ID A0A290PWR0_9LACT Unreviewed; 814 AA.
AC A0A290PWR0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=AAA domain-containing protein {ECO:0000313|EMBL:QIW54496.1};
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:MBW9330905.1};
GN ORFNames=D9N18_05980 {ECO:0000313|EMBL:MBW9330905.1}, GU335_01195
GN {ECO:0000313|EMBL:QIW55312.1}, GU336_10340
GN {ECO:0000313|EMBL:QIW54496.1};
OS Lactococcus raffinolactis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1366 {ECO:0000313|EMBL:QIW54496.1, ECO:0000313|Proteomes:UP000501945};
RN [1] {ECO:0000313|EMBL:MBW9330905.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=3042 {ECO:0000313|EMBL:MBW9330905.1};
RA Meslier V., Dridi B., Almeida M., Abraham A.-L., Pons N., Renault P.;
RT "Lactococcus raffinolactis, an underestimated dairy Lactococci revealed by
RT genomic and metagenomic analysis.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QIW54496.1, ECO:0000313|Proteomes:UP000501945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lr_19_4S {ECO:0000313|EMBL:QIW55312.1,
RC ECO:0000313|Proteomes:UP000501197}, and Lr_19_5
RC {ECO:0000313|EMBL:QIW54496.1, ECO:0000313|Proteomes:UP000501945};
RA Ybazeta G., Ross M., Brabant-Kirwan D., Saleh M., Dillon J.A., Splinter K.,
RA Nokhbeh R.;
RT "Whole genome sequences of Lactococcus raffinolactis strains isolated from
RT sewage.";
RL Submitted (DEC-2019) 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}.
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DR EMBL; RCHZ01000006; MBW9330905.1; -; Genomic_DNA.
DR EMBL; CP047616; QIW54496.1; -; Genomic_DNA.
DR EMBL; CP050534; QIW55312.1; -; Genomic_DNA.
DR STRING; 1348633.GCA_001591765_01370; -.
DR Proteomes; UP000501197; Chromosome.
DR Proteomes; UP000501945; Chromosome.
DR Proteomes; UP000709450; 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; 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 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:MBW9330905.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Hydrolase {ECO:0000313|EMBL:MBW9330905.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:MBW9330905.1};
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"
SQ SEQUENCE 814 AA; 89669 MW; E0E5D43010EAEA57 CRC64;
MTQNYTHILE DILKTARVFA AGNGYDYAET SHVLAGMLSS NDSFGQNILT DHDVTIEMAL
DEIEQHQLPE KMQTVQNIQF SPKVEQLLLE ADALAAQNHL AETGSEHLLY VILTDDDNVA
KKLLELNKIK ITEIVKDLIE LGNMNVKKIA KKAVTPMGKR DIASGVAATS ITPTLDSVAR
DVTEDARQGR IDPMIGRDKE IERVIHILSR RTKNNPVLVG EPGVGKSAII EGLAQRMIDG
NIPANMQGVR LMSLNIANVV AGTKFRGEFE DRMTAIVDEV SQDANTIVFV DELHTIVGAG
GGTDSVTDAS NIMKPALARG EFQLIGATTF NEYQKYIEKD AALERRFAKV TVEEPSSDES
IVILQGLQSK FEAFHQVNFD ADAVKAAVQL SVRYMPSRRL PDKAIDLLDE AAAAVKISAK
NNLSEQSKLD KKASQLDEQL QEAIINQDFV LAKSLNKDLQ KLEAKREKLT VKTKSSRVSE
GDVFAVVSNL TGVPVTQMSQ SEMTRLINLE KELHKRVIGQ SEAVTAVASA IRRSRSGISD
DRRPMGSFMF LGPTGVGKTE LAKALAETVF GDENSMIRID MSEYMEKFNT SRLVGAPPGY
VGYDEGGQLT EQVRNKPYAV VLFDEAEKAH PDVFNLLLQI LDDGFITDGK GRKVDFRNTI
IIMTSNLGAT SLRDDKTVGF GAANASTDYV AMKSRILEEL KKRYRPEFLN RIDESIVFHP
LSEQELSDIV KIMAKPLIKR LAERHITLKL SATAYQLIAK NGFEPEYGAR PIRKALEKKL
ENPLSDKILS GEIKAGNSVT VGVSKGELTI KVID
//