ID   SRAP_STAAU              Reviewed;        2283 AA.
AC   Q8VQ99;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Serine-rich adhesin for platelets;
DE   AltName: Full=Adhesin SraP {ECO:0000305};
DE   AltName: Full=Staphylococcus aureus surface protein A;
DE   Flags: Precursor;
GN   Name=sraP;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FRI326;
RA   Sharp L.J., Henderson B., Poole S., Nair S.;
RT   "Identification of a putative serine-threonine rich antigen from
RT   Staphylococcus aureus.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mediates binding to human platelets, possibly through a
CC       receptor-ligand interaction. Probably associated with virulence in
CC       endovascular infection (By similarity). {ECO:0000250|UniProtKB:Q2FUW1}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}. Note=Exported by the accessory SecA2/SecY2 system.
CC       Anchored to the cell wall by sortase A (By similarity).
CC       {ECO:0000250|UniProtKB:Q2FUW1}.
CC   -!- PTM: Proteolytically cleaved by a metalloprotease.
CC       {ECO:0000250|UniProtKB:Q2FUW1}.
CC   -!- PTM: Glycosylated (By similarity). It is probable that most of the Ser
CC       residues in SSR1 and SSR2 are O-GlcNAcylated. Sequential glycosylation
CC       by sugar transferases are able to generate complex sugar polymorphisms
CC       (By similarity). {ECO:0000250|UniProtKB:A0A0H2URK1,
CC       ECO:0000250|UniProtKB:Q2FUW1}.
CC   -!- SIMILARITY: Belongs to the serine-rich repeat protein (SRRP) family.
CC       {ECO:0000305}.
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DR   EMBL; AF459093; AAL58470.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8VQ99; -.
DR   SMR; Q8VQ99; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR022263; KxYKxGKxW.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF19258; KxYKxGKxW_sig; 1.
DR   SUPFAM; SSF49313; SSF49313; 2.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   TIGRFAMs; TIGR03715; KxYKxGKxW; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   3: Inferred from homology;
KW   Cell adhesion; Cell wall; Glycoprotein; Peptidoglycan-anchor; Secreted;
KW   Signal; Virulence.
FT   SIGNAL          1..89
FT                   /evidence="ECO:0000250|UniProtKB:Q2FUW1"
FT   CHAIN           90..2244
FT                   /note="Serine-rich adhesin for platelets"
FT                   /id="PRO_0000273918"
FT   PROPEP          2245..2283
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000273919"
FT   REGION          90..230
FT                   /note="Serine-rich repeat region 1, SRR1"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FUW1"
FT   REGION          100..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..751
FT                   /note="Non-repeat region (NRR)"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FUW1"
FT   REGION          691..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          751..2255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..2244
FT                   /note="Serine-rich repeat region 2, SRR2"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FUW1"
FT   MOTIF           2241..2245
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        751..2231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2244
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   2283 AA;  228867 MW;  9C0991E0E59B24B0 CRC64;
     MSKRQKAFHD SLANEKTRVR LYKSGKNWVK SGIKEIEMFK IMGLPFISHR IVSQDNQSIS
     KKMTGYGLKT TAVIGGAFTV NMLHDQQAFA ASDAPLTSEL NTQSETVGNQ NSTTIEASTS
     TADSTSVTKN SSSVQTSNSD TVSSEKSENV TSTTNSTSNQ QEKLTSTSES TSSKNTTSSS
     DTKSVASTSS TEQPINTSTN QSTASNNTSQ STTPSSANLN KTSTTSTSTA PVKLRTFSRL
     AMSTFASAAT TTAVTANTIT VNKDNLKQYM TASGNATYDQ STGIVTLTQD AYSQKGAITL
     GTRIDSNKSF HFSGKVNLGN KYEGHGNGGD GIGFAFSPGV LGETGLNGAA VGIGGLSNAF
     GFKLDTYHNT STPNASAKAK ADPSSVAGGG AFGAFVTTDS YGVASTYTSS SAADNAAKLN
     VQPTNNAFQD FDINYNGDTK VMTVTYAGQT WTRNISDWIA KSGTTNFSLS MTASTGGATN
     LQQVQFGTFE YTESAVTQVR YVDVTTGKDI IPPKTYSGNV DQVVTIDNQQ SALTAKGYNY
     TSVDSSYAST YNDTNKTVKM TNAGQSVTYY FTDVKAPTVT VGNQTIEVGK TMNPIVLTTT
     DNGTGTVTNT VTGLPSGLSY DSATNSIIGT PTKIGQSTVT VVSTDQANNK STTTFTINVV
     DTTAPTVTPI GDQSSEVYSP ISPIKIATQD NSGNAVTNKS TGLPSGLTFD STNNTISGTP
     TNIGTSTITI VSTDASGNKT TTTFKYEVTR NSMSDSVSTS GSTQQSQSVS TSKADSQSAS
     TSTSGSIVVS TSASTSKSTS VSLSDSVSAS KSLSTSESNS VSSSTSTSLV NSQSVSSSMS
     DSASKSTSLS DSISNSSSTE KSESLSTSTS DSLRTSTSLS DSLSMSTSGS LSKSQSLSTS
     TSDSASTSQS VSDSTSNSIS TAESLSESAS TSDSISISNS IANSQSASTS KSDSQSTSIS
     LSTSDSKSMS TSESLSDSTS TSDSVSGSLS VAGSQSVSTS TSDSMSTSEI VSDSISTSGS
     LSASDSKSMS VSSSMSTSQS GSTSESLSDS QSTSDSDSKS LSLSTSQSGS TSTSTSTSSS
     VRTSESQSTS GSMSTSQSDS TSISTSFSDP TSDSKSASTA SSESISQSVS TSTSGSVSTS
     TSLSTSNSER TSTSMSDSTS LSTSESDSTS DSTSTSDSIS EAISGSESTS ISLSESNSTG
     DSESKSASAF LSESLSESTS ESTSESLSGS TSDSTSLSDS NSESGSTSTS LSNSTSGSTS
     ISTSTSGSAS TSTVKSESVS TSLSTSTSTS LSDSTSLSTS LSDSTSGSKS NSLSASMSTS
     DSISTRKSES LSASTSLSGS TSESESGSTS SSASQSDSTS MSLSMSQSIS GSTSTSTSTS
     LSDSTSTSLS LSASMNQSGV DSNSASQSAS TSTSISTSES DSQSTSTYTS QSTSQSESTS
     TSTSISDSTS ISKSTSQSGS TSTSASLSGS ESESDSQSVS TSASESTSES ASTSLSDSTS
     TSNSTSESTS NAISTSASAS ESDSSSTSLS DSTSASMQSS ESDSQSTSTS LSNSQSTSTS
     IRMSTIVSES VSESTSESGS TSESTSESDS TSTSLSDSQS TSRSTSASGS ASTSTSTSDS
     RSTSAPTSTS MRTSTLDSQS MSLSTSTSTS VSDSTSLSDS VSDSTSDSTS TSTSGSMSAS
     ISLSDSTSTS TSASEVMSAS ISDSQSMSES VNDSESVSES NSESDSKSMS GSTSVSDSGS
     LSVSTSLRKS ESVSESSSLS GSQSMSDSVS TSDSSSLSVS MSLRSSESVS ESDSLSDSKS
     TSGSTSTSTS GSLSTSLSGS ESVSESTSLS DSISMSDSTS TSDSDSLSGS ISLSGSTSLS
     TSDSLSDSKS LSSSQSMSGS ESTSTSVSDS QSSSASNSQF DSMSISASES DSVSTSDSSS
     ISGSNSTSTS LSTSDSMSGS VSVSTSTSLS DSISGSISVS DSSSTSTSES LSDSMAQSQS
     TSTSASGSLS TSISTSMSMS ASTSTSQSTS VSTSLSTSDS ISDSTSISIS GSQSAVESES
     TSDSTSISDS ESLSTSDSDS TSTSTSVSTS GSTSTSVSES LSTSGSGSTS VSDSTSMSES
     DSTSASMSQD KSDSTSISNS ESVSTSTSTS LSTSDSTSTS ESLSTSMSGS QSISDSTSTS
     MSNSTSMSNS TSTSMSGSTS TSESNSMHPS DSMSMHHTHS TSTSISTSEA TTSTSDSQST
     LSATSEATKH NGTRAQSEER LPDTGESIKQ NGLLGGIMTL LVGLGLMKRK KKKDENDQDD
     SQA