ID A0A318KGB7_9FIRM Unreviewed; 578 AA.
AC A0A318KGB7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=DES51_11568 {ECO:0000313|EMBL:PXX76089.1};
OS Dielma fastidiosa.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Dielma.
OX NCBI_TaxID=1034346 {ECO:0000313|EMBL:PXX76089.1, ECO:0000313|Proteomes:UP000247612};
RN [1] {ECO:0000313|EMBL:PXX76089.1, ECO:0000313|Proteomes:UP000247612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC118 {ECO:0000313|EMBL:PXX76089.1,
RC ECO:0000313|Proteomes:UP000247612};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-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:PXX76089.1}.
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DR EMBL; QJKH01000015; PXX76089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318KGB7; -.
DR STRING; 1034346.GCA_000313565_03118; -.
DR Proteomes; UP000247612; Unassembled WGS sequence.
DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR GO; GO:0008408; F:3'-5' exonuclease activity; 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; IPR001270; ClpA/B.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR004622; DNA_pol_HolB.
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 NCBIfam; TIGR00678; holB; 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; 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|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU364063};
KW Reference proteome {ECO:0000313|Proteomes:UP000247612};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..178
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 578 AA; 65778 MW; F4EDE89E006F4ACC CRC64;
MAYKALYRTY RPTNFDEVAG QQHIVKTLQN AVRQNKIAHA YLFCGPRGTG KTTIAKIFAK
AINCEADDNK PCLKCSNCLA VQDGSHPDVI EIDAASNNGV DEVRELIEKV KYAPLKGKYK
VYIIDEVHMM SAGAFNALLK TIEEPPEHVI FIFATTEPQK VLPTIISRCQ RYDFTKVSIN
DMKQRLITVL NYENIKYDDE AIRLICQLAD GGVRDAFSIL DQVIAYAQDE VQVHHVNEIY
GIMTVKEKIE LLQMVGDKDA LNLMNKVSAL IEKGIDIKRC TMDLIDILKE TVIHDYTQDS
SMLKILADDE IHSAKINKST KERLKMIEYL MDAYDKYRFA ANVGSYFEVC LLNMIEPEVQ
TTVQTPIKSE ERKNVSRETS KPVQTIPEPE AFYMPEPEFM DMPQEIVVER KAKPMVVREA
KSAKPLKDEM ILRLLVGANK AFKQADSDKM KALDDYYHDP AWAKEANLLR GSKIVASGEQ
YVILSVDNQA IANQINELDS DNKFLSFMNL VLSKSKKVFA ITATHQSEVI KEFVRRQKNG
TLPEPMSFEI EEEKKTEKSD REIVTDLFGE ENLIIKED
//
