ID   RECU_STROR              Reviewed;         198 AA.
AC   Q00579;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Holliday junction resolvase RecU;
DE            EC=3.1.21.10 {ECO:0000255|HAMAP-Rule:MF_00130};
DE   AltName: Full=Recombination protein U homolog;
GN   Name=recU;
OS   Streptococcus oralis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1624444; DOI=10.1128/jb.174.13.4517-4523.1992;
RA   Martin C., Briese T., Hakenbeck R.;
RT   "Nucleotide sequences of genes encoding penicillin-binding proteins from
RT   Streptococcus pneumoniae and Streptococcus oralis with high homology to
RT   Escherichia coli penicillin-binding proteins 1a and 1b.";
RL   J. Bacteriol. 174:4517-4523(1992).
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 (By similarity).
CC       {ECO:0000250}.
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; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RecU family. {ECO:0000305}.
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DR   EMBL; M90528; AAA26957.1; -; Genomic_DNA.
DR   RefSeq; WP_000248760.1; NZ_JADMYA010000002.1.
DR   AlphaFoldDB; Q00579; -.
DR   SMR; Q00579; -.
DR   STRING; 1303.SORDD17_00135; -.
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.
FT   CHAIN           1..198
FT                   /note="Holliday junction resolvase RecU"
FT                   /id="PRO_0000212311"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         81
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            98
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   198 AA;  23099 MW;  FDF7F106F0A8BD4A CRC64;
     MVNYPHKISS QKRQAPPSQT KNFANRGMSF EKMINATNDY YLSHGLAVIH KKPTPIQIVR
     VDYPQRSRAK IVEAYFRQAS TTDYSGVYDG YYIDFEAKET RQKHAIPMKN FHHHQIQHME
     QVLAQRGICF VLLHFASQQE TYLLPAVDLI RFYHQDKGQK SMPLGYIREN GYRIELGAFP
     QIPYLDIIKE HLLGGKTR