ID   DPO3A_STRP1             Reviewed;        1036 AA.
AC   P0C0F3; Q48YG4; Q9FDF6;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=SPy_1284, M5005_Spy0990;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA   Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of serotype
RT   M1 group A Streptococcus involved multiple horizontal gene transfer
RT   events.";
RL   J. Infect. Dis. 192:771-782(2005).
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. The alpha chain
CC       is the DNA polymerase (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE004092; AAK34132.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ51608.1; -; Genomic_DNA.
DR   RefSeq; NP_269411.1; NC_002737.2.
DR   AlphaFoldDB; P0C0F3; -.
DR   SMR; P0C0F3; -.
DR   STRING; 1314.HKU360_01033; -.
DR   PaxDb; P0C0F3; -.
DR   EnsemblBacteria; AAK34132; AAK34132; SPy_1284.
DR   KEGG; spy:SPy_1284; -.
DR   KEGG; spz:M5005_Spy0990; -.
DR   PATRIC; fig|160490.10.peg.1122; -.
DR   HOGENOM; CLU_001600_0_1_9; -.
DR   OMA; NECRRMG; -.
DR   Proteomes; UP000000750; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.1600; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR   InterPro; IPR041931; DNA_pol3_alpha_thumb_dom.
DR   InterPro; IPR040982; DNA_pol3_finger.
DR   InterPro; IPR029460; DNAPol_HHH.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   InterPro; IPR004805; PolC_alpha.
DR   PANTHER; PTHR32294; PTHR32294; 2.
DR   Pfam; PF07733; DNA_pol3_alpha; 1.
DR   Pfam; PF17657; DNA_pol3_finger; 1.
DR   Pfam; PF14579; HHH_6; 1.
DR   Pfam; PF02811; PHP; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF89550; SSF89550; 1.
DR   TIGRFAMs; TIGR00594; polc; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA replication; DNA-directed DNA polymerase;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..1036
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103350"
SQ   SEQUENCE   1036 AA;  119172 MW;  D7EA4C544EC781AD CRC64;
     MFAQLDTKTV YSFMDSLIDL NHYFERAKQF GYHTIGIMDK DNLYGAYHFI KGCQKNGLQP
     VLGLEIEILY QERQVLLNLI AQNTQGYHQL LKISTAKMSG KLHMDYFCQH LEGIAVIIPS
     KGWSDTLVVP FDYYIGVDQY TDLSHMDSKR QLIPLRTVRY FAQDDMETLH MLHAIRDNLS
     LAETPVVESD QELADCQQLT AFYQTHCPQA LQNLEDLVSG IYYDFDTNLK LPHFNRDKSA
     KQELQDLTEA GLKEKGLWKE PYQSRLLHEL VIISDMGFDD YFLIVWDLLR FGRSKGYYMG
     MGRGSAAGSL VAYALNITGI DPVQHDLLFE RFLNKERYSM PDIDIDLPDI YRSEFLRYVR
     NRYGSDHSAQ IVTFSTFGPK QAIRDVFKRF GVPEYELTNL TKKIGFKDSL ATVYEKSISF
     RQVINSRTEF QKAFAIAKRI EGNPRQTSIH AAGIVMSDDA LTNHIPLKSG DDMMITQYDA
     HAVEANGLLK MDFLGLRNLT FVQKMQEKVA KDYGCQIDIT AIDLEDPQTL ALFAKGDTKG
     IFQFEQNGAI NLLKRIKPQR FEEIVATTSL NRPGASDYTT NFIKRREGQE KIDLIDPVIA
     PILEPTYGIM LYQEQVMQIA QVYAGFTLGK ADLLRRAMSK KNLQEMQKME EDFIASAKHL
     GRAEETARGL FKRMEKFAGY GFNRSHAFAY SALAFQLAYF KAHYPAVFYD IMMNYSSSDY
     ITDALESDFQ VAQVTINSIP YTDKIEASKI YMGLKNIKGL PRDFAYWIIE QRPFNSVEDF
     LTRTPEKYQK KVFLEPLIKI GLFDCFEPNR KKILDNLDGL LVFVNELGSL FSDSSFSWVD
     TKDYSVTEKY SLEQEIVGVG MSKHPLIDIA EKSTQTFTPI SQLVKESEAV VLIQIDSIRI
     IRTKTSGQQM AFLSVNDTKK KLDVTLFPQE YAIYKDQLKE GEFYYLKGRI KERDHRLQMV
     CQQVQMAISQ KYWLLVENHQ FDSQISEILG AFPGTTPVVI HYQKNKETIA LTKIQVHVTE
     NLKEKLRPFV LKTVFR