ID A0A1H9LHA9_9FLAO Unreviewed; 576 AA.
AC A0A1H9LHA9;
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=SAMN05421824_3038 {ECO:0000313|EMBL:SER10748.1};
OS Hyunsoonleella jejuensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=419940 {ECO:0000313|EMBL:SER10748.1, ECO:0000313|Proteomes:UP000198999};
RN [1] {ECO:0000313|EMBL:SER10748.1, ECO:0000313|Proteomes:UP000198999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21035 {ECO:0000313|EMBL:SER10748.1,
RC ECO:0000313|Proteomes:UP000198999};
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; FOFN01000006; SER10748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9LHA9; -.
DR STRING; 419940.SAMN05421824_3038; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000198999; 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:UP000198999};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 38..168
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 576 AA; 65709 MW; 868581698674DE8B CRC64;
MEHFVVSARK YRPQTFKDVV GQQAITNTLL NAIENNHLAQ ALLFTGPRGV GKTTCARILA
KMINSDGTET EEEDFAFNIF ELDAASNNSV DDIRNLTDQV RIPPQVGKYK VYIIDEVHML
SQAAFNAFLK TLEEPPKHCI FILATTEKHK IIPTILSRCQ IFDFKRITVK DAKEYLKYIA
EEQSISAEDD ALHIIAQKAD GAMRDALSIF DRVVSFSGKN LTRQAVTENL NVLDYETYFT
STDFILENKI PELLLQFNNT LSKGFDGHHY IAGLASHFRD LLVSKTQSTI ELLEVGDQIK
QKYLEQSKKA SHEFLLKGIE LANECDLKYK TSKNQRLLVE LCLMQLASIT YDGEKKNNKR
FIIPASYFQK KGITPIPVTK PTESLVETSS RDIDKEKAPV SGKSEVIEKF QVKDPPKIEL
TPQTKRTSGL SLKSIKAKKE HQIKQMEVVI DEKDLPTEDF TENQLIDCWN AFTRKIQKQG
KHNLASILAI DIPKVKGTTV YLEFPNETNK VELERQQYEL MGFLRKTLNN FDIKLSITVN
ETASKKYAYT TREKFEKMKE KNPAIDALRK TFDLDI
//