ID A5EY35_DICNV Unreviewed; 665 AA.
AC A5EY35;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
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:ABQ13414.1};
GN OrderedLocusNames=DNO_0955 {ECO:0000313|EMBL:ABQ13414.1};
OS Dichelobacter nodosus (strain VCS1703A).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Dichelobacter.
OX NCBI_TaxID=246195 {ECO:0000313|EMBL:ABQ13414.1, ECO:0000313|Proteomes:UP000000248};
RN [1] {ECO:0000313|EMBL:ABQ13414.1, ECO:0000313|Proteomes:UP000000248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VCS1703A {ECO:0000313|EMBL:ABQ13414.1,
RC ECO:0000313|Proteomes:UP000000248};
RX PubMed=17468768; DOI=10.1038/nbt1302;
RA Myers G.S., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA Songer J.G., Rood J.I., Paulsen I.T.;
RT "Genome sequence and identification of candidate vaccine antigens from the
RT animal pathogen Dichelobacter nodosus.";
RL Nat. Biotechnol. 25:569-575(2007).
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; CP000513; ABQ13414.1; -; Genomic_DNA.
DR RefSeq; WP_012031268.1; NC_009446.1.
DR AlphaFoldDB; A5EY35; -.
DR STRING; 246195.DNO_0955; -.
DR KEGG; dno:DNO_0955; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_0_7_6; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000000248; Chromosome.
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; 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; 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 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:ABQ13414.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000248};
KW Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:ABQ13414.1}.
FT DOMAIN 36..179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 368..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 665 AA; 75244 MW; 80C4D05CB6D399E6 CRC64;
MYQVLARKWR PKTFRELVGQ QHITQALSYA LDHDRLHHAY LFTGTRGVGK TSLARIYAKS
LNCLINGTSA QPCGQCEHCL EIDQGRFPDL IEVDAASRRG IDETKELLDN LPYAPVKGRY
KVYLIDEVHM FTRESFNALL KTLEEPPPHV KFILATTDIQ KVPTTVLSRC LQFHLKNINP
EQLRQHLAHI LQVERIDYEA EALVLLAQAA RGSMRDGLSF LDQAIAYGQG VVKTDDVAYL
LGAVPTAQIY RLLTKIAESD ARAVRAILTE LDAFSPDYMD VLRHVFQGLQ QITVAQLQAQ
QNPNEIDQTL VRLAQQLPVE LVQLWYQIIS DAWQSMPYQP DMRVALEMTF LRMIALQPLL
PETTISEKHI IPEPDNDVDL PPWRDDESEM NTAPLESSEN DVPDNNDVDL PPWHDDESEM
INTAPAEPLE NDAPDNNGVD LPPWRDDELE MMNTAPAEAS ENDVPNDNDA DMPPWRDDEL
EMINTAPLES SENDVPDNND VDLPPWHNDE LEMNTVPLKS SENKSVIQLE QAVNQLQLWS
QFLNTLPVED VFLQSLVEQS IPVSFQNDSL QLAVLSAAAS WVNEQRLADL TRILSASCAR
KIAVSITFDD TIATSAMLRQ QESDQMHQMA KQKLLQNPVV RTLMTDFHGK IMRDSICVLD
KKESI
//
