CLPB_COREF
ID CLPB_COREF Reviewed; 852 AA.
AC Q8FM94;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=CE2613;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(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; BA000035; BAC19423.1; -; Genomic_DNA.
DR RefSeq; WP_011076009.1; NZ_GG700685.1.
DR AlphaFoldDB; Q8FM94; -.
DR SMR; Q8FM94; -.
DR STRING; 196164.23494457; -.
DR EnsemblBacteria; BAC19423; BAC19423; BAC19423.
DR KEGG; cef:CE2613; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_11; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 44062at2; -.
DR Proteomes; UP000001409; 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..852
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191115"
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; 93445 MW; 426359F92D8BAB0B CRC64;
MSSFNPTTKT SEAMQAALQQ ASANGNPDIR PAHLLVAILD QADGVAAPVL TAAGVDPKTI
LAEAQKLVDG YPKASGSNLA NPNFNRDALN ALTASQELAG ELGDEYVSTE VLLAGIARGK
SDAADLLKGK GATYDAIKAA FQSVRGSQKV TSQDPEGQFQ ALEKYSTDLT KLAREGKIDP
VIGRDQEIRR VVQVLSRRTK NNPVLIGEPG VGKTAIVEGL ARRIVAGDVP ESLKGKTLIS
LDLGSMVAGA KYRGEFEERL KAVLDEIKGA NGEIVTFIDE LHTIVGAGAS GESAMDAGNM
IKPLLARGEL RLVGATTLNE YRKYIEKDTA LERRFQQVYV GEPSVEDTVG ILRGLKERYE
VHHGVRIQDS ALVAAAELSH RYITSRFLPD KAIDLVDEAA SRLRMEIDSS PQEIDELERI
VRRLEIEEVA LTKETDVASR ERLERLRSEL ADEREKLSEL KARWQNEKAV IDDVRKFKEE
LEALRSESDI AEREGDYGRV AELRYGRIPE LEKKIAEAEE KIGGADNSML TEEVTPEVIA
EVVSAWTGIP AGKMMQGETE KLLNMERFLG KRVVGQHEAV TAVSDAVRRS RAGVADPNRP
TGSFLFLGPT GVGKTELAKA VSEFLFDDER AMVRIDMSEY SEKHSVARLV GAPPGYVGYD
QGGQLTEAVR RRPYTTVLFD EVEKAHPDVF DILLQVLDDG RLTDGQGRTV DFRNTILILT
SNLGAGGTRE QMMDAVKMAF KPEFINRLDD IVVFDPLSQE QLASIVEIQI SQLAERLSDR
RLTLRVSDAA KLWLAERGYD PAYGARPLRR LIQQAIGDQL AKELLAGEIR DGDRVLVDVA
DGGQYLAVSR EH
