SPLC_STAA8
ID SPLC_STAA8 Reviewed; 239 AA.
AC Q2FXC4; Q9KH49;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Serine protease SplC;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=splC; OrderedLocusNames=SAOUHSC_01939;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 37-46, 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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 37-239.
RX PubMed=16516230; DOI=10.1016/j.jmb.2006.01.098;
RA Popowicz G.M., Dubin G., Stec-Niemczyk J., Czarny A., Dubin A., Potempa J.,
RA Holak T.A.;
RT "Functional and structural characterization of Spl proteases from
RT Staphylococcus aureus.";
RL J. Mol. Biol. 358:270-279(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}.
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DR EMBL; AF271715; AAF97927.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD31002.1; -; Genomic_DNA.
DR RefSeq; WP_001038867.1; NZ_LS483365.1.
DR RefSeq; YP_500440.1; NC_007795.1.
DR PDB; 2AS9; X-ray; 1.70 A; A/B=37-239.
DR PDBsum; 2AS9; -.
DR AlphaFoldDB; Q2FXC4; -.
DR SMR; Q2FXC4; -.
DR STRING; 1280.SAXN108_1844; -.
DR MEROPS; S01.283; -.
DR EnsemblBacteria; ABD31002; ABD31002; SAOUHSC_01939.
DR GeneID; 3921023; -.
DR KEGG; sao:SAOUHSC_01939; -.
DR PATRIC; fig|93061.5.peg.1765; -.
DR eggNOG; COG3591; Bacteria.
DR HOGENOM; CLU_073589_2_0_9; -.
DR OMA; DYPGNED; -.
DR EvolutionaryTrace; Q2FXC4; -.
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; -; 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 Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR01774; EXFOLTOXIN.
DR PRINTS; PR00839; V8PROTEASE.
DR SUPFAM; SSF50494; SSF50494; 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..36
FT /evidence="ECO:0000269|PubMed:11179322"
FT CHAIN 37..239
FT /note="Serine protease SplC"
FT /id="PRO_0000359560"
FT ACT_SITE 75
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT ACT_SITE 113
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2AS9"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:2AS9"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2AS9"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:2AS9"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2AS9"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:2AS9"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:2AS9"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:2AS9"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:2AS9"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:2AS9"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:2AS9"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:2AS9"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:2AS9"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2AS9"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:2AS9"
FT TURN 160..164
FT /evidence="ECO:0007829|PDB:2AS9"
FT STRAND 168..178
FT /evidence="ECO:0007829|PDB:2AS9"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:2AS9"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:2AS9"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:2AS9"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:2AS9"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:2AS9"
SQ SEQUENCE 239 AA; 26098 MW; BA797E14786B2DBA CRC64;
MNKNIVIKSM AALAILTSVT GINAAVVEET QQIANAEKNV TQVKDTNIFP YNGVVSFKDA
TGFVIGKNTI ITNKHVSKDY KVGDRITAHP NGDKGNGGIY KIKSISDYPG DEDISVMNIE
EQAVERGPKG FNFNENVQAF NFAKDAKVDD KIKVIGYPLP AQNSFKQFES TGTIKRIKDN
ILNFDAYIEP GNSGSPVLNS NNEVIGVVYG GIGKIGSEYN GAVYFTPQIK DFIQKHIEQ
