ID   DPO1_STRPN              Reviewed;         877 AA.
AC   P59199; P13252;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=DNA polymerase I;
DE            Short=POL I;
DE            EC=2.7.7.7;
GN   Name=polA; OrderedLocusNames=SP_0032;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 3'-5' and 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; AE005672; AAK74222.1; -; Genomic_DNA.
DR   PIR; E95003; E95003.
DR   RefSeq; WP_001808750.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; P59199; -.
DR   SMR; P59199; -.
DR   STRING; 170187.SP_0032; -.
DR   EnsemblBacteria; AAK74222; AAK74222; SP_0032.
DR   KEGG; spn:SP_0032; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   OMA; NRPPMPD; -.
DR   PhylomeDB; P59199; -.
DR   BioCyc; SPNE170187:G1FZB-37-MON; -.
DR   Proteomes; UP000000585; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
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: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; IPR002562; 3'-5'_exonuclease_dom.
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; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10133; PTHR10133; 2.
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; SM00474; 35EXOc; 1.
DR   SMART; SM00475; 53EXOc; 1.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF47807; SSF47807; 1.
DR   SUPFAM; SSF53098; SSF53098; 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; Transferase.
FT   CHAIN           1..877
FT                   /note="DNA polymerase I"
FT                   /id="PRO_0000101253"
FT   DOMAIN          177..270
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          302..465
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   877 AA;  99253 MW;  2621865B94586913 CRC64;
     MDKKKLLLID GSSVAFRAFF ALYQQLDRFK NVAGLHTNAI YGFQLMLSHL LERVEPSHIL
     VAFDAGKTTF RTEMYADYKG GRAKTPDEFR EQFPFIRELL DHMGIRHYDL AQYEADDIIG
     TLDKLAEQDG FDITIVSGDK DLIQLTDEHT VVEISKKGVA EFEAFTPDYL MEEMGLTPAQ
     FIDLKALMGD KSDNIPGVTK VGEKTGIKLL LEHGSLEGIY ENIDGMKTSK MKENLINDKE
     QAFLSKTLAT IDTKAPIAIG LEDLVYSGPD VENLGKFYDE MGFKQLKQAL NVSSADVSES
     LDFTIVDQIS QDMLSEESIF HFELFGENYH TDNLVGFVWS CGDKLYATDK LELLQDPIFK
     DFLEKTSLRV YDFKKVKVLL QRFGVDLQAP AFDIRLAKYL LSTVEDNEIA TIASLYGQTY
     LVDDETFYGK GVKKAIPERE KFLEHLACKL AVLVETEPIL LEKLSENGQL ELLYDMEQPL
     AFVLAKMEIA GIMVKKETLL EMQAENELVI EKLTQEIYEL AGEEFNVNSP KQLGVLLFEK
     LGLPLEYTKK TKTGYSTAVD VLERLAPIAP IVKKILDYRQ IAKIQSTYVI GLQDWILADG
     KIHTRYVQDL TQTGRLSSVD PNLQNIPARL EQGRLIRKAF VPEWEDSVLL SSDYSQIELR
     VLAHISKDEH LIKAFQEGAD IHTSTAMRVF GIERPDDVTA NDRRNAKAVN FGVVYGISDF
     GLSNNLGISR KEAKAYIDTY FERFPGIKNY MDEVVREARD KGYVETLFKR RRELPDINSR
     NFNIRGFAER TAINSPIQGS AADILKIAMI QLDKALVAGG YQTKMLLQVH DEIVLEVPKS
     ELVEMKKLVK QTMEEAIQLS VPLIADENEG ATWYEAK