ID C0Q8L4_SALPC Unreviewed; 140 AA.
AC C0Q8L4;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=SamA {ECO:0000313|EMBL:ACN48820.1};
GN Name=samA {ECO:0000313|EMBL:ACN48820.1};
GN OrderedLocusNames=SPC_p050 {ECO:0000313|EMBL:ACN48820.1};
OS Salmonella paratyphi C (strain RKS4594).
OG Plasmid pSPCV {ECO:0000313|EMBL:ACN48820.1,
OG ECO:0000313|Proteomes:UP000001599}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213 {ECO:0000313|EMBL:ACN48820.1, ECO:0000313|Proteomes:UP000001599};
RN [1] {ECO:0000313|EMBL:ACN48820.1, ECO:0000313|Proteomes:UP000001599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594 {ECO:0000313|EMBL:ACN48820.1,
RC ECO:0000313|Proteomes:UP000001599};
RC PLASMID=pSPCV {ECO:0000313|EMBL:ACN48820.1,
RC ECO:0000313|Proteomes:UP000001599};
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
CC -!- SIMILARITY: Belongs to the peptidase S24 family.
CC {ECO:0000256|ARBA:ARBA00007484, ECO:0000256|RuleBase:RU003991}.
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DR EMBL; CP000858; ACN48820.1; -; Genomic_DNA.
DR RefSeq; WP_000925627.1; NC_012124.1.
DR AlphaFoldDB; C0Q8L4; -.
DR SMR; C0Q8L4; -.
DR MEROPS; S24.003; -.
DR KEGG; sei:SPC_p050; -.
DR HOGENOM; CLU_066192_0_0_6; -.
DR Proteomes; UP000001599; Plasmid pSPCV.
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 Plasmid {ECO:0000313|EMBL:ACN48820.1};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW SOS mutagenesis {ECO:0000256|ARBA:ARBA00023199};
KW SOS response {ECO:0000256|ARBA:ARBA00023236}.
FT DOMAIN 17..129
FT /note="Peptidase S24/S26A/S26B/S26C"
FT /evidence="ECO:0000259|Pfam:PF00717"
SQ SEQUENCE 140 AA; 15524 MW; 598604FBA0E32064 CRC64;
MLLLVAPEQE PVQSTAPLFT ERCPAGFPSP AADYTEEELD LNAYCIRRPA ATFFVRAIGD
SMKEMGLHSG DLMVVDKAEK PMQGDIVIAE TDGEFTVKRL QLKPRIALLP INPAYPTLYP
EELQIFGVVT AFIHKTRSTD
//
