ID A0A425Y2P3_9BACT Unreviewed; 589 AA.
AC A0A425Y2P3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=DWB61_07680 {ECO:0000313|EMBL:RRG22086.1};
OS Ancylomarina euxinus.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC Ancylomarina.
OX NCBI_TaxID=2283627 {ECO:0000313|EMBL:RRG22086.1, ECO:0000313|Proteomes:UP000285794};
RN [1] {ECO:0000313|EMBL:RRG22086.1, ECO:0000313|Proteomes:UP000285794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1P {ECO:0000313|EMBL:RRG22086.1,
RC ECO:0000313|Proteomes:UP000285794};
RA Yadav S., Villanueva L., Damste J.S.S.;
RT "Draft genome sequence of Ancylomarina sp. M1P.";
RL Submitted (JUL-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:RRG22086.1}.
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DR EMBL; QQWG01000006; RRG22086.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A425Y2P3; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000285794; 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; 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 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 ECO:0000313|EMBL:RRG22086.1};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:RRG22086.1}.
FT DOMAIN 38..181
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 390..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 66025 MW; 2054762FD9FCE6EB CRC64;
MENFIVSARK YRPSSFQTVV GQQSITVTLK NAIKNAHLAH AYLFCGPRGV GKTSCARIFA
KTINCSNVSS DFEACNTCES CLAFNENRSY NIHELDAASN NSVDDIRTLI DQVRIPPQIG
KYSVYIIDEV HMLSQSAFNA FLKTLEEPPA HAIFVLATTE KHKIIPTILS RCQIFDFSRI
KVADAVNHLA HIAQEEGITI NEEALNVIAQ KADGAMRDAL SIFDQIVSFS GKNINFENVI
QNLNVLDYDY YFKMVDAFLQ GKVTDVLILF NEIVEKGFDG HHFVAGLSSH IRDILVGKDV
ATLQLLEVSD SVKEKYTEQA KKCEVDFLYD ALGILNECDI HYKSSQNHRL LIELTLIQLS
QIIESKKKGA SLKKNFRRLL KIRVEGRASA PKVAGAKDKA PVHPQQEAQK PAQTHSGQSQ
QKVSTTSSPS PTSISIKAAM SRGIVNRPAS SSSPEIKSKE SEAKYTNVQN QAYTSESVVE
KLKEYTIVRK KSDRIRLAIA NCEAEIRTGG QLVVKVSNQI QEDDIAAVKN EMVNYLKREL
QNSTIDFIIE ITQTETKKRL YTDTDKFKYL CQKNPLLEQL KQKFSLDFE
//
