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Database: UniProt
Entry: A0A2N0FYQ8_9FLAO
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ID   A0A2N0FYQ8_9FLAO        Unreviewed;       611 AA.
AC   A0A2N0FYQ8;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-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=B0O79_3257 {ECO:0000313|EMBL:PKA99545.1};
OS   Flavobacteriaceae bacterium MAR_2009_75.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1250285 {ECO:0000313|EMBL:PKA99545.1, ECO:0000313|Proteomes:UP000232536};
RN   [1] {ECO:0000313|EMBL:PKA99545.1, ECO:0000313|Proteomes:UP000232536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mar_2009_75 {ECO:0000313|EMBL:PKA99545.1,
RC   ECO:0000313|Proteomes:UP000232536};
RA   Teeling H.;
RT   "A large-scale integrated study on North Sea by COGITO (Coastal Microbe
RT   Genomic & Taxonomic Observatory).";
RL   Submitted (NOV-2017) 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:PKA99545.1}.
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DR   EMBL; PHTZ01000001; PKA99545.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N0FYQ8; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000232536; 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; 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   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   Transferase {ECO:0000256|RuleBase:RU364063}.
FT   DOMAIN          38..168
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          386..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   611 AA;  69715 MW;  391DB8217C02B9DF CRC64;
     MEHFVVSARK YRPQTFKDVV GQQAITNTLT NAIEHNHLAQ ALLFCGPRGV GKTTCARILA
     KKINQDGTER EDEDFAFNIF ELDAASNNSV DDIRNLIDQV RIPPQVGKYK VYIIDEVHML
     SQSAFNAFLK TLEEPPKHAI FILATTEKHK IIPTILSRCQ IFDFKRITVK DAAEYLKYIA
     ESQDINAEDD ALHIIAQKAD GAMRDALSIF DRVVSFSGKE LTRKAVTENL NVLDYDTYFA
     ATDFMLEHNI PELLLLFNKT LSLGFDGHHF ISGLASHFRD LMVCQHQDTI NLLEVGDNAK
     QHYLEQSKKT GNSFLLKALD LANDCDLKYK TSRNQRLLVE LTLMKLASID FGAEKKNLDG
     NVVSEAPADY ILPASHFKDI QTKTKVVEKP QPEQKYIDTK PPSEVGEHAE PIANYERTSE
     RAEKEIAVAE PKPQKTEEGT ERPELSKEAK KLKSEIVSKR ISALSISSLK AKKAHENNKK
     DHSIDIDSLP RSPFSEEEMQ KHWAEFVNEI DVKGRKILAS NLNSDVPKLL QDTTIWIELP
     NSTMKKEIER EQYDLMEYLK TQLNNYFINL KITVNEETAK KFAFTPEEKY EKLREKNPTI
     DLLRQTFDLD L
//
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