ID   DPO3A_STAES             Reviewed;        1065 AA.
AC   Q8CNX0;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=SE_1378;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04977.1; -; Genomic_DNA.
DR   RefSeq; NP_764933.1; NC_004461.1.
DR   RefSeq; WP_002485290.1; NZ_WBME01000042.1.
DR   AlphaFoldDB; Q8CNX0; -.
DR   SMR; Q8CNX0; -.
DR   STRING; 176280.SE_1378; -.
DR   EnsemblBacteria; AAO04977; AAO04977; SE_1378.
DR   KEGG; sep:SE_1378; -.
DR   PATRIC; fig|176280.10.peg.1346; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_9; -.
DR   OMA; NECRRMG; -.
DR   Proteomes; UP000001411; 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_0000103346"
SQ   SEQUENCE   1065 AA;  123311 MW;  42D8A0CC0AEFFB8D CRC64;
     MVAHLNIHTS FDLLDSSLRI DALIDKAKKE GYRALAITDT NVLYGYPKFY DACIAAHIHP
     IFGMTIYLTD GLYTIETVVL AKNNQGLKSL YQISSAIMMR NKEEVPIEWL KRYDEHLIII
     FKEAELSHKQ IIDAFEGKKE LYLNHNSNNT LTGKRVWMQS ARYLNEDDAE TIPALHAIRD
     NTKLDLIHEK ETLDEHFPSI EELQTLNLSE DMITNANEIE ELCQAEIAYH QSLLPQFVTP
     NGETSKDYLW TILIHRLREW ELNDKTYFNR LKHEYKIITD MGFEDYFLIV SDLIHFAKTH
     EVMVGPGRGS SAGSLVSYLL GITTIDPLKY NLLFERFLNP ERVTMPDIDI DFEDTRREKV
     IKYVQDKYGE HHVSGIVTFG HLLARAVARD VGRIMGFDET SLNEISKLIP HKLGITLEEA
     YQKPEFKAFV HRNHRNERWF EVSKKLEGLP RHTSTHAAGI IINDQPLFKF APLTTGDTGL
     LTQWTMTEAE RIGLLKIDFL GLRNLSIIHQ IILQVKKDLN INIDIEAIPY DDKKVFDLLS
     NGDTTGIFQL ESDGVRSVLK RLQPEHFEDI VAVTSLYRPG PMEEIPTYIT RRHNPNQVAY
     LHPDLEPILK NTYGVIIYQE QIMLIASQVA GFSYGEADIL RRAMSKKNRA ILESERQHFI
     DGAKNNGYGE QISKQIFDLI LKFADYGFPR AHAVSYSKIA YIMSYLKVHY PHYFYANILS
     NVIGSEKKTA AMIDEAKHQR ISILPPNINQ SHWYYKASNK GIYLSLGTIK GIGYQSVKLI
     IDERQQNGPY RDFFDFSRRI PKRVKNRKLL ESLILVGAFD TFGKTRATLL QAIDQVLDLN
     SDVEQDEMLF DLLTPKQSYE EKEELPDQLL SDYEKEYLGF YISKHPVEKK FEKKQYLGIF
     QLSNGSHYQP ILVQFDHIKQ IRTKNGQNMA FVTMNDGRTM MDGVIFPDKF KKFETSISKE
     QMYIVLGKFE KRNQQMQLII NQLFEVEAYE QTKLSNSKKV ILRNVTHLEP QFEHSKVESN
     EQHALNIYGF DESANKMTML GQIERQRQNF DLLIQTYSPA DIRFI