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Database: UniProt
Entry: Q04GF8_OENOB
LinkDB: Q04GF8_OENOB
Original site: Q04GF8_OENOB 
ID   Q04GF8_OENOB            Unreviewed;       823 AA.
AC   Q04GF8;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   24-JAN-2024, entry version 106.
DE   SubName: Full=ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones {ECO:0000313|EMBL:ABJ56464.1};
GN   OrderedLocusNames=OEOE_0514 {ECO:0000313|EMBL:ABJ56464.1};
OS   Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Oenococcus.
OX   NCBI_TaxID=203123 {ECO:0000313|EMBL:ABJ56464.1, ECO:0000313|Proteomes:UP000000774};
RN   [1] {ECO:0000313|EMBL:ABJ56464.1, ECO:0000313|Proteomes:UP000000774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-331 / PSU-1 {ECO:0000313|Proteomes:UP000000774};
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA   Kozyavkin S., Weimer B., Mills D.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000411; ABJ56464.1; -; Genomic_DNA.
DR   RefSeq; WP_011677498.1; NC_008528.1.
DR   AlphaFoldDB; Q04GF8; -.
DR   STRING; 203123.OEOE_0514; -.
DR   KEGG; ooe:OEOE_0514; -.
DR   PATRIC; fig|203123.7.peg.524; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_9; -.
DR   OMA; SKMMQGE; -.
DR   Proteomes; UP000000774; 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: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   Hydrolase {ECO:0000313|EMBL:ABJ56464.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ABJ56464.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000774};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          423..458
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          147..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   823 AA;  91479 MW;  45BE88F42DB2E997 CRC64;
     MDNQYTASAK NVLLLAQEQA KYFKHEIVGS EHLLSALTLE KDGLASKVLQ DYNVTDDDIR
     NEIEQFTGYG THTNIKAGFL AYSPKAQEIL KNAALQAQSL GARQIGTEHL LLALLTDESI
     LSSRILASLD VRLQDLTRAI FKRIGVDPNQ QKPKSKQQGQ ANQQGTPTLD SMSRDLTALA
     SAGQIDPVVG RDQEVHRVIQ ILSRRTKNNP VLIGEPGVGK TAIAEGLAHK IATGQVPFDL
     ANKRLMALDM GALIAGTKYR GEFEDRLKKI INEIHQDGQV ILFIDELHTL IGAGGAEGAL
     DASNLLKPAL ARGELQTIGA TTFDEYQKYI ESDQALERRF ASVTIDEPSQ EDSVEILKGL
     RPRYEEHHRV NISDEAINAA VKLSSRYIAD RFLPDKAIDL MDEAAAKVRI DTVQPEDKKV
     DLERQLNGLR DQLDDAVSSG DFDQATKIRQ QEIKIRKELA VVETDNLING TKDHKYQLTV
     REKDITDVVG QQTGIPVTQL QKSESERLLH LEEILHRRVI GQNEAISAVS RAIRRARSGI
     KDPSRPIGTF LFLGPTGVGK TELAKALAEA MFDSEDNMIR VDMSEYQESY SASRLIGSAP
     GYVGYDEGGQ LTERVRNHPY SVVLLDEAEK AHPDIFNLLL QVFDDGYMTD SKGRKVDFRN
     TIIIMTSNLG ATRIRDNKHV GFGAIEPQDS YKAMSSEIQT ALKERFRPEF INRIDETIIF
     HSLSKPELHK IVELMSHGIL QRVAEQGVSI KMNKAAIDLV AQVGFDPEYG ARPIRRAFQN
     QVEDKVSDAL LSKDIRPGDS VTVGSRKGKI DLMIHHQIEK STK
//
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