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Database: UniProt
Entry: L7VTW3_THES1
LinkDB: L7VTW3_THES1
Original site: L7VTW3_THES1 
ID   L7VTW3_THES1            Unreviewed;       865 AA.
AC   L7VTW3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB2 {ECO:0000313|EMBL:AGC69023.1};
GN   Synonyms=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=Cst_c20500 {ECO:0000313|EMBL:AGC69023.1};
OS   Thermoclostridium stercorarium (strain ATCC 35414 / DSM 8532 / NCIMB 11754)
OS   (Clostridium stercorarium).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Thermoclostridium.
OX   NCBI_TaxID=1121335 {ECO:0000313|EMBL:AGC69023.1, ECO:0000313|Proteomes:UP000011220};
RN   [1] {ECO:0000313|EMBL:AGC69023.1, ECO:0000313|Proteomes:UP000011220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35414 / DSM 8532 / NCIMB 11754
RC   {ECO:0000313|Proteomes:UP000011220};
RX   PubMed=23516204; DOI=10.1128/genomeA.00073-13;
RA   Poehlein A., Zverlov V.V., Daniel R., Schwarz W.H., Liebl W.;
RT   "Complete genome sequence of Clostridium stercorarium subsp. stercorarium
RT   strain DSM 8532, a thermophilic degrader of plant cell wall fibers.";
RL   Genome Announc. 1:E0007313-E0007313(2013).
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; CP004044; AGC69023.1; -; Genomic_DNA.
DR   RefSeq; WP_015359702.1; NC_020887.2.
DR   AlphaFoldDB; L7VTW3; -.
DR   STRING; 1121335.Cst_c20500; -.
DR   KEGG; csd:Clst_1959; -.
DR   KEGG; css:Cst_c20500; -.
DR   PATRIC; fig|1121335.3.peg.2056; -.
DR   eggNOG; COG0542; Bacteria.
DR   Proteomes; UP000011220; 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:UP000011220};
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          414..528
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   865 AA;  98614 MW;  A294A942CB13CBC1 CRC64;
     MKFEKFTEKA QEAVVEAQQL ALKLDHQQVD VEHLHMALLE QEDGLIPKLL EIIGVNTQNM
     KQDLQQELDR LPKVYGTNVE QVYATRRFNQ VLLKAEDEAK RFKDEYVSVE HIYLVIINEK
     NTPSSRILAK YGVDREKLLS ALSRVRGNER VTSKNPEEGY QALQKYGRDL VELARQGKLD
     PVIGRDQEIR RVIRILSRRT KNNPVLIGEP GVGKTAVVEG LAQRILKGDV PEGLKDKTIF
     ALDMGALIAG AKFRGEFEER LKAVLNEIAK SEGRIILFID ELHTIVGAGR TDGALDAGNI
     LKPMLARGEL HCIGATTLDE YRKYIEKDAA LERRFQPVLV DQPTVEDTIS ILRGLKERFE
     IHHGVRITDN AIIACAVLSD RYISDRFLPD KAIDLMDEAA SMLRMEIDSM PYELDEINRK
     IMQYEIEYQV LSKETDINSV ERRNQLSQEI QRLKQEAESM KAQWEMEKSY IKREKELKEE
     IEKVKHEIEN AERVYDLETL AKLRYGRLPE LEKEMEECKK RLNSLGTQLL KEEVTEQEIA
     EIVAKWTGIP VAKLVEEEKQ KLLNLENILK KRVIGQDEAV KAVSDAVLRA RAGLKDLNRP
     IGSFIFLGPT GVGKTQLAKT LAEALFDSEE NLIRIDMSEY MEKHSVAKLI GAPPGYVGYE
     EGGQLTEAVR RKPYSVILFD EIEKAHPDVF NLLLQLLDDG RLTDSQGRTV NFKNAVIIMT
     SNIGSDILLE SITENGEISE TVRNMVMDSL KNYFRPEFLN RVDDIVLFKP LGRKEIYGII
     DLILNELRER LKDRNIKLEI TDEAKEVILD RAYSPSYGAR PLRRFIQKVI ETDLGRRIIA
     GEIHEGSVAT IDADNRKGEL IVKVS
//
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