ID A0A0S7BCD7_9CHLR Unreviewed; 861 AA.
AC A0A0S7BCD7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=LARV_00681 {ECO:0000313|EMBL:GAP12941.1};
OS Longilinea arvoryzae.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Longilinea.
OX NCBI_TaxID=360412 {ECO:0000313|EMBL:GAP12941.1};
RN [1] {ECO:0000313|EMBL:GAP12941.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KOME-1 {ECO:0000313|EMBL:GAP12941.1};
RA Sekiguchi Y., Ohashi A., Matsuura N., Tourlousse M.D.;
RT "Draft Genome Sequences of Anaerolinea thermolimosa IMO-1, Bellilinea
RT caldifistulae GOMI-1, Leptolinea tardivitalis YMTK-2, Levilinea
RT saccharolytica KIBI-1,Longilinea arvoryzae KOME-1, Previously Described as
RT Members of the Anaerolineaceae (Chloroflexi).";
RL Submitted (JUL-2015) 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; DF967972; GAP12941.1; -; Genomic_DNA.
DR RefSeq; WP_075072319.1; NZ_DF967972.1.
DR AlphaFoldDB; A0A0S7BCD7; -.
DR STRING; 360412.LARV_00681; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000055060; 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 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:UP000055060};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 410..524
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 861 AA; 96259 MW; CFD548B75F6A16D8 CRC64;
MNLEKFTQKS REAVFDAQQL ARDLNHQTIE PAHLLLALIR QDEGVAPAIV TRVAGSVQAL
REELVKDLDS RPKITGASSE VGLSQTAADA LDAAERYAKG MQDDYVSTEH ILLGLTESIE
RKRMASFGLT KDAILNALKA IRGSQRVTGE NPEETYQALE KYGRDLTALA RQGKLDPVIG
RDEEIRRVIQ ILSRRTKNNP ALIGEPGVGK TAIAEGLAQR IVQGDVPEGL KKKRIMQLDL
GAMVAGAKYR GEFEERLKAA LKEIVDAQGE IIVFLDEMHT VVGAGAAEGA MDASNMLKPL
LARGELHLIG ATTLDEYRKH IEKDAALERR FQPVLIEEPS VEDTISILRG LKEKYEVHHG
VRITDPAVIA AATLSARYIP DRRLPDKAID LIDEAGARLR TEIDSKPLEL DEVDRQIMQL
EIEREALKKE KDKASKERLE KLEGELADLK ERSSQLTGRW QNEKQAIAAL REVKSQIEQT
RQEIERAERK SDLETASRLR YGTLRDLETR RTEAERHLKE LQAGGLLLKE EVDAEEIAAI
VSRWTGIPVS RLVEGETQKL LHMEEALHQR VVGQDEAVQV VSNAVRRARA GLQDPNRPIG
SFIFLGPTGV GKTELARALA EFLFDDEHAM IRIDMSEYQE KHTVSRLIGA PPGYVGYDEG
GQLTEAVRRR PYSVVLFDEI EKAHSEVFNV LLQVLDDGRL TDGQGRTVDF RNTVIIMTSN
LGNQLWEGGH TVSRDEITRV LQTQFRPEFL NRIDEIVIFH PLGREHLNGI VNIQLRRVSK
LLADRGYTLQ VSEAAREYLA DVGYNPDFGA RPLKRAIQRE LQDPLAMKVL GGEFREGDTI
LVDRGKEGLT FQIAVQGEVV E
//
