RECU_STRPN
ID RECU_STRPN Reviewed; 198 AA.
AC P0A455; P38034;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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; OrderedLocusNames=SP_0370;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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}.
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; AE005672; AAK74537.1; -; Genomic_DNA.
DR PIR; H95042; H95042.
DR RefSeq; WP_000248787.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P0A455; -.
DR SMR; P0A455; -.
DR STRING; 170187.SP_0370; -.
DR EnsemblBacteria; AAK74537; AAK74537; SP_0370.
DR GeneID; 60232713; -.
DR GeneID; 66805563; -.
DR KEGG; spn:SP_0370; -.
DR eggNOG; COG3331; Bacteria.
DR OMA; TDYNGIY; -.
DR PhylomeDB; P0A455; -.
DR BioCyc; SPNE170187:G1FZB-381-MON; -.
DR Proteomes; UP000000585; 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..198
FT /note="Holliday junction resolvase RecU"
FT /id="PRO_0000212312"
FT REGION 1..22
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; 23131 MW; F89949CF643B72CA CRC64;
MVNYPHKVSS QKRQTSLSQP KNFANRGMSF EKMINATNDY YLSQGLAVIH KKPTPIQIVQ
VDYPQRSRAK IVEAYFRQAS TTDYSGVYNG YYIDFEVKET KQKRAIPMKN FHPHQIQHME
QVLAQQGICF VLLHFSSQQE TYLLPAFDLI RFYHQDKGQK SMPLEYIREY GYEIKAGAFP
QIPYLNVIKE HLLGGKTR