ID   DPO3A_ECOL6             Reviewed;        1160 AA.
AC   Q8FL05;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=c0221;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; AE014075; AAN78713.1; -; Genomic_DNA.
DR   RefSeq; WP_001294736.1; NC_004431.1.
DR   AlphaFoldDB; Q8FL05; -.
DR   SMR; Q8FL05; -.
DR   STRING; 199310.c0221; -.
DR   EnsemblBacteria; AAN78713; AAN78713; c0221.
DR   KEGG; ecc:c0221; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_6; -.
DR   OMA; NECRRMG; -.
DR   BioCyc; ECOL199310:C0221-MON; -.
DR   Proteomes; UP000001410; 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..1160
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000239872"
SQ   SEQUENCE   1160 AA;  129891 MW;  897DD479B3547988 CRC64;
     MSEPRFVHLR VHSDYSMIDG LAKTAPLVKK AAALGMPALA ITDFTNLCGL VKFYGAGHGA
     GIKPIVGADF NVQCDLLGDE LTHLTVLAAN NIGYQNLTLL ISKAYQRGYG AAGPIIDRDW
     LIELNEGLIL LSGGRMGDVG RSLLRGNSAL VDECVAFYEE HFPDRYFLEL IRTGRPDEES
     YLHAAVELAE ARGLPVVATN DVRFIDSSDF DAHEIRVAIH DGFTLDDPKR PRNYSPQQYM
     RSEEEMCELF ADIPEALANT VEIAKRCNVT VRLGEYFLPQ FPTGDMSTED YLVKRAKEGL
     EERLAFLFPD EEERLKRRPE YDERLDTELQ VINQMGFPGY FLIVMEFIQW SKDNGVPVGP
     GRGSGAGSLV AYALKITDLD PLEFDLLFER FLNPERVSMP DFDVDFCMEK RDQVIEHVAD
     MYGRDAVSQI ITFGTMAAKA VIRDVGRVLG HPYGFVDRIS KLIPPDPGMT LAKAFEAEPQ
     LPEIYEADEE VKALIDMARK LEGVTRNAGK HAGGVVIAPT KITDFAPLYC DEEGKHPVTQ
     FDKSDVEYAG LVKFDFLGLR TLTIINWALE MINKRRAKNG EPPLDIAAIP LDDKKSFDML
     QRSETTAVFQ LESRGMKDLI KRLQPDCFED MIALVALFRP GPLQSGMVDN FIDRKHGREE
     ISYPDVQWQH ESLKPVLEPT YGIILYQEQV MQIAQVLSGY TLGGADMLRR AMGKKKPEEM
     AKQRSVFAEG AEKNGINAEL AMKIFDLVEK FAGYGFNKSH SAAYALVSYQ TLWLKAHYPA
     EFMAAVMTAD MDNTEKVVGL VDECWRMGLK ILPPDINSGL YHFHVNDDGE IVYGIGAIKG
     VGEGPIEAII EARNKGGYFR ELFDLCARTD TKKLNRRVLE KLIMSGAFDR LGPHRAALMN
     SLGDALKAAD QHAKAEAIGQ ADMFGVLAEE PEQIEQSYAS CQPWPEQVVL DGERETLGLY
     LTGHPINQYL KEIERYVGGV RLKDMHPTER GKVTTAAGLV VAARVMVTKR GNRIGICTLD
     DRSGRLEVML FTDALDKYQQ LLEKDRILIV SGQVSFDDFS GGLKMTAREV MDIDEAREKY
     ARGLAISLTD RQIDDQLLNR LRQSLEPHRS GTIPVHLYYQ RADARARLRF GATWRVSPSD
     RLLNDLRGLI GSEQVELEFD