ID A0A1H9LCG6_9LACT Unreviewed; 823 AA.
AC A0A1H9LCG6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SER08663.1};
GN ORFNames=SAMN05421767_11828 {ECO:0000313|EMBL:SER08663.1};
OS Granulicatella balaenopterae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Granulicatella.
OX NCBI_TaxID=137733 {ECO:0000313|EMBL:SER08663.1, ECO:0000313|Proteomes:UP000198556};
RN [1] {ECO:0000313|EMBL:SER08663.1, ECO:0000313|Proteomes:UP000198556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15827 {ECO:0000313|EMBL:SER08663.1,
RC ECO:0000313|Proteomes:UP000198556};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; FOGF01000018; SER08663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9LCG6; -.
DR STRING; 137733.SAMN05421767_11828; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000198556; Unassembled WGS sequence.
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 InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF193; CHAPERONE PROTEIN CLPB; 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.
DR PROSITE; PS50151; UVR; 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:SER08663.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SER08663.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198556};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 2..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 432..467
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT COILED 428..474
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 823 AA; 91592 MW; 64C9BD670E5017D7 CRC64;
MTELFTDKAK NAILIGASEA IAFKHPEVGS EHLLLGLVIE PDGIAGNILR DLPIDERMIK
RAIIKIVGRG TSTKEKDPYL MPYSPRAKKL VTSASNEAKR LQAPLIGTEH LLLALLKEES
IANKILMDLE INITSLVHEI YSTIGLAKPN KPQPKVPTGG PGFKQQQTKM PQVGTPLLNS
LARDLTELAK EGKMDPVVGR HDEIKRMIQI ISRRTKNNPV LVGEPGVGKT AIVEGLAQLM
VAGKVPNDIA NKRLMMLDMG SLVAGTKYRG EFEDRMKKIL EEIYREKDVI LFIDELHTLI
GAGGAEGAID ASNILKPALA RGELQVIGAT TLDEYQKYIE KDAALERRFS SVKVNEPSTE
DTIAILKGLK QRYEEHHHIK ITDEAIEASV KLSSRYITAR RLPDKAIDLI DEAAAKARLE
TTLAPSKIEK LEAEIEKIEK EKQLAIKEQD FEVAANLRKK EMSKRKKAEK LMEEAIEHPT
EIIYNDKITT NDVSEIIAQW TGIPLKQMEK KESDRLINLE KELHKRVIGQ DEAVNAISKA
IRRARSGLKD PNRPIGSFLF LGPTGVGKTE LAKTLAEAMF GDSNALVRID MSEYMEKHAV
SRLVGSPPGY VGFDEGGQLT EKIRQKPYSV ILLDEIEKAH PDVFNILLQV LDDGHLTDTK
GRQVDFKNTI LIMTSNLGAT ALRDEKSVGF AAKNIQHDHK AMEKRIRQEL KHSFKPELLN
RIDEVIVFHK LSKEELSQIV ALMSQSIIKR LNELDINAKI TRSALGVIAE AGFDPEYGAR
PIRRALQKQV EDPLSEKLLS GEIIAGDSIT IGAKQNKIYI KHT
//
