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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//