ID   DPO3A_RICPR             Reviewed;        1182 AA.
AC   O05974;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=RP778;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-780.
RC   STRAIN=Madrid E;
RX   PubMed=9274032; DOI=10.1099/00221287-143-8-2783;
RA   Andersson J.O., Andersson S.G.E.;
RT   "Genomic rearrangements during evolution of the obligate intracellular
RT   parasite Rickettsia prowazekii as inferred from an analysis of 52015 bp
RT   nucleotide sequence.";
RL   Microbiology 143:2783-2795(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 822-1182.
RC   STRAIN=B, and Madrid E;
RX   PubMed=10486973; DOI=10.1093/oxfordjournals.molbev.a026208;
RA   Andersson J.O., Andersson S.G.E.;
RT   "Genome degradation is an ongoing process in Rickettsia.";
RL   Mol. Biol. Evol. 16:1178-1191(1999).
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; AJ235273; CAA15204.1; -; Genomic_DNA.
DR   EMBL; Y11785; CAA72479.1; -; Genomic_DNA.
DR   EMBL; AJ238755; CAB56087.1; -; Genomic_DNA.
DR   EMBL; AJ238756; CAB56091.1; -; Genomic_DNA.
DR   PIR; D71638; D71638.
DR   RefSeq; NP_221128.1; NC_000963.1.
DR   RefSeq; WP_004599648.1; NC_000963.1.
DR   AlphaFoldDB; O05974; -.
DR   SMR; O05974; -.
DR   STRING; 272947.gene:17555847; -.
DR   EnsemblBacteria; CAA15204; CAA15204; CAA15204.
DR   GeneID; 57569901; -.
DR   KEGG; rpr:RP778; -.
DR   PATRIC; fig|272947.5.peg.814; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_5; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000002480; 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   CDD; cd04485; DnaE_OBF; 1.
DR   CDD; cd07433; PHP_PolIIIA_DnaE1; 1.
DR   Gene3D; 1.10.150.870; -; 1.
DR   Gene3D; 1.10.10.1600; Bacterial DNA polymerase III alpha subunit, thumb domain; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 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; IPR004805; DnaE2/DnaE/PolC.
DR   InterPro; IPR029460; DNAPol_HHH.
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; IPR049821; PolIIIA_DnaE1_PHP.
DR   NCBIfam; TIGR00594; polc; 1.
DR   PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR32294:SF0; DNA POLYMERASE III SUBUNIT ALPHA; 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; PHP domain-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA replication; DNA-directed DNA polymerase;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..1182
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103336"
FT   CONFLICT        376
FT                   /note="I -> V (in Ref. 2; CAA72479)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1182 AA;  133463 MW;  0FE9B56969C2E52A CRC64;
     MQPEFIHLRT QSSYSFLESA LTIEKVVELA LLHKMPALCL SDRGNLFGSL EFSLYAVKKK
     LQPIHGVILN IQYDINAFAQ ILLIAKDETG YKNLLKLSSL TFTKNDRKIC EHIGFEDLIK
     YQEGVIALCC YTDGIVGKCL LARKQEQAIL FARRLQAILG DRFYFEIMRH DLPEEQFIEN
     SYIQIASELS IPIVATNKVL FSEKSMHYAH DVLLCISEGV TKEYPDRKTV SENCYFKSPA
     EMRKLFSDLP NAIQNTINLR ERCYFAAHPN PPMLPNFSTQ DISETYLIRK YATEGLLARL
     VTKFKAENIS LEHQEKLKTE YFTRLNYELD IICNMNFAGY FLIVSDFIKW SKKQGILVGP
     GRGSGAGSVV AWSLLITDLD PIKFGLLFER FLNPERISMP DFDIDFCQER REEVINYVRS
     KYGPNRVGQI ITFGKMQAKA VIKDVARVLS LPYKLADYLT ELVPFSAINP VSLEQAIREV
     PELANAAKGN GLYNLEGDAE LIKLVLDTSL ILEGLHRHSS THAAGIVIAG TDLVDIVPVY
     KDANADMLIV GYSMKYSEIA GLIKFDFLGL QTLTVITNCK KLLKEQGIKI DFDDMTFDDK
     KTYQMLCKGK GVGVFQFESI GMKDALRRLK PDSIHDLIAL GALYRPGPME NIPTYIACKH
     KLQQPDYLHK LLEPILEETY GVVIYQEQVQ RIAQVLAGYT LGAADLLRRA MGKKIKKEME
     EQEEIFVKGA IANNISPSQA KSIFSTVAKF AGYGFNKAHA AAYGVISYQT AYLKANYPAE
     FLVACLNLEL NNHDKINLFL QEAKDNGIKI IAPNINISEG YFSVKSSNTV ITHSTKSVIS
     RLNCDIKKIA KDTAVKPLYC KDESTIIFAL GAIKGVTANF GKLVTDERKA RGAFKSITDF
     IERLPPKSIN SKLLENLIKA GCFDELHDNR LQLFLSIPKL IAYSTSYHQE QESNQFSLIK
     VSSLSPTILV SSDYADKNTL AFYEFEAMGL FLSNHPLTEY QGIFSRLNIL NTRDLYNKLP
     NGTNRVTLAG VIQKKDSRMS ARGRFVTLVL SDPENIFELT IFSEEVLKDY VHLLDVKSLV
     VVNCDVVKDE GGIKLTAKSF LSIEDVMNNR QFELQLYPQN YAELEQIITL LASRTSNGYQ
     SNAKATIYLQ SKDVKHFIAK ITLSETFFLQ VQDFEVLNQY IR
//