ID A0A387BDA4_9LACT Unreviewed; 867 AA.
AC A0A387BDA4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:AYG00022.1};
GN ORFNames=D7I46_02310 {ECO:0000313|EMBL:AYG00022.1};
OS Lactococcus allomyrinae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=2419773 {ECO:0000313|EMBL:AYG00022.1, ECO:0000313|Proteomes:UP000269374};
RN [1] {ECO:0000313|EMBL:AYG00022.1, ECO:0000313|Proteomes:UP000269374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1JSPR-7 {ECO:0000313|EMBL:AYG00022.1,
RC ECO:0000313|Proteomes:UP000269374};
RA Heo J., Kim S.-J., Kwon S.-W.;
RT "Genome sequencing of strain 1JSPR-7.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|ARBA:ARBA00025613}.
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|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; CP032627; AYG00022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A387BDA4; -.
DR KEGG; lact:D7I46_02310; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000269374; 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:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
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 104; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000269374};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 407..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 867 AA; 97172 MW; ABC04A6B0147F87E CRC64;
MDIEKMTTTM QESLAAAQQI AQTRHQQAIE IPHLWRIFVQ PNSFGANFYK DLGINLDEFT
SMIEQEIDKI PSVEGGSVSY GQGLSQDLFK LLNEADQIAK KMGDEYLSTE IVLLALFELK
QNPLTQYLMA HGASKQKADE AVKNLRGGDK VTSQNAEETY KALEKYGVDL VAQVKSGKQD
PVIGRDEEIR DVIRVLSRKT KNNPVLIGEP GVGKTAIVEG LAQRIVRKDV PENLKDKTIF
SLDIGALIAG AKYRGEFEER LKAVLNEVKK SDGQIILFID ELHTIVGAGK TEGSMDAGNL
LKPMLARGEL HLIGATTLDE YRKYMETDKA LERRFQKVLV TEPTVEDTIS ILRGLKERFE
IHHGVTIHDN ALVAAATLSN RYITDRFLPD KAIDLVDEAC ATIRVEMNSL PTELDQANRR
LMQLEIEEAA LKKERDDASK KRLEILHAEI AELREENNQL KSQWEAEKKE VSKISEKRNE
LEKARHDLDE AQNDGNLEKA AALRYGKIPE IEKTLKGLEE QAKSDDLTLV QESVTEEQIA
EVVGRMTGIP ITKLVEGERE KLLHLPETLH ERVVGQDEAV EAVSDAIIRA RAGIQDPNRP
LGSFLFLGPT GVGKTELAKA LAENLFDSEE HMVRIDMSEY MEKHSVSRLV GAPPGYVGYD
EGGQLTEAVR RNPYTIILLD EIEKAHPDVF NILLQVLDDG RLTDSKGVLV DFKNTVLIMT
SNVGSQYLLD NVDENGKISE ETIENVLGQL RLHFKPEFLN RIDDTILFKP LSLENIKNII
VKMTSLLVKR LEEMEVTLEL TDEVKTWIAE NAYEPAYGAR PLKRYLTKVI ENPLAKLIVG
GKILPKAKVV VNLEDNKIDF AIQTTAE
//