ID   DPO3A_BORBU             Reviewed;        1147 AA.
AC   O51526;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=BB_0579;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC66944.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000783; AAC66944.1; ALT_INIT; Genomic_DNA.
DR   PIR; B70172; B70172.
DR   RefSeq; NP_212713.1; NC_001318.1.
DR   AlphaFoldDB; O51526; -.
DR   SMR; O51526; -.
DR   STRING; 224326.BB_0579; -.
DR   PRIDE; O51526; -.
DR   EnsemblBacteria; AAC66944; AAC66944; BB_0579.
DR   KEGG; bbu:BB_0579; -.
DR   PATRIC; fig|224326.49.peg.970; -.
DR   HOGENOM; CLU_001600_0_0_12; -.
DR   OMA; NECRRMG; -.
DR   Proteomes; UP000001807; 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..1147
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103311"
SQ   SEQUENCE   1147 AA;  130656 MW;  0A8F7EFE74C57B2F CRC64;
     MSFRSRFIHL HVHSDYSLLD GAAKISDIIS KAKKCNMSHI ALTDHGNLFG AIKFYKEAKK
     AGIKPIIGIE AYMAKTSKFL KKQDDLGKMS YHLILLAKNE LGYKNLLKLT SISYLEGFYY
     RPRIDKDDLE KYSEGLICTS ACIGGLIPRL ILANRFEDAK NEILWFKKVF GNDFYLELQR
     HGIKDQDIVN ERLVKYSREL GVPLTAANDS HYVNREDATA QDIIVCIGTG AKKSDENRLK
     METNEFYIKS QEEMCELFND LPEALENTVR IAEKCDDFKI TFPGPILPDY QIPVEFNTLG
     EYLEHLTLEG LKFRYKNLTS KIKDRAFYEL SVIIGMGFEG YFLIVWDFIK FAHDNDIPVG
     AGRGSGAGSI VAYALRITDI DPLKYNLLFE RFLNPERISM PDFDIDFCFE GRDEIIKYVT
     NKYGEDKVAQ IITFGTLKPK AVVKDVARVL DIPFAESNEL TKFIPDGPKV SLKEVLDDNS
     LKECFTSKPV YKELMNAALV LEGMNRHAST HAAGIVISKT PLTDYVPLYK DYKQGSVSTQ
     YTMDLLEECG LVKMDFLGLK TLTLIKNAEN LIRSVNPDFK IKNIPDNDVK TFNMLGEGRS
     ASVFQFESEG MQQILKDAKP DSIEDLIALN ALYRPGPMQF IPQFIAAKKG VKRIKYPHPD
     LKEVLRPTYG VIVYQEQVME VAKIIGGFSL GKADILRRAM GKKKEDEMNE MKVDFLRGAI
     EKGYDKEIAS EIFELLKPFS GYGFNKSHAA AYSLIAYQTA YLKANYPEYF MAANLTNEIN
     NNDKLSYYIE ESKAIGINVL KPDINRSFRE FRVTDSGISY GLNGIKNLGG IVVDLIIDER
     EKNGKYSSFE DFIRRVDDKV INKKFLESAI KSGLFDSLDQ NRKTLFENLD HLIEVVSEDK
     NNKKLGQNSL FGALESQDPI QQSFNYQTFK EYSYSELLGF EKELLGFYVS GHPLDPYKKA
     IDSFSSLNVL TDLAAKKDSI VQFSGILNSV KVIQTKRNNA KMAFGVIEDF KGAIDIVVFT
     ESYERYRNFL LEGNVIGVVG RLTFNRDKFS IVVEKVVNIE RLSEYKINNI HIKFLNNKLN
     DLQLLNSLKE SISNFEDNSG FSNVYFYLRE NGKDLKLKMN SILNFVPDED KLDKLRKCVI
     VEDVWVD