ID A0A1G9U3G2_9FIRM Unreviewed; 225 AA.
AC A0A1G9U3G2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Repressor LexA {ECO:0000313|EMBL:SDM54412.1};
GN ORFNames=SAMN04515677_11470 {ECO:0000313|EMBL:SDM54412.1};
OS Romboutsia lituseburensis DSM 797.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Romboutsia.
OX NCBI_TaxID=1121325 {ECO:0000313|EMBL:SDM54412.1, ECO:0000313|Proteomes:UP000199068};
RN [1] {ECO:0000313|EMBL:SDM54412.1, ECO:0000313|Proteomes:UP000199068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 797 {ECO:0000313|EMBL:SDM54412.1,
RC ECO:0000313|Proteomes:UP000199068};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNGW01000014; SDM54412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9U3G2; -.
DR STRING; 1121325.SAMN04515677_11470; -.
DR Proteomes; UP000199068; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 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:UP000199068};
KW SOS response {ECO:0000256|ARBA:ARBA00023236}.
FT DOMAIN 8..62
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
SQ SEQUENCE 225 AA; 25619 MW; FFEEA9CF3C71297E CRC64;
MDTFGKRLKE ERISKRLTQQ DVADIFHLNK SSISRYEKDQ QVPDVATIQK MANYFGVTTD
YLLGNKNKKT DDTDLFNLKG DVRFLKKVKE DEMVKIPVLG VIKAGIPMFA EENIIDYEYV
HQEELVMGEE YFYLQIKGDS MINAGIPDGS RVLIRKQNFI ESDGEIMAVR VNGDEATLKR
VYRQQSGLVL QSENSKYGPM FFPASDVDTG YVGIIGKAIK VEIKL
//
