ID   DPO3A_NEIMA             Reviewed;        1144 AA.
AC   Q9JVX8; A1IQ69;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=NMA0632;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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; AL157959; CAM07897.1; -; Genomic_DNA.
DR   PIR; A81983; A81983.
DR   RefSeq; WP_002247062.1; NC_003116.1.
DR   AlphaFoldDB; Q9JVX8; -.
DR   SMR; Q9JVX8; -.
DR   EnsemblBacteria; CAM07897; CAM07897; NMA0632.
DR   KEGG; nma:NMA0632; -.
DR   HOGENOM; CLU_001600_0_0_4; -.
DR   OMA; NECRRMG; -.
DR   BioCyc; NMEN122587:NMA_RS03205-MON; -.
DR   Proteomes; UP000000626; 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   Gene3D; 2.40.50.140; -; 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; 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   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; Transferase.
FT   CHAIN           1..1144
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103331"
SQ   SEQUENCE   1144 AA;  126976 MW;  95270191E29EB412 CRC64;
     MTEPTYIPLR LHTEFSITDG MVRIKKLIAK AQEYGLPALG ISDLMNEFGL VKFYKACRSA
     GIKPIGAADV RIGNPDAPDK PFRAMLIIRN DAGYLRLSEL LTAAYVGKDR NVHHAELNPE
     WLENGDNSGL ICLSGAHYGE VGVNLLNGNE DAARAAALKY AAWFPDAFYL ELQRLPERPE
     WEACVSGSVK LAEELGLPVV ATHPTQFMSR DDFNAHEARV CIAGGWVLTD KKRPRDFTPS
     QFFIPPETMA ERFSDLPEAL ENTVEIAKRC NLHITLGKNF LPLFPTPDGL SLDDYLVKLS
     NEGLQERMVQ LYPDEAERAA KMPEYQERLD FELNIIIQMK FPGYFLIVQD FINWAKTHGC
     PVGPGRGSGA GSLVAYSLKI TDLDPLKYAL LFERFLNPER VSMPDFDVDF CQANRGRVIE
     YVREKYGAEA VSQIVTFGTM SSKAVIRDVG RVLELPFTLC DKLSKLIPLE ANKPLGLDDA
     MKAEPQIQEL IEAEEADELI TLAKKLEDLT RGLGMHAGGV LIAPGKISDY SPVYQADESA
     SPVSMYDKGD VEDVGLVKFD FLGLRNLTII EMAQNNIKNT TGDIVDVGTI PLDDQTAYQI
     FRDANTTAVF QFESTGMKKM LKTAHTTKFE ELIAFVSLYR PGPMDNIPDF VARMKGQEFQ
     YIHPLLEGIL APTYGIMVYQ EQVMQAAQII GGYSLGGADL LRRAMGKKKP EEMVKHREIF
     AEGAAKQGIS REKSDEIFNY MEKFAGYGFN KSHAAAYALI SYQTAWLKAH YPAEFMAATM
     SSELDNTDQL KHFYDDCRAN GIEFLPPDIN ESDYRFTPYP DMKIRYALGA IKGTGEAAVE
     SITSARQSGG KFTGLLDFCE RVGKEHMNRR TLEALIRGGA FDSIEPNRAM LLANIDLAMN
     NADQKAANAN QGGLFDMMED AIEPVRLIDA PMWSESEKLA EEKTVIGFYL SGHPFGPYAQ
     EVRQIAPQKL SKLKPQDSVR LAGFVTAVRT MMGKRGKIAF VSLEDLSGQV EIMVGGQTLE
     NCADCLKADQ VLIIESKVSR DDYGGGDGLR ILANQVMTLQ TARERYARSL SLALAPHHDI
     GELVQLLAAH QLPDTPRIPL QLSYANEKAS GRLQVPPKWT VTPSSALFGE LETLLGSRSV
     RVNW