RECU_GEOKA
ID RECU_GEOKA Reviewed; 200 AA.
AC Q5KXY4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=GK2167;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
RN [2]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF ASP-86.
RX PubMed=12237459; DOI=10.1110/ps.0216802;
RA Rigden D.J., Setlow P., Setlow B., Bagyan I., Stein R.A., Jedrzejas M.J.;
RT "PrfA protein of Bacillus species: prediction and demonstration of
RT endonuclease activity on DNA.";
RL Protein Sci. 11:2370-2381(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, AND
RP SUBUNIT.
RX PubMed=17557334; DOI=10.1002/prot.21418;
RA Kelly S.J., Li J., Setlow P., Jedrzejas M.J.;
RT "Structure, flexibility, and mechanism of the Bacillus stearothermophilus
RT RecU Holliday junction resolvase.";
RL Proteins 68:961-971(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RG Midwest center for structural genomics (MCSG);
RT "X-ray crystal structure of penicillin-binding protein-related factor A
RT from Bacillus stearothermophilus.";
RL Submitted (JAN-2005) to the PDB data bank.
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, ECO:0000269|PubMed:12237459}.
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 Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12237459,
CC ECO:0000269|PubMed:17557334}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RecU family. {ECO:0000255|HAMAP-
CC Rule:MF_00130}.
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DR EMBL; BA000043; BAD76452.1; -; Genomic_DNA.
DR RefSeq; WP_011231652.1; NC_006510.1.
DR PDB; 1Y1O; X-ray; 2.20 A; A/B/C/D=1-200.
DR PDB; 2FCO; X-ray; 1.40 A; A/B=1-200.
DR PDBsum; 1Y1O; -.
DR PDBsum; 2FCO; -.
DR AlphaFoldDB; Q5KXY4; -.
DR SMR; Q5KXY4; -.
DR STRING; 235909.GK2167; -.
DR EnsemblBacteria; BAD76452; BAD76452; GK2167.
DR KEGG; gka:GK2167; -.
DR eggNOG; COG3331; Bacteria.
DR HOGENOM; CLU_096340_0_0_9; -.
DR OMA; TDYNGIY; -.
DR EvolutionaryTrace; Q5KXY4; -.
DR Proteomes; UP000001172; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome.
FT CHAIN 1..200
FT /note="Holliday junction resolvase RecU"
FT /id="PRO_1000016723"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT SITE 101
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305"
FT MUTAGEN 86
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12237459"
FT HELIX 33..46
FT /evidence="ECO:0007829|PDB:2FCO"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:2FCO"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:1Y1O"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1Y1O"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:1Y1O"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:2FCO"
FT STRAND 94..104
FT /evidence="ECO:0007829|PDB:2FCO"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:2FCO"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2FCO"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:2FCO"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:2FCO"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:2FCO"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:2FCO"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:2FCO"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:2FCO"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:2FCO"
FT HELIX 169..175
FT /evidence="ECO:0007829|PDB:2FCO"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:2FCO"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:2FCO"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:2FCO"
SQ SEQUENCE 200 AA; 23034 MW; F5565DDC72C2ABBE CRC64;
MALKYPSGKE YRGNKPNAAR RPAADYANRG MTLEDDLNAT NEYYRERGIA VIHKKPTPVQ
IVRVDYPKRS AAVITEAYFR QASTTDYNGV YRGKYIDFEA KETKNKTAFP LKNFHAHQIR
HMEQVVAHGG ICFAILRFSL LNETYLLDAS HLIAWWNKQE AGGRKSIPKQ EIERHGHSIP
LGYQPRIDYI SVVDNVYFTR
