ID   DPO3A_ECO57             Reviewed;        1160 AA.
AC   Q8X8X5; Q7AHM0;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=Z0196, ECs0186;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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.
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: The DNA polymerase holoenzyme is a complex that contains 10
CC       different types of subunits. These subunits are organized into 3
CC       functionally essential subassemblies: the pol III core, the beta
CC       sliding clamp processivity factor and the clamp-loading complex. The
CC       pol III core (subunits alpha,epsilon and theta) contains the polymerase
CC       and the 3'-5' exonuclease proofreading activities. The polymerase is
CC       tethered to the template via the sliding clamp processivity factor. The
CC       clamp-loading complex assembles the beta processivity factor onto the
CC       primer template and plays a central role in the organization and
CC       communication at the replication fork. This complex contains delta,
CC       delta', psi and chi, and copies of either or both of two different DnaX
CC       proteins, gamma and tau. The composition of the holoenzyme is,
CC       therefore: (alpha,epsilon,theta)[2]-(gamma/tau)[3]-delta,delta',
CC       psi,chi-beta[4] (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; AE005174; AAG54486.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33609.1; -; Genomic_DNA.
DR   PIR; B85503; B85503.
DR   PIR; B90652; B90652.
DR   RefSeq; NP_308213.1; NC_002695.1.
DR   RefSeq; WP_001294772.1; NZ_SEKU01000001.1.
DR   AlphaFoldDB; Q8X8X5; -.
DR   SMR; Q8X8X5; -.
DR   STRING; 155864.EDL933_0189; -.
DR   PRIDE; Q8X8X5; -.
DR   EnsemblBacteria; AAG54486; AAG54486; Z0196.
DR   EnsemblBacteria; BAB33609; BAB33609; ECs_0186.
DR   GeneID; 913906; -.
DR   KEGG; ece:Z0196; -.
DR   KEGG; ecs:ECs_0186; -.
DR   PATRIC; fig|386585.9.peg.289; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_2_6; -.
DR   OMA; NECRRMG; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; Reference proteome; Transferase.
FT   CHAIN           1..1160
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000239871"
SQ   SEQUENCE   1160 AA;  129900 MW;  52E9F4B19C98176D CRC64;
     MSEPRFVHLR VHSDYSMIDG LAKTAPLVKK AAALGMPALA ITDFTNLCGL VKFYGAGHGA
     GIKPIVGADF NVQCDLLGDE LTHLTVLAAN NTGYQNLTLL ISKAYQRGYG AAGPIIDRDW
     LIELNEGLIL LSGGRMGDVG RSLLRGNSAL VDECVAFYEE HFPDRYFLEL IRTGRPDEES
     YLHAAVELAE ARGLPVVATN DVRFIDSSDF DAHEIRVAIH DGFTLDDPKR PRNYSPQQYM
     RSEEEMCELF ADIPEALANT VEIAKRCNVT VRLGEYFLPQ FPTGDMSTED YLVKRAKEGL
     EERLAFLFPD EEERVKRRPE YDERLETELQ 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 GKVITAAGLV VAARVMVTKR GNRIGICTLD
     DRSGRLEVML FTDALDKYQH LLEKDRILIV SGQVSFDDFS GGLKMTAREV MDIDEAREKY
     ARGLAISLTD RQIDDQLLNR LRQSLEPHRS GTIPVHLYYQ RADARARLRF GATWRVSPSD
     RLLNDLRGLI GSEQVELEFD