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Database: UniProt
Entry: R4K947_CLOPA
LinkDB: R4K947_CLOPA
Original site: R4K947_CLOPA 
ID   R4K947_CLOPA            Unreviewed;       867 AA.
AC   R4K947;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=Clopa_3446 {ECO:0000313|EMBL:AGK98236.1};
OS   Clostridium pasteurianum BC1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=86416 {ECO:0000313|EMBL:AGK98236.1, ECO:0000313|Proteomes:UP000013523};
RN   [1] {ECO:0000313|EMBL:AGK98236.1, ECO:0000313|Proteomes:UP000013523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC1 {ECO:0000313|EMBL:AGK98236.1,
RC   ECO:0000313|Proteomes:UP000013523};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Dunn J.,
RA   Taghavi S., Francis A., van der Lelie D., Woyke T.;
RT   "Complete sequence of chromosome of Clostridium pasteurianum BC1.";
RL   Submitted (JAN-2012) 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}.
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DR   EMBL; CP003261; AGK98236.1; -; Genomic_DNA.
DR   RefSeq; WP_015616520.1; NC_021182.1.
DR   AlphaFoldDB; R4K947; -.
DR   STRING; 86416.Clopa_3446; -.
DR   KEGG; cpas:Clopa_3446; -.
DR   PATRIC; fig|86416.3.peg.3440; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_9; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000013523; 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   Reference proteome {ECO:0000313|Proteomes:UP000013523};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..151
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          417..531
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   867 AA;  98717 MW;  8FEEF78C7FEB2919 CRC64;
     MNVERLTTKV KQAINDSQLV AVRFNHQTID SIHLFMALVS QEDGLIPNIF SKMGVDIQSL
     IRDIEGELDK MPKVLGEGAQ SSSVYATRRF EEIFIKAEKI SKDFKDSYVS SEHVMIALME
     SDKNDTVVAI LNRHNIVKKE FLKTLAEIRG NQRVETEDPE GTYDALSKYG RNLVEEAKKH
     KLDPVIGRDE EIRRVVRILS RRTKNNPVLI GEPGVGKTAI VEGLAERIIR GDIPEGLKNK
     IIFSLDMGSL IAGAKYRGEF EERLKAVLKE VQNSEGKIIL FIDEIHTIVG AGKTEGAMDA
     GNLIKPLLAR GELHCIGATT FDEYRKYIEK DKALERRFQP VIVSEPTVED SISILRGLKE
     RFEIHHGVRI HDSAIIAAAK LSDRYITDRF LPDKAIDLVD EAGAMIRTEI DSMPTEMDML
     KRKIFQMEIE KEALSKEKDE ATRERLKTLE EELSNLKEKD KEMTSKYENE KSQIIEVKEL
     KTKLDEVRGQ IEKAEREYDL NKAAELKYGT VPNLEKEIDE KEKLIKGKTE NALLKEEVTE
     EEISQIVSKW TGIPVSRLVE GERKKLLRLE DELRMRVIGQ DEAIKAVSNA VIRARAGLKD
     IKRPIGSFIF LGPTGVGKTE LAKTLARTLF DTEENIIRID MSEYMEKYSV SRLIGAPPGY
     VGYEEGGQLT EAVRRKPYSV ILFDEIEKAH DDVFNIFLQI LDDGRLTDNK GKTVDFKNCI
     IIMTSNIGSN YLLDNKGEIG IDENIKKYVM DEMKARFKPE FLNRLDDIIM FKPLSTNEIT
     KIIDIFIEDI RKRLNEKNIK LVITEEAEKL MAREGYDPIY GARPLKRYIE NTLETEIARK
     IIGGEIYEGT AVKVDGKDDN IVIEKMN
//
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