CLPB_CAUVC
ID CLPB_CAUVC Reviewed; 859 AA.
AC Q9A9T4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=CC_0878;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK22863.1; -; Genomic_DNA.
DR PIR; C87358; C87358.
DR RefSeq; NP_419695.1; NC_002696.2.
DR RefSeq; WP_010918763.1; NC_002696.2.
DR AlphaFoldDB; Q9A9T4; -.
DR SMR; Q9A9T4; -.
DR STRING; 190650.CC_0878; -.
DR EnsemblBacteria; AAK22863; AAK22863; CC_0878.
DR KEGG; ccr:CC_0878; -.
DR PATRIC; fig|190650.5.peg.891; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_5; -.
DR OMA; SKMMQGE; -.
DR BioCyc; CAULO:CC0878-MON; -.
DR Proteomes; UP000001816; 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: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 3: Inferred from homology;
KW ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Repeat; Stress response.
FT CHAIN 1..859
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191103"
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..543
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 553..763
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 764..859
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 391..522
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 603..610
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 859 AA; 94060 MW; 953185451860D424 CRC64;
MNIDLYSDRA KQAVQSAQSL ALARGHQQFA PEHILKVLLE EKDGLSRALI QSAGGRPDQL
DGGVETLLAK TPRVDGAGGQ LYMKPDTARV FAEAEKSAKA AGDAFVTTER LLIAIAKEGG
EAAKLFKEAG VSAQSLETAA NAMRKGRTAD SANAEEGYEA LKRYARDLTA AARDGKLDPV
IGRDEEIRRT IQVLSRRTKN NPVLIGEPGV GKTAIVEGLA LRIVNGDVPE SLKDKKLLSL
DMGSLIAGAK YRGEFEERLK AVLGEVTAAE GSIILFIDEM HTLVGAGKGD GAMDASNLLK
PALARGELHC VGATTLDEYR KHVEKDAALA RRFQPVFVSE PTVEDTVSIL RGLKEKYEVH
HGVRISDSAI VAAATLSNRY IADRFLPDKA IDLVDEASSR VRMQIDSKPE ELDEIDRRLV
QLKIEREALS KETDAASKQR LENLEVEIDD LQFRSDEMTA RWKAEKEKVG GAAQAREALD
RLRADLANAQ RAGDFARAGQ IQYGEIPALE RRLAEAEAGD TQALTPEVVD AEQIAAVVSR
WTGVPVEKML EGEREKLLKM EDELRGRVVG QDEALEAVSD AVRRARAGLQ DPSKPIGSFL
FLGPTGVGKT ELTKSLAEFL FADEAAITRM DMSEYMEKHS VSRLIGAPPG YVGYDEGGAL
TEAIRRRPYQ VVLFDEIEKA HPDVFNVLLQ VLDDGRLTDG QGRTVDFRNT LIIMTSNLGA
EYLASQEDGE DVEAVRPMVM NTVRGHFRPE FLNRIDEIIL FKRLSRHNMG DIVRIQLQRV
EKLLADRRMA LALDAEALNW LADKGYDPVY GARPLKRVIQ KELVDPIAKK LLAGEIEDGG
VIAVGVTDGQ LSFGKAVLQ
