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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//