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 03-AUG-2022, entry version 105.
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; Proteobacteria; 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 PRIDE; Q88Q71; -.
DR EnsemblBacteria; AAN66250; AAN66250; PP_0625.
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 PhylomeDB; Q88Q71; -.
DR BioCyc; PPUT160488:G1G01-682-MON; -.
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 transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR Gene3D; 1.10.1780.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81923; SSF81923; 1.
DR TIGRFAMs; TIGR03346; chaperone_ClpB; 1.
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
