ID SPLA_STAA8 Reviewed; 235 AA. AC Q2FXC2; Q9KH51; DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 27-MAR-2024, entry version 85. DE RecName: Full=Serine protease SplA; DE EC=3.4.21.-; DE Flags: Precursor; GN Name=splA; OrderedLocusNames=SAOUHSC_01942; OS Staphylococcus aureus (strain NCTC 8325 / PS 47). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=93061; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-50, SUBCELLULAR RP LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION. RX PubMed=11179322; DOI=10.1128/iai.69.3.1521-1527.2001; RA Reed S.B., Wesson C.A., Liou L.E., Trumble W.R., Schlievert P.M., RA Bohach G.A., Bayles K.W.; RT "Molecular characterization of a novel Staphylococcus aureus serine RT protease operon."; RL Infect. Immun. 69:1521-1527(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 8325 / PS 47; RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.; RT "The Staphylococcus aureus NCTC 8325 genome."; RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.); RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington RL D.C. (2006). CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11179322}. CC -!- DEVELOPMENTAL STAGE: Maximally expressed during early stationary phase. CC {ECO:0000269|PubMed:11179322}. CC -!- INDUCTION: Positively regulated by agr (accessory gene regulator). CC {ECO:0000269|PubMed:11179322}. CC -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF271715; AAF97925.1; -; Genomic_DNA. DR EMBL; CP000253; ABD31004.1; -; Genomic_DNA. DR RefSeq; WP_001039435.1; NZ_LS483365.1. DR RefSeq; YP_500442.1; NC_007795.1. DR PDB; 2W7S; X-ray; 1.80 A; A/B/C/D=36-235. DR PDB; 2W7U; X-ray; 2.43 A; A/B/C/D=36-235. DR PDB; 3UFA; X-ray; 1.80 A; A/B=36-235. DR PDB; 4MVN; X-ray; 1.70 A; A/B/C/D=36-235. DR PDBsum; 2W7S; -. DR PDBsum; 2W7U; -. DR PDBsum; 3UFA; -. DR PDBsum; 4MVN; -. DR AlphaFoldDB; Q2FXC2; -. DR SMR; Q2FXC2; -. DR STRING; 93061.SAOUHSC_01942; -. DR MEROPS; S01.503; -. DR PaxDb; 1280-SAXN108_1846; -. DR GeneID; 3921025; -. DR KEGG; sao:SAOUHSC_01942; -. DR PATRIC; fig|93061.5.peg.1767; -. DR eggNOG; COG3591; Bacteria. DR HOGENOM; CLU_073589_2_0_9; -. DR OrthoDB; 9766361at2; -. DR EvolutionaryTrace; Q2FXC2; -. DR PHI-base; PHI:11221; -. DR Proteomes; UP000008816; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR008256; Peptidase_S1B. DR InterPro; IPR008353; Peptidase_S1B_tx. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR028301; V8_his_AS. DR PANTHER; PTHR43019; SERINE ENDOPROTEASE DEGS; 1. DR PANTHER; PTHR43019:SF62; SERINE ENDOPROTEASE DEGS; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR01774; EXFOLTOXIN. DR PRINTS; PR00839; V8PROTEASE. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS00672; V8_HIS; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Hydrolase; Protease; KW Reference proteome; Secreted; Serine protease; Signal. FT SIGNAL 1..35 FT /evidence="ECO:0000269|PubMed:11179322" FT CHAIN 36..235 FT /note="Serine protease SplA" FT /id="PRO_0000359533" FT ACT_SITE 74 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 113 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 189 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT STRAND 39..43 FT /evidence="ECO:0007829|PDB:4MVN" FT HELIX 50..52 FT /evidence="ECO:0007829|PDB:4MVN" FT STRAND 53..56 FT /evidence="ECO:0007829|PDB:4MVN" FT STRAND 59..65 FT /evidence="ECO:0007829|PDB:4MVN" FT STRAND 68..71 FT /evidence="ECO:0007829|PDB:4MVN" FT HELIX 73..82 FT /evidence="ECO:0007829|PDB:4MVN" FT STRAND 86..89 FT /evidence="ECO:0007829|PDB:4MVN" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:4MVN" FT STRAND 102..107 FT /evidence="ECO:0007829|PDB:4MVN" FT STRAND 109..113 FT /evidence="ECO:0007829|PDB:4MVN" FT STRAND 115..119 FT /evidence="ECO:0007829|PDB:4MVN" FT HELIX 129..132 FT /evidence="ECO:0007829|PDB:4MVN" FT STRAND 147..152 FT /evidence="ECO:0007829|PDB:4MVN" FT HELIX 156..158 FT /evidence="ECO:0007829|PDB:4MVN" FT STRAND 163..174 FT /evidence="ECO:0007829|PDB:4MVN" FT STRAND 177..180 FT /evidence="ECO:0007829|PDB:4MVN" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:4MVN" FT STRAND 200..207 FT /evidence="ECO:0007829|PDB:4MVN" FT STRAND 215..220 FT /evidence="ECO:0007829|PDB:4MVN" FT HELIX 223..231 FT /evidence="ECO:0007829|PDB:4MVN" SQ SEQUENCE 235 AA; 25549 MW; DBC6B23C6648BCF9 CRC64; MNKNVMVKGL TALTILTSLG FAENISNQPH SIAKAEKNVK EITDATKEPY NSVVAFVGGT GVVVGKNTIV TNKHIAKSND IFKNRVSAHH SSKGKGGGNY DVKDIVEYPG KEDLAIVHVH ETSTEGLNFN KNVSYTKFAD GAKVKDRISV IGYPKGAQTK YKMFESTGTI NHISGTFMEF DAYAQPGNSG SPVLNSKHEL IGILYAGSGK DESEKNFGVY FTPQLKEFIQ NNIEK //