ID Q5M6G1_STRT2 Unreviewed; 816 AA.
AC Q5M6G1;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE SubName: Full=ATP-dependent Clp protease, ATP-binding subunit {ECO:0000313|EMBL:AAV59806.1};
GN Name=clpC {ECO:0000313|EMBL:AAV59806.1};
GN OrderedLocusNames=stu0077 {ECO:0000313|EMBL:AAV59806.1};
OS Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=264199 {ECO:0000313|EMBL:AAV59806.1, ECO:0000313|Proteomes:UP000001170};
RN [1] {ECO:0000313|EMBL:AAV59806.1, ECO:0000313|Proteomes:UP000001170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-250 / LMG 18311 {ECO:0000313|Proteomes:UP000001170};
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(2004).
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; CP000023; AAV59806.1; -; Genomic_DNA.
DR RefSeq; WP_011225298.1; NC_006448.1.
DR AlphaFoldDB; Q5M6G1; -.
DR STRING; 264199.stu0077; -.
DR GeneID; 66898008; -.
DR KEGG; stl:stu0077; -.
DR PATRIC; fig|264199.4.peg.80; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_9; -.
DR BRENDA; 3.4.21.92; 5956.
DR Proteomes; UP000001170; 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};
KW Hydrolase {ECO:0000313|EMBL:AAV59806.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AAV59806.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001170};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..152
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
SQ SEQUENCE 816 AA; 90284 MW; B2A31A2A494D0ED8 CRC64;
MTIYSRKMQA IFHRAQLEAE RFESPFLETW HVLLAMVEVP GSVAYLTFTD FEDRIHSEEI
ETAAVLAMEK RPKDLSESDI IDLRAQSPAL EAMLQEAQGI ASVTGAVEVG SEHVLMAFLL
HKDLMVCRLL EVAGFQYKDD SDKPRIIDLR RSLERNAGLS KQDLKAIHDL RKPKKSKASA
NFANMMQPPQ SSTGELADYT KDLTALAESG NLDPIIGRDE EISRMIQVLS RKTKNNPVLV
GEAGVGKTAL ALGLAQRIAS GEVPFELADM RILELDMMSV VAGTRFRGDF EERMNQIIDE
IEADGKIILF IDELHTIIGS GSGIDSTLDA ANILKPALAR GTLHMVGATT QAEYQKHIEK
DAALSRRFAK ITIEEPSVSE AIDILNGLRS SYEDYHRVTI TDAAVETAVK AAHRYLTSKN
LPDSAIDLLD EASATVQVRI KKEAKREITP LDEALISGDI GAAVKQYKAN QKAKFPKPAL
VDADQIMQTL SRLSGIPVEK MTQTDSKRYL NLESELHKRV IGQDEAVSAI SRAIRRNQSG
IRTGKRPIGS FMFLGPTGVG KTELAKALAE VLFDDESALL RFDMSEYMEK FAASRLNGAP
PGYVGYDEGG ELTEKVRNKP YSVLLFDEIE KAHPDIFNVL LQVLDDGVLT DSRGRKVDFS
NTIIIMTSNL GATALRDDKT VGFGAQTISH NHQAMQARIM EELKKSYRPE FINRIDEKVV
FHSLEEEQLH DIVKIMVKPL ISALADKGIS LKFQPAALKH LAKDGYDIEM GARPLRRTIQ
TQVEDKLSEL LLGGQVVSGQ TLKIGCSKDK LTFTVV
//
