ID A0A1I3TNU8_9BACL Unreviewed; 593 AA.
AC A0A1I3TNU8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=SAMN02799624_05632 {ECO:0000313|EMBL:SFJ72029.1};
OS Paenibacillus sp. UNC496MF.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1502753 {ECO:0000313|EMBL:SFJ72029.1, ECO:0000313|Proteomes:UP000198714};
RN [1] {ECO:0000313|EMBL:SFJ72029.1, ECO:0000313|Proteomes:UP000198714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNC496MF {ECO:0000313|EMBL:SFJ72029.1,
RC ECO:0000313|Proteomes:UP000198714};
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; FORE01000018; SFJ72029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3TNU8; -.
DR STRING; 1502753.SAMN02799624_05632; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000198714; 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; IPR048448; DnaX-like_C.
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 Pfam; PF20964; DnaX_C; 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:UP000198714};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..182
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 406..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 65115 MW; 3C6EB773E3ADF93A CRC64;
MSHIALYRAW RPQTFRDMVG QQHIIQTLQN AIREDRVSHA YLFNGPRGTG KTTTAKVMAK
AINCERGPAT EPCNECDACR GITSGTVMDV VEIDAASNRG IDEIRDIRDK VRYAPSEVRF
KVYIIDEVHM LTSEAFNALL KTLEEPPAHV IFILATTEPH KLPATIISRC QRFDFRQVSL
PEQTERLRQI CEEEGILADE DALAYIARLS DGGMRDAISL LEQVSAYGGE RITLNDAVDV
TGGLAAEQFE QLAEAIRDRN AGAILPLVEG LMQAGKSADK CLENLVYYFR DLLVLKLAPK
GKASTERIVD QDKYARMAEA FSAELLFRMI DVLNQYQLEI RQAALPQTIF EVALMKICTL
REAGDQGSAS AYAAATDTSE AAASGSEVQR LQQRIDTLER KIEQLLQSGV KPGSPAPEQG
VSRGGGNRAG NNFSRGGSGG AGSSIARVKL DPFLAAADSP ASGQVRMKWA DILQRVKSNN
ISTHAWFVNG EPVAAADNTI LVAFKNSIHR ETTEKPANRD VIERVLNEVY NRPVRLATVM
LKEWQTAAEN GASPAEELTL LHEDEGGGPP PEPEWVEEAV KLFGEDLVVV EDK
//
