CLPB_PSEAE
ID CLPB_PSEAE Reviewed; 854 AA.
AC Q9HVN5; Q79JA9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=PA4542;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PA14;
RX PubMed=14983043; DOI=10.1073/pnas.0304622101;
RA He J., Baldini R.L., Deziel E., Saucier M., Zhang Q., Liberati N.T.,
RA Lee D., Urbach J., Goodman H.M., Rahme L.G.;
RT "The broad host range pathogen Pseudomonas aeruginosa strain PA14 carries
RT two pathogenicity islands harboring plant and animal virulence genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2530-2535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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}.
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; AY273871; AAP81264.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07930.1; -; Genomic_DNA.
DR PIR; D83077; D83077.
DR RefSeq; NP_253232.1; NC_002516.2.
DR RefSeq; WP_003094682.1; NZ_QZGE01000004.1.
DR AlphaFoldDB; Q9HVN5; -.
DR SMR; Q9HVN5; -.
DR STRING; 287.DR97_1845; -.
DR PaxDb; Q9HVN5; -.
DR PRIDE; Q9HVN5; -.
DR EnsemblBacteria; AAG07930; AAG07930; PA4542.
DR GeneID; 879457; -.
DR KEGG; pae:PA4542; -.
DR PATRIC; fig|208964.12.peg.4753; -.
DR PseudoCAP; PA4542; -.
DR HOGENOM; CLU_005070_4_0_6; -.
DR InParanoid; Q9HVN5; -.
DR OMA; SKMMQGE; -.
DR PhylomeDB; Q9HVN5; -.
DR BioCyc; PAER208964:G1FZ6-4635-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; 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 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_0000191161"
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; 95006 MW; 4EDECFC3F877B793 CRC64;
MRIDRLTSKL QLALSDAQSL AVGHDHPAIE PVHLLSALLE QQGGSIKPLL MQVGFDIAAL
RSGLNKELDA LPKIQSPTGD VNLSQDLARL LNQADRLAQQ KGDQFISSEL VLLAAMDENT
RLGKLLLGQG VSRKALENAV ANLRGGEAVN DPNVEESRQA LDKYTVDMTK RAEEGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPD GLKDKRLLAL
DMGALIAGAK FRGEFEERLK AVLNELGKQE GRVILFIDEL HTMVGAGKAE GAMDAGNMLK
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVLVDE PSEEDTIAIL RGLKERYEVH
HGVSITDGAI IAAAKLSHRY ITDRQLPDKA IDLIDEAASR IRMEIDSKPE ELDRLDRRLI
QLKIEREALK KEDDEATRKR LAKLEEDIVK LEREYADLEE IWKSEKAEVQ GSAQIQQKIE
QAKQEMEAAR RKGDLESMAR IQYQTIPDLE RSLQMVDQHG KTENQLLRNK VTDEEIAEVV
SKWTGIPVSK MLEGEREKLL RMEQELHRRV IGQDEAVVAV SNAVRRSRAG LADPNRPSGS
FLFLGPTGVG KTELCKALAE FLFDTEEALV RIDMSEFMEK HSVARLIGAP PGYVGFEEGG
YLTEAIRRKP YSVVLLDEVE KAHPDVFNIL LQVLEDGRLT DSHGRTVDFR NTVVVMTSNL
GSAQIQELAG DREAQRAAVM DAVNAHFRPE FINRIDEVVV FEPLAREQIA GIAEIQLGRL
RKRLAERELS LELSQEALDK LIAVGFDPVY GARPLKRAIQ RWIENPLAQL ILAGKFAPGA
SISAKVEGDE IVFA
