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Database: UniProt
Entry: A0A1E5GQY8_9ENTE
LinkDB: A0A1E5GQY8_9ENTE
Original site: A0A1E5GQY8_9ENTE 
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
//
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