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Database: UniProt
Entry: A0A380LI00_9FIRM
LinkDB: A0A380LI00_9FIRM
Original site: A0A380LI00_9FIRM 
ID   A0A380LI00_9FIRM        Unreviewed;       197 AA.
AC   A0A380LI00;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=CI-like repressor, S. pneumoniae bacteriophage EJ-1 {ECO:0000313|EMBL:SUO03488.1};
DE            EC=3.4.21.88 {ECO:0000313|EMBL:SUO03488.1};
GN   Name=lexA {ECO:0000313|EMBL:SUO03488.1};
GN   ORFNames=NCTC11087_00350 {ECO:0000313|EMBL:SUO03488.1};
OS   Faecalicoccus pleomorphus.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Faecalicoccus.
OX   NCBI_TaxID=1323 {ECO:0000313|EMBL:SUO03488.1, ECO:0000313|Proteomes:UP000255523};
RN   [1] {ECO:0000313|EMBL:SUO03488.1, ECO:0000313|Proteomes:UP000255523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC11087 {ECO:0000313|EMBL:SUO03488.1,
RC   ECO:0000313|Proteomes:UP000255523};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S24 family.
CC       {ECO:0000256|ARBA:ARBA00007484, ECO:0000256|RuleBase:RU003991}.
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DR   EMBL; UHFX01000003; SUO03488.1; -; Genomic_DNA.
DR   RefSeq; WP_022789666.1; NZ_UHFX01000003.1.
DR   AlphaFoldDB; A0A380LI00; -.
DR   GeneID; 77461341; -.
DR   OrthoDB; 9802364at2; -.
DR   Proteomes; UP000255523; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR   CDD; cd00093; HTH_XRE; 1.
DR   CDD; cd06529; S24_LexA-like; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
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   PANTHER; PTHR33516; LEXA REPRESSOR; 1.
DR   PANTHER; PTHR33516:SF13; PROPHAGE REPRESSOR COHE-RELATED; 1.
DR   Pfam; PF01381; HTH_3; 1.
DR   Pfam; PF00717; Peptidase_S24; 1.
DR   PRINTS; PR00726; LEXASERPTASE.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR   PROSITE; PS50943; HTH_CROC1; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003991};
KW   Reference proteome {ECO:0000313|Proteomes:UP000255523};
KW   SOS response {ECO:0000256|ARBA:ARBA00023236}.
FT   DOMAIN          7..62
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50943"
SQ   SEQUENCE   197 AA;  22599 MW;  9029232F52605A51 CRC64;
     MRLKELLIQY ELQNDLNHTA MAQKIGVSTS TYYRWINEES TELKKTTLKK IAQVLDCDIE
     KVLNDDGECV KPILGFAKAG YDLFAEQQIE GYIEVNASDA KKGDYFLRIQ GDSMEGSHIY
     DGDLVYVQKC DVVEDGKIAV VLIGEEATVK KVRYKKNLMI LEASNPKYEP KYFTPQEIEE
     IPVRILGRVR FVRTDFD
//
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