ID   DPO1_RICPR              Reviewed;         867 AA.
AC   O05949;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=DNA polymerase I;
DE            Short=POL I;
DE            EC=2.7.7.7;
GN   Name=polA; OrderedLocusNames=RP776;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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: In addition to polymerase activity, this DNA polymerase
CC       exhibits 5'-3' exonuclease activity. {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: Single-chain monomer with multiple functions. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR   EMBL; Y11784; CAA72476.1; -; Genomic_DNA.
DR   EMBL; AJ235273; CAA15203.1; -; Genomic_DNA.
DR   EMBL; AJ238755; CAB56085.1; -; Genomic_DNA.
DR   EMBL; AJ238756; CAB56089.1; -; Genomic_DNA.
DR   PIR; C71638; C71638.
DR   RefSeq; NP_221127.1; NC_000963.1.
DR   RefSeq; WP_004596955.1; NC_000963.1.
DR   AlphaFoldDB; O05949; -.
DR   SMR; O05949; -.
DR   STRING; 272947.RP776; -.
DR   EnsemblBacteria; CAA15203; CAA15203; CAA15203.
DR   GeneID; 57569899; -.
DR   KEGG; rpr:RP776; -.
DR   PATRIC; fig|272947.5.peg.811; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_5; -.
DR   OMA; NRPPMPD; -.
DR   Proteomes; UP000002480; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR   CDD; cd09898; H3TH_53EXO; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR   InterPro; IPR002421; 5-3_exonuclease.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR020045; DNA_polI_H3TH.
DR   InterPro; IPR018320; DNA_polymerase_1.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10133; PTHR10133; 1.
DR   Pfam; PF01367; 5_3_exonuc; 1.
DR   Pfam; PF02739; 5_3_exonuc_N; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00475; 53EXOc; 1.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF47807; SSF47807; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
DR   TIGRFAMs; TIGR00593; pola; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Exonuclease; Hydrolase; Nuclease;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..867
FT                   /note="DNA polymerase I"
FT                   /id="PRO_0000101251"
FT   DOMAIN          1..283
FT                   /note="5'-3' exonuclease"
SQ   SEQUENCE   867 AA;  98652 MW;  557194B38FB69BA2 CRC64;
     MTKKNTLLLI DGYGFVFRAY YAQKSLSSAK GEPVGALYGF TSMLLKLLSD FKPQYVAIVF
     DSGGKNFRHK IYQNYKANRP LPPKDLIAQL PLVRDVASNF KFAILEKNGY EADDIIATFA
     TKTVSLGEEV IIISSDKDLL QLMSKNIKIY DPIKCKYITE DNVVTKFGTT PDKLREVMAL
     IGDRSDNIPG VPSIGPKTAS SLITKFGSVE NIFNSLDQIS SIKQRKTLQN AREAALISWK
     LIGLDSNVDL DFDLNNLKWS PPNSKKLTGF LQEYGFKSLY KRVENLFDIK INDHEEIVDN
     KVTEAKEISN ASELANFAKE AERIGIFGIY LLQQKGENRA LILSLQNQSY IIKITNNNYN
     IKNNNDWFSH IILNLLTNKS IKKITYSLKH LLKFYANQSH QITAIEDLEL MQYALSAGLV
     QKNLFTKTLT KDNIINESAR IVINFISLYK QTLLELQKNK AFRLYREIDL PTCFILDKME
     KVGIKVDANY LNRLSDEFGT EILKIEEEIF ALSGTKFNIG SQKQLGEILF KKMQLPSGNT
     LAKTSSYSTR AGILKKLSED GYHIATLLLR WRQLTKLKNT YTDSLPKQIN NITKRIHTTF
     LQTSTTTGRL SSQEPNLQNV PIRSSDGNKI REAFIAEEGY KLISADYSQI ELRILSHIAN
     IDVLKQAFIN KEDIHTQTAC QIFNLKKHEL TSEHRRKAKA INFGIIYGIS AFGLAKQLNV
     SNSTASEYIK QYFAEYKGVQ EYMTQTKACA SRNGYVTNFF GRKCFIPLIH DKKLKQFAER
     AAINAPIQGT NADIIKIAMI KLDKEIEERK LKTRLILQIH DELLFEVPEI EVEIVIPIIK
     KIMEHSTNMN VPIITEIKAG NNWKEIH