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Database: UniProt
Entry: A0A268JYC3_9BACI
LinkDB: A0A268JYC3_9BACI
Original site: A0A268JYC3_9BACI 
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
//
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