ID A0A1H2W6W9_9FLAO Unreviewed; 573 AA.
AC A0A1H2W6W9;
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=SAMN05444411_102115 {ECO:0000313|EMBL:SDW75829.1};
OS Lutibacter oricola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=762486 {ECO:0000313|EMBL:SDW75829.1, ECO:0000313|Proteomes:UP000199595};
RN [1] {ECO:0000313|EMBL:SDW75829.1, ECO:0000313|Proteomes:UP000199595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24956 {ECO:0000313|EMBL:SDW75829.1,
RC ECO:0000313|Proteomes:UP000199595};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNNJ01000002; SDW75829.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2W6W9; -.
DR STRING; 762486.SAMN05444411_102115; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000199595; 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 Reference proteome {ECO:0000313|Proteomes:UP000199595};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 38..168
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 573 AA; 64989 MW; BEDBD84D307EBFE7 CRC64;
MEQFIVSARK YRPQVFEDVV GQQAITNTLE NAIKNNHLAQ ALLFTGPRGV GKTTCARILA
KKINENAGET SEDDFAFNIF ELDAASNNSV DDIRNLTEQV RIPPQTGKYK VYIIDEVHML
SQAAFNAFLK TLEEPPAHAI FILATTEKHK IIPTILSRCQ IFDFKRIGVL DAKNYLVKIA
KEEGINADDD ALHIIAQKAD GAMRDALSIF DRVVSFSGTE LTRKAVTENL NVLDYDEYFI
TTSLLLENKI PEVLVHFNTI LAKGFDGHHF IAGLAAHFRD LMVAKDRITV GLLEVGDNAK
QKYLEQSEQC DLTFLLKAIE LSNDCDLKYK TSKNQRLLVE LTLMQLASIN FDGEKKNNKP
FIIAALHFNK GIKARTKKAP IPTTEIKEQL KKEAIAPTPV SKPIIKEKEK HAPKPTIDAK
NRRPSALSLK SIGRKKEIDE IEVKDAEEVD NKPTDDFAEN QAQLLWKKYS EKLSEKGRIS
ASSIMTANVP KVIDKNIHFV VASEMMKSQL EKFKPNILGY IRERLNSYKI QLIITVNEEQ
LKRYAYTPQE KYQKLKEINT HIEEFKKTFD LDI
//
