ID   DPO3A_STAAR             Reviewed;        1065 AA.
AC   Q6GG04;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=SAR1781;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(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; BX571856; CAG40772.1; -; Genomic_DNA.
DR   RefSeq; WP_000226930.1; NC_002952.2.
DR   AlphaFoldDB; Q6GG04; -.
DR   SMR; Q6GG04; -.
DR   KEGG; sar:SAR1781; -.
DR   HOGENOM; CLU_001600_0_0_9; -.
DR   OMA; NECRRMG; -.
DR   OrthoDB; 561611at2; -.
DR   Proteomes; UP000000596; 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   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; 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..1065
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103343"
SQ   SEQUENCE   1065 AA;  123044 MW;  538477045413129C CRC64;
     MVAYLNIHTA YDLLNSSLKI EDAVRLAVSE NVDALAITDT NVLYGFPKFY DTCIANNIKP
     IFGMTIYVTN GLNNIETVVL AKDNYGLKDL YQLSSEIKMN ALEHVSFELL KRFSNNMIII
     FKNVADEHRD IVRVFDSHED TYLDHRSVLV QGIKHVWIQD VCYQTRHDAD TISALAAIRD
     NTKLDLIHDQ EDFGAHFLTE NEIHQLDVNP EYFTQADRIA QKCNAELKYH QSLLPQYQTP
     NDESAKKYLW RVLVTQLKKL ELNYDVYLER LKYEYKVITN MGFEDYFLIV SDLIHYAKTN
     DVMVGPGRGS SAGSLVSYLL GITTIDPIKF NLLFERFLNP ERVTMPDIDI DFEDTRREKV
     IQYVQEKYGE LHVSGIVTFG HLLARAVARD VGRIMGFDEV TLNEISSLIP HKLGITLDEA
     YQIDDFKKFV HRNHRHERWF SICKKLEGLP RHTSTHAAGI IINDHPLYEY APLTKGDTGL
     LTQWTMTEAE RIGLLKIDFL GLRNLSIIHQ ILTQVKKDLG INIDIEKIPF DDQKVFELLS
     QGDTTGIFQL ESDGVRSVLK KLKPEHFEDI VAVTSLYRPG PMEEIPTYIT RRHDPSKVQY
     LHPHLEPILK NTYGVIIYQE QIMQIASTFA NFSYGEADIL RRAMSKKNRA VLESERQHFI
     EGTKQNGYHE DISKQIFDLI LKFADYGFPR AHAVSYSKIA YIMSFLKVHY PNYFYANILS
     NVIGSEKKTA QMIEEAKKQG ITILPPNINE SHWFYKPSQE GIYLSIGTIK GVGYQSVKVI
     VEERYQNGKF KDFFDFARRI PKRVKTRKLL EALILVGAFD AFGKTRSTLL QAIDQVLDGD
     LNIEQDGFLF DILTPKQMYE DKEELPDALI SQYEKEYLGF YVSQHPVDKK FVAKQYLTIF
     KLSNAQNNKP ILVQFDKVKQ IRTKNGQNMA FVTLNDGIET LDGVIFPNQF KKYEELLSHN
     DLFIVSGKFD LRKQQRQLII NEIQTLATFE EQKLAFAKQI IIRNKSQIDM FEEMIKATKE
     NANDVVLSFY DETIKQMTTL GYINQKDSMF NNFIQSFNPS DIRLI