ID I3DEK6_9PAST Unreviewed; 680 AA.
AC I3DEK6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
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:EIJ70149.1};
GN ORFNames=HMPREF1052_1580 {ECO:0000313|EMBL:EIJ70149.1};
OS Pasteurella bettyae CCUG 2042.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=1095749 {ECO:0000313|EMBL:EIJ70149.1, ECO:0000313|Proteomes:UP000006457};
RN [1] {ECO:0000313|EMBL:EIJ70149.1, ECO:0000313|Proteomes:UP000006457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 2042 {ECO:0000313|EMBL:EIJ70149.1,
RC ECO:0000313|Proteomes:UP000006457};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (MAR-2012) 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:EIJ70149.1}.
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DR EMBL; AJSX01000022; EIJ70149.1; -; Genomic_DNA.
DR RefSeq; WP_005760076.1; NZ_AJSX01000022.1.
DR AlphaFoldDB; I3DEK6; -.
DR PATRIC; fig|1095749.3.peg.909; -.
DR eggNOG; COG2812; Bacteria.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000006457; 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:EIJ70149.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006457};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:EIJ70149.1}.
FT DOMAIN 37..178
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 396..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 76168 MW; 83E5010BEAE1936F CRC64;
MSYQVLARKW RPKTFSEVVG QEHILTALSN GLKENRLHHA YLFSGTRGVG KTSIARLFAK
GLNCVNGVTA EPCGVCEHCK AIEEGNFIDL IEIDAASRTK VEDTRELLDN VQYKPVQGRY
KVYLIDEVHM LSRHSFNALL KTLEEPPEYV KFLLATTDPQ KLPVTILSRC MQFHLKALEQ
QQIALHLEHI LEQEQIPYET TALDKLAKAA QGSIRDALSL TDQAIAMSNG NITLDIVRTM
LGLLDDNQPI EVVYALQQGN GENLMKVIQS VADKGGDWEQ LLIEVSDVLH QIAMQQLLSA
NNNEESQIAF LAKHISPEDV QFFYQIVVNG RKELAFAPNP RVGVEMTLLR ALAFHPKLIK
SQPVEIANQS EQIAVRKSEK LVDMPVVSQS IKAQYQTASQ SPVEPQTAPA QTTGSAAMNA
LAQIQKLRSQ ASENNEKKNT SVAVTSLSSN SEEISQNVTA LPVVSHKLKK QTDLLDRLVS
LSNPKTEDKP ELEEPVEANE DEETNLAETY RWEWSNPELA QDNTGIRPSD IKQAILQEKT
PEVIAKVIAM AETRDEWGKT ISQLNLDSIK LVKQIALNAV LLEKTDNTIK LGLRSAQKHL
ITEKSVEILQ QTLTTFYACS ISLSIDFCDD ESLLTPLDYR RQIYHELSEQ AKQNLLKDKK
IKLLQDIFDA KLDMDSIRPV
//
