ID   RECU_BACAH              Reviewed;         200 AA.
AC   A0RC02;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=BALH_1402;
OS   Bacillus thuringiensis (strain Al Hakam).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=412694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Al Hakam;
RX   PubMed=17337577; DOI=10.1128/jb.00241-07;
RA   Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA   McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT   "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL   J. Bacteriol. 189:3680-3681(2007).
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}.
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DR   EMBL; CP000485; ABK84745.1; -; Genomic_DNA.
DR   RefSeq; WP_000155593.1; NC_008600.1.
DR   AlphaFoldDB; A0RC02; -.
DR   SMR; A0RC02; -.
DR   EnsemblBacteria; ABK84745; ABK84745; BALH_1402.
DR   GeneID; 59158167; -.
DR   KEGG; btl:BALH_1402; -.
DR   HOGENOM; CLU_096340_0_0_9; -.
DR   OMA; TDYNGIY; -.
DR   Proteomes; UP000000761; 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.
FT   CHAIN           1..200
FT                   /note="Holliday junction resolvase RecU"
FT                   /id="PRO_1000016715"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         85
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT   BINDING         87
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT   BINDING         100
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT   BINDING         119
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT   SITE            102
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
SQ   SEQUENCE   200 AA;  23313 MW;  A5188C7DB39473FB CRC64;
     MTIRYPNGKR YNQASQPHKT PIKKHTYSNR GMSLEEELNE TNEYYLTHNI ACVHKKPTPL
     QIVKVDYPAR SAAVVKEAYF KQPSTTDYNG VYKGKYIDFE AKETKNKTSF PLQNFHLHQI
     EHMKQVIAHN GIAFVIIKFT LFDELYLLDA KHIIAFWNRQ NTGGRKSITK EEIVEHGSLL
     SCGYHPRIDY IRVLDTVYFS