CLPB_BRUSU
ID CLPB_BRUSU Reviewed; 874 AA.
AC Q7CEG6; G0K7T0; Q9AEM5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=BR1864, BS1330_I1858;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11274130; DOI=10.1128/jb.183.8.2677-2681.2001;
RA Ekaza E., Teyssier J., Ouahrani-Bettache S., Liautard J.-P., Koehler S.;
RT "Characterization of Brucella suis clpB and clpAB mutants and participation
RT of the genes in stress responses.";
RL J. Bacteriol. 183:2677-2681(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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 -!- INDUCTION: By heat and acid shock.
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; AJ251205; CAC36094.1; -; Genomic_DNA.
DR EMBL; AE014291; AAN30759.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM19176.1; -; Genomic_DNA.
DR RefSeq; WP_006190898.1; NZ_KN046804.1.
DR AlphaFoldDB; Q7CEG6; -.
DR SMR; Q7CEG6; -.
DR PRIDE; Q7CEG6; -.
DR EnsemblBacteria; AEM19176; AEM19176; BS1330_I1858.
DR GeneID; 45052820; -.
DR KEGG; bms:BR1864; -.
DR KEGG; bsi:BS1330_I1858; -.
DR PATRIC; fig|204722.22.peg.2148; -.
DR HOGENOM; CLU_005070_4_0_5; -.
DR OMA; SKMMQGE; -.
DR PhylomeDB; Q7CEG6; -.
DR PRO; PR:Q7CEG6; -.
DR Proteomes; UP000007104; Chromosome I.
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: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 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 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding; Repeat;
KW Stress response.
FT CHAIN 1..874
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191100"
FT DOMAIN 3..147
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..147
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 160..341
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 342..545
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 555..765
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 766..874
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 392..524
FT /evidence="ECO:0000250"
FT BINDING 207..214
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 874 AA; 96906 MW; 7C6AB3DF5582B447 CRC64;
MNIEKYTERV RGFIQSAQTF ALSSGNQQFT PEHILKVLID DDEGLAASLV ERAGGRVGDV
RMGLQSALEK LPKVSGGNDQ LYLSQPLAKV FSLAEELASK AGDSFVTVER LLTALAMEKS
AKTSEILSAA GVTPTALNRV INDMRKGRTA DSASAESNYD ALKKYARDLT EDARAGKLDP
VIGRDEEIRR TIQVLSRRTK NNPVLIGEPG VGKTAIAEGL ALRIVNGDVP ESLKDKQLMA
LDMGALIAGA KYRGEFEERL KAVLSEVQTA AGQIILFIDE MHTLVGAGKT DGAMDASNLL
KPALARGELH CVGATTLEEY RKYVEKDAAL ARRFQPVFVD EPTVEDTISI LRGLKEKYEQ
HHKVRVSDSA LVAAATLSNR YITDRFLPDK AIDLVDEAAS RLRMHVDSKP EELDEIDRRI
MQLKIEREAL KVETDAASKD RLQRIEKELS DLEEESAELT AKWQAEKQKL GLAADLKRQL
EEARNALAIA QRNGEFQKAG ELAYGTIPQL EKQLADAESQ ENKGSLLEET VTPDHVAQVI
SRWTGIPVDR MLEGEREKLL RMEDEIGKRV VGQGEAVQAI SKAVRRARAG LQDPNRPIGS
FIFLGPTGVG KTELTKALAS FLFQDDTAMV RIDMSEFMEK HSVSRLIGAP PGYVGYEEGG
VLTEAVRRRP YQVILFDEIE KAHPDVFNVL LQVLDDGRLT DGQGRTVDFR NTVIIMTSNL
GAEYLVNLGE NDDVETVRDD VMGVVRASFR PEFLNRVDEI ILFHRLRRED MGAIVDIQMQ
RLQYLLSDRK ITLQLEDDAR EWLANKGYDP AYGARPLKRV IQKEVQDPLA ERILLGDILD
GSLVKITAGS DRLNFRPISG AFSAAEPERE DEKA
