CLPB_CORDI
ID CLPB_CORDI Reviewed; 849 AA.
AC Q6NF05;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=DIP2104;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(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; BX248360; CAE50634.1; -; Genomic_DNA.
DR RefSeq; WP_010935575.1; NC_002935.2.
DR AlphaFoldDB; Q6NF05; -.
DR SMR; Q6NF05; -.
DR STRING; 257309.DIP2104; -.
DR PRIDE; Q6NF05; -.
DR EnsemblBacteria; CAE50634; CAE50634; DIP2104.
DR KEGG; cdi:DIP2104; -.
DR HOGENOM; CLU_005070_4_0_11; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 44062at2; -.
DR Proteomes; UP000002198; 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..849
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191114"
FT DOMAIN 1..147
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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..546
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 556..754
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 755..849
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 393..525
FT /evidence="ECO:0000250"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 207..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 606..613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 849 AA; 92902 MW; 9347D93A64A2C32A CRC64;
MAGFNPTTKT QEALQEALQK ASAAGNPDIR PEHLLAAILG QEDGIAIPVL RATGVDPDVV
RREAEALVAK LPKAEGANLA NPNFNRDALS VLNNAQELAG ELGDEYVSTE VLLAAVARGT
NDAAELLTKR GATYDVIKGV FPSVRGNKKV TTESPEDQFQ ALEKYSTDLT ARAREGKIDP
VIGRDQEIRR VVQVLSRRTK NNPVLIGEPG VGKTAIVEGL ARRIVAGDVP ESLKGKTLIS
LDLGSMVAGA KYRGEFEERL KAVLDEIKSA EGEIITFIDE LHTIVGAGAT GDSAMDAGNM
IKPLLARGEL RLVGATTLDE YRKYIEKDAA LERRFQQVFV GEPSVEDAVG ILRGLKERYE
VHHGVRIQDS ALVAAATLSD RYITSRFLPD KAIDLVDEAA SRLRMEIDSS PQEIDELERI
VRRLEIEEVA LSKETDAASK DRLIKLRQEL ADEREKLGEL VARWNNEKGA INKVREAKEE
LERLRSESEI AERDGDYGKV AELRYGRIPE LEKQVAEAEE HTVETTMLSE EVTPDTIAEV
VSAWTGIPAG KMLQGETEKL LNMEAELGKR VVGQSEAVVA VSDAVRRARA GVADPNRPTG
SFLFLGPTGV GKTELAKALA EFMFDDDRAM VRIDMSEYGE KHAVARLVGA PPGYVGYDQG
GQLTEAVRRR PYTVVLFDEV EKAHPDVFDI LLQVLDEGRL TDGQGRTVDF RNTVLILTSN
LGAGGTKDEM MDAVKRAFKP EFVNRLDDVV IFDPLSQEQL THIVEIQIAQ LAQRLAARRL
TLAVSDSAKL WLAERGYEPA YGARPLRRLI QQAIGDQLAK KLLSGEVRDG SEVHVDADLD
NDGLVISAS
