ID A0A1I6YN98_9FIRM Unreviewed; 538 AA.
AC A0A1I6YN98;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMN02910301_1502 {ECO:0000313|EMBL:SFT51956.1};
OS Lachnospiraceae bacterium XBD2001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520820 {ECO:0000313|EMBL:SFT51956.1, ECO:0000313|Proteomes:UP000199425};
RN [1] {ECO:0000313|EMBL:SFT51956.1, ECO:0000313|Proteomes:UP000199425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XBD2001 {ECO:0000313|EMBL:SFT51956.1,
RC ECO:0000313|Proteomes:UP000199425};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FPAN01000005; SFT51956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6YN98; -.
DR STRING; 1520820.SAMN02910301_1502; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000199425; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000199425};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..185
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 300..327
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 538 AA; 60074 MW; 546F620E86155C48 CRC64;
MSYMALYRKF RPQEFSEVKG QDHIVTTLKN QLKNDRIGHA YLFTGTRGTG KTTVAKLFAK
AVNCENRQED GSPCGECPSC RAIAEGRSMN VVEMDGASNN GVDHARSIIE EIAYPPTEGR
YKVYIIDEVH MLSTGAFNAL LKTIEEPPSY AIFILATTEV QKVPITILSR VQRYDFHRIS
IDTISARLAD LMEREGVDAE EKALRYVAKV GDGSMRDSLS LLDQCIAFYP DQTLTYDNVL
NVLGAVDNEV FSKILRGIMN RDVSEVIRVV DEIIIEGREI GQFVTDFTWY LRNLLLVKNI
ENMEDILDIS TDNLKVMQEE AQKLDEAVLM RYIRVLSTLS DQLRNATQKR VMTEIAMIRL
CRPQMERDND SMIDRIRSLE QQLANGVVVA AGSAGADPAT AGSAAAADLT KRPFPDARPE
EVDAVLKQWN EVLSLLDPMR RQFYQTATPT ATADGELLLV VDIAAGSDGS LAYSVLTSET
AQQEFQQVLN NFTGANVKVR VESNQTGVPA EKLYTSGPEF FKRAEEFGML VEEDDIEE
//
