ID D7GFJ0_PROFC Unreviewed; 860 AA.
AC D7GFJ0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB 2 {ECO:0000313|EMBL:CBL57301.1};
GN Synonyms=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=PFREUD_17920 {ECO:0000313|EMBL:CBL57301.1};
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 {ECO:0000313|EMBL:CBL57301.1, ECO:0000313|Proteomes:UP000000936};
RN [1] {ECO:0000313|EMBL:CBL57301.1, ECO:0000313|Proteomes:UP000000936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1
RC {ECO:0000313|Proteomes:UP000000936};
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).
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. {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; FN806773; CBL57301.1; -; Genomic_DNA.
DR RefSeq; WP_013161658.1; NC_014215.1.
DR AlphaFoldDB; D7GFJ0; -.
DR STRING; 754252.PFREUD_17920; -.
DR KEGG; pfr:PFREUD_17920; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_11; -.
DR Proteomes; UP000000936; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Hydrolase {ECO:0000313|EMBL:CBL57301.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:CBL57301.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000936};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 407..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 860 AA; 94375 MW; C6AC5BED8862C8AC CRC64;
MDTEKLTTMS RDAVSAAVRN ALAAGNPSVE PAHLLHALLM VPENSVGPLL ESVGVDPAQI
DQRAQAAISK LPSSQGSSVA QPQLSGSFAR VLADAEIRAD KLGDSYVSTE HLLIALTSIP
SEAQTILVGA GATTEKLEEA FAGARGDRRV TSPEAEGGES ALSKYSVDLT ERAREGKLDP
VIGRDQEIRR VMQVLARRTK NNPVLIGEPG VGKTAVVEGL AQRVIAGDVP DSLRGRRVVS
LDLSSMVAGA KYRGEFEERL KAVLKEIKEA EGQIITFIDE LHTVVGAGAS GEGAMDAGNM
LKPMLARGEL RMIGATTLDE YRERIEKDPA LERRFQQVYV GEPSVEDTIA ILRGLRERYE
AHHKVRITDG ALVAAASLSH RYITNRRLPD KAIDLIDEAA SRLRMEIDSS PEEIDALRRQ
VDRLKMEQFA IKKETDAASK ARLARLEQEL ADAEEKLRLL ESRWAQEKAA LNRIGELKTQ
IDQLRIEAEK AQRVGDLATA AEIAYGRIPA LERELEQAKQ AENEEKASRM VADEVTTEDI
AEVVSAWTGI PVGKMLQGES DKLLHMEEHI GKRLIGQKRA VKAVADAVRR SRAGISDPNR
PTGSFLFLGP TGVGKTELAK SLADFLFDDE TAMIRIDMSE YSEKHSVSRL VGAPPGYVGY
EEGGQLTEAV RRRPYSVVLL DEVEKAHPDL FNILLQVLDD GRLTDGQGRT VDFRNTILIM
TSNLGSQFLA DTSLDTKAKH EAVMGVVRSA FRPEFLNRLD EIVMFDPLTL EDLTHIVDAN
LRKINARLAE RRIVIDVTDR GKEWLARNGF DPVYGARPLR RLVQSTIENQ LAIKLLAGEI
IDGAVVTFDV DPDTDQLRIG
//
