ID   DPO3A_STAEQ             Reviewed;        1065 AA.
AC   Q5HNK2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=SERP1266;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW54654.1; -; Genomic_DNA.
DR   RefSeq; WP_010959192.1; NC_002976.3.
DR   AlphaFoldDB; Q5HNK2; -.
DR   SMR; Q5HNK2; -.
DR   STRING; 176279.SERP1266; -.
DR   EnsemblBacteria; AAW54654; AAW54654; SERP1266.
DR   KEGG; ser:SERP1266; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_9; -.
DR   OMA; NECRRMG; -.
DR   OrthoDB; 561611at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome; Transferase.
FT   CHAIN           1..1065
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103347"
SQ   SEQUENCE   1065 AA;  123361 MW;  A86C2FD020752E91 CRC64;
     MVAHLNIHTS FDLLDSSLRI DALIDKAKKE GYRALAITDT NVLYGYPKFY DACIAAHIHP
     IFGMTIYLTD GLYTIETVVL AKNNQGLKSL YQLSSAIMMR NKEEVPIEWL KRYDEHLIII
     FKEAELSHKQ VIDAFEGKKE 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 PMEEISTYIT RRHNPNQVAY
     LHPDLEPILK NTYGVIIYQE QIMLIASQVA GFSYGEADIL RRAMSKKNRA ILESERQHFI
     DGAKNNGYDE 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 KKYETSISKE
     QMYIVLGKFE KRNQQMQLII NQLFEVEAYE QTKLSNSKKV ILRNVTHLEP QFEHSKVESN
     EQHALNIYGF DESANKMTML GQIERQRQNF DLLIQTYSPA DIRFI