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Entry: A0A1G5CUM4_9FLAO
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Original site: A0A1G5CUM4_9FLAO 
ID   A0A1G5CUM4_9FLAO        Unreviewed;       361 AA.
AC   A0A1G5CUM4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, 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=SAMN02927903_00648 {ECO:0000313|EMBL:SCY06155.1};
OS   Flavobacterium caeni.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=490189 {ECO:0000313|EMBL:SCY06155.1, ECO:0000313|Proteomes:UP000199354};
RN   [1] {ECO:0000313|EMBL:SCY06155.1, ECO:0000313|Proteomes:UP000199354}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7031 {ECO:0000313|EMBL:SCY06155.1,
RC   ECO:0000313|Proteomes:UP000199354};
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; FMVF01000003; SCY06155.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5CUM4; -.
DR   STRING; 490189.SAMN02927903_00648; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000199354; 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   Reference proteome {ECO:0000313|Proteomes:UP000199354};
KW   Transferase {ECO:0000256|RuleBase:RU364063}.
FT   DOMAIN          38..168
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   361 AA;  40551 MW;  05D9EAEA17548C29 CRC64;
     MEQFVVSARK YRPQTFKDVV GQQAITNTLL NAIETNHLAS ALLFTGPRGV GKTTCARILA
     RKINQPGYDD PNEDFTFNVF ELDAASNNSV DDIRNLIDQV RIPPQTGQFK VYIIDEVHML
     SQAAFNAFLK TLEEPPKHAI FILATTEKHK IIPTILSRCQ IFDFKRITVK DAKEHLAEVA
     KSQGVQFEDD ALHIIAQKAD GAMRDALSIF DRVVSYCGNN LTRAAVTENL NVLDYETYIN
     VTDLILENKI PDLLMSFNDI LSRGFDAHHF VSGLASHFRD LLVCKTPATL VLLEAGEQAQ
     KMYHAQSLKA SQEFLLKGIE VANDCDLKYK TSQNQRLLVE LCLMQLASIT YDGEKKKLTD
     L
//
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