ID   DPO3A_SALTY             Reviewed;        1160 AA.
AC   P14567;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; Synonyms=polC; OrderedLocusNames=STM0231;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2676978; DOI=10.1128/jb.171.10.5581-5586.1989;
RA   Lancy E.D., Lifsics M.R., Munson P., Maurer R.;
RT   "Nucleotide sequences of dnaE, the gene for the polymerase subunit of DNA
RT   polymerase III in Salmonella typhimurium, and a variant that facilitates
RT   growth in the absence of another polymerase subunit.";
RL   J. Bacteriol. 171:5581-5586(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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].
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; M29701; AAA27057.1; -; Genomic_DNA.
DR   EMBL; M26046; AAA27191.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL19195.1; -; Genomic_DNA.
DR   PIR; A45915; A45915.
DR   RefSeq; NP_459236.1; NC_003197.2.
DR   RefSeq; WP_001294826.1; NC_003197.2.
DR   AlphaFoldDB; P14567; -.
DR   SMR; P14567; -.
DR   STRING; 99287.STM0231; -.
DR   PaxDb; P14567; -.
DR   PRIDE; P14567; -.
DR   EnsemblBacteria; AAL19195; AAL19195; STM0231.
DR   GeneID; 1251749; -.
DR   KEGG; stm:STM0231; -.
DR   PATRIC; fig|99287.12.peg.244; -.
DR   HOGENOM; CLU_001600_0_2_6; -.
DR   OMA; NECRRMG; -.
DR   PhylomeDB; P14567; -.
DR   BioCyc; SENT99287:STM0231-MON; -.
DR   Proteomes; UP000001014; 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_0000103338"
FT   CONFLICT        405
FT                   /note="D -> S (in Ref. 1; AAA27191)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        782
FT                   /note="F -> I (in Ref. 1; AAA27191)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        997
FT                   /note="A -> S (in Ref. 1; AAA27191)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1127
FT                   /note="R -> G (in Ref. 1; AAA27057/AAA27191)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1160 AA;  130218 MW;  2E9651A7C7429533 CRC64;
     MSEPRFVHLR VHSDYSMIDG LAKTGPLVKK AASLGMPALA ITDFTNLCGL VKFYGAGHGA
     GIKPIVGADF NVHNELLGDE LTHLTVLAAN NTGYQNLTLL ISKAYQRGYG AAGPIIERDW
     LVELKEGLIL LSGGRMGDVG RCLLRGNQAL VEECVAFYEA HFPDRYFLEL IRTGRQDEET
     YLHAAVELAE ARGLPVVATN DVRFLESDDF DAHEIRVAIH DGFTLDDPKR PRNYSPQQYM
     RSEEEMCELF SDIPEALENT VEIAKRCNVT VRLGEYFLPQ FPTGDMTTED YLVKKAKEGL
     EERLAFLFPD EEERKKRRPE YDERLDIELQ VINQMGFPGY FLIVMEFIQW SKDNGVPVGP
     GRGSGAGSLV AYALKITDLD PLEFDLLFER FLNPERVSMP DFDVDFCMEK RDQVIEHVAD
     MYGRDAVSQI ITFGTMAAKA VIRDVGRVLG HPYGFVDRIS KLVPPDPGMT LAKAFEAEPQ
     LPEIYEADEE VRALIDMARK LEGVTRNAGK HAGGVVIAPT KITDFAPLYC DEEGKHPVTQ
     FDKSDVEYAG LVKFDFLGLR TLTIINWALE MINKRRAKNG EPPLDIAAIP LDDKKSFDML
     QRSETTAVFQ LESRGMKDLI KRLQPDCFED MIALVALFRP GPLQSGMVDN FIDRKHGREE
     LSYPDVQWQH ESLKPVLEPT YGIILYQEQV MQIAQVLSGY TLGGADMLRR AMGKKKPEEM
     AKQRSVFEEG AKKNGIDGEL AMKIFDLVEK FAGYGFNKSH SAAYALVSYQ TLWLKAHYPA
     EFMAAVMTAD MDNTEKVVGL VDECWRMGLK ILPPDINSGL YHFHVNDEGE IVYGIGAIKG
     VGEGPIEAII DARNQGGYFR ELFDLCARTD TKKLNRRVLE KLIMSGAFDR LGPHRAALMN
     SLGDALKAAD QHAKAEAIGQ TDMFGVLAEE PEQIEQSYAS CQPWPEQVVL DGERETLGLY
     LTGHPINQYL KEIERYVGGV RLKDMHPTER GKVTTAAGLV IAARVMVTKR GNRIGICTLD
     DRSGRLEVML FTDALDKYQQ LLEKDRILIV SGQVSFDDFS GGLKMTAREV MDIDEAREKY
     ARGLAISLTD RQIDDQLLNR LRQSLEPHRS GTIPVHLYYQ RADARARLRF GATWRVSPSD
     RLLNDLRGLI GSEQVELEFD