IMPA_ECOLX
ID IMPA_ECOLX Reviewed; 145 AA.
AC Q7M1C0; Q7DJY8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Protein ImpA;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=Protein ImpA';
OS Escherichia coli.
OG Plasmid IncI1 ColIb-P9.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sampei G., Mizobuchi K.;
RT "Organization and diversification of plasmid genomes: complete nucleotide
RT sequence of the ColIb-P9 genome.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in UV protection and mutation.
CC {ECO:0000250|UniProtKB:P0AG11}.
CC -!- SIMILARITY: Belongs to the peptidase S24 family. {ECO:0000255}.
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DR EMBL; AB021078; BAA75114.1; -; Genomic_DNA.
DR PIR; A36069; A36069.
DR RefSeq; WP_000109071.1; NZ_WVVQ01000037.1.
DR RefSeq; YP_002756645.1; NC_012487.1.
DR RefSeq; YP_003108104.1; NC_013120.1.
DR RefSeq; YP_004119773.1; NC_014843.1.
DR RefSeq; YP_006940046.1; NC_018995.1.
DR RefSeq; YP_006952317.1; NC_019061.1.
DR RefSeq; YP_006954375.1; NC_019097.1.
DR RefSeq; YP_008826374.1; NC_022885.1.
DR RefSeq; YP_008998745.1; NC_023329.1.
DR RefSeq; YP_009060006.1; NC_024955.2.
DR RefSeq; YP_009061218.1; NC_024976.1.
DR RefSeq; YP_009061320.1; NC_024977.1.
DR RefSeq; YP_009061451.1; NC_024978.1.
DR RefSeq; YP_009061578.1; NC_024979.1.
DR RefSeq; YP_009061709.1; NC_024980.1.
DR RefSeq; YP_009068480.1; NC_025140.1.
DR RefSeq; YP_009068769.1; NC_025142.1.
DR RefSeq; YP_009068963.1; NC_025143.1.
DR RefSeq; YP_009069084.1; NC_025144.1.
DR RefSeq; YP_009069609.1; NC_025147.1.
DR RefSeq; YP_009071358.1; NC_025180.1.
DR RefSeq; YP_009328622.1; NC_032100.1.
DR RefSeq; YP_190180.1; NC_006671.1.
DR AlphaFoldDB; Q7M1C0; -.
DR SMR; Q7M1C0; -.
DR MEROPS; S24.003; -.
DR GeneID; 39692666; -.
DR GeneID; 60904328; -.
DR OMA; HETARNG; -.
DR OrthoDB; 1933795at2; -.
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_0000252112"
FT CHAIN 29..145
FT /note="Protein ImpA'"
FT /evidence="ECO:0000250"
FT /id="PRO_0000252113"
FT ACT_SITE 64
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000250|UniProtKB:P0AG11"
FT ACT_SITE 101
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000250|UniProtKB:P0AG11"
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
