ID A0A413I0T8_9FIRM Unreviewed; 549 AA.
AC A0A413I0T8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-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=DXA57_09255 {ECO:0000313|EMBL:RGY00646.1};
OS Blautia sp. OF03-15BH.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=2292287 {ECO:0000313|EMBL:RGY00646.1, ECO:0000313|Proteomes:UP000285119};
RN [1] {ECO:0000313|EMBL:RGY00646.1, ECO:0000313|Proteomes:UP000285119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OF03-15BH {ECO:0000313|EMBL:RGY00646.1,
RC ECO:0000313|Proteomes:UP000285119};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-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:RGY00646.1}.
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DR EMBL; QSCM01000007; RGY00646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A413I0T8; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000285119; 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; 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; 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; 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:RGY00646.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000285119};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:RGY00646.1}.
FT DOMAIN 37..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 549 AA; 61425 MW; 43A6083F826DB8FA CRC64;
MGYTALYRKF RPDSFASVKG QDHIVKTLKN QIMADRIGHA YLFCGTRGTG KTTVAKILAK
AVNCEHPVDG NPCGECETCK AIAAGTSMNV IEIDAASNNG VDNIREIREE VAYSPTTGKY
KVYIIDEVHM LSIGAFNALL KTLEEPPSYV IFILATTEAH KIPITILSRC QRYDFKRISI
NTISSRLMEL MEKENVEVEE RAIRYIAKKA DGSMRDALSL LDQCIAFYLG QKLTYDHVLD
VLGAVDTEVF SRFLREILKN DVAQVMKHLE ELVMQGRELG QFVSDFTWYL RNLLLLKSSE
ELEEVLDVSS DNLVLLKEEA GMVREDTLIR FIRVFSELSG QMKFSGSKRV LLEVALIKLC
RPQMETDEVS LLERIRMLEK KLESGMIAVR QTPPGQRMQV PDHGTGEDAF FGGLDIPGDG
NGASGMDALS FEEKAAPEDL QRVMSMWPSI VAQTTGRFKM TLISAVPKYN AAGEDNRLFV
VFSDFMGERY ANDPEAKKQL ETIISGRLGK EVEVKMVLPD EEHLAPGRLA KINVSDGLSK
IHADIEIEE
//
