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VSR_ECOLI
ID   VSR_ECOLI               Reviewed;         156 AA.
AC   P09184;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 172.
DE   RecName: Full=DNA mismatch endonuclease Vsr;
DE            EC=3.1.-.-;
DE   AltName: Full=Type II nicking enzyme {ECO:0000303|PubMed:12654995};
DE   AltName: Full=V.EcoKDcm {ECO:0000303|PubMed:12654995};
DE   AltName: Full=Very short patch repair protein;
DE   AltName: Full=Vsr mismatch endonuclease {ECO:0000303|PubMed:1944537};
GN   Name=vsr {ECO:0000303|PubMed:2198248}; OrderedLocusNames=b1960, JW1943;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2527357; DOI=10.1093/nar/17.14.5844;
RA   Hanck T., Gerwin N., Fritz H.-J.;
RT   "Nucleotide sequence of the dcm locus of Escherichia coli K12.";
RL   Nucleic Acids Res. 17:5844-5844(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2198248; DOI=10.1128/jb.172.8.4214-4221.1990;
RA   Sohail A., Lieb M., Dar M., Bhagwat A.S.;
RT   "A gene required for very short patch repair in Escherichia coli is
RT   adjacent to the DNA cytosine methylase gene.";
RL   J. Bacteriol. 172:4214-4221(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   FUNCTION.
RX   PubMed=1944537; DOI=10.1038/353776a0;
RA   Hennecke F., Kolmar H., Bruendi K., Fritz H.-J.;
RT   "The vsr gene product of E. coli K-12 is a strand- and sequence-specific
RT   DNA mismatch endonuclease.";
RL   Nature 353:776-778(1991).
RN   [7]
RP   FUNCTION.
RX   PubMed=10871403; DOI=10.1093/nar/28.13.2535;
RA   Fox K.R., Allinson S.L., Sahagun-Krause H., Brown T.;
RT   "Recognition of GT mismatches by Vsr mismatch endonuclease.";
RL   Nucleic Acids Res. 28:2535-2540(2000).
RN   [8]
RP   NOMENCLATURE.
RX   PubMed=12654995; DOI=10.1093/nar/gkg274;
RA   Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA   Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA   Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA   Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA   Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA   Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA   Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA   Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA   Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT   "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT   endonucleases and their genes.";
RL   Nucleic Acids Res. 31:1805-1812(2003).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=10612397; DOI=10.1016/s0092-8674(00)81550-0;
RA   Tsutakawa S.E., Jingami H., Morikawa K.;
RT   "Recognition of a TG mismatch: the crystal structure of very short patch
RT   repair endonuclease in complex with a DNA duplex.";
RL   Cell 99:615-623(1999).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-157.
RX   PubMed=10360178; DOI=10.1016/s1097-2765(00)80355-x;
RA   Tsutakawa S.E., Muto T., Kawate T., Jingami H., Kunishima N., Ariyoshi M.,
RA   Kohda D., Nakagawa M., Morikawa K.;
RT   "Crystallographic and functional studies of very short patch repair
RT   endonuclease.";
RL   Mol. Cell 3:621-628(1999).
CC   -!- FUNCTION: Deamination of 5-methylcytosine in DNA results in T/G
CC       mismatches. If unrepaired, these mismatches can lead to C-to-T
CC       transition mutations. The very short patch (VSP) repair process in
CC       E.coli counteracts the mutagenic process by repairing the mismatches in
CC       favor of the G-containing strand. This enzyme is an endonuclease that
CC       nicks double-stranded DNA within the sequence CT(AT)GN or NT(AT)GG next
CC       to the thymidine residue that is mismatched to 2'-deoxyguanosine. The
CC       incision is mismatch-dependent and strand-specific.
CC       {ECO:0000269|PubMed:10871403, ECO:0000269|PubMed:1944537}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 2 magnesium ions per subunit.;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- INTERACTION:
CC       P09184; P23367: mutL; NbExp=3; IntAct=EBI-765033, EBI-554913;
CC   -!- SIMILARITY: Belongs to the Vsr family. {ECO:0000305}.
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DR   EMBL; X13330; CAA31707.1; -; Genomic_DNA.
DR   EMBL; M32307; AAA03724.1; -; Unassigned_DNA.
DR   EMBL; U00096; AAC75026.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15787.1; -; Genomic_DNA.
DR   PIR; JS0264; JS0264.
DR   RefSeq; NP_416469.1; NC_000913.3.
DR   RefSeq; WP_000786005.1; NZ_STEB01000050.1.
DR   PDB; 1CW0; X-ray; 2.30 A; A=2-156.
DR   PDB; 1ODG; X-ray; 2.80 A; A=23-156.
DR   PDB; 1VSR; X-ray; 1.80 A; A=21-156.
DR   PDBsum; 1CW0; -.
DR   PDBsum; 1ODG; -.
DR   PDBsum; 1VSR; -.
DR   AlphaFoldDB; P09184; -.
DR   SMR; P09184; -.
DR   BioGRID; 4263264; 75.
DR   BioGRID; 850827; 2.
DR   DIP; DIP-11114N; -.
DR   IntAct; P09184; 10.
DR   STRING; 511145.b1960; -.
DR   REBASE; 13373; V.EcoW3110DcmP.
DR   REBASE; 175269; V.Rga4872ORF487P.
DR   REBASE; 175272; V.Rga4872ORF19P.
DR   REBASE; 232039; V.Sen4024DcmP.
DR   REBASE; 232757; V.Sen4839DcmP.
DR   REBASE; 3641; V.EcoKDcm.
DR   PaxDb; P09184; -.
DR   PRIDE; P09184; -.
DR   EnsemblBacteria; AAC75026; AAC75026; b1960.
DR   EnsemblBacteria; BAA15787; BAA15787; BAA15787.
DR   GeneID; 946476; -.
DR   KEGG; ecj:JW1943; -.
DR   KEGG; eco:b1960; -.
DR   PATRIC; fig|1411691.4.peg.292; -.
DR   EchoBASE; EB1061; -.
DR   eggNOG; COG3727; Bacteria.
DR   HOGENOM; CLU_111913_1_1_6; -.
DR   InParanoid; P09184; -.
DR   OMA; HDCYLFK; -.
DR   PhylomeDB; P09184; -.
DR   BioCyc; EcoCyc:EG11068-MON; -.
DR   EvolutionaryTrace; P09184; -.
DR   PRO; PR:P09184; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043765; F:T/G mismatch-specific endonuclease activity; IDA:EcoCyc.
DR   GO; GO:0006298; P:mismatch repair; IDA:EcoCyc.
DR   CDD; cd00221; Vsr; 1.
DR   InterPro; IPR004603; DNA_mismatch_endonuc_vsr.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   Pfam; PF03852; Vsr; 1.
DR   PIRSF; PIRSF018267; VSR_endonuc; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
DR   TIGRFAMs; TIGR00632; vsr; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA damage; DNA repair; Endonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Nuclease; Reference proteome; Zinc.
FT   CHAIN           1..156
FT                   /note="DNA mismatch endonuclease Vsr"
FT                   /id="PRO_0000200289"
FT   BINDING         51
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   BINDING         51
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   BINDING         63
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   HELIX           7..15
FT                   /evidence="ECO:0007829|PDB:1CW0"
FT   STRAND          19..21
FT                   /evidence="ECO:0007829|PDB:1CW0"
FT   HELIX           26..34
FT                   /evidence="ECO:0007829|PDB:1VSR"
FT   STRAND          40..42
FT                   /evidence="ECO:0007829|PDB:1VSR"
FT   STRAND          51..54
FT                   /evidence="ECO:0007829|PDB:1VSR"
FT   HELIX           55..57
FT                   /evidence="ECO:0007829|PDB:1VSR"
FT   STRAND          59..64
FT                   /evidence="ECO:0007829|PDB:1VSR"
FT   TURN            66..70
FT                   /evidence="ECO:0007829|PDB:1VSR"
FT   STRAND          80..82
FT                   /evidence="ECO:0007829|PDB:1VSR"
FT   HELIX           83..106
FT                   /evidence="ECO:0007829|PDB:1VSR"
FT   STRAND          110..115
FT                   /evidence="ECO:0007829|PDB:1VSR"
FT   HELIX           116..119
FT                   /evidence="ECO:0007829|PDB:1VSR"
FT   HELIX           127..139
FT                   /evidence="ECO:0007829|PDB:1VSR"
FT   STRAND          144..148
FT                   /evidence="ECO:0007829|PDB:1VSR"
FT   STRAND          151..154
FT                   /evidence="ECO:0007829|PDB:1VSR"
SQ   SEQUENCE   156 AA;  18016 MW;  24F98A111C31E098 CRC64;
     MADVHDKATR SKNMRAIATR DTAIEKRLAS LLTGQGLAFR VQDASLPGRP DFVVDEYRCV
     IFTHGCFWHH HHCYLFKVPA TRTEFWLEKI GKNVERDRRD ISRLQELGWR VLIVWECALR
     GREKLTDEAL TERLEEWICG EGASAQIDTQ GIHLLA
 
 
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