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Database: UniProt
Entry: A0A387BDA4_9LACT
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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
//
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