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Database: UniProt
Entry: Q46L61_PROMT
LinkDB: Q46L61_PROMT
Original site: Q46L61_PROMT 
ID   Q46L61_PROMT            Unreviewed;       144 AA.
AC   Q46L61;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=SOS response UmuD protein, Serine peptidase, MEROPS family S24 {ECO:0000313|EMBL:AAZ57767.1};
GN   OrderedLocusNames=PMN2A_0275 {ECO:0000313|EMBL:AAZ57767.1};
OS   Prochlorococcus marinus (strain NATL2A).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=59920 {ECO:0000313|EMBL:AAZ57767.1, ECO:0000313|Proteomes:UP000002535};
RN   [1] {ECO:0000313|EMBL:AAZ57767.1, ECO:0000313|Proteomes:UP000002535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL2A {ECO:0000313|EMBL:AAZ57767.1,
RC   ECO:0000313|Proteomes:UP000002535};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- SIMILARITY: Belongs to the peptidase S24 family.
CC       {ECO:0000256|ARBA:ARBA00007484, ECO:0000256|RuleBase:RU003991}.
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DR   EMBL; CP000095; AAZ57767.1; -; Genomic_DNA.
DR   RefSeq; WP_011293809.1; NC_007335.2.
DR   AlphaFoldDB; Q46L61; -.
DR   STRING; 59920.PMN2A_0275; -.
DR   MEROPS; S24.003; -.
DR   KEGG; pmn:PMN2A_0275; -.
DR   HOGENOM; CLU_066192_0_0_3; -.
DR   OrthoDB; 9802364at2; -.
DR   PhylomeDB; Q46L61; -.
DR   Proteomes; UP000002535; Chromosome.
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; cd06529; S24_LexA-like; 1.
DR   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
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; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003991};
KW   Protease {ECO:0000256|ARBA:ARBA00022825};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002535};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   SOS mutagenesis {ECO:0000256|ARBA:ARBA00023199};
KW   SOS response {ECO:0000256|ARBA:ARBA00023236}.
FT   DOMAIN          20..133
FT                   /note="Peptidase S24/S26A/S26B/S26C"
FT                   /evidence="ECO:0000259|Pfam:PF00717"
SQ   SEQUENCE   144 AA;  16142 MW;  CE13063A0C75EF15 CRC64;
     MGSNRSRSSS TEGLSSLLIP TISAGFPSPA EDYIELGIDL NKYLIKNPIS TFFLRVSGNS
     MNNAGIYNND LLIIDRSINP NPGHIVVALL DGEFTLKRLI KKQDSYYLKA DKENYPAINL
     YEYIDIQIWG VAIYSIHELQ QSKV
//
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