ID   DPO3A_RICTY             Reviewed;        1180 AA.
AC   Q68VX1;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=RT0765;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU04221.1; -; Genomic_DNA.
DR   RefSeq; WP_011191196.1; NC_006142.1.
DR   AlphaFoldDB; Q68VX1; -.
DR   SMR; Q68VX1; -.
DR   STRING; 257363.RT0765; -.
DR   EnsemblBacteria; AAU04221; AAU04221; RT0765.
DR   KEGG; rty:RT0765; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_5; -.
DR   OMA; NECRRMG; -.
DR   OrthoDB; 561611at2; -.
DR   Proteomes; UP000000604; 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; Transferase.
FT   CHAIN           1..1180
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000280958"
SQ   SEQUENCE   1180 AA;  133515 MW;  D78D3B1C77A39A71 CRC64;
     MQSEFIHLRT QSSYSFLESA LTIEKVVELA LLHKMPALCL SDRGNLFGSL EFALYAVKKK
     LQPIHGVILN IQYDINVFAQ ILLIAKDETG YKNLLKLSSL TFTKNDRKIC DHINFEDLIK
     YQEGLIALCC YTDGIVGKCL LARKQEHAIM FARRLQAILG DRFYFEIMRH DLPEEQFIEN
     SYIQIASELS IPIVATNKVL FSEKSMHYAH DVLLCISEGV TKEYPDRKTV SENCYFKSPA
     EMKKLFSDLP NAIQNTVNLR ERCYFAAHPN PPMLPNFSTQ DISETYLIRK YAKEGLLARL
     VTKFKAENIS REHQEKLKTE YFTRLNYELD IICNMNFAGY FLIVSDFIKW SKKHGILVGP
     GRGSGAGSVV AWSLLITDLD PIKFGLLFER FLNPERISMP DFDIDFCQER REEVINYVCS
     KYGNNRVGQI ITFGKMQAKA VIKDVARVLS LPYKCADYLT ELVPFSAVNP VSLEQAIREV
     PELANAAKGK GLYNLEGDAE LIKLVLDTSL ILEGLHRHSS THAAGIVIAG TDLVDIVPVY
     KDANSDMLIV GYSMKYSEIA GLIKFDFLGL QTLTVITNCK KLLKEQGIEI DFDDMTFDDN
     KTYQMLCKGK GVGVFQFESI GMKDALRRLK PDSIHDLIAL GALYRPGPME NIPTYIACKH
     KLQQPDYLHK LLKPILEETY GVVIYQEQVQ RIAQVLAGYT LGAADLLRRA MGKKIKKEME
     EQEEIFVKGA IANNISQSQA KSIFATVAKF AGYGFNKAHA AAYGVISYQT AYLKANYPAE
     FLVACLNLEL NNHDKINLFL QEAKDNGIKI IAPNINISEG YFSVKSSDTV ITHNTKPLIP
     RLNNEIDIKD TAVKSLYYKD ESTIIFALGA IKGVTPNFGK LVTDERKARG AFKSITDFIE
     RLPPKSINSK LLENLIKAGC FDELHDNRLQ LFLSVPKLIA YSTSYHQEQE SNQFSLIKVS
     SLSPTILVSS NYADKNTLAF YEFESMGLFI SNHPLTEYQE IFSRLNILNT RDLYNKLPNG
     TNQVTLAGVI QKKDSRMSAR GRFVTLVLSD PENIFELTIF SEEVLKDYVH LLDVKSLVVV
     NCDIVKDEGG IKLTAKSFLS IEDAINNRQF ELQLYPQNYA ELEQIITLLV SRTGHGYQSN
     AKATIYLQSK DVKHFVAKIT LSETFFLQVQ DFEILSQYIR