SAMA_SALTY
ID SAMA_SALTY Reviewed; 140 AA.
AC P23831;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein SamA;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=Protein SamA';
GN Name=samA; OrderedLocusNames=PSLT055;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OG Plasmid pSLT, and Plasmid 60-MDa cryptic.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2; PLASMID=60-MDa cryptic;
RX PubMed=1991707; DOI=10.1128/jb.173.3.1051-1063.1991;
RA Nohmi T., Hakura A., Nakai Y., Watanabe M., Murayama S.Y., Sofuni T.;
RT "Salmonella typhimurium has two homologous but different umuDC operons:
RT cloning of a new umuDC-like operon (samAB) present in a 60-megadalton
RT cryptic plasmid of S. typhimurium.";
RL J. Bacteriol. 173:1051-1063(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720; PLASMID=pSLT;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Involved in UV protection and mutation.
CC -!- SIMILARITY: Belongs to the peptidase S24 family. {ECO:0000305}.
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DR EMBL; D90202; BAA14225.1; -; Genomic_DNA.
DR EMBL; AE006471; AAL23541.1; -; Genomic_DNA.
DR PIR; A38176; A38176.
DR RefSeq; NP_490545.1; NC_003277.2.
DR RefSeq; WP_000925627.1; NC_003277.2.
DR RefSeq; YP_003264428.1; NC_013437.1.
DR RefSeq; YP_003864205.1; NC_014476.2.
DR RefSeq; YP_006955248.1; NC_019108.1.
DR RefSeq; YP_006955388.1; NC_019109.1.
DR RefSeq; YP_006955594.1; NC_019001.1.
DR AlphaFoldDB; P23831; -.
DR SMR; P23831; -.
DR MEROPS; S24.003; -.
DR EnsemblBacteria; AAL23541; AAL23541; PSLT055.
DR GeneID; 1256182; -.
DR KEGG; stm:PSLT055; -.
DR PATRIC; fig|99287.12.peg.4913; -.
DR HOGENOM; CLU_066192_0_0_6; -.
DR OMA; VQIWGVA; -.
DR PhylomeDB; P23831; -.
DR BioCyc; SENT99287:PSLT055-MON; -.
DR Proteomes; UP000001014; Plasmid pSLT.
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; Reference proteome; Serine protease; SOS mutagenesis;
KW SOS response.
FT CHAIN 1..140
FT /note="Protein SamA"
FT /id="PRO_0000041987"
FT CHAIN 26..140
FT /note="Protein SamA'"
FT /id="PRO_0000027303"
FT ACT_SITE 61
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 98
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000250"
FT SITE 25..26
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 140 AA; 15524 MW; 598604FBA0E32064 CRC64;
MLLLVAPEQE PVQSTAPLFT ERCPAGFPSP AADYTEEELD LNAYCIRRPA ATFFVRAIGD
SMKEMGLHSG DLMVVDKAEK PMQGDIVIAE TDGEFTVKRL QLKPRIALLP INPAYPTLYP
EELQIFGVVT AFIHKTRSTD