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Database: UniProt
Entry: CLPB_PSEPK
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Original site: CLPB_PSEPK 
ID   CLPB_PSEPK              Reviewed;         854 AA.
AC   Q88Q71;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 112.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=PP_0625;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The Clp repeat (R) domain probably functions as a substrate-
CC       discriminating domain, recruiting aggregated proteins to the ClpB
CC       hexamer and/or stabilizing bound proteins. The NBD2 domain is
CC       responsible for oligomerization, whereas the NBD1 domain stabilizes the
CC       hexamer probably in an ATP-dependent manner. The movement of the
CC       coiled-coil domain is essential for ClpB ability to rescue proteins
CC       from an aggregated state, probably by pulling apart large aggregated
CC       proteins, which are bound between the coiled-coils motifs of adjacent
CC       ClpB subunits in the functional hexamer (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR   EMBL; AE015451; AAN66250.1; -; Genomic_DNA.
DR   RefSeq; NP_742786.1; NC_002947.4.
DR   RefSeq; WP_010951887.1; NC_002947.4.
DR   AlphaFoldDB; Q88Q71; -.
DR   SMR; Q88Q71; -.
DR   STRING; 160488.PP_0625; -.
DR   PaxDb; 160488-PP_0625; -.
DR   GeneID; 83677956; -.
DR   KEGG; ppu:PP_0625; -.
DR   PATRIC; fig|160488.4.peg.666; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_6; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   PhylomeDB; Q88Q71; -.
DR   BioCyc; PPUT160488:G1G01-682-MONOMER; -.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
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   InterPro; IPR002078; Sigma_54_int.
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; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW   Reference proteome; Repeat; Stress response.
FT   CHAIN           1..854
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191162"
FT   DOMAIN          3..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          6..71
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          83..146
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          159..340
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          341..545
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          555..763
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          764..854
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          391..524
FT                   /evidence="ECO:0000250"
FT   BINDING         206..213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         605..612
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   854 AA;  94862 MW;  7750EEFA06D9F534 CRC64;
     MRIDRLTSKL QLAISDAQSL AVGMDHPAIE PVHLLQALLE QQGGSIKPLL MQVGFDINGL
     RQGLVKELDQ LPKIQNPTGD VNMSQDLARL LNQADRLAQQ KGDQFISSEL VLLAAMDENS
     KLGKLLLSQG VSKKALENAI NNLRGGAAVN DANAEESRQA LDKYTVDLTK RAEEGKLDPV
     IGRDDEIRRT VQVLQRRTKN NPVLIGEPGV GKTAIAEGLA QRIINGEVPD GLKGKRLLAL
     DMGALIAGAK YRGEFEERLK SLLNELSKQE GQIILFIDEL HTMVGAGKGE GAMDAGNMLK
     PALARGELHC VGATTLNEYR QFIEKDAALE RRFQKVLVEE PSEEDTIAIL RGLKERYEVH
     HKVAITDGAI IAAAKLSHRY ITDRQLPDKA IDLIDEAASR IRMEIDSKPE VLDRLDRRLI
     QLKVESQALK KEEDEAAKKR LEKLTEEIER LEREYSDLEE IWASEKAEVQ GSAQIQQKIE
     QSRQELEAAR RKGDLNRMAE LQYGVIPDLE RSLQMVDQHG KTDNQLLRNK VTEEEIAEVV
     SKWTGIPVAK MLEGEREKLL KMEELLHQRV IGQSEAVTAV ANAVRRSRAG LSDPNRPSGS
     FLFLGPTGVG KTELCKALAE FLFDTEEAMV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
     YLTEAVRRKP YSVVLLDEVE KAHPDVFNVL LQVLEDGRLT DSHGRTVDFR NTVIVMTSNL
     GSAQIQELVG DREAQRAAVM DAVGAHFRPE FINRIDEVVV FEPLGREQIA GITEIQLGRL
     RSRLLERELS LSLSPEALDK LIAVGYDPVY GARPLKRAIQ RWIENPLAQL ILAGKFLPGT
     AITAKVEGDE IVFG
//
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