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Database: UniProt/TrEMBL
Entry: F6G341_RALS8
LinkDB: F6G341_RALS8
Original site: F6G341_RALS8 
ID   F6G341_RALS8            Unreviewed;       736 AA.
AC   F6G341;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=DNA polymerase III subunit gamma/tau {ECO:0000256|RuleBase:RU364063};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU364063};
GN   Name=dnaX {ECO:0000256|RuleBase:RU364063,
GN   ECO:0000313|EMBL:AEG69474.1};
GN   OrderedLocusNames=RSPO_c02177 {ECO:0000313|EMBL:AEG69474.1};
OS   Ralstonia solanacearum (strain Po82).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=1031711 {ECO:0000313|EMBL:AEG69474.1, ECO:0000313|Proteomes:UP000007953};
RN   [1] {ECO:0000313|EMBL:AEG69474.1, ECO:0000313|Proteomes:UP000007953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Po82 {ECO:0000313|EMBL:AEG69474.1,
RC   ECO:0000313|Proteomes:UP000007953};
RX   PubMed=21685279; DOI=10.1128/JB.05384-11;
RA   Xu J., Zheng H.J., Liu L., Pan Z.C., Prior P., Tang B., Xu J.S., Zhang H.,
RA   Tian Q., Zhang L.Q., Feng J.;
RT   "Complete genome sequence of the plant pathogen Ralstonia solanacearum
RT   strain Po82.";
RL   J. Bacteriol. 193:4261-4262(2011).
CC   -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC       responsible for most of the replicative synthesis in bacteria. This DNA
CC       polymerase also exhibits 3' to 5' exonuclease activity.
CC       {ECO:0000256|RuleBase:RU364063}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00024632,
CC         ECO:0000256|RuleBase:RU364063};
CC   -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, epsilon
CC       and theta chains) that associates with a tau subunit. This core
CC       dimerizes to form the POLIII' complex. PolIII' associates with the
CC       gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC       and with the beta chain to form the complete DNA polymerase III
CC       complex. {ECO:0000256|RuleBase:RU364063}.
CC   -!- SIMILARITY: Belongs to the DnaX/STICHEL family.
CC       {ECO:0000256|ARBA:ARBA00006360, ECO:0000256|RuleBase:RU364063}.
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DR   EMBL; CP002819; AEG69474.1; -; Genomic_DNA.
DR   RefSeq; WP_014617336.1; NC_017574.1.
DR   AlphaFoldDB; F6G341; -.
DR   KEGG; rsn:RSPO_c02177; -.
DR   PATRIC; fig|1031711.3.peg.2122; -.
DR   eggNOG; COG2812; Bacteria.
DR   HOGENOM; CLU_006229_6_1_4; -.
DR   OMA; PGHIVSH; -.
DR   Proteomes; UP000007953; Chromosome.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd18137; HLD_clamp_pol_III_gamma_tau; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 3.30.300.150; DNA polymerase III, tau subunit, domain V; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR022754; DNA_pol_III_gamma-3.
DR   InterPro; IPR012763; DNA_pol_III_sug/sutau_N.
DR   InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038249; PolIII_tau_V_sf.
DR   NCBIfam; TIGR02397; dnaX_nterm; 1.
DR   PANTHER; PTHR11669:SF0; PROTEIN STICHEL-LIKE 2; 1.
DR   PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR   Pfam; PF13177; DNA_pol3_delta2; 1.
DR   Pfam; PF12169; DNA_pol3_gamma3; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU364063};
KW   DNA replication {ECO:0000256|RuleBase:RU364063};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU364063};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364063};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU364063};
KW   Transferase {ECO:0000256|RuleBase:RU364063}.
FT   DOMAIN          37..184
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          366..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..515
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   736 AA;  76263 MW;  56646DEB653F3B09 CRC64;
     MSYQVLARKW RPRDFTTLVG QEHVVKALTH ALEQQRLHHA YLFTGTRGVG KTTLSRILAK
     SLNCIGTDGQ GGITAQPCGV CRACTEIDAG RFVDYIEMDA ASNRGVDEMA QLLDRAVYAP
     TAGRFKVYMI DEVHMLTNHA FNAMLKTLEE PPEHVKFILA TTDPQKIPVT VLSRCLQFNL
     KQMPPGHIVS HLDRILGEEG IAHESNALRL LAAAAQGSMR DALSLTDQAI AYSAGEVTET
     AVRGMLGAID QSYLVRLLDA LADENGAALI EIADEMAGRS LSFSGALQDL ASLLQKIALA
     QVVPAAVQDD WPEADDIRRL AERFDAQSVQ LFYQFANLGR NELALAPDEY AGFTMTLLRM
     LAFQPGQSGG DATPPSGAGK RAVPSAGAPG GSPRPAVAAA AAAATGPVAQ AVPAASAERV
     VEEPRATYQA DRPAAAAPAA APASATPAPA SAPARRSPAL EALAAARQAS SRGARGGAAA
     PASTPAAVPA PAPAPAARPA MAGPRPNPAA APASPSPRRE PATASAPADD FAPPPWEELP
     GEFASPSLDQ IDAAFAGWET APTTRPGAQA SAGARPAQAE PPVAAPVPAK AAAPEPVAAA
     TPPDLSASGL TAFDGDWPTL AAGLPLRGLA QQLAHQSELT AVEGATVRLR VPLPALTEAG
     VVERLEAALT ERFGMPVRVA CDIGAARATA AAVDAEQRAQ RQRDAEDAIA ADPFVQALVR
     DFAATVVPGS IQPHAH
//
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