ID A0A2T0Q6U2_9ACTN Unreviewed; 664 AA.
AC A0A2T0Q6U2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-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=CLV72_103109 {ECO:0000313|EMBL:PRX99511.1};
OS Allonocardiopsis opalescens.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Allonocardiopsis.
OX NCBI_TaxID=1144618 {ECO:0000313|EMBL:PRX99511.1, ECO:0000313|Proteomes:UP000237846};
RN [1] {ECO:0000313|EMBL:PRX99511.1, ECO:0000313|Proteomes:UP000237846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45601 {ECO:0000313|EMBL:PRX99511.1,
RC ECO:0000313|Proteomes:UP000237846};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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:PRX99511.1}.
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DR EMBL; PVZC01000003; PRX99511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0Q6U2; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000237846; 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; 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 PRINTS; PR01217; PRICHEXTENSN.
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 Reference proteome {ECO:0000313|Proteomes:UP000237846};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 36..180
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 386..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..409
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..449
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..477
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..627
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 664 AA; 69318 MW; BB89E361AFA4FB64 CRC64;
MSIALYRKYR PATFAEVRGQ DHVTVPLRQA LRNGRINHAY LFSGPRGCGK TTSARILARS
LNCEQGPTPD PCGSCDSCVA LAPDGPGSID VIEIDAASHG GVDDARDLRE RAFFAPVSAR
FKVYIIDEAH MVTREGFNAL LKLVEEPPEH LKFVFATTEP EKVIGTIRSR THHYPFRLIP
PSTLRGLLEE ILRQEGVAYE PAALPLVVRA GAGSARDSLS ILDQLLAGSD EAGITHAGAV
SLLGYTDGGL LDEAVDAFAA RDGAAVFQTI DRVVEGGHDP RRFAADLLER LRDLLVLAAV
PEAASNGLLD VAPDEAERLR EQAGRMGAGE LTRAAEVFNA GLTEMRGATA PRLLLELMCA
RVLLPAADGG DAGVLARLER LERRAPSGPA PAAAPSGPAA VPAPPVRPAA EPASGAAAAR
QAVAESRRPP SRPAAPEPEP RPAPPEPAPR AESGGWSEPS RPSAPPPAAP PPAPAAPAGG
RLDAAAVREA WPRILETLKG QSRVAWMVVN SGGVSVAEVN GGTLVLAFER EGERRGFQAG
NRGAPLAAAI RTVLGADLRV ETVTGAPPTR SAPRAAPPEP PPPPPDPGAS WSAPPPERPA
PAAAPPAPPV ESRPEPPPPP PDPGPDVADP LHDADADDGP EPTGERLIRE ELGGELIQEF
DQAG
//
