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Database: UniProt
Entry: A0A290PWR0_9LACT
LinkDB: A0A290PWR0_9LACT
Original site: A0A290PWR0_9LACT 
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
//
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