ID CLPB_PROFC Reviewed; 866 AA.
AC Q7WSY8; D7GFV6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=PFREUD_19250;
OS Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM
OS 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=754252;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1;
RX PubMed=20668525; DOI=10.1371/journal.pone.0011748;
RA Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S.,
RA Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P.,
RA Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., Gaillardin C.,
RA Lortal S.;
RT "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a hardy
RT actinobacterium with food and probiotic applications.";
RL PLoS ONE 5:E11748-E11748(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-729, AND INDUCTION.
RX PubMed=12839748; DOI=10.1128/aem.69.7.3809-3818.2003;
RA Leverrier P., Dimova D., Pichereau V., Auffray Y., Boyaval P., Jan G.;
RT "Susceptibility and adaptive response to bile salts in Propionibacterium
RT freudenreichii: physiological and proteomic analysis.";
RL Appl. Environ. Microbiol. 69:3809-3818(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 -!- INDUCTION: By heat shock, bile salts stress and other stress
CC conditions. {ECO:0000269|PubMed:12839748}.
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=CBL57417.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FN806773; CBL57417.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ535195; CAD59396.1; -; Genomic_DNA.
DR RefSeq; WP_041704245.1; NC_014215.1.
DR AlphaFoldDB; Q7WSY8; -.
DR SMR; Q7WSY8; -.
DR STRING; 754252.PFREUD_19250; -.
DR GeneID; 61221488; -.
DR KEGG; pfr:PFREUD_19250; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_11; -.
DR Proteomes; UP000000936; 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 CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
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; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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..866
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191157"
FT DOMAIN 3..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..341
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 342..548
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 515..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..766
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 767..866
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 392..526
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"
FT CONFLICT 685
FT /note="A -> V (in Ref. 2; CAD59396)"
FT /evidence="ECO:0000305"
FT CONFLICT 692
FT /note="I -> F (in Ref. 2; CAD59396)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="A -> V (in Ref. 2; CAD59396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 866 AA; 94436 MW; 8DFEAE2139803CC7 CRC64;
MDTEKLTTMS RDAVTAAVRL ALTKGNPTAE PVHLLHAMLM VPESSVAPLL KAVGADAARV
DGAASAAIDK LPSSSGSSVA QPQLSGALAR VLADAETRAD KLGDQFVSTE HLLIALAEVD
SDAKNILASN GVTTAALEKA FNDSRGDKRI TSAESEGGES ALDKYSIDLT QRAKDGKLDP
VIGRDSEIRR VAQVLSRRTK NNPVLIGEAG VGKTAVVEGL AQRIVKGDVP DSLKGRRLVS
LDLASMVAGA KYRGEFEERL KAVLNEIKSA EGQIITFIDE LHTVVGAGAS EGSMDASNML
KPLLARGELR LIGATTLDEY REHIEKDPAL ERRFQQVYVG EPSVEDTVAI LRGLRERYEA
HHKVRITDSA LVAAAQLSHR YITGRQLPDK AIDLVDEAAS RLRMEIDSSP EEIDTLRRQV
DRLTMEQFAV EKEEDPGSKA RLARINSDLA DAKEQLRGLE ARWAAEKEGL NKVGELKTRI
DALRTEADKH TRDGDLAKAS EILYGEIPEL NKQLDEASAA EEDSQGKSMV SEEVTSDDIA
EVVSAWTGVP VGKMLEGESE KLLDMENRIG KRLVGQQAAV KAVSDAVRRS RAGISDPNRP
TGSFMFLGPT GVGKTELAKA LADFLFDDET AMVRIDMSEY MEKHSVSRLV GAPPGYVGYE
EGGQLTEAVR RRPYSVVLLD EIEKAHPDVF NILLQVLDDG RLTDGQGRTV DFRNVILIMT
SNLGSQFMAD PSMSPEERRN QVMAVVKDHF RPEFLNRLDE IVLFDELSRE DLDKIVDISL
DKLNRRLAER RISIDVSAAA REWLARTGYD PVYGARPLRR LIQTTVEDQL ARAMLAGTIS
DDQKVSVDMN QAGDGVDVKG EAPVSA
//
