ID   SPL_GEOSY               Reviewed;         341 AA.
AC   C9RZ55;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Spore photoproduct lyase;
DE            EC=4.1.99.14;
GN   Name=splG; OrderedLocusNames=GYMC61_0226;
OS   Geobacillus sp. (strain Y412MC61).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=544556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y412MC61;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brumm P.,
RA   Mead D.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y412MC61.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND COFACTOR.
RX   PubMed=16968710; DOI=10.1074/jbc.m607053200;
RA   Pieck J.C., Hennecke U., Pierik A.J., Friedel M.G., Carell T.;
RT   "Characterization of a new thermophilic spore photoproduct lyase from
RT   Geobacillus stearothermophilus (SplG) with defined lesion containing DNA
RT   substrates.";
RL   J. Biol. Chem. 281:36317-36326(2006).
CC   -!- FUNCTION: Involved in repair of UV radiation-induced DNA damage during
CC       spore germination. Can repair thymine dimer 5-thyminyl-5,6-
CC       dihydrothymine (known as spore photoproduct (SP)) by in situ
CC       monomerization of SP to two thymines. {ECO:0000269|PubMed:16968710}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine in DNA = a
CC         thymidine dimer in DNA; Xref=Rhea:RHEA:56132, Rhea:RHEA-COMP:14387,
CC         Rhea:RHEA-COMP:14449, ChEBI:CHEBI:139518, ChEBI:CHEBI:139519;
CC         EC=4.1.99.14; Evidence={ECO:0000269|PubMed:16968710};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:16968710};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated
CC       with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000269|PubMed:16968710};
CC   -!- COFACTOR:
CC       Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC         Evidence={ECO:0000269|PubMed:16968710};
CC       Note=Binds 1 S-adenosyl-L-methionine per subunit.
CC       {ECO:0000269|PubMed:16968710};
CC   -!- SUBUNIT: Monomer or homodimer. {ECO:0000269|PubMed:16968710}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. SPL family.
CC       {ECO:0000305}.
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DR   EMBL; CP001794; ACX76924.1; -; Genomic_DNA.
DR   RefSeq; WP_012820568.1; NC_013411.1.
DR   AlphaFoldDB; C9RZ55; -.
DR   SMR; C9RZ55; -.
DR   PRIDE; C9RZ55; -.
DR   KEGG; gyc:GYMC61_0226; -.
DR   HOGENOM; CLU_057301_0_0_9; -.
DR   OMA; AYCYVPR; -.
DR   GO; GO:0042601; C:endospore-forming forespore; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003913; F:DNA photolyase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023897; Spore_PP_lysase.
DR   InterPro; IPR034560; Spore_PP_lysase_Bacilli.
DR   SFLD; SFLDF00292; spore_photoproduct_lyase_1; 1.
DR   TIGRFAMs; TIGR04070; photo_TT_lyase; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; DNA damage; DNA repair; DNA-binding; Iron; Iron-sulfur; Lyase;
KW   Metal-binding; S-adenosyl-L-methionine; Sporulation.
FT   CHAIN           1..341
FT                   /note="Spore photoproduct lyase"
FT                   /id="PRO_0000397845"
FT   DOMAIN          76..304
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   DNA_BIND        217..234
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255"
FT   BINDING         90
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   341 AA;  39573 MW;  1849E1900743E69E CRC64;
     MKPFVPKLVY FEPEALSYPL GQELYEKFTQ MGIEIRETTS HNQVRGIPGE TELARYRNAK
     STLVVGVRRT LKFDSSKPSA EYAIPLATGC MGHCHYCYLQ TTLGSKPYIR VYVNLDDIFA
     QAQKYIDERA PEITRFEAAC TSDIVGIDHL THSLKKAIEF IGATDYGRLR FVTKYEHVDH
     LLDAKHNGKT RFRFSVNSRY VINHFEPGTS SFDARLQAAR KVAGAGYKLG FVVAPIYRHD
     GWEQGYFELF QELARQLEGV DLSDLTFELI QHRFTKPAKR VIEQRYPKTK LDLDESKRKY
     KWGRYGIGKY VYRDKEAREL EETMRSYIAR FFPSAQVQYF T