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Database: UniProt
Entry: B1KUL4_CLOBM
LinkDB: B1KUL4_CLOBM
Original site: B1KUL4_CLOBM 
ID   B1KUL4_CLOBM            Unreviewed;       866 AA.
AC   B1KUL4;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 106.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:ACA57067.1};
GN   OrderedLocusNames=CLK_3600 {ECO:0000313|EMBL:ACA57067.1};
OS   Clostridium botulinum (strain Loch Maree / Type A3).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498214 {ECO:0000313|EMBL:ACA57067.1, ECO:0000313|Proteomes:UP000000722};
RN   [1] {ECO:0000313|EMBL:ACA57067.1, ECO:0000313|Proteomes:UP000000722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Loch Maree / Type A3 {ECO:0000313|Proteomes:UP000000722};
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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; CP000962; ACA57067.1; -; Genomic_DNA.
DR   RefSeq; WP_012344856.1; NC_010520.1.
DR   AlphaFoldDB; B1KUL4; -.
DR   KEGG; cbl:CLK_3600; -.
DR   HOGENOM; CLU_005070_4_0_9; -.
DR   OMA; GPEHILM; -.
DR   Proteomes; UP000000722; 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 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   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..496
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   866 AA;  98333 MW;  E4D46F389666FC02 CRC64;
     MDIEKLTLKV QQAINDSQLV AVKYNHQQID TIHLFSALIS QDDGLIPNIL GKMGVNIRDI
     NAETNRVLDN MPKVLGEGAQ SSSVYPTRRF EEVFVKAEQI AKDFKDSYIS VEHVLLAIMD
     VDKNNVYPIL EKFGVKKSEF LKALSAVRGS QRVDSQDPEG TYEALVKYGR NLVEEAKKHK
     LDPVIGRDEE IRRVVRILSR RTKNNPVLIG EPGVGKTAIV EGLAERIVRG DVPESLKNKI
     IFSLDMGALI AGAKYRGEFE ERLKAVLKEV QNSEGRIILF IDEIHTIVGA GKTEGSMDAG
     NLIKPMLARG ELHCIGATTF DEYRQYIEKD KALERRFQPV ITDEPTVEDT VSILRGLKER
     FEIYHGIRIH DSAIVAAAKL SSRYITDRYL PDKAIDLIDE ACAMIRTDID SMPTEMDSMK
     RKIFQLEIEK EALSKEKDVA SKERLEVLER ELSELKEKDK EMTAKYENEK SHITKIRDLK
     ERLDDVRGQM EKAEREYDLN KVAELKYGLI PALQREIEEK EKLIRENSNG NAMLKEEVTE
     QEISEIISKW TGIPVTRLVE TERQKLLQLG DQLETRVIGQ GEAVKAVTNA VIRARAGLKD
     PRKPIGSFIF LGPTGVGKTE LAKTLARTLF DTEENIIRID MSEYMEKYSV SRLIGAPPGY
     VGYEEGGQLT EAVRRKPYSV ILFDEIEKAH DDVFNIFLQI LDDGRLTDNK GKVIDFKNTI
     IIMTSNLGSN YLLDNESKEG IDESVRTRVK EALKARFKPE FLNRVDDIIM FKPLTVEDIK
     RIIDIFLDDI RKRLKDKNIQ LRITDSAKDI MAKEGYDPIY GARPLKRYIE DTIETEIAKQ
     IIAGNIYEGT TVGVDLKGES IVIERI
//
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