHR RVIGQDEAVE LVADAVLRAR AGMKDPNRPI
GSFLFLGPTG VGKTELAKAL AEALFDSEEQ LIRLDMSEYM EKHAVSRLIG APPGYVGYEE
GGQLTEAVRR KPYSVLLFDE IEKAHPDVFN ILLQLLDDGR LTDSQGRTVD FKNTVVIMTS
NIGSPLLLEN KQGDIDEETR KQVFDQLRAH FRPEFLNRID DIVLFKPLSM NEVKGIVEKF
ARELSARLAD RHIELVLTEA AKQYIAEAGF DPVYGARPLK RFMQKQIETP LAKELIAGRV
KDYSTVTVDV DNGQIVIRPS AQTS
//
