SPLB_STAA8
ID SPLB_STAA8 Reviewed; 240 AA.
AC Q2FXC3; Q9KH50;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Serine protease SplB;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=splB; OrderedLocusNames=SAOUHSC_01941;
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 37-57, PROTEASE
RP ACTIVITY, SUBCELLULAR 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 PROTEIN SEQUENCE OF 37-41, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 37-240, PROTEIN SEQUENCE OF
RP N-TERMINUS, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-193, AND ACTIVE SITE.
RX PubMed=18448121; DOI=10.1016/j.jmb.2008.03.059;
RA Dubin G., Stec-Niemczyk J., Kisielewska M., Pustelny K., Popowicz G.M.,
RA Bista M., Kantyka T., Boulware K.T., Stennicke H.R., Czarna A.,
RA Phopaisarn M., Daugherty P.S., Thoegersen I.B., Enghild J.J.,
RA Thornberry N., Dubin A., Potempa J.;
RT "Enzymatic activity of the Staphylococcus aureus SplB serine protease is
RT induced by substrates containing the sequence Trp-Glu-Leu-Gln.";
RL J. Mol. Biol. 379:343-356(2008).
CC -!- FUNCTION: Serine protease that cleaves specifically after the sequence
CC Trp-Glu-Leu-Gln. {ECO:0000269|PubMed:18448121}.
CC -!- ACTIVITY REGULATION: Maintained latent until the signal peptide is
CC removed by signal peptidase. {ECO:0000269|PubMed:16516230}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:18448121};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11179322,
CC ECO:0000269|PubMed:16516230}.
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; AAF97926.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD31003.1; -; Genomic_DNA.
DR RefSeq; WP_001039447.1; NZ_LS483365.1.
DR RefSeq; YP_500441.1; NC_007795.1.
DR PDB; 2VID; X-ray; 1.80 A; A/B=37-240.
DR PDB; 4K1S; X-ray; 1.96 A; A/B=37-240.
DR PDB; 4K1T; X-ray; 1.60 A; A/B/C=37-240.
DR PDB; 6YV5; X-ray; 1.10 A; A=37-240.
DR PDB; 6YV6; X-ray; 1.36 A; A=37-240.
DR PDBsum; 2VID; -.
DR PDBsum; 4K1S; -.
DR PDBsum; 4K1T; -.
DR PDBsum; 6YV5; -.
DR PDBsum; 6YV6; -.
DR AlphaFoldDB; Q2FXC3; -.
DR SMR; Q2FXC3; -.
DR STRING; 1280.SAXN108_1845; -.
DR MEROPS; S01.282; -.
DR EnsemblBacteria; ABD31003; ABD31003; SAOUHSC_01941.
DR GeneID; 3921024; -.
DR KEGG; sao:SAOUHSC_01941; -.
DR PATRIC; fig|93061.5.peg.1766; -.
DR eggNOG; COG3591; Bacteria.
DR HOGENOM; CLU_073589_2_0_9; -.
DR OMA; NKYVLHE; -.
DR EvolutionaryTrace; Q2FXC3; -.
DR PRO; PR:Q2FXC3; -.
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 ECO:0000269|PubMed:16516230, ECO:0000269|PubMed:18448121"
FT CHAIN 37..240
FT /note="Serine protease SplB"
FT /id="PRO_0000359547"
FT ACT_SITE 75
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:18448121"
FT ACT_SITE 113
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:18448121"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:18448121"
FT MUTAGEN 193
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18448121"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:6YV5"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:6YV5"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6YV5"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:6YV5"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:6YV5"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:6YV5"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:6YV5"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2VID"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:6YV5"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:6YV5"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:6YV5"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:6YV5"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:6YV5"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:6YV5"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:6YV5"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:6YV6"
FT STRAND 168..178
FT /evidence="ECO:0007829|PDB:6YV5"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:6YV5"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:6YV5"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:6YV5"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:6YV5"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:6YV5"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:6YV5"
FT HELIX 228..236
FT /evidence="ECO:0007829|PDB:6YV5"
SQ SEQUENCE 240 AA; 26097 MW; 00A3349F1FE5D52E CRC64;
MNKNVVIKSL AALTILTSVT GIGTTLVEEV QQTAKAENNV TKVKDTNIFP YTGVVAFKSA
TGFVVGKNTI LTNKHVSKNY KVGDRITAHP NSDKGNGGIY SIKKIINYPG KEDVSVIQVE
ERAIERGPKG FNFNDNVTPF KYAAGAKAGE RIKVIGYPHP YKNKYVLYES TGPVMSVEGS
SIVYSAHTES GNSGSPVLNS NNELVGIHFA SDVKNDDNRN AYGVYFTPEI KKFIAENIDK
