ID A0A1E5GQY8_9ENTE Unreviewed; 829 AA.
AC A0A1E5GQY8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:OEG15092.1};
GN ORFNames=BCR23_09630 {ECO:0000313|EMBL:OEG15092.1};
OS Enterococcus quebecensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=903983 {ECO:0000313|EMBL:OEG15092.1, ECO:0000313|Proteomes:UP000094764};
RN [1] {ECO:0000313|EMBL:OEG15092.1, ECO:0000313|Proteomes:UP000094764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26306 {ECO:0000313|EMBL:OEG15092.1,
RC ECO:0000313|Proteomes:UP000094764};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEG15092.1}.
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DR EMBL; MIKB01000016; OEG15092.1; -; Genomic_DNA.
DR RefSeq; WP_069635585.1; NZ_MIKB01000016.1.
DR AlphaFoldDB; A0A1E5GQY8; -.
DR STRING; 903983.BCR23_09630; -.
DR PATRIC; fig|903983.4.peg.1559; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000094764; 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: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.
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:OEG15092.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:OEG15092.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 429..464
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 151..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 425..474
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 154..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 829 AA; 92485 MW; 0BC64E7ACA1727D8 CRC64;
MDELFTESAK AVLAIAQEEA KYFRHQSVGS EHLLLALVLE PNGIAGKALR QLNAEKNDIR
EEIEHLTGYG TVKGYPKGAY LPYSPRAKQV FAYAGDEAKR LGAPNIGTEH ILLGLLRDED
ILASRILLNL GLSLSKMRQL IMKKIGVTDP QMSGNVGRRR NNQAQKAAPK GTPTLDSLAR
DLTKLAREND LDPVVGRSQE VRRLIQILSR RTKNNPVLVG EPGVGKTAIA EGLAQKIVNG
EVPDDMLEKR LMMLDMGALV AGTKYRGEFE DRLKKVIDEI YQDGEVILFI DELHTLIGAG
GAEGAIDASN ILKPALARGE LQTIGATTLD EYQKYIEKDS ALERRFARVQ VDEPNPEEAE
EILKGLRPRY EEHHGVEITD DALHAAVHLS VRYINSRQLP DKAIDLMDES AAKVRLDLAD
EPSEINDLRL EISRLMQEKE EAIQSQSFES AARLRQKEKK LARKLENILL LEQKEASGYA
NRVTEQDVAN VVSQWTGVPL QQLEKKESER LLELESILHH RVVGQDEAVQ AVSRAIRRAR
SGLKDPNRPI GSFMFLGPTG VGKTELAKTL AETMFGSEDA LVRVDMSEFM EKYSTSRLIG
SPPGYVGYEE GGQLTEKIRQ KPYSVILLDE VEKAHPDVFN ILLQVLDDGH LTDSKGRKVD
FRNTILIMTS NIGATAIREE KNVGFNVKDL TKDYDAMQKR IMEELKKAFR PEFLNRVDET
VVFRSLDQAE IHEIVKIMSK SIVQRLREQD VNVKITAAAI EVIGKVGFDP EYGARPIRRA
LQKEVEDRLS EALLSGQIHL GDKVTIGASK GKITLNVKTP KQESLLQPV
//