DPO3X_MYCGE
ID DPO3X_MYCGE Reviewed; 597 AA.
AC P47658; P47659;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=DNA polymerase III subunit gamma/tau;
DE EC=2.7.7.7;
GN Name=dnaX; Synonyms=dnaH, dnaZ; OrderedLocusNames=MG419; ORFNames=MG420;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP SEQUENCE REVISION.
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=16407165; DOI=10.1073/pnas.0510013103;
RA Glass J.I., Assad-Garcia N., Alperovich N., Yooseph S., Lewis M.R.,
RA Maruf M., Hutchison C.A. III, Smith H.O., Venter J.C.;
RT "Essential genes of a minimal bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:425-430(2006).
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 -!- 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 -!- 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 complex
CC (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Probably essential, it was not disrupted in a
CC global transposon mutagenesis study. {ECO:0000269|PubMed:16407165}.
CC -!- SIMILARITY: Belongs to the DnaX/STICHEL family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be two separate ORFs named DnaX and
CC DnaZ. {ECO:0000305|PubMed:7569993}.
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DR EMBL; L43967; AAC71650.2; -; Genomic_DNA.
DR PIR; D64246; D64246.
DR PIR; T09748; T09748.
DR RefSeq; WP_009885609.1; NZ_AAGX01000001.1.
DR AlphaFoldDB; P47658; -.
DR SMR; P47658; -.
DR STRING; 243273.MG_419; -.
DR EnsemblBacteria; AAC71650; AAC71650; MG_419.
DR KEGG; mge:MG_419; -.
DR eggNOG; COG2812; Bacteria.
DR HOGENOM; CLU_006229_0_3_14; -.
DR OMA; RCQSFFF; -.
DR OrthoDB; 556582at2; -.
DR BioCyc; MGEN243273:G1GJ2-514-MON; -.
DR Proteomes; UP000000807; 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:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR CDD; cd18137; HLD_clamp_pol_III_gamma_tau; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_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 SMART; SM00382; AAA; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02397; dnaX_nterm; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-directed DNA polymerase;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..597
FT /note="DNA polymerase III subunit gamma/tau"
FT /id="PRO_0000105498"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 597 AA; 69043 MW; DCD8DAF5DBB0323A CRC64;
MHQVFYQKYR PINFKQTLGQ ESIRKILVNA INRDKLPNGY IFSGERGTGK TTFAKIIAKA
INCLNWDQID VCNSCDVCKS INTNSAIDIV EIDAASKNGI NDIRELVENV FNHPFTFKKK
VYILDEAHML TTQSWGGLLK TLEESPPYVL FIFTTTEFNK IPLTILSRCQ SFFFKKITSD
LILERLNDIA KKEKIKIEKD ALIKIADLSQ GSLRDGLSLL DQISNFSDSE KISITDVEKT
FNIVDRNAKF TFIKAVLSGD IKEAFNLLDD FESNGLNFTY FLRELFALTV NLYAYAKLKN
INVLDSTEKT MIETLNFEKQ HYAFLIKAIE ENTNFGLSQL TLIDRLKAIV ISYNEFFNQK
PLTISSPSNE KSLHLETEYL EKKKIKKSNH KQDQKHFSLF EKSFIDKSEK TPKNDEVTNN
KFLDTSKLNL ANIALAINAF NDNKWINHFQ NLLSVFQTKF NDKDKQNNLS YFNNFIDKYS
ARDIVKATKI VKASSFGIVI LFEDQKIAMR LWKEAIEEGN VQATIFQIFN QNLFLASFSE
HQYKTTITEE TKNQKYQTEV LNLTQLENLA KPFLKEKKRS LSQKMVDKYF KGLFEEK
