ID   RECU_STRMU              Reviewed;         197 AA.
AC   Q8DVL3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Holliday junction resolvase RecU {ECO:0000255|HAMAP-Rule:MF_00130};
DE            EC=3.1.21.10 {ECO:0000255|HAMAP-Rule:MF_00130};
DE   AltName: Full=Recombination protein U homolog {ECO:0000255|HAMAP-Rule:MF_00130};
GN   Name=recU {ECO:0000255|HAMAP-Rule:MF_00130}; OrderedLocusNames=SMU_469;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC   -!- FUNCTION: Endonuclease that resolves Holliday junction intermediates in
CC       genetic recombination. Cleaves mobile four-strand junctions by
CC       introducing symmetrical nicks in paired strands. Promotes annealing of
CC       linear ssDNA with homologous dsDNA. Required for DNA repair, homologous
CC       recombination and chromosome segregation. {ECO:0000255|HAMAP-
CC       Rule:MF_00130}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage at a junction such as a reciprocal
CC         single-stranded crossover between two homologous DNA duplexes
CC         (Holliday junction).; EC=3.1.21.10; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00130};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00130};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00130};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00130}.
CC   -!- SIMILARITY: Belongs to the RecU family. {ECO:0000255|HAMAP-
CC       Rule:MF_00130}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014133; AAN58217.1; -; Genomic_DNA.
DR   RefSeq; NP_720911.1; NC_004350.2.
DR   RefSeq; WP_002263052.1; NC_004350.2.
DR   AlphaFoldDB; Q8DVL3; -.
DR   SMR; Q8DVL3; -.
DR   STRING; 210007.SMU_469; -.
DR   PRIDE; Q8DVL3; -.
DR   EnsemblBacteria; AAN58217; AAN58217; SMU_469.
DR   GeneID; 66818058; -.
DR   KEGG; smu:SMU_469; -.
DR   PATRIC; fig|210007.7.peg.411; -.
DR   eggNOG; COG3331; Bacteria.
DR   HOGENOM; CLU_096340_0_0_9; -.
DR   OMA; TDYNGIY; -.
DR   PhylomeDB; Q8DVL3; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1350.10; -; 1.
DR   HAMAP; MF_00130; RecU; 1.
DR   InterPro; IPR004612; Resolv_RecU.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR   Pfam; PF03838; RecU; 1.
DR   PIRSF; PIRSF037785; RecU; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
DR   TIGRFAMs; TIGR00648; recU; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA recombination; DNA repair; Endonuclease;
KW   Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome.
FT   CHAIN           1..197
FT                   /note="Holliday junction resolvase RecU"
FT                   /id="PRO_1000016746"
FT   BINDING         82
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT   BINDING         84
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT   BINDING         97
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT   SITE            99
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
SQ   SEQUENCE   197 AA;  22815 MW;  ACD1D4DACD0AEE2E CRC64;
     MVNYPHHFIR KQSKPSQISK TINFANRGMS FEAAINATNN YYLSQKIAVI HKKPTPIQIV
     RVDYPRRSRA KIVEAYFRQA STTDYSGVYK GYYIDFEAKE TRHKTSIPMK NFHAHQIKHM
     SQVLDQKGIC FVLLHFSTLR ETYLLPASHL IHFYRIDNGG KSMPLDYIKK NGYQVNVSAF
     PQVPYLDIID KNILGGD