ID A0A1U7EDK4_9LACT Unreviewed; 832 AA.
AC A0A1U7EDK4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:APZ49786.1};
GN ORFNames=BW721_09160 {ECO:0000313|EMBL:APZ49786.1};
OS Jeotgalibaca sp. PTS2502.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Jeotgalibaca.
OX NCBI_TaxID=1903686 {ECO:0000313|EMBL:APZ49786.1, ECO:0000313|Proteomes:UP000187137};
RN [1] {ECO:0000313|EMBL:APZ49786.1, ECO:0000313|Proteomes:UP000187137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTS2502 {ECO:0000313|EMBL:APZ49786.1,
RC ECO:0000313|Proteomes:UP000187137};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; CP019433; APZ49786.1; -; Genomic_DNA.
DR RefSeq; WP_076768055.1; NZ_CP019433.1.
DR AlphaFoldDB; A0A1U7EDK4; -.
DR STRING; 1903686.BW721_09160; -.
DR KEGG; jep:BW721_09160; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000187137; 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 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 Hydrolase {ECO:0000313|EMBL:APZ49786.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:APZ49786.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000187137};
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 425..460
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
SQ SEQUENCE 832 AA; 92696 MW; 7492A790770971EB CRC64;
MDELFTQKAS RALSLATEEA HYFKHQTIGT EHILLGLIRE TEGIAGKVLR SFHIDEAIIR
DEVEHLTGYG TARPLANQFA PMPFSPRAKK VMMYATAESQ KLGVPQVGTE HILLGTLREE
ILAVKILKNI GVDLNQLQRT LYEKIGLKDV PKSATKGAKK AQKAADGTPT LDALARDMTD
LARSGQLDPI VGRDREVKRI LQVISRRTKN NPVLVGEPGV GKTAIVEGLA QKIVNGEVPE
TLANKRLMML DMGSLVAGTK YRGEFEERMK KIIDEVYHDG NVILFIDELH TLIGAGGAEG
AIDASNILKP ALARGELQTI GATTLDEYQK YIEKDAALER RFAPITIDEP TAEETTQILK
GVRSRYEEHH HVEITDEAIE AAVALSVRYI TARRLPDKAI DLIDESAAKV RLDVTHGDTP
AGKLEDEIER LAQEKEEAIL AQDFEKAARI RKKELSRKQR LEKVRAQSSA QDEGHYTLSV
DETDVAQVVA LWTGIPVYQM EQKESERLMR LEKVLHERVI GQETAVSAVS RAIRRARSGL
KDPARPIGSF LFLGPTGVGK TELAKTLAEA MFGEEDALVR IDMSEYMEKF STSRLVGSPP
GYVGYDEGGQ LTEKIRQKPY SVILLDEVEK AHPDVFNILL QVLDDGHLTD SKGRKVDFRN
TILIMTSNLG ATALRDEKMV GFNAKDAKHD YTAMEKRIRE ELKNSFRPEF LNRIDESIVF
HSLGEKELSE IVKLMANNIV KRLEDLDIHV KVTPAAIQVI AKAGFDPEYG ARPIRRAIQK
EIEDRLSEEI LSGAIKYGDH VTLGARNGTI RMTVKEKKET PIMEEKGELV NN
//
