ID   IMPA_SALTM              Reviewed;         145 AA.
AC   P18641; Q79VW6;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Protein ImpA;
DE            EC=3.4.21.-;
DE   Contains:
DE     RecName: Full=Protein ImpA';
GN   Name=impA;
OS   Salmonella typhimurium.
OG   Plasmid IncI1 TP110, and Plasmid IncI1 R64.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=IncI1 TP110;
RX   PubMed=2129552; DOI=10.1093/nar/18.17.5045;
RA   Lodwick D., Owen D., Strike P.;
RT   "DNA sequence analysis of the imp UV protection and mutation operon of the
RT   plasmid TP110: identification of a third gene.";
RL   Nucleic Acids Res. 18:5045-5050(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=IncI1 R64;
RA   Sampei G., Komano T., Sasaki T., Tachibana K., Furuya N., Saito Y.,
RA   Suzuki T., Mizobuchi K.;
RT   "Organization and diversification of plasmid genomes: complete nucleotide
RT   sequence of R64 genome.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in UV protection and mutation.
CC   -!- SIMILARITY: Belongs to the peptidase S24 family. {ECO:0000305}.
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DR   EMBL; X53528; CAA37607.1; -; Genomic_DNA.
DR   EMBL; AP005147; BAB91615.1; -; Genomic_DNA.
DR   PIR; JQ0660; JQ0660.
DR   RefSeq; NP_863407.1; NC_005014.1.
DR   RefSeq; WP_000109071.1; NZ_WWEW01000280.1.
DR   RefSeq; YP_004823695.1; NC_015965.1.
DR   RefSeq; YP_006955753.1; NC_019111.1.
DR   RefSeq; YP_008994915.1; NC_023275.1.
DR   RefSeq; YP_008995022.1; NC_023276.1.
DR   RefSeq; YP_008997551.1; NC_023290.1.
DR   RefSeq; YP_009022403.1; NC_023900.1.
DR   AlphaFoldDB; P18641; -.
DR   SMR; P18641; -.
DR   MEROPS; S24.003; -.
DR   GeneID; 39692666; -.
DR   GeneID; 60904328; -.
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_0000041984"
FT   CHAIN           29..145
FT                   /note="Protein ImpA'"
FT                   /id="PRO_0000027297"
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