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Database: UniProt
Entry: A0A178IFS7_9BACT
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ID   A0A178IFS7_9BACT        Unreviewed;       388 AA.
AC   A0A178IFS7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=AW736_20000 {ECO:0000313|EMBL:OAM87949.1};
OS   Opitutaceae bacterium TSB47.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX   NCBI_TaxID=1184151 {ECO:0000313|EMBL:OAM87949.1, ECO:0000313|Proteomes:UP000078486};
RN   [1] {ECO:0000313|EMBL:OAM87949.1, ECO:0000313|Proteomes:UP000078486}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSB47 {ECO:0000313|EMBL:OAM87949.1,
RC   ECO:0000313|Proteomes:UP000078486};
RA   Wang Y., Shi Y., Qiu Z., Liu S., Yang H.;
RT   "High potential of lignocellulose degradation of a new Verrucomicrobia
RT   species.";
RL   Submitted (JAN-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}.
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:OAM87949.1}.
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DR   EMBL; LRRQ01000153; OAM87949.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178IFS7; -.
DR   STRING; 1184151.AW736_20000; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000078486; 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; 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   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:UP000078486};
KW   Transferase {ECO:0000256|RuleBase:RU364063}.
FT   DOMAIN          40..182
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   388 AA;  41885 MW;  A77DA3557DE32832 CRC64;
     MMSTAYQVIA RKWRPQTFDD VVGQDHVVRT LKNAIARNRI AHAYLLVGPR GTGKTTTARI
     FAKALNCTGG PKADFDPQDP ACLAIAEGSH LDVIEIDGAS NNGVDQVRDL RDTVQYAPAQ
     GKFKVYIIDE VHMLSTAAFN ALLKTLEEPP EHVKFVFATT DPQKVLPTIV SRCQRFDLKP
     IPAPLIIERL KKIAAEEKIN ATDEALACIA RMADGGMRDA QSIFDQMISF CGNDIGEPDV
     LDVYGLVSGE KIAALAAALA AGDHPKIIGI VDECDQSGRD LVRLLADLQA LVREALIEAI
     GQGGRTDRLG GVQMTTEQLT RLLDGLREGE GAVKLGLAEK INFEVTLLKA VEASRARAID
     SLIKELTSLA AEAPESAPAP ENSEKKKT
//
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