ID A0A098F7G8_9BACI Unreviewed; 324 AA.
AC A0A098F7G8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=SOS-response transcriptional repressor {ECO:0000313|EMBL:CEG29602.1};
GN ORFNames=BN1002_04560 {ECO:0000313|EMBL:CEG29602.1};
OS Bacillus sp. B-jedd.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1476857 {ECO:0000313|EMBL:CEG29602.1, ECO:0000313|Proteomes:UP000042335};
RN [1] {ECO:0000313|EMBL:CEG29602.1, ECO:0000313|Proteomes:UP000042335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-jedd {ECO:0000313|EMBL:CEG29602.1,
RC ECO:0000313|Proteomes:UP000042335};
RA Urmite Genomes Urmite Genomes;
RL Submitted (SEP-2014) 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; CCXR01000002; CEG29602.1; -; Genomic_DNA.
DR RefSeq; WP_052445670.1; NZ_CCXR01000002.1.
DR AlphaFoldDB; A0A098F7G8; -.
DR STRING; 1476857.BN1002_04560; -.
DR OrthoDB; 194368at2; -.
DR Proteomes; UP000042335; 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; 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; 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 NCBIfam; TIGR00498; lexA; 1.
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 DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003991};
KW Reference proteome {ECO:0000313|Proteomes:UP000042335};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW SOS response {ECO:0000256|ARBA:ARBA00023236}.
FT DOMAIN 10..65
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
SQ SEQUENCE 324 AA; 37002 MW; E6A158E92ECF4139 CRC64;
MDQKEFGEYL RSLRQERKLT IRQLEALSGV SNAYLSQMEN GKRGIPTVEI LKKIHTPLGV
SFDELMLKAG YISSDTKEKL TPEVIDMLNN FEVFSELLSN AADVFISSVT DNTGNLHKEY
KEYLIEEAPE EYKSNPGFLT MFEDQDIFRE MFERLTLEEK VIFLNKIIKD FVDQKIDPKV
ALKSKPEEIS KVKFLKVPIL GHIAAGQPIF AEDHIDDWTE IPDMWNLKPG EAFVLKVKGD
SMIGSRIYDG DRVVVKVQPE VENGEIAVVN VNGDEATLKR VKRASNGQII LYPDNPRYEP
TFVNNEKARI VGKVIQVMFE PKRV
//
