ID   DPO3A_STRP8             Reviewed;        1036 AA.
AC   Q8P0S5;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, 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=spyM18_1232;
OS   Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=186103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232;
RX   PubMed=11917108; DOI=10.1073/pnas.062526099;
RA   Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA   Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA   Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA   Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18 group
RT   A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009949; AAL97842.1; -; Genomic_DNA.
DR   RefSeq; WP_011017834.1; NC_003485.1.
DR   AlphaFoldDB; Q8P0S5; -.
DR   SMR; Q8P0S5; -.
DR   KEGG; spm:spyM18_1232; -.
DR   HOGENOM; CLU_001600_0_0_9; -.
DR   OMA; NECRRMG; -.
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; Transferase.
FT   CHAIN           1..1036
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103353"
SQ   SEQUENCE   1036 AA;  119187 MW;  04D7224EF3A889EC CRC64;
     MFAQLDTKTV YSFMDSLIDL NHYFERAKQF GYHTIGIMDK DNLYGAYHFI KGCQKNGLQP
     VLGLEVEILY QERQVLLNLI AQNTQGYHQL LKISTAKMSG KLHMDYLCQH LEGIAVIIPS
     KGWSDTLVVP FDYYIGVDQY TDLSHMDSKR QLIPLRTVRY FAQDDMETLH MLHAIRDNLS
     LAETPVVESD QELADCQQLT TFYQTHCPQA LQNLEDLVSG IYYDFDTNLK LPHFNRDKSA
     KQELQDLTEA GLKEKGLWKE PYQSRLLHEL VIISDMGFDD YFLIVWDLLR FGRSKGYYMG
     MGRGSAAGSL VAYALDITGI DPVQHDLLFE RFLNKERYSM PDIDIDLPDI YRSEFLRYVR
     NRYGSDHSAQ IVTFSTFGPK QAIRDVFKRF GVPEYELTNL TKKIGFKDSL ATVYEKSISF
     RQVINSRTEF QKAFAIAKRI EGNPRQTSIH AAGIVMSDDT LTNHIPLKSG DDMMITQYDA
     HAVEANGLLK MDFLGLRNLT FVQKMQEKVA KDYGCQIDIA 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 GLFDYFEPNR KKILDNLDGL LVFVNELGSL FSDSSFSWVD
     TKDYSATEKY SLEQEIVGVG MSKHPLIDIA EKSTQTFTPI SQLVKESEAV VLIQIDSIRI
     IRTKTSGQQM AFLSVNDTKK KLDVTLFPQE YAIYKDQLKE GEFYYLKGRI KERDHRLQMV
     CQQVQMAISQ KYWLLVENHQ FDSQISEILG AFPGTTPVVI HYQKNKETIA LTKIQVHVTE
     NLKEKLRPFV LKTVFR