ID X6KTA2_9RHOB Unreviewed; 586 AA.
AC X6KTA2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 2.
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=P279_25795 {ECO:0000313|EMBL:ETA49226.2};
OS Rhodobacteraceae bacterium PD-2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1169855 {ECO:0000313|EMBL:ETA49226.2, ECO:0000313|Proteomes:UP000023196};
RN [1] {ECO:0000313|EMBL:ETA49226.2, ECO:0000313|Proteomes:UP000023196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PD-2 {ECO:0000313|EMBL:ETA49226.2,
RC ECO:0000313|Proteomes:UP000023196};
RX PubMed=25700405;
RA Zheng L., Cui Z., Xu L., Sun C., Powell R.J., Hill R.T.;
RT "Draft Genome Sequence of Rhodobacteraceae Strain PD-2, an Algicidal
RT Bacterium with a Quorum-Sensing System, Isolated from the Marine Microalga
RT Prorocentrum donghaiense.";
RL Genome Announc. Announc.3:e01549-14(2015).
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:ETA49226.2}.
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DR EMBL; AWRV02000002; ETA49226.2; -; Genomic_DNA.
DR AlphaFoldDB; X6KTA2; -.
DR HOGENOM; CLU_006229_0_7_5; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000023196; 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 ECO:0000313|EMBL:ETA49226.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000023196};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:ETA49226.2}.
FT DOMAIN 41..188
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 381..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 63261 MW; 05F10A5115C0A336 CRC64;
MTDSPAYQVL ARKYRPETFA DLVGQDAMVR TLRNAFKAER IAQAFIMTGI RGTGKTTTAR
IIAKGMNCIG PDGNGGPTTE PCGQCEHCVA IMEGRHVDVM EMDAASRTGI GDIREIIESV
HYRAASARYK IYIIDEVHML STQAFNGLLK TLEEPPAHVK FIFATTEIRK VPVTVLSRCQ
RFDLRRIEPE VMIGLLRKIA GAEEAEITDE ALALITRAAE GSARDATSLL DQAISHGAGE
TGADQVRAML GLADRGRVMD LFERIMRGDA AGALSELSAQ YSDGADPLAV LRDLAELTHW
VSVVKITPDA AEDPTIAPDE RARGLAFADG LGMRPLSRAW QMLLKAIEEV ANAPSAMMAA
EMAVIRLTHV AELPSPEELL RRLQDSPPPP APGPGGGGGG MGHGQGGDVQ AQGMPQPTHP
GPRGPSASYG NTVVALAADQ ALARYPTFEH VLDLIRANRD VQLLVEVESG LRLAAYQPGR
IEFPPTETAP ADLAQRLGSA LQRWTGNRWG VSVVNGCDAQ TVFERRDAAR VAIEDEARQH
PLVQAALSAF PKARIKSVKT AEEAQVEAEL DALPEVEDEW DPFEEE
//
