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Database: UniProt
Entry: E1QH41_DESB2
LinkDB: E1QH41_DESB2
Original site: E1QH41_DESB2 
ID   E1QH41_DESB2            Unreviewed;       142 AA.
AC   E1QH41;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Peptidase S24/S26A/S26B, conserved region {ECO:0000313|EMBL:ADK84884.1};
GN   OrderedLocusNames=Deba_1516 {ECO:0000313|EMBL:ADK84884.1};
OS   Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS   / 2st14).
OC   Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC   Desulfarculaceae; Desulfarculus.
OX   NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK84884.1, ECO:0000313|Proteomes:UP000009047};
RN   [1] {ECO:0000313|EMBL:ADK84884.1, ECO:0000313|Proteomes:UP000009047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC   {ECO:0000313|Proteomes:UP000009047};
RX   PubMed=21304732; DOI=10.4056/sigs.1243258;
RA   Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA   Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA   Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT   "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL   Stand. Genomic Sci. 3:276-284(2010).
CC   -!- SIMILARITY: Belongs to the peptidase S24 family.
CC       {ECO:0000256|ARBA:ARBA00007484, ECO:0000256|RuleBase:RU003991}.
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DR   EMBL; CP002085; ADK84884.1; -; Genomic_DNA.
DR   RefSeq; WP_013258337.1; NC_014365.1.
DR   AlphaFoldDB; E1QH41; -.
DR   STRING; 644282.Deba_1516; -.
DR   MEROPS; S24.001; -.
DR   KEGG; dbr:Deba_1516; -.
DR   eggNOG; COG1974; Bacteria.
DR   HOGENOM; CLU_066192_0_2_7; -.
DR   OrthoDB; 9802364at2; -.
DR   Proteomes; UP000009047; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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   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   PANTHER; PTHR33516:SF2; LEXA REPRESSOR; 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   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003991};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009047};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   SOS response {ECO:0000256|ARBA:ARBA00023236};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          19..132
FT                   /note="Peptidase S24/S26A/S26B/S26C"
FT                   /evidence="ECO:0000259|Pfam:PF00717"
SQ   SEQUENCE   142 AA;  16020 MW;  08275473D524864D CRC64;
     MRLCDIGFEE IDIQDVEIPF MGVVAAGMPI EAVPEERAIA IPKDMVGRFR TFALEVRGTS
     MIDEHIAPGD VIVVEERQTA ENGQMVVALI NQSDVTLKKF YLERDHIRLQ PANPGMEPII
     LRHEDVRVLG VVAGLIRHYR HH
//
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