ID F8JQ47_STREN Unreviewed; 740 AA.
AC F8JQ47; G8WS70;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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 OrderedLocusNames=SCATT_29390 {ECO:0000313|EMBL:AEW95310.1};
OS Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925
OS / NBRC 14057 / NRRL 8057) (Streptomyces cattleya).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptantibioticus.
OX NCBI_TaxID=1003195 {ECO:0000313|EMBL:AEW95310.1, ECO:0000313|Proteomes:UP000007842};
RN [1] {ECO:0000313|Proteomes:UP000007842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057
RC {ECO:0000313|Proteomes:UP000007842};
RA Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.;
RT "Complete genome sequence of Streptomyces cattleya strain DSM 46488.";
RL Submitted (DEC-2011) 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}.
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DR EMBL; CP003219; AEW95310.1; -; Genomic_DNA.
DR RefSeq; WP_014143686.1; NC_017586.1.
DR AlphaFoldDB; F8JQ47; -.
DR STRING; 1003195.SCATT_29390; -.
DR KEGG; scy:SCATT_29390; -.
DR PATRIC; fig|1003195.11.peg.4429; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_3_1_11; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000007842; 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; 3.40.50.300; 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 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:UP000007842};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 36..180
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 412..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..461
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..544
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..696
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 75713 MW; B2EE5D2316CA1652 CRC64;
MSLALYRRYR PETFAEVIGQ EHVTDPLQQA LRNNRVNHAY LFSGPRGCGK TTSARILARC
LNCEQGPTPT PCGECRSCQD LARGGPGSID VIEIDAASHG GVDDARDLRE KAFFGPASSR
YKIYIIDEAH MVTPQGFNAL LKVVEEPPEH LKFIFATTEP EKVIGTIRSR THHYPFRLVP
PGTLRDYLAE VCGRESIPVE EGVLPLVVRA GAGSVRDSMS VMDQLLAGAG ADGVTYAMAT
ALLGYTDGAL LDDVVDAFAA GDGAAAFGVV DRVIEGGHDP RRFVADLLER LRDLVILAAV
PDAGEKGLID APADVVERMT AQAAVFGAAE LSRAADVVNA GLTEMRGATS PRLQLELICA
RVLLPAAYGD EQSVQARLDR LERQALAGGL AAGAGPAPSV GYEPVGHAPG AAAARAAVRP
QPAPEPAPAP PAPSASAPSA PAPTPAPEPR APQPPAAPEQ APAASAPGAW PTATAPAAQP
ARTPAPGAWP TATAPGSAAP SPAAEPGRRP GAWPTAAPAG GGAPVPPAQP AQPPAAPAPA
PSAAAPVGDP SRVRQMWPDI LEAVKNRRRF TWILLSQNAQ VVGFDGSTLQ VGFANPGARD
SFVNGGSEEV LRQAVGDLLN VEWKIEAVVD PSGGAGSPAA GPAGPPGGGY GGAGGPGGFG
GGAPARRPAP DRPAAPPTAA PPAPPAPAPS GPAAEEPPPV SIEDDIPQED DPDLDDTALS
GHELFVRELG ATVIEEITHD
//