ID A0A1P8K9C4_9BURK Unreviewed; 866 AA.
AC A0A1P8K9C4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=RS694_08690 {ECO:0000313|EMBL:APW42598.1};
OS Rhodoferax saidenbachensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=1484693 {ECO:0000313|EMBL:APW42598.1, ECO:0000313|Proteomes:UP000186110};
RN [1] {ECO:0000313|EMBL:APW42598.1, ECO:0000313|Proteomes:UP000186110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22694 {ECO:0000313|EMBL:APW42598.1,
RC ECO:0000313|Proteomes:UP000186110};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
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; CP019239; APW42598.1; -; Genomic_DNA.
DR RefSeq; WP_029708832.1; NZ_CP019239.1.
DR AlphaFoldDB; A0A1P8K9C4; -.
DR STRING; 1484693.RS694_08690; -.
DR KEGG; rsb:RS694_08690; -.
DR eggNOG; COG0542; Bacteria.
DR Proteomes; UP000186110; 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:UP000186110};
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..490
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 866 AA; 95258 MW; 6AC6F11EABB7FF5C CRC64;
MRIEKLTTKF QEALAEAQSL ALGNDNQYIE PVHVLAAMIR TDDAPKALMN RAGVNVAGLL
ASAEAAVKKL PQVQGHEQVQ VGRDMVTLLQ ASEKEAIKRG DQFVAGELFL LAVADNKGDV
GNMARANGLT RKSLEAAIEA VRGGQNVNSA DAEEQRESLQ KYCIDLTERA RMGKLDPVIG
RDDEIRRAIQ VLQRRTKNNP VLIGEPGVGK TAIVEGLAQR IVAGEVPDSL KGKRVLSLDM
ASLLAGAKFR GEFEERLKNV LKDLAKDEGQ TIVFIDELHT MVGAGKAEGA MDAGNMLKPA
LARGELHCVG ATTLDEYRKY IEKDAALERR FQKILVGEPT VEATIAILRG LKERYEVHHG
VQITDPAIVA AAELSHRYIT DRFLPDKAID LIDEAASKIK IELDSKPEVM DKKDRRLIQL
QIEREAVKRE KDEASQKRLE LINEEITALQ REIADLDELW KAEKAQAQGS KTIMQEVEKV
RQQIKELTDK GDFNKAGELQ YGKLPELEKR LTDAQAAEAG KTKDAKHGGR AQLLRTMVGA
EEIAEVVSRA TGIPVSKMMQ GEKDKLLQME TKLHDRVVGQ DEAIAAVANA IRRSRSGLSD
PNRPTGSFLF LGPTGVGKTE LCKALAGFLF DSEEHLVRID MSEFMEKHSV ARLIGAPPGY
VGYEEGGYLT EAVRRKPYAV LLLDEIEKAH PDVFNVLLQV LDDGRLTDGQ GRTVDFKNTV
IVMTSNIGSQ LIQSMVGQDY EDVKDAVTGE LKNHFRPEFL NRIDETVVFH SLDAANIASI
AKIQLATLMA RLAKMDLTLN VSDAAVAELA KVGFDPVFGA RPLKRAIQQR IENPLSRLLL
EGKFLPKDTI SVGVDPIRAP GEFSFS
//