ID A0A1N7ER33_9RHOB Unreviewed; 594 AA.
AC A0A1N7ER33;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN05421666_0461 {ECO:0000313|EMBL:SIR90526.1};
OS Roseovarius nanhaiticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=573024 {ECO:0000313|EMBL:SIR90526.1, ECO:0000313|Proteomes:UP000186019};
RN [1] {ECO:0000313|EMBL:SIR90526.1, ECO:0000313|Proteomes:UP000186019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29590 {ECO:0000313|EMBL:SIR90526.1,
RC ECO:0000313|Proteomes:UP000186019};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; FTNV01000001; SIR90526.1; -; Genomic_DNA.
DR RefSeq; WP_076530632.1; NZ_FTNV01000001.1.
DR AlphaFoldDB; A0A1N7ER33; -.
DR STRING; 573024.SAMN05216208_1674; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000186019; 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 Reference proteome {ECO:0000313|Proteomes:UP000186019};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 43..191
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 387..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 594 AA; 63566 MW; 78C5B05AB6CB26BC CRC64;
MTDSAPSGYR VLARKYRPET FADLVGQDAM VRTLKNAFEA DRIAQAFIMT GIRGTGKTTT
ARIIAKGMNC IGPDGNGGPT TDPCGTCEHC VAIMEGRHVD VMEMDAASHT GVQNIRDAII
ETVSYRAASA RYKIFIIDEV HMLSTSAFNA LLKTLEEPPA HVKFIFATTE IRKVPVTVLS
RCQRFDLRRI EPEVMLKLMR KIAGSEGAEI TDDALALITR AAEGSARDAT SLLDQAISHG
AGETGADQVR AMLGLADRGR VLDLFDMILK GDAAGALTEL GAQYSDGADP LAVLRDLAEI
THWTSVVKIT PEAADDPTIG PDERARGLQM AEALPMRVLT RMWQMLLKAL EEVAGAPNAM
MAAEMAVIRL THVADLPSPE ELLRKLKDTP VPASPPGGGT AASGTGGGPS AQASAPYSAP
ASQPQQTHQP RASGGNGVSA SLAVAANEAL AHYPTFHHVV EVIRANRDVK LLVEVETCVQ
LAAYQPGRIE FVPTEGAPHD LAQRLGAALQ RWTGNRWAVT LVNEGGGETI AARRDADKLA
LHNEAESHPL VQAVKDAFPG AEIIEIRTAR QIENAALADA LPEVEDEWDP FEED
//
