ID A0A3S0ZDX6_9RHOB Unreviewed; 588 AA.
AC A0A3S0ZDX6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=EGN72_17620 {ECO:0000313|EMBL:RUS58746.1};
OS Pseudorhodobacter sp. E13.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudorhodobacter.
OX NCBI_TaxID=2487931 {ECO:0000313|EMBL:RUS58746.1, ECO:0000313|Proteomes:UP000267424};
RN [1] {ECO:0000313|EMBL:RUS58746.1, ECO:0000313|Proteomes:UP000267424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E13 {ECO:0000313|EMBL:RUS58746.1,
RC ECO:0000313|Proteomes:UP000267424};
RA Lee H., Kim S.;
RT "Pseudorhodobacter sp. isolated from seawater.";
RL Submitted (NOV-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:RUS58746.1}.
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DR EMBL; RPEN01000159; RUS58746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0ZDX6; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000267424; 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; 3.40.50.300; 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; IPR022107; DNA_pol_III_gamma/tau_C.
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 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; PF12362; DUF3646; 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 ECO:0000313|EMBL:RUS58746.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000267424};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:RUS58746.1}.
FT DOMAIN 43..190
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 386..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 63146 MW; FFCB50AAA428FAB3 CRC64;
MSDTAPKAYQ VLARKYRPET FADLVGQDAM VRTLKNAFAA DRIAQAFIMT GIRGTGKTTT
ARIIAKGLNC VGPDGKGGPT TEPCGQCDQC KSIMEGRHVD VMEMDAASRT GVDDIREIIA
SVAYRATSAR YKIYIIDEVH MLSNNAFNAL LKTLEEPPAH VKFIFATTEI RKVPVTVLSR
CQRFDLKRIE PEAQIALLQK IAKAEGANIS EDALALITRA AEGSARDATS LLDQAISHGA
GETTADQVRA MLGLADRGRV LDLFDMVVRG DAAAALTELS NQYADGADPM AVLRDFAEIT
HWLSVIKITP EAAEDPTIPP DERRRGLDMA GRLPMRVLTR MWQMLLKALE EVSLAPNAMM
AAEMAVIRLT HVADLPDPES LIRKLQSSQP GPVVGGAPAG GGGGGGMVHA STRLSAPAMG
PVHGATMMHG AAQGGQATAV ALAPGALESY VSFDHVVDLI RERRDMKLLV EVETTLRLAK
YAPGRIEFEP TADAPRDLAS RLATRLQGWT GARWAVTVVN AGGKATLAEE QDKERLAAEA
KAMENPLVQA VIAAFPGAKI SAMRQPELEA AFEALPEVED EWDPFEEG
//
