ID   DPO3A_STAAS             Reviewed;        1065 AA.
AC   Q6G8M4;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=SAS1630;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
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; BX571857; CAG43432.1; -; Genomic_DNA.
DR   RefSeq; WP_000226910.1; NC_002953.3.
DR   AlphaFoldDB; Q6G8M4; -.
DR   SMR; Q6G8M4; -.
DR   KEGG; sas:SAS1630; -.
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   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; 1.
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_0000103344"
SQ   SEQUENCE   1065 AA;  122915 MW;  6E6E2976A5687ACB CRC64;
     MVAYLNIHTA YDLLNSSLKI EDAVRLAVSE NVDALAITDT NVLYGFPKFY DACIANNIKP
     IFGMTIYVTN GLNTVETVVL AKNNDGLKDL YQLSSEIKMN ALEHVSFELL KRFSNNMIII
     FKKVGDQHRD IVQVFETHND TYMDHLSISI QGRKHVWIQN VCYQTRQDAD TISALAAIRD
     NTKLDLIHDQ EDFGAHFLTE KEINQLDINQ EYLTQVDVIA QKCDAELKYH QSLLPQYETP
     NDESAKKYLW RVLVTQLKKL ELNYDVYLER LKYEYKVITN MGFEDYFLIV SDLIHYAKTN
     DVMVGPGRGS SAGSLVSYLL GITTIDPIKF NLLFERFLNP ERVTMPDIDI DFEDTRRERV
     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
     EGAKQNGYHE DISKQIFDLI LKFADYGFPR AHAVSYSKIA YIMSFLKVHY PNYFYANILS
     NVIGSEKKTA QMIEEAKKQG ITILPPNINE SHWFYKPSQE GIYLSIGTIK GVGYQSVKVI
     VDERYQNGKF KDFFDFARRI PKRVKTRKLL EALILVGAFD AFGKTRSTLL QAIDQVLDGD
     LNIEQDGFLF DILTPKQMYE DKEELPDALI SQYEKEYLGF YVSQHPVDKK FVAKQYLTIF
     KLSNAQNNKP ILVQFDKVKQ IRTKNGQNMA FVTLNDGIET LDGVIFPNQF KKYEELLSHN
     DLFIVSGKFD HRKQQRQLII NEIQTLATFE EQKLAFAKQI IIRNKSQIDM FEEMIKATKE
     NANDVVLSFY DETIKQMTTL GYINQKDSMF NNFIQSFNPS DIRLI