ID   SPLC_STAAC              Reviewed;         239 AA.
AC   Q5HEW2;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Serine protease SplC;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=splC; OrderedLocusNames=SACOL1867;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RX   PubMed=11681202;
RX   DOI=10.1002/1615-9861(200104)1:4<480::aid-prot480>3.0.co;2-o;
RA   Ziebandt A.-K., Weber H., Rudolph J., Schmid R., Hoeper D., Engelmann S.,
RA   Hecker M.;
RT   "Extracellular proteins of Staphylococcus aureus and the role of SarA and
RT   sigma B.";
RL   Proteomics 1:480-493(2001).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- INDUCTION: Negatively regulated by sigma-B factor.
CC       {ECO:0000269|PubMed:11681202}.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR   EMBL; CP000046; AAW36882.1; -; Genomic_DNA.
DR   RefSeq; WP_001038867.1; NC_002951.2.
DR   AlphaFoldDB; Q5HEW2; -.
DR   SMR; Q5HEW2; -.
DR   MEROPS; S01.283; -.
DR   EnsemblBacteria; AAW36882; AAW36882; SACOL1867.
DR   KEGG; sac:SACOL1867; -.
DR   HOGENOM; CLU_073589_2_0_9; -.
DR   OMA; DYPGNED; -.
DR   Proteomes; UP000000530; 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   Hydrolase; Protease; Secreted; Serine protease; Signal.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000250"
FT   CHAIN           37..239
FT                   /note="Serine protease SplC"
FT                   /id="PRO_0000359553"
FT   ACT_SITE        75
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        193
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
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