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Database: UniProt
Entry: Q9CHS9_LACLA
LinkDB: Q9CHS9_LACLA
Original site: Q9CHS9_LACLA 
ID   Q9CHS9_LACLA            Unreviewed;       816 AA.
AC   Q9CHS9;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 128.
DE   SubName: Full=ATP-dependent protease ATP-binding subunit {ECO:0000313|EMBL:AAK04740.1};
GN   Name=clpC {ECO:0000313|EMBL:AAK04740.1};
GN   ORFNames=L0222 {ECO:0000313|EMBL:AAK04740.1};
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623 {ECO:0000313|EMBL:AAK04740.1, ECO:0000313|Proteomes:UP000002196};
RN   [1] {ECO:0000313|EMBL:AAK04740.1, ECO:0000313|Proteomes:UP000002196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403 {ECO:0000313|EMBL:AAK04740.1,
RC   ECO:0000313|Proteomes:UP000002196};
RX   PubMed=11337471; DOI=10.1101/gr.GR-1697R;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; AE005176; AAK04740.1; -; Genomic_DNA.
DR   PIR; B86705; B86705.
DR   RefSeq; NP_266798.1; NC_002662.1.
DR   RefSeq; WP_010905472.1; NC_002662.1.
DR   AlphaFoldDB; Q9CHS9; -.
DR   PaxDb; 272623-L0222; -.
DR   EnsemblBacteria; AAK04740; AAK04740; L0222.
DR   KEGG; lla:L0222; -.
DR   PATRIC; fig|272623.7.peg.686; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_9; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000002196; 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   Gene3D; 4.10.860.10; UVR domain; 1.
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 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|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:AAK04740.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AAK04740.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002196};
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          151..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          420..447
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        166..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   816 AA;  90456 MW;  3F7B183CC7D56870 CRC64;
     MKFENIKYTP TLDRILEKAE EYAHQYQYGT IESAHLLAAM ATTSGSIAYS LLAGMNVDSS
     DLLIDLEDLS SHVKVKRSTL RFSPRAEEVM TAASFLAIHN NSEAVGTEHL LYALLQVEDG
     FGLQLLKLQK INIVSLRKEL EKRTGLKVPE SKKAVTPMSK RKMAKGVAEN STTPTLDSVS
     SDLTEEARLG KLDPMIGREA EIDRLIHILS RRTKNNPVLV GEPGVGKSAI IEGLAQRIVN
     GQVPIGLMNS RIMALNMATV VAGTKFRGEF EDRLTAIVEE VSSDPDVIIF IDELHTIIGA
     GGGMDSVNDA ANILKPALAR GDFQMVGATT YHEYQKYIEK DEALERRLAR INVDEPSPDE
     AIAILQGLRE KFEDYHQVKF TDQAIKSAVM LSVRYMTSRK LPDKAIDLLD EAAAAVKISV
     KNQQTKRLDL EKELTEAQEE LSEAVIKLDI KASRTKEKAV EKIADKIYKF SVKEDKRQEV
     TDQAVVAVAS TLTGVPITQM TKSESDRLIN LEKELHKRVV GQEEAISAVS RAIRRARSGV
     ADSRRPMGSF MFLGPTGVGK TELAKALADS VFGSEDNMIR VDMSEFMEKH STSRLIGAPP
     GYVGYDEGGQ LTERVRNKPY SVVLLDEVEK AHPDVFNIML QILDDGFVTD TKGRKVDFRN
     TIIIMTSNLG ATALRDDKTV GFGAKNITAD YSAMKSRILE ELKRHYRPEF LNRIDENIVF
     HSLESQEIEQ IVKIMSKSLI KRLAEQDIHV KLTPSAVKLI AEVGFDPEYG ARPLRKALQK
     EVEDLLSEQL LSGEIKAGNH VSIGASNKKI KIAQIV
//
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