RECU_BACC7
ID RECU_BACC7 Reviewed; 200 AA.
AC B7HL64;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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};
GN OrderedLocusNames=BCAH187_A1717;
OS Bacillus cereus (strain AH187).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405534;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH187;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA Okstad O.A., Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH187.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001177; ACJ79364.1; -; Genomic_DNA.
DR RefSeq; WP_000155592.1; NC_011658.1.
DR AlphaFoldDB; B7HL64; -.
DR SMR; B7HL64; -.
DR EnsemblBacteria; ACJ79364; ACJ79364; BCAH187_A1717.
DR GeneID; 58156672; -.
DR GeneID; 64203006; -.
DR KEGG; bcr:BCAH187_A1717; -.
DR HOGENOM; CLU_096340_0_0_9; -.
DR OMA; TDYNGIY; -.
DR OrthoDB; 1756221at2; -.
DR Proteomes; UP000002214; 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_1000117725"
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; 23343 MW; A5189E4C909473FB CRC64;
MTIRYPNGKR YNQASQPHKT PIKKHTYSNR GMSLEEELNE TNEYYLTHNI ACVHKKPTPL
QIVKVDYPAR SAAVVKEAYF KQPSTTDYNG VYKGKYIDFE AKETKNKTSF PLQNFHLHQI
EHMKQVIAHN GIAFVIIKFT LFDELYLLDA KHIIAFWNRQ NTGGRKSITK EEIEEHGSLL
SCGYHPRIDY IRVLDTVYFS