CLPB_CORGL
ID CLPB_CORGL Reviewed; 852 AA.
AC P53532;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=Cgl2780, cg3079;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RA Jaeger W.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(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 Necessary for survival of C.glutamicum at high temperatures.
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 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; U43536; AAB49540.1; -; Genomic_DNA.
DR EMBL; BA000036; BAC00174.1; -; Genomic_DNA.
DR EMBL; BX927156; CAF20801.1; -; Genomic_DNA.
DR RefSeq; NP_601973.1; NC_003450.3.
DR RefSeq; WP_011015370.1; NC_006958.1.
DR AlphaFoldDB; P53532; -.
DR SMR; P53532; -.
DR STRING; 196627.cg3079; -.
DR World-2DPAGE; 0001:P53532; -.
DR PRIDE; P53532; -.
DR KEGG; cgb:cg3079; -.
DR KEGG; cgl:Cgl2780; -.
DR PATRIC; fig|196627.13.peg.2711; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_11; -.
DR OMA; SKMMQGE; -.
DR Proteomes; UP000000582; 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 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Repeat; Stress response.
FT CHAIN 1..852
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191116"
FT DOMAIN 1..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 84..147
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 160..342
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 343..548
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 558..756
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 757..852
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 393..527
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 608..615
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 852 AA; 93232 MW; A00B41BC3DEB30D8 CRC64;
MSSFNPTTKT NEAMQAALQQ ASSAGNPDIR PAHLLAAILE QTDGVAAPVL MATGVDPKEI
LAEAKKLVAS YPKASGANMA NPNFNRDALN AFTAAQELAG ELGDEYVSTE VLLAGIARGK
SDAADLLTNK GATYDAIKEA FPSVRGSQRV TTQDPEGQFQ ALEKYSTDLT KLAREGKIDP
VIGRDQEIRR VVQVLSRRTK NNPVLIGEPG VGKTAIVEGL ARRIVAGDVP ESLKGKTLIS
LDLGSMVAGA KYRGEFEERL KAVLDEIKGA NGEVVTFIDE LHTIVGAGAS GESAMDAGNM
IKPLLARGEL RLVGATTLNE YRKYIEKDAA LERRFQQVYV GEPTVEDAIG ILRGLKERYE
VHHGVRIQDS ALVAAAELSN RYITSRFLPD KAIDLVDEAA SRLRMEIDSS PQEIDELERI
VRRLEIEEMA LSKESDAASK ERLEKLRSEL ADEREKLSEL KARWQNEKTA IDDVREMKEE
LEALRSESDI AERDGNYGRV AELRYGRIPE LEKQIEDAES KVEVNENAML TEEVTPDTIA
DVVSAWTGIP AGKMMQGETE KLLNMERVLG NRVVGQLEAV TAVSDAVRRS RAGVADPNRP
TGSFLFLGPT GVGKTELAKA VAEFLFDDDR AMIRIDMSEY GEKHSVARLV GAPPGYVGYD
QGGQLTEAVR RRPYTVVLFD EVEKAHPDVF DILLQVLDEG RLTDGQGRTV DFRNTILILT
SNLGAGGTRE QMMDAVKMAF KPEFVNRLDD VVIFDRLSPE QLTSIVDIQI KQLTDRLAGR
RLNLRVSDSA KAWLAERGYD PAYGARPLRR LIQQAIGDTL AKELLAGNVR DGDGVLVDVA
DGGQKLDVSR AV
