ID   DPO3A_STRCO             Reviewed;        1179 AA.
AC   Q9Z618;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 125.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=SCO2064; ORFNames=SC4G6.33c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=10048037; DOI=10.1046/j.1365-2958.1999.01237.x;
RA   Flett F., Jungmann-Campello D., Mersinias V., Koh S.L.-M., Godden R.,
RA   Smith C.P.;
RT   "A 'Gram-negative-type' DNA polymerase III is essential for replication of
RT   the linear chromosome of Streptomyces coelicolor A3(2).";
RL   Mol. Microbiol. 31:949-958(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(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   -!- 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}.
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DR   EMBL; AF108191; AAD16978.1; -; Genomic_DNA.
DR   EMBL; AL939111; CAB51456.1; -; Genomic_DNA.
DR   PIR; T35093; T35093.
DR   RefSeq; NP_626324.1; NC_003888.3.
DR   RefSeq; WP_003976751.1; NZ_VNID01000001.1.
DR   AlphaFoldDB; Q9Z618; -.
DR   SMR; Q9Z618; -.
DR   STRING; 100226.SCO2064; -.
DR   PRIDE; Q9Z618; -.
DR   GeneID; 1097498; -.
DR   KEGG; sco:SCO2064; -.
DR   PATRIC; fig|100226.15.peg.2096; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_11; -.
DR   InParanoid; Q9Z618; -.
DR   OMA; NECRRMG; -.
DR   PhylomeDB; Q9Z618; -.
DR   Proteomes; UP000001973; 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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.1600; -; 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; 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   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..1179
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103348"
FT   REGION          77..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         802
FT                   /note="E -> K (in mutant TS-38)"
SQ   SEQUENCE   1179 AA;  130796 MW;  7E4B58675B634CD3 CRC64;
     MSKPPFTHLH VHTQYSLLDG AARLKDMFDA CNEMGMSHIA MSDHGNLHGA YDFFHSAKKA
     GVTPIIGIEA YVAPESRRNK RKIQWGQPHQ KRDDVSGSGG YTHKTMWATN SKGLHNLFRL
     SSDAYAEGWL QKWPRMDKET ISQWSEGIVA STGCPSGEVQ TRLRLGHFDE ALKAAADYQD
     IFGKDRYFLE LMDHGIEIEH RVRDGLLEIG RKLGIPPLVT NDSHYTYAHE ATAHDALLCI
     QTGKNLSDPD RFRFDGTGYY LKSTDEMYAI DSSDAWQEGC ANTRLIAEMI DTTGMFEKRD
     LMPKFDIPEG FTEITWFQEE VRRGMERRFP GGVPEDRQKQ AEYEMDVIIQ MGFPGYFLVV
     ADFIMWAKNQ GIAVGPGRGS AAGSIVAYAM GITDLDPIPH GLIFERFLNP ERVSMPDVDI
     DFDERRRVEV IRYVTEKYGA DKVAMIGTYG KIKAKNAIKD SARVLGYPYA MGDRLTKAMP
     ADVLGKGIDL NGITDPTHPR YSEAGEIRSM YESEPDVKKV IDTAKGVEGL VRQMGVHAAG
     VIMSSEPIVD HAPIWVRHTD GVTITQWDYP QCESLGLLKM DFLGLRNLTI MDDAVKMVKS
     NKGIDLDLLS LPLDDPTTFE LLQRGDTLGV FQFDGGPMRS LLRLMKPDNF EDISAVSALY
     RPGPMGMDSH TNYALRKNGL QEITPIHKEL EEPLQEVLAV TYGLIVYQEQ VQKAAQIIAG
     YSLGEADILR RVMGKKKPDE LAKNFVLFQA GARKNGYSDE AIQALWDVLV PFAGYAFNKA
     HSAAYGLVSY WTGYLKANYP AEYMAALLTS VKDDKDKSAV YLNECRRMGI KVLPPNVNES
     MSNFAAQGDD VILFGLSAVR NVGTNVVESI IKCRKAKGKY ASFPDYLDKV EAVVCNKRTT
     ESLIKAGAFD EMGHTRKGLT AQYEPMIDNV VAVKRKEAEG QFDLFGGMGD EQSDEPGFGL
     DVVFGEDEWD KTYLLAQERE MLGLYVSDHP LFGLEHVLSD KADAGISQLT GGDFGDGAVV
     TIGGIISGLQ RKMTKQGNAW AIATVEDLAG SLECMFFPAT YQLVSTQLVE DAVVFVKGRL
     DKREDVPRLV AMELMIPDLS NAGTNAPVVL TIPATRITPP MVSRLGEILT HHRGDSEVRI
     KLQGPTKTTV LRLDRHRVKP DPALFGDLKV LLGPSCLAG