ID   DPO3A_MYCLE             Reviewed;        1177 AA.
AC   Q9X7F0;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=ML1207; ORFNames=MLCB458.21;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(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=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; AL049478; CAB39586.1; -; Genomic_DNA.
DR   EMBL; AL583921; CAC31588.1; -; Genomic_DNA.
DR   PIR; A87060; A87060.
DR   RefSeq; NP_301875.1; NC_002677.1.
DR   RefSeq; WP_010908196.1; NC_002677.1.
DR   AlphaFoldDB; Q9X7F0; -.
DR   SMR; Q9X7F0; -.
DR   STRING; 272631.ML1207; -.
DR   EnsemblBacteria; CAC31588; CAC31588; CAC31588.
DR   KEGG; mle:ML1207; -.
DR   PATRIC; fig|272631.5.peg.2215; -.
DR   Leproma; ML1207; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_11; -.
DR   OMA; NECRRMG; -.
DR   Proteomes; UP000000806; 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; Reference proteome; Transferase.
FT   CHAIN           1..1177
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103328"
SQ   SEQUENCE   1177 AA;  128972 MW;  E53599FE950DDB6B CRC64;
     MNQSSFVHLH NHTEYSMLDG AAKITPMFAE VERLQMPAVG MTDHGNMFGA SEFYNTAIKA
     GIKPIIGVEA YIAPGSRFDT RRITWGDPSQ KADDVSAGGA YTHLTMVAEN AAGLRNLFKL
     SSLASFEGQL SKWSRMDAEL IGEYAEGIIV TTGCPSGEVQ TRLRLGHDRE ALESAAKWRE
     IVGPDNYFLE LMDHGLSIEQ RVREGLLNIG RKLNIPPLAT NDCHYVTRDA VHNHEALLCV
     QTGKTLSDPN RFKFHGDGYY LKSAAEMRQL WDDEVPGACD STLLIAERVQ SYADVWEPRN
     RMPVFPVPVG HDQASWLRHE VDAGLKRRFP DGPPNGYVER AAYEIDVICD KGFPAYFLIV
     ADLVNHARSV GIRVGPGRGS AAGSLAAYAL GITDIDPIPH GLLFERFLNP ERTSMPDIDI
     DFDDRRRGEM VRYAADKWGH DRVAQVITFG TIKTKAALKD SARIHYGQPG FAMADRITKA
     LPPAIMAKDI PLSGITDPAH ERFKEAAEVR SLIETDSDVR IIYQTARGLE GLIRNAGVHA
     CAVILSSEPL TEAIPLWKRP QDGAIITGWD YPACEAIGLL KMDFLGLRNL TIIGDAIENI
     KTNRGIDLDL ESVPLDDQAT YELLGRGDTL GVFQLDGGPM RDLLRRMQPT GFEDIVAVLA
     LYRPGPMGMN AHNDYADRKN NRQVIKPIHP ELEEPLREIL AETYGLIVYQ EQIMRIAQKV
     AGYSLARADI LRKAMGKKKR EVLEKEFEGF SEGMQANGFS VHAIKALWDI ILPFADYAFN
     KSHAAGYGLI SYWTAYLKAN FAGEYMAGLL TSVGDDKDKA AVYLADCRKF GITVLPPDVN
     ESVLDFASVG ADIRYGLGAV RNVGANVVGS LIKTRNAKGK FADFSDYLNK IDITSCNKKV
     TESLIKAGAF DSLGHSRKGL FLVHADAVDS VLGTKKAEAI GQFDLFGGTD GGTDAVFTIK
     VPDDEWEDKH KLALEREMLG LYVSGHPLNG VAHLLAAQVD TAIPTILDGG VSNDTQVRVG
     GILAAVNRRV NKNGIPWASA QLDDLTGGIE VMFFPHTYSS YGADIIDDAV VLVNAKVVVR
     DDRIALIANQ LVVPDFSNVQ EDRPLAVSLL TRQCTFDKVN ALKQVLARHP GTSQVHLRLI
     SGDRITTLEL DQSLRVTSSP ALMGDLKALL GPGCLGD