ID   DPO3A_BACSU             Reviewed;        1115 AA.
AC   O34623;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=BSU29230;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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; AF008220; AAC00338.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14883.1; -; Genomic_DNA.
DR   PIR; D69617; D69617.
DR   RefSeq; NP_390801.1; NC_000964.3.
DR   RefSeq; WP_003229412.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34623; -.
DR   SMR; O34623; -.
DR   IntAct; O34623; 5.
DR   STRING; 224308.BSU29230; -.
DR   BindingDB; O34623; -.
DR   ChEMBL; CHEMBL5283; -.
DR   PaxDb; O34623; -.
DR   DNASU; 936593; -.
DR   EnsemblBacteria; CAB14883; CAB14883; BSU_29230.
DR   GeneID; 936593; -.
DR   KEGG; bsu:BSU29230; -.
DR   PATRIC; fig|224308.179.peg.3174; -.
DR   eggNOG; COG0587; Bacteria.
DR   InParanoid; O34623; -.
DR   OMA; NECRRMG; -.
DR   PhylomeDB; O34623; -.
DR   BioCyc; BSUB:BSU29230-MON; -.
DR   Proteomes; UP000001570; 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; 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; Reference proteome; Transferase.
FT   CHAIN           1..1115
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103310"
SQ   SEQUENCE   1115 AA;  125350 MW;  E8B04E3398E512FE CRC64;
     MSFVHLQVHS GYSLLNSAAA VEELVSEADR LGYASLALTD DHVMYGAIQF YKACKARGIN
     PIIGLTASVF TDDSELEAYP LVLLAKSNTG YQNLLKISSV LQSKSKGGLK PKWLHSYREG
     IIAITPGEKG YIETLLEGGL FEQAAQASLE FQSIFGKGAF YFSYQPFKGN QVLSEQILKL
     SEETGIPVTA TGDVHYIRKE DKAAYRCLKA IKAGEKLTDA PAEDLPDLDL KPLEEMQNIY
     REHPEALQAS VEIAEQCRVD VSLGQTRLPS FPTPDGTSAD DYLTDICMEG LRSRFGKPDE
     RYLRRLQYEL DVIKRMKFSD YFLIVWDFMK HAHEKGIVTG PGRGSAAGSL VAYVLYITDV
     DPIKHHLLFE RFLNPERVSM PDIDIDFPDT RRDEVIQYVQ QKYGAMHVAQ IITFGTLAAK
     AALRDVGRVF GVSPKEADQL AKLIPSRPGM TLDEARQQSP QLDKRLRESS LLQQVYSIAR
     KIEGLPRHAS THAAGVVLSE EPLTDVVPLQ EGHEGIYLTQ YAMDHLEDLG LLKMDFLGLR
     NLTLIESITS MIEKEENIKI DLSSISYSDD KTFSLLSKGD TTGIFQLESA GMRSVLKRLK
     PSGLEDIVAV NALYRPGPME NIPLFIDRKH GRAPVHYPHE DLRSILEDTY GVIVYQEQIM
     MIASRMAGFS LGEADLLRRA VSKKKKEILD RERSHFVEGC LKKEYSVDTA NEVYDLIVKF
     ANYGFNRSHA VAYSMIGCQL AYLKAHYPLY FMCGLLTSVI GNEDKISQYL YEAKGSGIRI
     LPPSVNKSSF PFTVENGSVR YSLRAIKSVG VSAVKDIYKA RKEKPFEDLF DFCFRVPSKS
     VNRKMLEALI FSGAMDEFGQ NRATLLASID VALEHAELFA ADDDQMGLFL DESFSIKPKY
     VETEELPLVD LLAFEKETLG IYFSNHPLSA FRKQLTAQGA VSILQAQRAV KRQLSLGVLL
     SKIKTIRTKT GQNMAFLTLS DETGEMEAVV FPEQFRQLSP VLREGALLFT AGKCEVRQDK
     IQFIMSRAEL LEDMDAEKAP SVYIKIESSQ HSQEILAKIK RILLEHKGET GVYLYYERQK
     QTIKLPESFH INADHQVLYR LKELLGQKNV VLKQW