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Database: UniProt
Entry: R6BCF8_9CLOT
LinkDB: R6BCF8_9CLOT
Original site: R6BCF8_9CLOT 
ID   R6BCF8_9CLOT            Unreviewed;       865 AA.
AC   R6BCF8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=BN491_00229 {ECO:0000313|EMBL:CDA51017.1};
OS   Clostridium sp. CAG:138.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262775 {ECO:0000313|EMBL:CDA51017.1, ECO:0000313|Proteomes:UP000017905};
RN   [1] {ECO:0000313|EMBL:CDA51017.1, ECO:0000313|Proteomes:UP000017905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:138 {ECO:0000313|Proteomes:UP000017905};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-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}.
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:CDA51017.1}.
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DR   EMBL; CBBZ010000022; CDA51017.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6BCF8; -.
DR   STRING; 1262775.BN491_00229; -.
DR   Proteomes; UP000017905; 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:UP000017905};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          443..501
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   865 AA;  96893 MW;  E7A01444A4EB9663 CRC64;
     MNANKMTQKT LETLQQAQSL AEERRNTQVG QIHVFHALLD DPDDLNAQLM ASMGISTDEL
     RAAIDTELDK QATFGSSGGG QVYMTPELNS VLTRAEEEAK RMGDSFVSVE HIMLGLIERA
     DYVVKPLLKR FGIVRDKYLE ALKAVRGNSR VNSDNPESTY DVLNKYGQDL TELARAQKLD
     PVIGRDNEIR SVIRILSRKT KNNPCLIGEP GVGKTAIAEG LALRIVRGDV PDNLKDRRLF
     ALDMGSLVAG AKYRGEFEER LKAVLNEIKR SEGRIIMFID ELHTIVGAGK TDGAMDAGNI
     LKPMLARGEL HCIGATTLDE YRKYIEKDAA LERRFQPVTV AEPSVEDTIA ILRGLKERYE
     VYHGVKIHDS ALIAAATLSD RYISDRFLPD KAIDLVDEAC ALIKTEMNSM PSEMDEISRE
     IMRLEIEETA LTGDNDEHTQ EHLVEIRREL AEKRDKFNNM KARWDNERNA ISKVQQLRER
     IEQVNADIAR AENEYDLNRA AQLKYGELPG LQKELQKEEA LAANRENSLL RDHVSSEEIA
     KIVARWTGIP VSKLMESERK KLLRLDSQLH KRIVGQDDAV QRVCDAILRS RAGIQNPNRP
     IGSFLFLGPT GVGKTELCKA LAEALFDDER SMVRIDMSEY MEQYSVSRLI GAPPGYVGYD
     EGGQLTEAVR RKPYAVLLFD EVEKAHPDVL NVLLQVLDDG RITDGQGRTV DFKNTIIILT
     SNIGSDLILN SMAKDGRITT ETEELLHKLL RTKFRPEFIN RLDEIVFFNA LSDADMHGIV
     DLLIADLAKR LQANRLNLSV SESAKAAIIK NGADPLFGAR PLKRYIQGHI ESLLARFIIE
     NSPEEGSTLT VDADEKGSFI IGQKQ
//
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