ID   DPO3A_NEIMB             Reviewed;        1144 AA.
AC   Q9JXZ2;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=NMB1827;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17038831; DOI=10.4161/hv.1.2.1651;
RA   Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.;
RT   "Characterization of the protein content of a meningococcal outer membrane
RT   vesicle vaccine by polyacrylamide gel electrophoresis and mass
RT   spectrometry.";
RL   Hum. Vaccin. 1:80-84(2005).
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   -!- MISCELLANEOUS: Present in outer membrane vesicle formulations which are
CC       used as vaccines in human.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE002098; AAF42162.1; -; Genomic_DNA.
DR   PIR; H81037; H81037.
DR   RefSeq; NP_274824.1; NC_003112.2.
DR   RefSeq; WP_002225661.1; NC_003112.2.
DR   AlphaFoldDB; Q9JXZ2; -.
DR   SMR; Q9JXZ2; -.
DR   STRING; 122586.NMB1827; -.
DR   PaxDb; Q9JXZ2; -.
DR   PRIDE; Q9JXZ2; -.
DR   EnsemblBacteria; AAF42162; AAF42162; NMB1827.
DR   KEGG; nme:NMB1827; -.
DR   PATRIC; fig|122586.8.peg.2326; -.
DR   HOGENOM; CLU_001600_0_2_4; -.
DR   OMA; NECRRMG; -.
DR   Proteomes; UP000000425; 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   1: Evidence at protein level;
KW   Cytoplasm; DNA replication; DNA-directed DNA polymerase;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..1144
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103332"
SQ   SEQUENCE   1144 AA;  127136 MW;  4CEABB86F90DD7EA CRC64;
     MTEPTYIPLR LHTEFSITDG MVRIKKLIAK AQEYGLPALG ISDLMNEFGL VKFYKACRSA
     GIKPIGAADV RIGNPDAPDK PFRAMLIIRN DAGYLRLSEL LTAAYVGKDR NVHHAELNPE
     WLENGDNSGL ICLSGAHYGE VGVNLLNGNE DAARTAALKY AAWFPDAFYM ELQRLPERPE
     WEACVSGSVK LAEELGLPVV ATHPTQFMSR DDFNAHEARV CIAGGWVLTD KKRPRDFTPG
     QFFIPPETMA ERFADLPEAL ENTVEIAKRC NLHITLGKNF LPLFPTPDGL SLDDYLIKLS
     NEGLQERMVQ LYPDEAERAA KMPEYQERLD FELNIIIQMK FPGYFLIVQD FINWAKTHGC
     PVGPGRGSGA GSLVAYSLKI TDLDPLKYAL LFERFLNPER VSMPDFDVDF CQSNRGRVIE
     YVREKYGAEA VSQIVTFGTM SSKAVIRDVG RVLELPFMLC DKLSKLIPLE ANKPLSLEKA
     METEPQIQEL IEAEEADELI TLAKKLEDLT RGLGMHAGGV LIAPGKISDY SPVYQADESA
     SPVSMYDKGD VEDVGLVKFD FLGLRNLTII EMAQNNIKNT TGDIIDVGKI PLDDQVAYQI
     FRDANTTAVF QFESTGMKKM LKTAHTTKFE ELIAFVSLYR PGPMDNIPDF VARMKGQEFQ
     YIHPLLEGIL APTYGIMVYQ EQVMQAAQII GGYSLGGADL LRRAMGKKKP EEMVKHREIF
     AEGAAKQGIS REKSDEIFNY MEKFAGYGFN KSHAAAYALI SYQTAWLKAH YPAEFMAATM
     SSELDNTDQL KHFYDDCRAN GIEFLPPDIN ESDYRFTPYP DMKIRYALGA IKGTGEAAVE
     SITAARQSGG KFTGLLDFCE RVGKEHMNRR TLEALIRGGA FDSIEPNRAM LLANIDLAMD
     NADQKAANAN QGGLFDMMED AIEPVRLIDA PMWSESEKLA EEKTVIGFYL SGHPFGPYAQ
     EVRQIAPTKL DRLKPQDSVR LAGFVTAVRT MMGKRGKIAF VSLEDLSGQV EIMVGGQTLE
     NCADCLKADQ VLIIESKVSR DDYGGGDGLR ILANQVMTLQ TARERYARSL SLALAPHHDI
     GGLVRLLAAH QLPDTPRIPL QLSYANEKAS GRLQVPPKWT VTPSSALFGE LETLLGSRSV
     RVNW