ID   DPO1_HELPJ              Reviewed;         897 AA.
AC   Q9ZJE9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=DNA polymerase I;
DE            Short=POL I;
DE            EC=2.7.7.7;
GN   Name=polA; OrderedLocusNames=jhp_1363;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR   EMBL; AE001439; AAD06938.1; -; Genomic_DNA.
DR   PIR; F71816; F71816.
DR   RefSeq; WP_000437564.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZJE9; -.
DR   SMR; Q9ZJE9; -.
DR   STRING; 85963.jhp_1363; -.
DR   EnsemblBacteria; AAD06938; AAD06938; jhp_1363.
DR   KEGG; hpj:jhp_1363; -.
DR   PATRIC; fig|85963.30.peg.1188; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   OMA; NRPPMPD; -.
DR   Proteomes; UP000000804; 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; 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; 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..897
FT                   /note="DNA polymerase I"
FT                   /id="PRO_0000101242"
FT   DOMAIN          1..317
FT                   /note="5'-3' exonuclease"
FT   DOMAIN          318..494
FT                   /note="3'-5' exonuclease"
FT   REGION          498..896
FT                   /note="Polymerase"
SQ   SEQUENCE   897 AA;  102433 MW;  0C2C77DF7ED4F2EE CRC64;
     MEQPVIKEGT LALIDTFAYL FRSYYMSAKN KPLTNDKGFP TGLLTGLVGM VKKFYKDRKN
     MPFIVFALES QTKTKRAEKL GEYKQNRKDA PKEMLLQIPI ALEWLQKMGF TCVEVGGFEA
     DDVIASLATL SPYKTRIYSK DKDFNQLLSD KIALFDGKTE FLAKDCVEKY GILPSQFTDY
     QGIVGDSSDN YKGVKGIGSK NAKELLQRLG SLEKIYENLD LAKNLLSPKM YQALIQDKGS
     AFLSKELATL ERGCIKEFDF LSCAFPSENP LLKIKDELKE YGFISTLRDL ENSPFIVENV
     PILNSTPILD NTPALDNAPK KSRMIVLESA EPLSMFLEKL ENPNARVFMR LVLDKDKKIL
     ALAFLLQDQG YFLPLEEALF SPFSLEFLQN AFSQMLQHAC IIGHDLKPLL SFLKAKYQVP
     LENIRIQDTQ ILAFLKNPEK VGFDEVLKEY LKEDLIPHEK IKDFKTKSKA EKSELLSMEL
     NALKRLCEYF EKGGLEEDLL TLARDIETPF VKVLMGMEFQ GFKIDAPYFK RLEQEFKNEL
     NVLERQILDL IGVDFNLNSP KQLGEVLYDK LGLPKNKSHS TDEKNLLKIL DKHPSIPLIL
     EYRELNKLFN TYTTPLLRLK DKDDKIHTTF IQTGTATGRL SSHSPNLQNI PVRSPKGLLI
     RKGFIASSKE YCLLGVDYSQ IELRLLAHFS QDKDLMEAFL KGRDIHLETS KALFGEDLAK
     EKRSIAKSIN FGLVYGMGSK KLSETLSIPL SEAKSYIEAY FKRFPSIKDY LNGMREEILK
     TSKAFTLLGR YRVFDFTGVN DYVKGNYLRE GVNAIFQGSA SDLLKLGMLK VSERFKNNPS
     VRLLLQVHDE LIFEIEEKNA PELQQEIQRI LNDEVYPLRV PLETSAFIAK RWNELKG