ID   DPO3A_YERPE             Reviewed;        1174 AA.
AC   O68770;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1999, sequence version 2.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=YPMT1.89/YPMT1.56c, Y1106;
OS   Yersinia pestis.
OG   Plasmid pMT1 (pMT-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=9826348; DOI=10.1128/iai.66.12.5731-5742.1998;
RA   Lindler L.E., Plano G.V., Burland V., Mayhew G.F., Blattner F.R.;
RT   "Complete DNA sequence and detailed analysis of the Yersinia pestis KIM5
RT   plasmid encoding murine toxin and capsular antigen.";
RL   Infect. Immun. 66:5731-5742(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-1174.
RC   STRAIN=KIM5 / Biovar Mediaevalis;
RX   PubMed=9748454; DOI=10.1128/jb.180.19.5192-5202.1998;
RA   Hu P., Elliott J., McCready P., Skowronski E., Garnes J., Kobayashi A.,
RA   Brubaker R.R., Garcia E.;
RT   "Structural organization of virulence-associated plasmids of Yersinia
RT   pestis.";
RL   J. Bacteriol. 180:5192-5202(1998).
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   -!- CAUTION: In strain CO-92 it seems to be a pseudogene which is encoded
CC       in two separate ORFs on the plasmid. {ECO:0000305}.
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DR   EMBL; AF074611; AAC82764.1; -; Genomic_DNA.
DR   EMBL; AL117211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF053947; AAC13215.1; -; Genomic_DNA.
DR   PIR; T14699; T14699.
DR   PIR; T15021; T15021.
DR   RefSeq; NP_857689.3; NC_004835.1.
DR   RefSeq; WP_002221186.1; NZ_WUCM01000058.1.
DR   RefSeq; WP_011114025.1; NC_004835.1.
DR   RefSeq; YP_093946.1; NC_006323.1.
DR   AlphaFoldDB; O68770; -.
DR   SMR; O68770; -.
DR   EnsemblBacteria; AAC82764; AAC82764; AAC82764.
DR   KEGG; ypk:Y1106.pl; -.
DR   HOGENOM; CLU_001600_0_1_6; -.
DR   OMA; DKRACAC; -.
DR   Proteomes; UP000000815; Plasmid pMT1 (pMT-1).
DR   Proteomes; UP000002490; Plasmid pMT-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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.470.10; -; 1.
DR   InterPro; IPR011708; DNA_pol3_alpha_NTPase_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; IPR004805; PolC_alpha.
DR   InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR   PANTHER; PTHR32294; PTHR32294; 2.
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; SSF52141; SSF52141; 1.
DR   TIGRFAMs; TIGR00594; polc; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA replication; DNA-directed DNA polymerase;
KW   Nucleotidyltransferase; Plasmid; Reference proteome; Transferase.
FT   CHAIN           1..1174
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103361"
SQ   SEQUENCE   1174 AA;  130370 MW;  79C14A2A803FFD0E CRC64;
     MKALMVRTDF SLGESALKAE NAVKIARDAG YTAVISADSM NIASVIPLQR AAGDDMAVIC
     GVKLNVVDDP TYEHRARLAK ESERCMESLV RDRSYCFTAL IKNEQGYRDV CELMTLANKR
     EQFYFVPRLA LDQLAAAYAK GNIILLTSDI GSVFQRRDFA KIIGTLVTAG GRDNFYSVVY
     PHPTPFYDQI NVRAMKVASA LKIEPVAFYP AYYEAVDDAD IKDIAHMVTN NIKIDQPHRL
     RIPHQRDNAV NGRRHLLEAL KAFSVRMDVP VTAAMASTTQ DTIIEACTWR WHELPPALPK
     MADDEPATLM KLAVAGLRKR LTTKEFGYTP PASEHRVYVD RLKYEMDTLT RLGFCGYFLM
     VRDLMNHSRE TGIPVGPGRG SSAGSLVAWC IGITNVDPIR HGLLFERFIN PERLDLPDAD
     LDFSQARRHE VIEYLNERYG EDYVAGIPNF TYLGAASALR DTARIYGVDA ADMAVSKEFK
     NLEDDSLSLE ELREQLASLD KYATKYPEAF KAACKLQSLM RGFGRHAAGM IVAGVPLVER
     TPVELRGNAR CIAFDKRYCE AMGLIKLDVL GLATLDLLDS AKRYIKESTG EDINLDAIPL
     DDRKVLDGFA AGYTQGVFQL ESGPMRKLLK DLGGGIEPMS FKTVVATTAL FRPGPIQSGM
     LDDYVSVAKG FMAPQSLHPV LDELTAETNG VILYQEQTMN ATRLLAGFTM AEADGVRKAI
     GKKDMEKMKS MGEKFVVQAQ AGWIDVEMED GTTQRIHRAE HFKCEDGALR TVEEALEAGV
     KLPMAAVRVT GSQPGLSETK AKEIWDAFEK NGAYQFNKSH PVAYSLISYQ SMWLKTHYPA
     EFFAAALTIL GEDKHQGLVK DALTYGIHVL PPDVNVSSNR IEIRTLEDGS QVLYAPFSAV
     KGCSENGCQA IMRAREKVGG KFESLEQFEE AVEKRACACN SRVRESLQKV GAFASIEPGS
     LPATDPERLR DQAELMGNLV IDAVKASRPF EMNPKRSAEV NVLMTRMAAE MGLGDDLIRP
     SIGIKPKIMV ILDNANGNDG RTGYFMENGY DDFKAKLLTA GDLRMGDLYV TGVCKKVKDK
     EKDYTKDEIG QFTDFMREEI NLVRPTYVLT CGSRATSLFN NKSKPSDLVG RKEYLPELDV
     TVFYGFNPNI LYFRPEEGEK LEAILAEVAE TISK