ID A0A370KAG5_9GAMM Unreviewed; 560 AA.
AC A0A370KAG5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ORFNames=DVT68_01975 {ECO:0000313|EMBL:RDI99639.1};
OS Dyella solisilvae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1920168 {ECO:0000313|EMBL:RDI99639.1, ECO:0000313|Proteomes:UP000254711};
RN [1] {ECO:0000313|EMBL:RDI99639.1, ECO:0000313|Proteomes:UP000254711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHG54 {ECO:0000313|EMBL:RDI99639.1,
RC ECO:0000313|Proteomes:UP000254711};
RA Gao Z., Qiu L.;
RT "Dyella solisilvae sp. nov., isolated from the pine and broad-leaved mixed
RT forest soil.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDI99639.1}.
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DR EMBL; QQSY01000001; RDI99639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370KAG5; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000254711; Unassembled WGS sequence.
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; IPR001270; ClpA/B.
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; IPR021029; DNA_pol_III_tau_dom-5.
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; 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 Pfam; PF12170; DNA_pol3_tau_5; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
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 ECO:0000313|EMBL:RDI99639.1};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:RDI99639.1}.
FT DOMAIN 37..178
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 364..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 60014 MW; 75F1E76D7C4AAA90 CRC64;
MSYQVLARKW RPRKFAELVG QEHVVRALTN ALDTGRMHHA YLFTGTRGVG KTTIARIFAK
SLNCERGESA DPCGECAVCT AVDAGRFVDL LEIDAASNTG VDDVREVIEN AQYAPARGRF
KVYLVDEVHM LSKPAFNALL KTLEEPPPHV KFLLATTDPQ KLPVTVLSRC LKFNLKRLLP
EQISGQMRHI LGAENIPYED AAIAELARGA DGSLRDGLSL LDQAIAYGGG SLRVDEVRAM
LGSVARGQVL GLLQALAEGS GEALMAECTR IASFSPDFGG VLDDLASVLH RLQLIQLVPG
YRPDQDGSDD DALIPLAQQL SPEDVQLYYQ IATSGRRDLA MAPDARTGFE MALLRMLAFR
PADGGGAPAE RAASPGAARA PAAAPRAAAP AANERMHMAS VAEAPRAAAP QPVTAASPAP
SAPRAPVALD ARGLPMWDVL IEQAGLRGPL GQLGQNAALR EREGQTLVLA LQPAHMHLAV
EPMVSQMEER ISQALGERIK LRFVEERGAS SETPAARAAN AREAAQSAAE RAIDEDPLVQ
SLKREFGARV VPQSIKPYEN
//
