ID B0TBS8_HELMI Unreviewed; 884 AA.
AC B0TBS8;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 107.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=HM1_1340 {ECO:0000313|EMBL:ABZ83917.1};
OS Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Heliobacteriaceae;
OC Heliomicrobium.
OX NCBI_TaxID=498761 {ECO:0000313|EMBL:ABZ83917.1, ECO:0000313|Proteomes:UP000008550};
RN [1] {ECO:0000313|EMBL:ABZ83917.1, ECO:0000313|Proteomes:UP000008550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51547 / Ice1 {ECO:0000313|Proteomes:UP000008550};
RX PubMed=18441057; DOI=10.1128/JB.00299-08;
RA Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T.,
RA Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT "The genome of Heliobacterium modesticaldum, a phototrophic representative
RT of the Firmicutes containing the simplest photosynthetic apparatus.";
RL J. Bacteriol. 190:4687-4696(2008).
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; CP000930; ABZ83917.1; -; Genomic_DNA.
DR RefSeq; WP_012282433.1; NC_010337.2.
DR AlphaFoldDB; B0TBS8; -.
DR STRING; 498761.HM1_1340; -.
DR KEGG; hmo:HM1_1340; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_9; -.
DR OMA; GPEHILM; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000008550; 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:UP000008550};
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 REGION 864..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..114
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 417..540
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 884 AA; 99846 MW; 42A398F35F5C4D33 CRC64;
MDFNKLTQKS QEAFAAAQSL AVQQGNPEVD LEHLLTALVE QEEGLTGRLL DKMGIDSDQF
GRKIRREMER KPRISGPGVE PGRVYITPRL QRLLVKAEEE ARNLKDEYVS VEHLLLAFLD
PVLDGPLKRI FAESNLTREN LLKALTAIRG HQRVTSANPE VTYEVLEKYG RELVQEARRG
RLDPVIGRDA EIRRVIRILS RKTKNNPVLI GEPGVGKTAI VEGLALRIVR GDVPEGLKDK
AIFALDLGAL VAGAKYRGEF EERLKAVLQE VKKSDGRILL FIDELHTIVG AGKAEGAMDA
GNMLKPMLAR GELHCIGATT LDEYRKYIEK DAALERRFQP VLVDAPDVED TISILRGLKE
RFEVHHGVKI HDSALVAAAT LSNRYISDRF LPDKAIDLVD EACALIRTEI DSLPTELDEV
NRRRVQLEVE EAALAREKDR ASQERLEALR RELADLREKE DQMRARWDLE KEAIRKVQSL
REEIEKVRRE VEEAERGYNY DLNRLAELRY GRLPQLERQL AQEEAELARK SGENRLLREE
VTEEEIADIV SRWTGIPVAR LVEGEREKLL RLGEILHERV VGQEEAVQLV TDAVLRARSG
IKDPRRPIGA FIFLGPTGVG KTELAKALAQ SLFDSEENLI RIDMSEYMEK HAVSRLIGAP
PGYVGYEEGG QLTEAVRRKP YSVILFDEIE KAHPDVFNIL LQILDDGRVT DSQGRTVDFK
NTVIIMTSNI GSQHLLEGAT EDGEIRPHAR DQVMGSLRTH FRPEFLNRVD DVILFKPLTF
REITAIIDIL TRDLQKRLAQ RRISLTLTEA AKSHIAREGF DPIYGARPLK RYLQRHVETP
VARALIAGSV GDGGRIMVDE RDGRLQVEQA NEGNTADDNN RKST
//