DPO1_STRR6
ID DPO1_STRR6 Reviewed; 877 AA.
AC P59200; P13252;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=DNA polymerase I;
DE Short=POL I;
DE EC=2.7.7.7;
GN Name=polA; OrderedLocusNames=spr0032;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2537309; DOI=10.1016/s0021-9258(19)84991-8;
RA Lopez P., Martinez S., Diaz A., Espinosa M., Lacks S.A.;
RT "Characterization of the polA gene of Streptococcus pneumoniae and
RT comparison of the DNA polymerase I it encodes to homologous enzymes from
RT Escherichia coli and phage T7.";
RL J. Biol. Chem. 264:4255-4263(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 3'-5' and 5'-3' exonuclease activity.
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.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR EMBL; J04479; AAA26954.1; -; Genomic_DNA.
DR EMBL; AE007317; AAK98836.1; -; Genomic_DNA.
DR PIR; A32949; A32949.
DR PIR; H97875; H97875.
DR RefSeq; NP_357626.1; NC_003098.1.
DR RefSeq; WP_000358433.1; NC_003098.1.
DR AlphaFoldDB; P59200; -.
DR SMR; P59200; -.
DR STRING; 171101.spr0032; -.
DR EnsemblBacteria; AAK98836; AAK98836; spr0032.
DR GeneID; 60234276; -.
DR KEGG; spr:spr0032; -.
DR PATRIC; fig|171101.6.peg.37; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR HOGENOM; CLU_004675_0_0_9; -.
DR OMA; NRPPMPD; -.
DR Proteomes; UP000000586; 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; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
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; Reference proteome; Transferase.
FT CHAIN 1..877
FT /note="DNA polymerase I"
FT /id="PRO_0000101254"
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"
FT CONFLICT 790
FT /note="R -> A (in Ref. 1; AAA26954)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 877 AA; 99164 MW; BC86196B88A2C7E4 CRC64;
MDKKKLLLID GSSVAFRAFF ALYQQLDRFK NAAGLHTNAI YGFQLMLSHL LERVEPSHIL
VAFDAGKTTF RTEMYADYKG GRAKTPDEFR EQFPFIRELL DHMGIRHYEL AQYEADDIIG
TLDKLAEQDG FDITIVSGDK DLIQLTDEHT VVEISKKGVA EFEAFTPDYL MEEMGLTPAQ
FIDLKALMGD KSDNIPGVTK VGEKTGIKLL LEHGSLEGIY ENIDGMKTSK MKENLINDKE
QAFLSKTLAT IDTKAPIAIG LEDLVYSGPD VENLGKFYDE MGFKQLKQAL NMSSADVAEG
LDFTIVDQIS QDMLSEESIF HFELFGENYH TDNLVGFAWS CGDQLYATDK LELLQDPIFK
DFLEKTSLRV YDFKKVKVLL QRFGVDLQAP AFDIRLAKYL LSTVEDNEIA TIASLYGQTY
LVDDETFYGK GVKKAIPERE KFLEHLACKL AVLVETEPIL LEKLSENGQL ELLYDMEQPL
AFVLAKMEIA GIVVKKETLL EMQAENELVI EKLTQEIYEL AGEEFNVNSP KQLGVLLFEK
LGLPLEYTKK TKTGYSTAVD VLERLAPIAP IVKKILDYRQ IAKIQSTYVI GLQDWILADG
KIHTRYVQDL TQTGRLSSVD PNLQNIPARL EQGRLIRKAF VPEWEDSVLL SSDYSQIELR
VLAHISKDEH LIKAFQEGAD IHTSTAMRVF GIERPDNVTA NDRRNAKAVN FGVVYGISDF
GLSNNLGISR KEAKAYIDTY FERFPGIKNY MDEVVREARD KGYVETLFKR RRELPDINSR
NFNIRGFAER TAINSPIQGS AADILKIAMI QLDKALVAGG YQTKMLLQVH DEIVLEVPKS
ELVEMKKLVK QTMEEAIQLS VPLIADENEG ATWYEAK
