SPLB_CLOAB
ID SPLB_CLOAB Reviewed; 336 AA.
AC Q97L63;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Spore photoproduct lyase;
DE EC=4.1.99.14;
GN Name=splB; OrderedLocusNames=CA_C0699;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=19178276; DOI=10.1021/ja807375c;
RA Chandra T., Silver S.C., Zilinskas E., Shepard E.M., Broderick W.E.,
RA Broderick J.B.;
RT "Spore photoproduct lyase catalyzes specific repair of the 5R but not the
RT 5S spore photoproduct.";
RL J. Am. Chem. Soc. 131:2420-2421(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=20405152; DOI=10.1007/s00775-010-0656-8;
RA Silver S.C., Chandra T., Zilinskas E., Ghose S., Broderick W.E.,
RA Broderick J.B.;
RT "Complete stereospecific repair of a synthetic dinucleotide spore
RT photoproduct by spore photoproduct lyase.";
RL J. Biol. Inorg. Chem. 15:943-955(2010).
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:19178276,
CC ECO:0000269|PubMed:20405152}.
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:19178276,
CC ECO:0000269|PubMed:20405152};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:20405152};
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:20405152};
CC -!- COFACTOR:
CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC Evidence={ECO:0000269|PubMed:20405152};
CC Note=Binds 1 S-adenosyl-L-methionine per subunit.
CC {ECO:0000269|PubMed:20405152};
CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. SPL family.
CC {ECO:0000305}.
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DR EMBL; AE001437; AAK78676.1; -; Genomic_DNA.
DR PIR; A96986; A96986.
DR RefSeq; NP_347336.1; NC_003030.1.
DR RefSeq; WP_010964018.1; NC_003030.1.
DR AlphaFoldDB; Q97L63; -.
DR SMR; Q97L63; -.
DR STRING; 272562.CA_C0699; -.
DR EnsemblBacteria; AAK78676; AAK78676; CA_C0699.
DR KEGG; cac:CA_C0699; -.
DR PATRIC; fig|272562.8.peg.902; -.
DR eggNOG; COG1533; Bacteria.
DR HOGENOM; CLU_057301_0_0_9; -.
DR OMA; AYCYVPR; -.
DR OrthoDB; 1341636at2; -.
DR BRENDA; 4.1.99.14; 1452.
DR Proteomes; UP000000814; Chromosome.
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; IDA:UniProtKB.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB.
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; IPR034559; Spore_PP_lysase_Clostridia.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDF00412; spore_photoproduct_lyase_2; 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; Reference proteome; S-adenosyl-L-methionine; Sporulation.
FT CHAIN 1..336
FT /note="Spore photoproduct lyase"
FT /id="PRO_0000397844"
FT DOMAIN 74..305
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DNA_BIND 215..232
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT BINDING 88
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
SQ SEQUENCE 336 AA; 39090 MW; 15F544BA7AB51F97 CRC64;
MENMFRRVIF EKKALDYPMG RDILRQFENT DIEIRYSETG RITGIPGKDE AQSFFEGKNT
LVVGVRRELD FQTCKPSANY QLPIVSGCAA MCEYCYLNTH GGKKPYVKIN VNLDDILSKA
GEYIEKRKPD ITVFEGAAIS DPVPVERYSG ALKKAIEYFG KNEYSRFRFV TKYADISELL
AVQHNNHTTI RFSINTPRVI KNYEHRTSSL EDRIESAYNI LNSGYKTGFI VGPVFLYENW
KKEYEELLKK ASDKLGDKEL EFEIISHRFT TSAKNKILKV FPNTKLPMDD EARKFKFGQF
GYGKYVYDKD DMQEIKEFFI NNINLYFNKA TIKYII
