ID   DPO3A_LACLA             Reviewed;        1060 AA.
AC   Q9CI70;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   02-SEP-2026, entry version 135.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=LL0496; ORFNames=L0307;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC         diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC         COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC         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; AE005176; AAK04594.1; -; Genomic_DNA.
DR   PIR; H86686; H86686.
DR   RefSeq; WP_003131504.1; NC_002662.1.
DR   AlphaFoldDB; Q9CI70; -.
DR   SMR; Q9CI70; -.
DR   EnsemblBacteria; AAK04594; AAK04594; L0307.
DR   KEGG; lla:L0307; -.
DR   PATRIC; fig|272623.7.peg.539; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_1_9; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000002196; 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-EC.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   CDD; cd04485; DnaE_OBF; 1.
DR   CDD; cd07431; PHP_PolIIIA; 1.
DR   Gene3D; 1.10.150.870; -; 1.
DR   Gene3D; 1.10.10.1600; Bacterial DNA polymerase III alpha subunit, thumb domain; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR004805; DnaE2/DnaE/PolC.
DR   InterPro; IPR029460; DNAPol_HHH.
DR   InterPro; IPR012340; NA-bd_OB-fold.
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   NCBIfam; TIGR00594; polc; 1.
DR   NCBIfam; NF005582; PRK07279.1; 1.
DR   PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR32294:SF0; DNA POLYMERASE III SUBUNIT ALPHA; 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; PHP domain-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA replication; DNA-directed DNA polymerase;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..1060
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103325"
SQ   SEQUENCE   1060 AA;  121572 MW;  44B03F0937A8D3E6 CRC64;
     MFAPLNTKTE YSFLDSVVKV DDYLETAHRL GYQTVGICDV GNLHAAFRFV RKAQKFNLQP
     IISIELNFEW RGLPIAFSFI AKDTEGYKNL LRISTLHNYG RRQFSDIQNH LSGIALIIPE
     TYGSLSELTE LSSVADEAFI GIDQLTDKGA KFNLPTLPFP AIRYLNFADN EILAILHAVR
     DGVSFDESLT ISSNELLQRP EAYETYFLKY FPQALKNLSA LTAKIAYQFD EKLELPRFDK
     KRQAVEHLRE EATLGLSARL EEKNLLTEVS SVNLQDLSVY QERLEKELSV IHQMGFDDYF
     LIVADLLRYA REQDIYCGMG RGSAAGSLVA YVLGITQVDP VQHNLFFERF LNPERVAMPD
     IDIDMPDDRR AELLAYMKNR YGSDHVAQIV TFSTLGKRQA LRDVGKAFGM TEAELSNLTR
     MLVRRFGTLA DEYENNQRFK AEVLKNGKLK RIYEVARRIE GMPRQTSTHA SGVVLSEESL
     VNYVSLKPSE DLALTQYEAP DVEAIGLLKI DFLGLRNLTI ISRLRDLVKR RQKIDIDPLK
     INLEDEDTLA LFRAGNTMGI FQFENPQMRR FLRNLAPSKF DDIVDATSIF RPGPSQFIPQ
     FVARRHGKEI VPTVDDSISE ILKPTYGIMI YQEQIMQVAQ AFAGFSLGKA DLLRRAISKK
     KGSELEKLRE DFLDSASHNG HSKEKAEEIY DLIERFANYG FNRSHGFAYG ALAFQIAYFK
     AHFPDEFYEI QLRDRKREVM ILDALENGFE IEKPSINLMK IGDFVKNKKI RLGLAHVQGI
     SRDLAKWIVE NQPYKDLADF VEKLPNNFHK KENILPLIQI GAFDYADSNR GKLAYNLADH
     ANLLNYYSDD IFMASSGGGF AYHEAEDYSE TEKYDFEKNL LGIGVTPHPL QNLARRFEGN
     FTPLAQLVKN RRMTILVEIN YIRTHRTKTG QTMAFLTVSD SRENFDVTLF PEIYRQFSGE
     LEQGKFYLIS GKVTERNDEL QLVTDRISPA LETDRKLWLN LRDDKYNQKI SQILREFPGS
     HQVILHYSNL KKTIQTKIYV EESEILQKRL EGYVIAGIYK
//