ID A0A268JYC3_9BACI Unreviewed; 864 AA.
AC A0A268JYC3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:PAE39378.1};
GN ORFNames=CHI06_16860 {ECO:0000313|EMBL:PAE39378.1};
OS Bacillus sp. 7884-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2021693 {ECO:0000313|EMBL:PAE39378.1, ECO:0000313|Proteomes:UP000216214};
RN [1] {ECO:0000313|EMBL:PAE39378.1, ECO:0000313|Proteomes:UP000216214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7884-1 {ECO:0000313|EMBL:PAE39378.1,
RC ECO:0000313|Proteomes:UP000216214};
RA Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT "Isolation and whole genome analysis of endospore-forming bacteria from
RT heroin.";
RL Submitted (JUL-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 -!- 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:PAE39378.1}.
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DR EMBL; NPDD01000142; PAE39378.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268JYC3; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000216214; 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: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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000216214};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..150
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 416..533
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 864 AA; 97055 MW; 1AAD6D59A4094EED CRC64;
MDLNRMTERL QNGIIDAQSL AIKSSHQEVD ELHLFLTLLR QEDSLLKTIL EKADIPTVSV
EKALQNALNK KPQVTGSGAE HGKLYITSKL QRLFVSAEEF ASKFSDDFIS IEHILLAACY
DKDAEMGKIV ISNGKTAEYI LSAIKEIRGN QRVTSQNPEA VYDALNKYGR DLVAEVKAGK
LDPVIGRDAE IRHVIRILSR KTKNNPVLIG EPGVGKTAIV EGLVQRIVRK DVPEGLKDKT
IFSLDMSALI AGAKFRGEFE ERLKAVLNEV KKSEGQILLF IDELHTIVGA GKTDGAMDAG
NMLKPMLARG ELHCIGATTL DEHRKYIEKD PALERRFQQV LVQEPNVEDT ISILRGLKER
FEVHHGVKIH DHALVAAATL SDRYITDRFL PDKAIDLVDE ACALIRTEID SMPTELDEVT
RRVMQLEIEE AALRKEQDDA SKKRLDSLLK ELAELKVQAN SKKAQWLHEK QGIQKLQEKR
EQLEKLRREL QQAEDKYDLN RAAELRHGQI PLAEKELLAL ESATANNERL LREEVTGEEI
SNIVSRWTGI PLSKLVEGER EKLLRLESIL HERVIGQNEA VQLVSDAVLR ARAGIKDPNR
PIGSFLFLGP TGVGKTELAK ALAEALFDSE EQIIRIDMSE YMEKHAVSRL IGAPPGYVGY
EEGGQLTEAV RRRPYSVILM DEIEKAHPEV FNILLQALDD GRITDSQGRT VDFKNTVIIM
TSNIGSHFLL ERNENEVEIS EATREKVLAQ LKSHFRPEFL NRVDETILFK PLSLTEIKDI
VVKMMKELQS RLKEQNIEIT ISDGAKEFIA VNGFDPIYGA RPLKRFIQRN IETKLARAII
AGKVIDHSVV SVTIENGELT ISIG
//