ID A0A0N1LM63_9SPHN Unreviewed; 620 AA.
AC A0A0N1LM63;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=IP83_08965 {ECO:0000313|EMBL:KPF85024.1};
OS Novosphingobium sp. AAP93.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523427 {ECO:0000313|EMBL:KPF85024.1, ECO:0000313|Proteomes:UP000037906};
RN [1] {ECO:0000313|EMBL:KPF85024.1, ECO:0000313|Proteomes:UP000037906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP93 {ECO:0000313|EMBL:KPF85024.1,
RC ECO:0000313|Proteomes:UP000037906};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-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}.
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:KPF85024.1}.
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DR EMBL; LJHZ01000049; KPF85024.1; -; Genomic_DNA.
DR RefSeq; WP_054121873.1; NZ_LJHZ01000049.1.
DR AlphaFoldDB; A0A0N1LM63; -.
DR STRING; 1523427.IP83_08965; -.
DR PATRIC; fig|1523427.4.peg.2614; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000037906; 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; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR022754; DNA_pol_III_gamma-3.
DR InterPro; IPR022107; DNA_pol_III_gamma/tau_C.
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 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; PF12362; DUF3646; 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 Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 115..262
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..76
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 65144 MW; 848DB4CF870283F3 CRC64;
MVDSTDMFGD PIADEPEDDA PSAAELEAAG QGSMFGDPAP GPAPGPAPGP APGPAPGPAP
AVREEHAPPP VAAPAPSGQP YRVLARKYRP QTFAELIGQD AMVQTLGNAI RRGRLAHAFL
MTGVRGVGKT STARLIAKAL NCIGPDGQGG PTIDPCGRCE PCVAIAEGRH IDVIEMDAAS
HTGVDDVREI IEAVRYAAVS ARYKIYIIDE VHMLSRNAFN ALLKTLEEPP AHVKFLFATT
EVDKLPVTVL SRCQRFDLRR IQTPVLAAHF GKVCDAEQVQ AEDEALAMIA AAAEGSVRDG
LSILDQAISH ADMAGGGAVT AEQVREMLGL ADKTMQRRLF AAVIGGKGDA VLDEVASQFA
LGIEPTAMMR AQLDLVHKVT VAQISGAADA RSAEEREALE GWAKKLGAGA LHRLWQLLLK
GYEEVRGAPD PLVAAQMALL RVMHAADLPD PGGLIKQLEA FAANPPAVQM AAPAGTAAPV
AAAPASAEMM LAQWEQLVEQ VEQISPLIGS SMRLSVRVVS LKPGHLVYAL AAGIPGDPTQ
DMRRGLEGAT GGHWQVERSM DLASAAPSLE EARAEAAARA EAALREDPLV RAAYAAFPGA
EMIDESAISA PERKSWSKRA
//
