ID   DPO3A_VIBCH             Reviewed;        1159 AA.
AC   P52022; Q9KPW7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 3.
DT   25-MAY-2022, entry version 136.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=VC_2245;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=El Tor Inaba C6706 / Serotype O1;
RX   PubMed=8917113; DOI=10.1016/0378-1119(96)00155-2;
RA   Franco A.A., Yeh P.E., Johnson J.A., Barry E.M., Guerra H., Maurer R.,
RA   Morris J.G. Jr.;
RT   "Cloning and characterization of dnaE, encoding the catalytic subunit of
RT   replicative DNA polymerase III, from Vibrio cholerae strain C6706.";
RL   Gene 175:281-283(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF95389.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U30472; AAC44578.1; -; Genomic_DNA.
DR   EMBL; AE003852; AAF95389.1; ALT_INIT; Genomic_DNA.
DR   PIR; G82100; G82100.
DR   RefSeq; NP_231876.1; NC_002505.1.
DR   RefSeq; WP_001909664.1; NZ_LT906614.1.
DR   AlphaFoldDB; P52022; -.
DR   SMR; P52022; -.
DR   STRING; 243277.VC_2245; -.
DR   DNASU; 2613167; -.
DR   EnsemblBacteria; AAF95389; AAF95389; VC_2245.
DR   GeneID; 57740868; -.
DR   KEGG; vch:VC_2245; -.
DR   PATRIC; fig|243277.26.peg.2141; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_6; -.
DR   OMA; NECRRMG; -.
DR   Proteomes; UP000000584; Chromosome 1.
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; Reference proteome; Transferase.
FT   CHAIN           1..1159
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103358"
FT   CONFLICT        343
FT                   /note="I -> V (in Ref. 1; AAC44578)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        480..482
FT                   /note="ALQ -> ELK (in Ref. 1; AAC44578)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        680
FT                   /note="T -> P (in Ref. 1; AAC44578)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        995
FT                   /note="V -> A (in Ref. 1; AAC44578)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1025
FT                   /note="M -> L (in Ref. 1; AAC44578)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1098
FT                   /note="E -> G (in Ref. 1; AAC44578)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1112
FT                   /note="V -> A (in Ref. 1; AAC44578)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1159 AA;  130057 MW;  4C3219115D108DAA CRC64;
     MSDPKFIHLR IHSDFSMVDG LSKVPPLVKK VAAMGMPAMA LTDFTNLCGL VKFYSTAHNC
     GVKPIIGADF TLQSEEFGDE LTKLTLLAKN NVGYKNLTLL ISKAYLRGHV QHQPVIDKAW
     LVEHAEGLIV LSGGKSGEVG RALLKGNQQQ VERCIEFYQT HFADHFYLEL IRTGRADEES
     YLHFALDVAE QYDLPVVATN EVVFITEESF EAHEIRVAIH DGYTLEDPRR PKNYSPKQYL
     RSEAEMCELF ADIPEALANS VEIAKRCNVT VRLGEYFLPN FPTGGMAIED FLVMKSREGL
     EERLEFLFPD PEVRAKRRPE YDERLQVELD VINQMGFPGY FLIVMEFIQW SKDNDIPVGP
     GRGSGAGSLV AYALKITDLD PLEYDLLFER FLNPERVSMP DFDVDFCMDK RDQVIDHVAE
     MYGRDAVSQI ITFGTMAAKA VIRDVGRVLG HPFGFVDRIS KLVPPDPGMT LEKAFIAEPA
     LQELYDADEE VKELIDKCRI LEGCTRNAGK HAGGVVISPT AITDFAPIYC DAEGNFPVTQ
     FDKNDVETAG LVKFDFLGLR TLTIIDWALG LVNPRLKKAG KPPVRIEAIP LDDARSFRNL
     QDAKTTAVFQ LESRGMKELI KRLQPDCFED IIALVALFRP GPLQSGMVDN FIDRKHGREA
     ISYPDEKWQH ESLKEILEPT YGIILYQEQV MQIAQVLSGY TLGGADMLRR AMGKKKPEEM
     AKQRAVFQEG AEKNGVDGEL AMKIFDLVEK FAGYGFNKSH SAAYALVSYQ TLWLKTHYPA
     EFMAAVMTAD MDNTEKVVGL VDECKNMGLT VLPPDINSGL YRFNVDDNGA IVYGIGAIKG
     VGEGPIEAIL EARNKGGYFK DLFDFCARID LKKVNKRVIE KLILAGALDR LGPHRAAMMA
     SVDDAVRAAS QHHQAEAFGQ ADMFGVLTDA PEEVEQKYTQ VPEWPEKVRL EGERETLGLY
     LTGHPVDEYL KELTKYTSCR LNEAAPTRRD QSLTVAGLVI AARVMTTKRG TRIGLMTLDD
     RSGRMEVMLY SEALDRYAEW LEKDKILVVS GQVSFDDFNG GLKMSAREVM DLGSAREKFA
     RGLSISILQS QIDQQFFERF SHILEPHRAG TVPVNVYYQR PDARARLTLG TEWRVTPSDT
     LLDELKQLLG HDQVELEFN