ID A0A2Z3JFA2_9DEIO Unreviewed; 730 AA.
AC A0A2Z3JFA2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=DKM44_11120 {ECO:0000313|EMBL:AWN23712.1};
OS Deinococcus irradiatisoli.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=2202254 {ECO:0000313|EMBL:AWN23712.1, ECO:0000313|Proteomes:UP000245368};
RN [1] {ECO:0000313|EMBL:AWN23712.1, ECO:0000313|Proteomes:UP000245368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17bor-2 {ECO:0000313|EMBL:AWN23712.1,
RC ECO:0000313|Proteomes:UP000245368};
RA Srinivasan S.;
RT "Complete Genome Sequence of Deinococcus sp. strain 17bor-2.";
RL Submitted (MAY-2018) 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; CP029494; AWN23712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z3JFA2; -.
DR KEGG; dez:DKM44_11120; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000245368; Chromosome.
DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR GO; GO:0008408; F:3'-5' exonuclease activity; 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: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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR004622; DNA_pol_HolB.
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 NCBIfam; TIGR00678; holB; 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.
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|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU364063};
KW Reference proteome {ECO:0000313|Proteomes:UP000245368};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 35..182
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 346..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..541
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..603
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..730
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 76322 MW; 8D4E3FC058871934 CRC64;
MSAIYQRARP ISWEQVVGQE HVKDVLQGAL EAGRVGHAYL FSGPRGVGKT TTARLIAMTA
NCQASGKKPC GECESCLSVR AGNHPDVLEI DAASNNSVDD VRDLREKVGL SAMRGGKKIY
ILDEAHMMSR AAFNALLKTL EEPPEHVIFI LATTEPEKII PTILSRCQHY RFRRLTAEEI
AGKLAQLTVQ EGARAEPEAL QLIGRLADGA MRDGESLLER MLAAGQAVTL GGVEAALGLP
PSERVRQMAQ ALLDLDAGPL LSGAAQLYRD GYAARTVVEG LVSALGAALH AELGLSPEGR
LERADVPRLL RLQAALDAQE ARFSRGADQL SLELALTHAL IAGEGQPEAG AAPAPQRASP
AQSGSLSADA AARLSKLERE VSALKAGGAP GRGAESASEI PAFNPAASRA PAAAPRAAAP
VPSGGTWADV MTLANMQMRA FLKPARTHAE AGYASLSYDA RGKFHAKQVY DKFDEVGALV
LKVFGPVTFE LISPDHNRKA KLGGAGAAPV SEVAATPEPE PEPAPRRPAP AARPAPPALD
DIPDFVPTGR PKAAAAAPRS TPAAPPQADV PDDLPPFEPS ARTARPVPIR PVPDPPSPDD
AAPAPLPEAG TKTPPRTTEL YIPLEPISQE PDWDDLGGPL ETQGSVQTAS PAPAPRASAP
PPRAAAERPA SRTPAPPGDV RAHPNYLEVT RLFSGRVKEI GKVKKTALSA ADDSDDADDL
DSAVDGAAEA
//
