ID   DPO3A_MYCBO             Reviewed;        1184 AA.
AC   P63978; A0A1R3XYN7; Q10779; X2BHX1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; Synonyms=dnaE1; OrderedLocusNames=BQ2027_MB1574;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU00177.1; -; Genomic_DNA.
DR   RefSeq; NP_855226.1; NC_002945.3.
DR   RefSeq; WP_003407751.1; NC_002945.4.
DR   AlphaFoldDB; P63978; -.
DR   SMR; P63978; -.
DR   EnsemblBacteria; SIU00177; SIU00177; BQ2027_MB1574.
DR   PATRIC; fig|233413.5.peg.1720; -.
DR   OMA; NECRRMG; -.
DR   Proteomes; UP000001419; 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: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; 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   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..1184
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103330"
SQ   SEQUENCE   1184 AA;  129323 MW;  A87AB7F0F2E08909 CRC64;
     MSGSSAGSSF VHLHNHTEYS MLDGAAKITP MLAEVERLGM PAVGMTDHGN MFGASEFYNS
     ATKAGIKPII GVEAYIAPGS RFDTRRILWG DPSQKADDVS GSGSYTHLTM MAENATGLRN
     LFKLSSHASF EGQLSKWSRM DAELIAEHAE GIIITTGCPS GEVQTRLRLG QDREALEAAA
     KWREIVGPDN YFLELMDHGL TIERRVRDGL LEIGRALNIP PLATNDCHYV TRDAAHNHEA
     LLCVQTGKTL SDPNRFKFDG DGYYLKSAAE MRQIWDDEVP GACDSTLLIA ERVQSYADVW
     TPRDRMPVFP VPDGHDQASW LRHEVDAGLR RRFPAGPPDG YRERAAYEID VICSKGFPSY
     FLIVADLISY ARSAGIRVGP GRGSAAGSLV AYALGITDID PIPHGLLFER FLNPERTSMP
     DIDIDFDDRR RGEMVRYAAD KWGHDRVAQV ITFGTIKTKA ALKDSARIHY GQPGFAIADR
     ITKALPPAIM AKDIPLSGIT DPSHERYKEA AEVRGLIETD PDVRTIYQTA RGLEGLIRNA
     GVHACAVIMS SEPLTEAIPL WKRPQDGAII TGWDYPACEA IGLLKMDFLG LRNLTIIGDA
     IDNVRANRGI DLDLESVPLD DKATYELLGR GDTLGVFQLD GGPMRDLLRR MQPTGFEDVV
     AVIALYRPGP MGMNAHNDYA DRKNNRQAIK PIHPELEEPL REILAETYGL IVYQEQIMRI
     AQKVASYSLA RADILRKAMG KKKREVLEKE FEGFSDGMQA NGFSPAAIKA LWDTILPFAD
     YAFNKSHAAG YGMVSYWTAY LKANYPAEYM AGLLTSVGDD KDKAAVYLAD CRKLGITVLP
     PDVNESGLNF ASVGQDIRYG LGAVRNVGAN VVGSLLQTRN DKGKFTDFSD YLNKIDISAC
     NKKVTESLIK AGAFDSLGHA RKGLFLVHSD AVDSVLGTKK AEALGQFDLF GSNDDGTGTA
     DPVFTIKVPD DEWEDKHKLA LEREMLGLYV SGHPLNGVAH LLAAQVDTAI PAILDGDVPN
     DAQVRVGGIL ASVNRRVNKN GMPWASAQLE DLTGGIEVMF FPHTYSSYGA DIVDDAVVLV
     NAKVAVRDDR IALIANDLTV PDFSNAEVER PLAVSLPTRQ CTFDKVSALK QVLARHPGTS
     QVHLRLISGD RITTLALDQS LRVTPSPALM GDLKELLGPG CLGS