CLPB_PHOPR
ID CLPB_PHOPR Reviewed; 857 AA.
AC Q6LMY0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=PBPRA3018;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAG21346.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR378672; CAG21346.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041394500.1; NC_006370.1.
DR AlphaFoldDB; Q6LMY0; -.
DR SMR; Q6LMY0; -.
DR STRING; 298386.PBPRA3018; -.
DR PRIDE; Q6LMY0; -.
DR EnsemblBacteria; CAG21346; CAG21346; PBPRA3018.
DR KEGG; ppr:PBPRA3018; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_6; -.
DR OrthoDB; 44062at2; -.
DR Proteomes; UP000000593; Chromosome 1.
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..857
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191154"
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..545
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 555..765
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 766..857
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 391..525
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 605..612
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 857 AA; 96239 MW; B4AE18F8370B1B44 CRC64;
MRLDRFTSKF QMAIFDGQSL ALGRDHQYIE PAHLMVALLN QDGSTIRPLL TMLNVDISQL
RSRLGELLDH LPKVTGIGGE VQLSNDMGLL LNMCDKLAQK RKDKFISSEL FILAAVDDKG
SLGKLLKELG LTAAKIEQAI NQVRGGQKVD DQNAEENRQA LEKFTIDLTE RAEQGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVIIGQPGV GKTAIVEGLA QRIVNGEVPE GLRHKRVLSL
DMGSLIAGAK YRGEFEERLK SVLNELSQEE GSVILFIDEL HTMVGAGKGE GSMDAGNMLK
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVLVDE PTVEDTIAIL RGLKERYELH
HHVEITDPAI VAAARLSHRY VSDRQLPDKA IDLIDEAASS IRMQIDSKPE SLDRLERRII
QLKIEQQALS KESDAASQKR LNDICEELDV KEREYAELEE VWNAEKAALS GTQHIKSELE
QARMNMEVAR RAGDLNRMSE LQYGKIPELE KQLDLAAQAE MQEMSLLKNK VTDAEIAEVL
SKQTGIPVAK MLEGERDKLL RMEDELHQRV IGQNEAVEAV ANAIRRSRAG LSDPNRPIGS
FLFLGPTGVG KTELCKTLAN FMFDSEDNMV RIDMSEFMEK HSVARLVGAP PGYVGYEEGG
YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVIIMTSNL
GSDRIQENFG NLNYEGIKNM VLEVVSQYFR PEFINRVDET VVFHPLGQEN IKHIASIQIE
RLVNRLKEKD YELTVQESAL DFVAKAGFDP VYGARPLKRA IQQYIENPLA QEILSGKLET
GKPIDLLIED EHLVTKQ
