ID   DPO3A_STRP6             Reviewed;        1036 AA.
AC   Q5XBV1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=M6_Spy0977;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
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; CP000003; AAT87112.1; -; Genomic_DNA.
DR   RefSeq; WP_011184574.1; NC_006086.1.
DR   AlphaFoldDB; Q5XBV1; -.
DR   SMR; Q5XBV1; -.
DR   EnsemblBacteria; AAT87112; AAT87112; M6_Spy0977.
DR   KEGG; spa:M6_Spy0977; -.
DR   HOGENOM; CLU_001600_0_0_9; -.
DR   OMA; NECRRMG; -.
DR   Proteomes; UP000001167; 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; Transferase.
FT   CHAIN           1..1036
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103352"
SQ   SEQUENCE   1036 AA;  119152 MW;  6433C1D005178DFC 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
     KQELQELTEA GLKEKGLWKE PYQSRLLHEL IIISDMGFDD YFLIVWDLLR FGRSKGYYMG
     MGRGSAAGSL VAYALNITGI 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 GLFDCFEPNR KKILDNLDGL LVFVNELGSL FSDSSFSWVD
     TQDYSATEKY SLEQEVVGVG MSKHPLIDIA EKSIQTFTPI SQLVKESEAV VLIQIDSIRI
     IRTKTSGQQM AFLSVNDTKK KLDVTLFPQE YAIYKDQLKE GEFYYLKGRI KERDHRLQMV
     CQQVQMAISQ KYWLLVENHQ FDSQISEILG AFPGTTPVVI HYQKNKETIA LTKIQVHVTE
     NLKEKLRPFV LKTVFR