CLPB_ENTFA
ID CLPB_ENTFA Reviewed; 868 AA.
AC Q831Y7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=EF_2355;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(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; AE016830; AAO82080.1; -; Genomic_DNA.
DR RefSeq; NP_816010.1; NC_004668.1.
DR RefSeq; WP_002356811.1; NZ_KE136528.1.
DR AlphaFoldDB; Q831Y7; -.
DR SMR; Q831Y7; -.
DR STRING; 226185.EF_2355; -.
DR PRIDE; Q831Y7; -.
DR EnsemblBacteria; AAO82080; AAO82080; EF_2355.
DR KEGG; efa:EF2355; -.
DR PATRIC; fig|226185.45.peg.1180; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_9; -.
DR OMA; GPEHILM; -.
DR Proteomes; UP000001415; 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..868
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191122"
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 6..70
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 84..148
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 161..342
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 343..548
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 558..770
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 771..868
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 393..526
FT /evidence="ECO:0000250"
FT BINDING 208..215
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 868 AA; 98071 MW; 75031DF16B6C652B CRC64;
MNIEKMTTTL QEAIAEAQKV AVTRQHQEID IAHLWKIFLQ PNHFGRNFYT DAGLDVDAFE
REVDNALDEY PSVAGGNVQY GQNLSQNLFH LLQEADSLRE EFQDEFLSTE IVLLALMKLK
NYRLTKYLMQ QGITEKELRK NIEEMRGGDR VTSQNQEEQY KALEKYGVDL VQQVKAGKQD
PIIGRDEEIR DVIRILSRKT KNNPVLIGEP GVGKTAIVEG LAQRIVRKDV PENLKDKTIF
SLDMGALIAG AKFRGEFEER LKAVLKEVKK SDGKIILFID EIHNIVGAGK TEGSMDAGNL
LKPMLARGEL HLIGATTLDE YRQYMEKDKA LERRFQKVLV KEPTVEDTIS ILRGLKERFE
IHHGVNIHDN ALVAAATLSD RYITDRFLPD KAIDLVDEAS ATIRVEMNSM PTELDQVTRR
LMQLEIEEAA LKKESDDASK KRLANLQEEL ADLREEANSM KMQWETEKEE VNAVSNKRAE
IDKAKHELED AENNYDLERA AVLRHGTIPQ LEHELKELEE KNAKDNVKMV QESVTENEIA
QVVGRLTGIP VTKLVEGERE KLMKLNETLH KRVIGQDEAV DAVSDAVIRS RAGLQDPNRP
LGSFLFLGPT GVGKTELAKA LAEDLFDSED HMVRIDMSEY MEKHAVSRLV GAPPGYVGYE
EGGQLTEAVR RNPYTIVLLD EIEKAHPDVF NILLQVLDDG RLTDSKGRVV DFKNTVLIMT
SNIGSQLLLE GVTPEGTIPE EVENQVMNIL KGHFKPEFLN RIDDTILFTP LSLDNVKGII
GKMTAQLAHR LEQQEIVLEI TDEAKTWIAE NGYEPAYGAR PLKRFITREV ETPLAKEIVS
GRVMPKTKVT ISLLDNQLVF ENEPIEEV
