ID   DPO1_BACSU              Reviewed;         880 AA.
AC   O34996;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=DNA polymerase I;
DE            Short=POL I;
DE            EC=2.7.7.7;
GN   Name=polA; OrderedLocusNames=BSU29090;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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; AF008220; AAC00350.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14869.1; -; Genomic_DNA.
DR   PIR; E69680; E69680.
DR   RefSeq; NP_390787.1; NC_000964.3.
DR   RefSeq; WP_004398870.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34996; -.
DR   SMR; O34996; -.
DR   IntAct; O34996; 8.
DR   STRING; 224308.BSU29090; -.
DR   PaxDb; O34996; -.
DR   PRIDE; O34996; -.
DR   EnsemblBacteria; CAB14869; CAB14869; BSU_29090.
DR   GeneID; 936617; -.
DR   KEGG; bsu:BSU29090; -.
DR   PATRIC; fig|224308.179.peg.3158; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   InParanoid; O34996; -.
DR   OMA; NRPPMPD; -.
DR   PhylomeDB; O34996; -.
DR   BioCyc; BSUB:BSU29090-MON; -.
DR   Proteomes; UP000001570; 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..880
FT                   /note="DNA polymerase I"
FT                   /id="PRO_0000101235"
FT   DOMAIN          174..268
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          302..470
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   880 AA;  99092 MW;  AFB434AFDF26F488 CRC64;
     MTERKKLVLV DGNSLAYRAF FALPLLSNDK GVHTNAVYGF AMILMKMLED EKPTHMLVAF
     DAGKTTFRHG TFKEYKGGRQ KTPPELSEQM PFIRELLDAY QISRYELEQY EADDIIGTLA
     KSAEKDGFEV KVFSGDKDLT QLATDKTTVA ITRKGITDVE FYTPEHVKEK YGLTPEQIID
     MKGLMGDSSD NIPGVPGVGE KTAIKLLKQF DSVEKLLESI DEVSGKKLKE KLEEFKDQAL
     MSKELATIMT DAPIEVSVSG LEYQGFNREQ VIAIFKDLGF NTLLERLGED SAEAEQDQSL
     EDINVKTVTD VTSDILVSPS AFVVEQIGDN YHEEPILGFS IVNETGAYFI PKDIAVESEV
     FKEWVENDEQ KKWVFDSKRA VVALRWQGIE LKGAEFDTLL AAYIINPGNS YDDVASVAKD
     YGLHIVSSDE SVYGKGAKRA VPSEDVLSEH LGRKALAIQS LREKLVQELE NNDQLELFEE
     LEMPLALILG EMESTGVKVD VDRLKRMGEE LGAKLKEYEE KIHEIAGEPF NINSPKQLGV
     ILFEKIGLPV VKKTKTGYST SADVLEKLAD KHDIVDYILQ YRQIGKLQST YIEGLLKVTR
     PDSHKVHTRF NQALTQTGRL SSTDPNLQNI PIRLEEGRKI RQAFVPSEKD WLIFAADYSQ
     IELRVLAHIS KDENLIEAFT NDMDIHTKTA MDVFHVAKDE VTSAMRRQAK AVNFGIVYGI
     SDYGLSQNLG ITRKEAGAFI DRYLESFQGV KAYMEDSVQE AKQKGYVTTL MHRRRYIPEL
     TSRNFNIRSF AERTAMNTPI QGSAADIIKK AMIDMAAKLK EKQLKARLLL QVHDELIFEA
     PKEEIEILEK LVPEVMEHAL ALDVPLKVDF ASGPSWYDAK