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Database: UniProt
Entry: CLPB_PSESM
LinkDB: CLPB_PSESM
Original site: CLPB_PSESM 
ID   CLPB_PSESM              Reviewed;         854 AA.
AC   Q889C2;
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=PSPTO_0829;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO54370.1; -; Genomic_DNA.
DR   RefSeq; NP_790675.1; NC_004578.1.
DR   RefSeq; WP_005614629.1; NC_004578.1.
DR   AlphaFoldDB; Q889C2; -.
DR   SMR; Q889C2; -.
DR   STRING; 223283.PSPTO_0829; -.
DR   GeneID; 1182454; -.
DR   KEGG; pst:PSPTO_0829; -.
DR   PATRIC; fig|223283.9.peg.844; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_6; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   PhylomeDB; Q889C2; -.
DR   Proteomes; UP000002515; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; ISS:JCVI.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0031249; F:denatured protein binding; ISS:JCVI.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; ISS:JCVI.
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; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW   Reference proteome; Repeat; Stress response.
FT   CHAIN           1..854
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191163"
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..523
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;  95188 MW;  CE22312AD16AD0EB CRC64;
     MRIDRLTSKL QLALSDSQSL AVGLDHPAIE PAHLMQALLE QQGGSIKPLL LQVGFDINSL
     RKELSAELDR LPKIQNPTGD VNMSQDLARL LNQADRLAQQ KGDQFISSEL VLLAAMDENS
     KLGKLLLGQG VSKKALENAI NNLRGEGAVN DPNIEESRQA LDKYTVDLTK RAEEGKLDPV
     IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIAEGLA QRIINGEVPD GLRGKRLLSL
     DMGALIAGAK YRGEFEERLK SLLNELSKQE GQIILFIDEL HTMVGAGKGE GSMDAGNMLK
     PALARGELHC VGATTLNEYR QYIEKDAALE RRFQKVLVDE PSEEDTIAIL RGLKERYEVH
     HKVAITDGAI IAAAKLSHRY ITDRQLPDKA IDLIDEAASR IRMEIDSKPE VLDRLERRLI
     QLKVEAQALK KEKDEAAIKR LEKLQEEIVR LEKEYADLEE IWTSEKAEVT GSAQIQQKIE
     QSRQELEAAR RRGDLNRMAE LQYGIIPDLE RSLQMVDQHG KPENQLLRSK VTEEEIAEVV
     SKWTGIPVSK MLEGEREKLL RMETLLHNRV IGQEEAVVAV SNAVRRSRAG LSDPNRPSGS
     FMFLGPTGVG KTELCKALAE FLFDTEEAMV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
     YLTEAVRRKP YSVILLDEVE KAHSDVFNIL LQVLEDGRLT DSHGRTVDFR NTVIVMTSNL
     GSAQIQELVG DREAQRAAVM DAVSTHFRPE FVNRIDEVVI FEPLARDQIA GITDIQLGRL
     RKRLAERELT MVLSPEALDK LIAVGYDPVY GARPLKRAIQ RWIENPLAQL ILSGGFEPGS
     SITGKVVDDE IVFG
//
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