ID Q04186_STAAU Unreviewed; 357 AA.
AC Q04186;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Serine protease {ECO:0000256|RuleBase:RU004296};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU004296};
GN Name=sspA {ECO:0000313|EMBL:SPZ97384.1};
GN ORFNames=NCTC7878_00781 {ECO:0000313|EMBL:SPZ97384.1};
OS Staphylococcus aureus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280 {ECO:0000313|EMBL:BAA00630.1};
RN [1] {ECO:0000313|EMBL:BAA00630.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 12600 {ECO:0000313|EMBL:BAA00630.1};
RX PubMed=1599945; DOI=10.1016/0167-4838(92)90358-K;
RA Yoshikawa K., Tsuzuki H., Fujiwara T., Nakamura E., Iwamoto H.,
RA Matsumoto K., Shin M., Yoshida N., Teraoka H.;
RT "Purification, characterization and gene cloning of a novel glutamic acid-
RT specific endopeptidase from Staphylococcus aureus ATCC 12600.";
RL Biochim. Biophys. Acta 1121:221-228(1992).
RN [2] {ECO:0000313|EMBL:SPZ97384.1, ECO:0000313|Proteomes:UP000249913}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC7878 {ECO:0000313|EMBL:SPZ97384.1,
RC ECO:0000313|Proteomes:UP000249913};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Preferentially cleaves peptide bonds on the carboxyl-terminal
CC side of aspartate and glutamate. Along with other extracellular
CC proteases it is involved in colonization and infection of human
CC tissues. Required for proteolytic maturation of thiol protease SspB and
CC inactivation of SspC, an inhibitor of SspB. It is the most important
CC protease for degradation of fibronectin-binding protein (FnBP) and
CC surface protein A, which are involved in adherence to host cells. May
CC also protect bacteria against host defense mechanism by cleaving the
CC immunoglobulin classes IgG, IgA and IgM. May be involved in the
CC stability of secreted lipases. {ECO:0000256|ARBA:ARBA00043910}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase S1B family.
CC {ECO:0000256|ARBA:ARBA00008764, ECO:0000256|RuleBase:RU004296}.
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; D00730; BAA00630.1; -; Genomic_DNA.
DR EMBL; UAUX01000004; SPZ97384.1; -; Genomic_DNA.
DR PIR; S21758; S21758.
DR RefSeq; WP_000676568.1; NZ_WKIS01000045.1.
DR MEROPS; S01.269; -.
DR PATRIC; fig|1280.3537.peg.1180; -.
DR Proteomes; UP000249913; Unassembled WGS sequence.
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; IPR028301; V8_his_AS.
DR InterPro; IPR000126; V8_ser_AS.
DR PANTHER; PTHR15462; SERINE PROTEASE; 1.
DR PANTHER; PTHR15462:SF8; SERINE PROTEASE; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR01774; EXFOLTOXIN.
DR PRINTS; PR00839; V8PROTEASE.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00672; V8_HIS; 1.
DR PROSITE; PS00673; V8_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004296, ECO:0000313|EMBL:BAA00630.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004296};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004296};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU004296};
KW Virulence {ECO:0000256|ARBA:ARBA00023026};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|RuleBase:RU004296"
FT CHAIN 30..357
FT /note="Serine protease"
FT /evidence="ECO:0000256|RuleBase:RU004296"
FT /id="PRO_5041479897"
FT REGION 33..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
FT ACT_SITE 237
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
SQ SEQUENCE 357 AA; 38651 MW; 58AA9A4E371E2577 CRC64;
MKGKFLKVSS LFVATLTTAT LVSSPAANAL SSKAMDNHPQ QTQTDKQQTP KIQKGGNLKP
LEQRERANVI LPNNDRHQIT DTTNGHYAPV TYIQVEAPTG TFIASGVVVG KDTLLTNKHV
VDATHGDPHA LKAFPSAINQ DNYPNGGFTA EQITKYSGEG DLAIVKFSPN EQNKHIGEVV
KPATMSNNAE TQVNQNITVT GYPGDKPVAT MWESKGKITY LKGEAMQYDL STTGGNSGSP
VFNEKNEVIG IHWGGVPNQF NGAVFINENV RNFLKQNIED INFANDDHPN NPDNPDNPNN
PDNPNNPDNP NNPDNPDNPN NPDNPNNPDN PNNPDQPNNP NNPDNGDNNN SDNPDAA
//
