ID W0J995_9BACT Unreviewed; 860 AA.
AC W0J995;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=OPIT5_26755 {ECO:0000313|EMBL:AHF93279.1};
OS Opitutaceae bacterium TAV5.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=794903 {ECO:0000313|EMBL:AHF93279.1, ECO:0000313|Proteomes:UP000003813};
RN [1] {ECO:0000313|EMBL:AHF93279.1, ECO:0000313|Proteomes:UP000003813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAV5 {ECO:0000313|EMBL:AHF93279.1};
RX PubMed=25744998;
RA Kotak M., Isanapong J., Goodwin L., Bruce D., Chen A., Han C.S.,
RA Huntemann M., Ivanova N., Land M.L., Nolan M., Pati A., Woyke T.,
RA Rodrigues J.L.;
RT "Complete Genome Sequence of the Opitutaceae Bacterium Strain TAV5, a
RT Potential Facultative Methylotroph of the Wood-Feeding Termite
RT Reticulitermes flavipes.";
RL Genome Announc. 3:0-0(2015).
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; CP007053; AHF93279.1; -; Genomic_DNA.
DR AlphaFoldDB; W0J995; -.
DR STRING; 794903.OPIT5_26755; -.
DR KEGG; obt:OPIT5_26755; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_0; -.
DR Proteomes; UP000003813; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:AHF93279.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AHF93279.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003813};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..150
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 86..113
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 416..496
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 860 AA; 96688 MW; FBDE438CCEFC437C CRC64;
MDPNQFTQMS RQAITDAQSE ARRRNNNEVD TWHLLHALLS QENGIVPAIV EKLGLTTSAL
QLALQRELDR LPRVSGSVDT SKVYVTQAVN DVLTRAEEEA KQLKDEFVSV EHLFLALIEV
AKPEAFARYL KSFGIDRRTV LKTLSELRGA QRVTTDNPEA TYNALKKYGI DLVELARKGK
MDPVIGRDDE IRRTIRILSR KTKNNPVLIG EPGVGKTAIV EGLAQRIVRG DVPEGLKDKT
IFSLDMGALV AGAKYRGEFE ERLKAVLNEV KQSDGRILLF IDELHTIVGA GKTEGAMDAG
NLLKPMLARG ELHCIGATTL DEYRQHIEKD AALERRFQPV QVEPPSVEDA ISILRGLRER
FELHHGVRIQ DNALVAAVTL SNRYISDRFL PDKAIDLVDE ACAMIRTEMD SMPQELDALT
RRALQLEIEE TALKLEKDDA SRQRLETLRK ELANTREQAD ALKRQWEREK ASIDRVRKVR
EELDAARLAM EKAERAYDLN KLAELRHGKI PQLEAELKKL ETTGAQTQLF KEEVSAEEVA
EIVAKWSGIP VTRLVESERE KLLRLGEVLH ERVIGQDEAV QLTSEAILRA RAGIKDPRRP
VGSFLFLGPT GVGKTELAKT LAETLFDSEA AMIRIDMSEY MEKHSVARLI GAPPGYVGYD
EGGQLTEAVR RKPYAVVLFD EIEKAHPDVF NVLLQVLDDG RITDSQGRTV DFKNTIIIMT
SNIGSRYLLD GVTGDTIPES VRESVMAELR KGFRPEFLNR IDETILFKPL TLEEITKIVD
LLLADLNKRL ADRRVTVELD KKAKTWAGEK GYDPVFGARP LKRFLQRQIE TRLARALITG
EVKEGSTVTF KVKNDELVMS
//
