ID A5HYV3_CLOBH Unreviewed; 866 AA.
AC A5HYV3;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:CAL81962.1};
GN Synonyms=htpM {ECO:0000313|EMBL:CAL81962.1};
GN OrderedLocusNames=CBO0409 {ECO:0000313|EMBL:CAL81962.1};
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL81962.1, ECO:0000313|Proteomes:UP000001986};
RN [1] {ECO:0000313|EMBL:CAL81962.1, ECO:0000313|Proteomes:UP000001986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC {ECO:0000313|Proteomes:UP000001986};
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(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; AM412317; CAL81962.1; -; Genomic_DNA.
DR RefSeq; YP_001252953.1; NC_009495.1.
DR AlphaFoldDB; A5HYV3; -.
DR GeneID; 5184664; -.
DR KEGG; cbo:CBO0409; -.
DR PATRIC; fig|413999.7.peg.413; -.
DR HOGENOM; CLU_005070_4_0_9; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; 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 Reference proteome {ECO:0000313|Proteomes:UP000001986};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251};
KW Stress response {ECO:0000256|RuleBase:RU362034,
KW ECO:0000313|EMBL:CAL81962.1}.
FT DOMAIN 3..150
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 416..537
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 866 AA; 98327 MW; 8928718B6DA59843 CRC64;
MNIEKLTLKV QQAINDSQLV AVKYNHQQID TIHLFSALIS QDDGLIPNIL GKMGVNIRDI
NAETNRVLDN MPKVLGEGAQ SSSVYPTRRF EEVFVRAEQI AKDFKDSYIS VEHVLLAIMD
VDRNTVLPIL EKFGVKKSEF LKALSAVRGS QRVDNQDPEG TYEALVKYGR NLVEEAKKHK
LDPVIGRDEE IRRVVRILSR RTKNNPVLIG EPGVGKTAIV EGLAERIVRG DVQESLKNKI
IFSLDMGALI AGAKYRGEFE ERLKAVLKEV QNSEGRIILF IDEIHTIVGA GKTEGSMDAG
NLIKPMLARG ELHCIGATTF DEYRQYIEKD KALERRFQPV ITDEPTIEDT VSILRGLKER
FEIYHGIRIH DSAIVAAAKL SSRYITDRYL PDKAIDLIDE ACAMIRTDID SMPTEMDSMK
RKIFQLEIEK EALSKEKDVA SKERLEVLEK ELSELKEKDK EMTAKYENEK SHITKIRDLK
EKLDDVRGQM EKAEREYDLN KVAELKYGLI PALQREIEEK EKLIKENSNG NAMLKEEVTE
QEISEIISKW TGIPVTRLVE TERQKLLQLG DQLETRVIGQ GEAVKAVTNA VIRARAGLKD
PRKPIGSFIF LGPTGVGKTE LAKTLARTLF DTEENIIRID MSEYMEKYSV SRLIGAPPGY
VGYEEGGQLT EAVRRKPYSV ILFDEIEKAH DDVFNIFLQI LDDGRLTDNK GKVIDFKNTI
IIMTSNLGSN YLLDNESKEG IDESIRTRVK EALKARFKPE FLNRVDDIIM FKPLTVEDIK
RIIDIFLDDI RKRLKDKNIQ LKITDSAKDI MAKEGYDPIY GARPLKRYIE DTIETEIAKQ
IIVGNIYEGT TVGVDLKGES IVIERI
//
