ID   IMPA_SALCH              Reviewed;         145 AA.
AC   Q5J3U9;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Protein ImpA;
DE            EC=3.4.21.-;
DE   Contains:
DE     RecName: Full=Protein ImpA';
GN   Name=impA; OrderedLocusNames=SCH_138;
OS   Salmonella choleraesuis (strain SC-B67).
OG   Plasmid pSC138.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
CC   -!- FUNCTION: Involved in UV protection and mutation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S24 family. {ECO:0000305}.
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DR   EMBL; AY509004; AAS76416.1; -; Genomic_DNA.
DR   RefSeq; WP_000109071.1; NC_006856.1.
DR   AlphaFoldDB; Q5J3U9; -.
DR   SMR; Q5J3U9; -.
DR   MEROPS; S24.003; -.
DR   EnsemblBacteria; AAS76416; AAS76416; SCH_138.
DR   GeneID; 60904328; -.
DR   KEGG; sec:SCH_138; -.
DR   HOGENOM; CLU_066192_0_0_6; -.
DR   OMA; HETARNG; -.
DR   Proteomes; UP000000538; Plasmid pSC138.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR   CDD; cd06529; S24_LexA-like; 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   Pfam; PF00717; Peptidase_S24; 1.
DR   PRINTS; PR00726; LEXASERPTASE.
DR   SUPFAM; SSF51306; SSF51306; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; DNA damage; DNA repair; Hydrolase; Plasmid;
KW   Protease; Serine protease; SOS mutagenesis; SOS response.
FT   CHAIN           1..145
FT                   /note="Protein ImpA"
FT                   /id="PRO_0000252114"
FT   CHAIN           29..145
FT                   /note="Protein ImpA'"
FT                   /id="PRO_0000252115"
FT   ACT_SITE        64
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        101
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000250"
FT   SITE            28..29
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   145 AA;  16219 MW;  C934B52A47C6DADB CRC64;
     MSTVYHRPAD PSGDDSYVRP LFADRCQAGF PSPATDYAEQ ELDLNSYCIS RPAATFFLRA
     SGESMNQAGV QNGDLLVVDR AEKPQHGDIV IAEIDGEFTV KRLLLRPRPA LEPVSDSPEF
     RTLYPENICI FGVVTHVIHR TRELR