ID W7Q7F9_9GAMM Unreviewed; 631 AA.
AC W7Q7F9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=Q427_21195 {ECO:0000313|EMBL:EWH00134.1};
OS Halomonas sp. BC04.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1403540 {ECO:0000313|EMBL:EWH00134.1, ECO:0000313|Proteomes:UP000019279};
RN [1] {ECO:0000313|EMBL:EWH00134.1, ECO:0000313|Proteomes:UP000019279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC04 {ECO:0000313|EMBL:EWH00134.1,
RC ECO:0000313|Proteomes:UP000019279};
RA Farooqui S., Greene A.C., Patel B.K.;
RT "Draft Genome Sequence of Halomonas Strain BC04, an Aromatic-degrading
RT moderate Halophilic Bacterium.";
RL Submitted (DEC-2013) 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:EWH00134.1}.
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DR EMBL; AZQX01000250; EWH00134.1; -; Genomic_DNA.
DR AlphaFoldDB; W7Q7F9; -.
DR PATRIC; fig|1403540.3.peg.3970; -.
DR Proteomes; UP000019279; 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: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; cd18137; HLD_clamp_pol_III_gamma_tau; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.30.300.150; DNA polymerase III, tau subunit, domain V; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR021029; DNA_pol_III_tau_dom-5.
DR InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038249; PolIII_tau_V_sf.
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 Pfam; PF12170; DNA_pol3_tau_5; 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|RuleBase:RU364063};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364063};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU364063};
KW Reference proteome {ECO:0000313|Proteomes:UP000019279};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 167..290
FT /note="DNA polymerase III gamma subunit"
FT /evidence="ECO:0000259|Pfam:PF12169"
FT DOMAIN 502..622
FT /note="DNA polymerase III tau subunit"
FT /evidence="ECO:0000259|Pfam:PF12170"
FT REGION 296..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 66885 MW; F57B1BD0F4C5D176 CRC64;
MTSTPCGECD SCRAIDEGRF VDLIEVDAAS RTKVEDTREL LDNVQYAPTQ GRYKVYLIDE
VHMLSTSSFN ALLKTLEEPP PHVKFLLATT DPQKLPPTVL SRCLQFTLKN MPPERIVEHL
GKVLVAEQVG FEESALWLLG KAADGSMRDA MSLTDQAIAF GQGRICHADV AAMLGTLDHR
HVVALVEALA EVDAARVLNE VSQLAEQGPD FAAVLDDVTG VLHRLAVAQM VPGALDNGHG
DRDLLLALAA RFTPEDIQLY YQIGIQGRGD MAHAPDLRTA LEMTLLRMLA FRPQGVPQPA
KTPLPLRGEP GPVTPPDAGA GGPGDIPPPD EAPAAARREN LDSPGSARGA ATSTAPVSPK
GEGGLPDVDG PVNRQSKAEV PAAQDRFEAP PPWEESLPDD SAALSVTVDA LNHGPEEAGQ
DVSENEAHGE VALAAAPTPL PTADEPAADT DAAVSRPTAD TASTVVPEPT AVADTDVTSA
TQPSVSADMP VEAGDSACFS HAAWLERFDS LGLGGLTRNL AAHCVVESDN GSRLILRLDP
SQEAMNAEIH VRRVREALAG IGVMRQLTIE AGPLPEAVET PRQRADRTAA ERHAVAVEAL
ERDPHVRQLQ EAFGARLITS SVKPADTSQR A
//
