HJE_SACS2
ID HJE_SACS2 Reviewed; 135 AA.
AC Q97YX6;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Holliday junction resolvase Hje;
DE Short=Hje;
DE EC=3.1.21.10;
GN Name=hje; OrderedLocusNames=SSO1176;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=10623519; DOI=10.1006/jmbi.1999.3363;
RA Kvaratskhelia M., White M.F.;
RT "An archaeal Holliday junction resolving enzyme from Sulfolobus
RT solfataricus exhibits unique properties.";
RL J. Mol. Biol. 295:193-202(2000).
RN [3]
RP FUNCTION.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10736227; DOI=10.1006/jmbi.2000.3624;
RA Kvaratskhelia M., White M.F.;
RT "Two Holliday junction resolving enzymes in Sulfolobus solfataricus.";
RL J. Mol. Biol. 297:923-932(2000).
RN [4]
RP FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=15921693; DOI=10.1016/j.jmb.2005.04.056;
RA Parker J.L., White M.F.;
RT "The endonuclease Hje catalyses rapid, multiple turnover resolution of
RT Holliday junctions.";
RL J. Mol. Biol. 350:1-6(2005).
RN [5]
RP PRELIMINARY CRYSTALLIZATION.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=12499561; DOI=10.1107/s0907444902019546;
RA Middleton C.L., Parker J.L., Richard D.J., White M.F., Bond C.S.;
RT "Crystallization and preliminary X-ray diffraction studies of Hje, a
RT HolliDay junction resolving enzyme from Sulfolobus solfataricus.";
RL Acta Crystallogr. D 59:171-173(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF SER-30.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=15479781; DOI=10.1093/nar/gkh869;
RA Middleton C.L., Parker J.L., Richard D.J., White M.F., Bond C.S.;
RT "Substrate recognition and catalysis by the Holliday junction resolving
RT enzyme Hje.";
RL Nucleic Acids Res. 32:5442-5451(2004).
CC -!- FUNCTION: A structure-specific endonuclease that resolves Holliday
CC junction (HJ) intermediates during genetic recombination. Acts only on
CC 4-way DNA junctions in a sequence non-specific manner; introduces
CC paired nicks in opposing strands 2 bases 3' of the point of strand
CC exchange only on continuous strands of 4-way junction DNA. Cleaves both
CC mobile and immobile junctions. {ECO:0000269|PubMed:10623519,
CC ECO:0000269|PubMed:10736227, ECO:0000269|PubMed:15921693}.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10623519, ECO:0000269|PubMed:15921693};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:10623519,
CC ECO:0000269|PubMed:15921693};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=73 nM for 4-way junction DNA at 5 mM MgCl2
CC {ECO:0000269|PubMed:10623519, ECO:0000269|PubMed:15921693};
CC KM=66 nM for 4-way junction DNA at 15 mM MgCl2
CC {ECO:0000269|PubMed:10623519, ECO:0000269|PubMed:15921693};
CC Note=kcat is 4.8 min(-1) and 10 min (-1) at 5 mM and 15 mM MgCl2
CC respectively.;
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. Could be higher with a
CC more thermally stable substrate. {ECO:0000269|PubMed:10623519,
CC ECO:0000269|PubMed:15921693};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15479781}.
CC -!- MISCELLANEOUS: A second Holliday junction resolving enzyme, Hjc, with
CC different substrate specificity exists in this organism.
CC -!- SIMILARITY: Belongs to the Holliday junction resolvase Hjc family. Hje
CC subfamily. {ECO:0000305}.
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DR EMBL; AE006641; AAK41424.1; -; Genomic_DNA.
DR PIR; A90271; A90271.
DR RefSeq; WP_009991563.1; NC_002754.1.
DR PDB; 1OB8; X-ray; 1.80 A; A/B=1-135.
DR PDB; 1OB9; X-ray; 2.00 A; A=1-135.
DR PDBsum; 1OB8; -.
DR PDBsum; 1OB9; -.
DR AlphaFoldDB; Q97YX6; -.
DR SMR; Q97YX6; -.
DR STRING; 273057.SSO1176; -.
DR EnsemblBacteria; AAK41424; AAK41424; SSO1176.
DR GeneID; 44130107; -.
DR KEGG; sso:SSO1176; -.
DR PATRIC; fig|273057.12.peg.1169; -.
DR eggNOG; arCOG00919; Archaea.
DR HOGENOM; CLU_1881165_0_0_2; -.
DR InParanoid; Q97YX6; -.
DR OMA; GIREWRY; -.
DR PhylomeDB; Q97YX6; -.
DR BRENDA; 3.1.21.10; 6163.
DR EvolutionaryTrace; Q97YX6; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd00523; archeal_HJR; 1.
DR Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR002732; Hjc.
DR InterPro; IPR014428; Hjc_arc.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR PANTHER; PTHR39651; PTHR39651; 1.
DR Pfam; PF01870; Hjc; 1.
DR PIRSF; PIRSF004985; Hlld_jn_rslvs_ar; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome.
FT CHAIN 1..135
FT /note="Holliday junction resolvase Hje"
FT /id="PRO_0000429159"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT SITE 54
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT MUTAGEN 30
FT /note="S->A,C,T: 100- to 1000-fold reduction in kcat."
FT /evidence="ECO:0000269|PubMed:15479781"
FT HELIX 7..19
FT /evidence="ECO:0007829|PDB:1OB8"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1OB8"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1OB9"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1OB8"
FT STRAND 47..63
FT /evidence="ECO:0007829|PDB:1OB8"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:1OB8"
FT STRAND 78..90
FT /evidence="ECO:0007829|PDB:1OB8"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1OB8"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1OB8"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:1OB8"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1OB8"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1OB8"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1OB8"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:1OB8"
SQ SEQUENCE 135 AA; 15452 MW; 13036E9997223BC2 CRC64;
MNRDIGKNAE RELVSILRGE GFNAVRIPTS NSSPNPLPDI FATKGNTLLS IECKSTWENK
VKVKEHQVRK LLDFLSMFTM KGVPLIAIKF KQVHEWRVLV PEKAEDIIVT IDNSIPIEDL
FKILEKRIEE KILTP
