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Database: UniProt
Entry: A0A0G0DRY4_9BACT
LinkDB: A0A0G0DRY4_9BACT
Original site: A0A0G0DRY4_9BACT 
ID   A0A0G0DRY4_9BACT        Unreviewed;       189 AA.
AC   A0A0G0DRY4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=LexA repressor {ECO:0000313|EMBL:KKP65795.1};
GN   ORFNames=UR64_C0018G0017 {ECO:0000313|EMBL:KKP65795.1};
OS   Candidatus Nomurabacteria bacterium GW2011_GWE1_35_16.
OC   Bacteria; Candidatus Nomurabacteria.
OX   NCBI_TaxID=1618761 {ECO:0000313|EMBL:KKP65795.1, ECO:0000313|Proteomes:UP000034952};
RN   [1] {ECO:0000313|EMBL:KKP65795.1, ECO:0000313|Proteomes:UP000034952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- SIMILARITY: Belongs to the peptidase S24 family.
CC       {ECO:0000256|ARBA:ARBA00007484, ECO:0000256|RuleBase:RU003991}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKP65795.1}.
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DR   EMBL; LBPY01000018; KKP65795.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0DRY4; -.
DR   Proteomes; UP000034952; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR   CDD; cd06529; S24_LexA-like; 1.
DR   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR006200; LexA.
DR   InterPro; IPR039418; LexA-like.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR006197; Peptidase_S24_LexA.
DR   InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR00498; lexA; 1.
DR   PANTHER; PTHR33516; LEXA REPRESSOR; 1.
DR   PANTHER; PTHR33516:SF13; PROPHAGE REPRESSOR COHE-RELATED; 1.
DR   Pfam; PF00717; Peptidase_S24; 1.
DR   PRINTS; PR00726; LEXASERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813,
KW   ECO:0000256|RuleBase:RU003991}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003991};
KW   Protease {ECO:0000256|ARBA:ARBA00022825};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   SOS mutagenesis {ECO:0000256|ARBA:ARBA00023199};
KW   SOS response {ECO:0000256|ARBA:ARBA00023236}.
FT   DOMAIN          68..174
FT                   /note="Peptidase S24/S26A/S26B/S26C"
FT                   /evidence="ECO:0000259|Pfam:PF00717"
SQ   SEQUENCE   189 AA;  21754 MW;  C937FD3363EBFD08 CRC64;
     MYNNYKEKLV RFYNRDKRMP TYTEMLDLFG FKSKNAVARL VDKFIEEGIV TKDHLGRLLA
     DASFNSIPML GSVKAGFPED VAEEMKETIN IEDYLIAKKE NSYMLTVDGD SMIDAHIADG
     DMVLVEKTNT AKDGQIVIAN VDGEFTMKYF RKDKNNRVWL EPANKDFKPI YPKIYLNITA
     VVKAVIRKY
//
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