GenomeNet

Database: UniProt
Entry: A0A1P8K9C4_9BURK
LinkDB: A0A1P8K9C4_9BURK
Original site: A0A1P8K9C4_9BURK 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system