ID A0A1A9HMD0_9BURK Unreviewed; 742 AA.
AC A0A1A9HMD0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=ABE85_12925 {ECO:0000313|EMBL:ANH68238.1};
OS Mitsuaria sp. 7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1658665 {ECO:0000313|EMBL:ANH68238.1, ECO:0000313|Proteomes:UP000078154};
RN [1] {ECO:0000313|EMBL:ANH68238.1, ECO:0000313|Proteomes:UP000078154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7 {ECO:0000313|EMBL:ANH68238.1,
RC ECO:0000313|Proteomes:UP000078154};
RA Bao W., Leung F.C.C., Jiang J.;
RT "Complete Genome Sequence of Mitsuaria sp. Strain 7, a Lignin-degrading
RT Bacterium Isolated from Forest Soil.";
RL Submitted (JUL-2015) 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; CP011514; ANH68238.1; -; Genomic_DNA.
DR RefSeq; WP_067274954.1; NZ_CP011514.1.
DR AlphaFoldDB; A0A1A9HMD0; -.
DR STRING; 1658665.ABE85_12925; -.
DR KEGG; miu:ABE85_12925; -.
DR PATRIC; fig|1658665.3.peg.2646; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000078154; Chromosome.
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; 3.30.300.150; DNA polymerase III, tau subunit, domain V; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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; 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 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:UP000078154};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 37..184
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 367..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..416
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..506
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 78139 MW; 0BE3A357883CE910 CRC64;
MSYQVLARKY RSRTFEELMG QEHVVQALAN ALTQQRLHHA YLFTGTRGVG KTSVSRILAK
SLNCVGPDGT GGITAQPCNV CDACRDIDAG RFVDYVELDA ASNRGVEEIS QLLDQAVYKP
VIGRFKVYMI DEVHMLSNTA FNAMLKTLEE PPEYLKFVLA TTDPQKVPVT VLSRCLQFNL
RPMAPQTVLE HLTRVLSNES VPNEPGALRL LARAARGSMR DALSLTDQAI AFGSGELKEA
GVRQMLGSVD RGHVLGILNA LIAGDGASLV GASDRLRDMG LSAGGTLEDL AVSLQHLAVA
QAAPGALDAG DPDLAELLPL ASQLPADEVQ LMYSMALHGR QELPLAPDEY AGLTMVLLRM
MAFRPNGPGA RQPSVPEGAA RPAPAPAVSA APVTRPQPAS AAQAPVPMPA APAPAPAVPR
VAEAAAPEPE PEPAQAPVAA PVVAAPEVAP AKVPPAIVEA AVEAEPEPEP VPIRASAPAL
APAPAPVVAA EPPRAAPAPV EAPAPRAPSG PLRAAQAGAP ATRFSERLRP RAGPPPAVKV
ESDAEEPEDL SPPHDDNGPP PWMDVPPPTD EEASVGLSMP DMDDPSPASA ESGSGGGGGI
YVSTAIEEVD LVPTPLGERW YAIVPQLGLN ALARELALQA ECLEIDESAE PQRWRFRVER
ESLRQPGLLE KLQSVLATFA GKSVRVDIEA GRASDSPALR DTQSTRARQR LAESIILEDP
EVQQLLAQFK TARILPGSIK PV
//
