DPO1_SALTY
ID DPO1_SALTY Reviewed; 928 AA.
AC Q9F173;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=DNA polymerase I;
DE Short=POL I;
DE EC=2.7.7.7;
GN Name=polA; OrderedLocusNames=STM3999;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RA Huang Y.P., Ito J.;
RT "DNA polymerase I sequence from Salmonella typhimurium.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 3'-5' and 5'-3' exonuclease activity. It is able to utilize
CC nicked circular duplex DNA as a template and can unwind the parental
CC DNA strand from its template.
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; AF071212; AAG43170.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22838.1; -; Genomic_DNA.
DR RefSeq; NP_462879.1; NC_003197.2.
DR RefSeq; WP_000249972.1; NC_003197.2.
DR AlphaFoldDB; Q9F173; -.
DR SMR; Q9F173; -.
DR STRING; 99287.STM3999; -.
DR PaxDb; Q9F173; -.
DR EnsemblBacteria; AAL22838; AAL22838; STM3999.
DR GeneID; 1255525; -.
DR KEGG; stm:STM3999; -.
DR PATRIC; fig|99287.12.peg.4214; -.
DR HOGENOM; CLU_004675_0_1_6; -.
DR OMA; NRPPMPD; -.
DR PhylomeDB; Q9F173; -.
DR BioCyc; SENT99287:STM3999-MON; -.
DR Proteomes; UP000001014; 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; 1.
DR Pfam; PF01367; 5_3_exonuc; 1.
DR Pfam; PF02739; 5_3_exonuc_N; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR Pfam; PF01612; DNA_pol_A_exo1; 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..928
FT /note="DNA polymerase I"
FT /id="PRO_0000101252"
FT DOMAIN 1..323
FT /note="5'-3' exonuclease"
FT DOMAIN 324..517
FT /note="3'-5' exonuclease"
FT REGION 324..928
FT /note="Klenow fragment"
FT REGION 521..928
FT /note="Polymerase"
FT CONFLICT 751
FT /note="G -> R (in Ref. 1; AAG43170)"
FT /evidence="ECO:0000305"
FT CONFLICT 848
FT /note="M -> T (in Ref. 1; AAG43170)"
FT /evidence="ECO:0000305"
FT CONFLICT 867
FT /note="L -> I (in Ref. 1; AAG43170)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 928 AA; 103129 MW; FF887BF1039C160A CRC64;
MVQIPENPLI LVDGSSYLYR AYHAFPPLTN SAGEPTGAMY GVLNMLRSLI MQYQPTHAAV
VFDAKGKTFR DELFEHYKSH RPPMPDDLRA QIEPLHAMVK AMGLPLLAVS GVEADDVIGT
LAREAEKVGR PVLISTGDKD MAQLVTPNIT LINTMTNTIL GPDEVVNKYG VPPELIIDFL
ALMGDSSDNI PGVPGVGEKT AQALLQGLGG LDTLYAEPEK IAGLTFRGAK TMAGKLAQNK
DVAYLSYKLA TIKTDVELEL TCEQLEVQQP IADELLGLFK KYEFKRWTAD VESGKWLQAK
GAKPAAKPQE TVVIDESPSE PAAALSYENY VTILDDVTLE SWIEKLKKAP VFAFDTETDS
LDNIAANLVG LSFAIEPGVA AYVPVAHDYL DAPDQISRQR ALELLKPLLE DEKVRKVGQN
LKYDRGVLQN YGIELRGIAF DTMLESYILN SVAGRHDMDS LSDRWLKHKT ITFEDIAGKG
KNQLTFNQIA LEEAGRYAAE DADVTLQLHL KMWPELQQHK GPLNVFENIE MPLVPVLSRV
ERNGVKIDPA VLHKHSEEIT LRLAELEKKA HDIAGEAFNL SSTKQLQTIL FEKQGIKPLK
KTPGGAPSTS EEVLEELALD YPLPKVILEY RGLAKLKSTY TDKLPLMINP KTGRVHTSYH
QAVTATGRLS STDPNLQNIP VRNEEGRRIR QAFIAPEDYL IVSADYSQIE LRIMAHLSRD
KGLLTAFAEG KDIHRATAAE VFGLPLDSVT GEQRRSAKAI NFGLIYGMSA FGLSRQLNIP
RKEAQKYMDL YFERYPGVLE YMERTRAQAK EQGYVETLEG RRLYLPDIKS SNAARRAGAE
RAAINAPMQG TAADIIKRAM IAVDAWLQAE QPRVRMIMQV HDELVFEVHK DDLDAVAKRI
HQLMENCTRI DVPLLVEVGS GENWDQAH
