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
//