ID A0A3N7HM15_9BURK Unreviewed; 630 AA.
AC A0A3N7HM15;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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 ECO:0000313|EMBL:RQP22076.1};
GN ORFNames=DZC73_23995 {ECO:0000313|EMBL:RQP22076.1};
OS Albitalea terrae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Albitalea.
OX NCBI_TaxID=2496871 {ECO:0000313|EMBL:RQP22076.1, ECO:0000313|Proteomes:UP000267464};
RN [1] {ECO:0000313|EMBL:RQP22076.1, ECO:0000313|Proteomes:UP000267464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-16 {ECO:0000313|EMBL:RQP22076.1,
RC ECO:0000313|Proteomes:UP000267464};
RA Khan S.A., Jeon C.O., Chun B.H., Jeong S.E.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RQP22076.1, ECO:0000313|Proteomes:UP000267464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-16 {ECO:0000313|EMBL:RQP22076.1,
RC ECO:0000313|Proteomes:UP000267464};
RA Shunsuke S.S.;
RT "Rhizobacter gummiphilus sp. nov., a rubber-degrading bacterium isolated
RT from the soil of a botanical garden in Japan.";
RL Submitted (DEC-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}.
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:RQP22076.1}.
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DR EMBL; QUSW01000008; RQP22076.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N7HM15; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000267464; 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; 3.30.300.150; 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; 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 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 ECO:0000313|EMBL:RQP22076.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000267464};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:RQP22076.1}.
FT DOMAIN 37..196
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 406..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..442
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 66513 MW; 7758ABB31E7E4AF0 CRC64;
MSYLVLARKY RPSNFEQLVG QEHVVQALAN ALTQGRLHHA YLFTGTRGVG KTTVSRLLAK
SLNCTGPDGQ GGITAHPCGV CNACRDIDSG RFVDYVELDA ASNRGVEEIS TLLDQSVYKP
VVGRFKVYMI DEVHMLSTTA FNAMLKTLEE PPEYLKFVLA TTDPQKVPPT VLSRCLQFNL
RPMAPQTVHS HLTNVLQAES IEAEPGALRL LARAARGSMR DALSLTDQAI AFGAGVLAEA
GVRQMLGAVD RGHAVRIIEA LAANDGAALI AAADALRGMG LSAAGTLEEL SELLQQMAVA
QAVPGSLDAN DPDSAAAVRL AAALPADEIQ LCYSMAIHGR AELGLAPDEY SGLVMVLLRM
LAFRPQGSGD AMPAPRKPSA QPAVASSAAV AAAPVRPVPP VAARPAAAPQ AMPSRPVASP
PPARPVAAPV AVPVARPNPS PAPRHDGPDD EPPPPWEDEP AAAPRVAARP ASDAMPDSPP
AMPPSPSTPR TSTVVKRTEL GDRWDETVTQ MVQQGSISAL VRELAMQAEC IGLAHEAGTA
VWTLRVEREM LRAGTHKDKL QAALSQHLGQ PVRLDVEGGA ATDSPALRAA AEAERRQVEA
EQIIHNDPLV QALMAQYKTA RIVPGSIKPH
//
