ID A0A387BFH0_9LACT Unreviewed; 816 AA.
AC A0A387BFH0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:AYF99716.1};
GN ORFNames=D7I46_00585 {ECO:0000313|EMBL:AYF99716.1};
OS Lactococcus allomyrinae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=2419773 {ECO:0000313|EMBL:AYF99716.1, ECO:0000313|Proteomes:UP000269374};
RN [1] {ECO:0000313|EMBL:AYF99716.1, ECO:0000313|Proteomes:UP000269374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1JSPR-7 {ECO:0000313|EMBL:AYF99716.1,
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 -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP032627; AYF99716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A387BFH0; -.
DR KEGG; lact:D7I46_00585; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000269374; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
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 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|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:AYF99716.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AYF99716.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000269374};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 162..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 420..447
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 162..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 90384 MW; DAD70EB650373AB9 CRC64;
MKFENIEYTT TVEQILDKAA EYAYYYQYGA IESAHILAAM TTTAGSIAFS VLAGMKVDSS
DLLIDVEDLS SHVVVKREKL RFSPRAEEII QLAGLLAIHN GAKVVGTEHL LYALLQIEDG
FALQLLKLQK VNIVSVRKEL EKRTGLKIPE ARKTVTPMSK RNLAKRVSAT STTPTLDSVS
SDLTESAREG KLDPMIGREA EVERLIHILS RRTKNNPVLV GEPGVGKSAI IEGLAQRIVT
GDVPVGLMNS RIMALNMATV VAGTKFRGEF EDRLTAIVEE VSSDPDVIIF IDELHTIIGA
GGGMDSVNDA ANILKPALAR GDFQMIGATT YHEYQKYIEK DEALERRLAR INVEEPTTDE
AISILQGLKE KFEDYHRVAF TDEAIKSAVT LSVRYMTNRK LPDKAIDLLD EAAASVKISV
KNQQTKRLEL EKELTEAKKE LAESVIQLDV KASREKEKVV QKIADKINKF SVSTDKKQEV
TDKAVIAVAS TLTGVPITQM TKSESERLIK LEQELHKRVV GQEEAISAVS RAIRRARSGV
SDSRRPMGSF MFLGPTGVGK TELAKALADS VFGSEDSMIR VDMSEYMEKH STSRLIGAPP
GYVGYDEGGQ LTERVRNKPY SVILLDEVEK AHPDVFNIML QILDDGFVTD TKGRKVDFRN
TIIIMTSNLG ATALRDDKTV GFGAKDISAD YKAMKARILE ELKRHYRPEF LNRIDETIVF
HPLATHEIEQ IVKIMSKSLI KRLSEQKVHI KLTSAAAKLI AEVGFDPEYG ARPLRKALQR
EVEDVLSEQL LTGEIKSGDS ISIGVANKKI KITHII
//
