ID   SRAP_STAAR              Reviewed;        1351 AA.
AC   Q6GDE9;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=sasA; OrderedLocusNames=SAR2734;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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,
CC       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. {ECO:0000250,
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; BX571856; CAG41711.1; -; Genomic_DNA.
DR   RefSeq; WP_001643619.1; NC_002952.2.
DR   AlphaFoldDB; Q6GDE9; -.
DR   SMR; Q6GDE9; -.
DR   KEGG; sar:SAR2734; -.
DR   HOGENOM; CLU_005804_0_0_9; -.
DR   OMA; YGETHEI; -.
DR   OrthoDB; 261055at2; -.
DR   Proteomes; UP000000596; Chromosome.
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   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
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..1312
FT                   /note="Serine-rich adhesin for platelets"
FT                   /id="PRO_0000273922"
FT   PROPEP          1313..1351
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000273923"
FT   REGION          90..230
FT                   /note="Serine-rich repeat region 1, SRR1"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FUW1"
FT   REGION          100..228
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          751..1323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..1312
FT                   /note="Serine-rich repeat region 1, SRR1"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FUW1"
FT   MOTIF           1309..1313
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        751..1308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1312
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   1351 AA;  138292 MW;  B68C5D54C2945D52 CRC64;
     MSKRQKEFHD SLANEKTRVR LYKSGKNWVK SGIKEIEMFK IMGLPFISHS LVSQDNQSIS
     KKITGYGLKT TAVIGGAFTV NMLHDQQAFA ASDAPLTSEL NTQSETVGNQ NSTTIEASTS
     TTDSTSVTKN SSSEQTSNSD TVSSEKSENV TSTTNSTSNQ QEKLTSTSES TSPKNTTSSS
     DTKSVTSISS TDQQTNTSTN QSTASNTTSQ STTPASANLN KTSTTSTSTA PIKLRTFSRL
     AMSTFASAAT TSAVTANTIT VNKDNLKQYM TTSGNATYDQ STGIVTLTQD AYSQKGAITL
     GTRIDSNKSF HFSGKVNLGN KYEGNGNGGD GIGFAFSPGV LGETGLNGAA VGIGGLSNAF
     GFKLDTYHNT SKPNAAAKAN ADPSNVAGGG AFGAFVTTDS YGVATTYTSS SAADNAAKLK
     VQPTNNTFQD 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 NSGNAVTNTV TGLPSGLTFD STNNTISGTP
     TNIGTSTITI VSTDASGNKT TTTFKYEVTR NSMSDSVSTS GSTQQSQSVS TSKADSQSAS
     TSTSGSIVVS TSASTSKSTS VSLSDSVSAS KSLSTSESNS VSSSTSTSLV NSQSVSSSMS
     GSVSKSTSLS DSISNSSSTE KSESLSTSTS DSLRTSTSLS DSVSMSTSGS LSKSQSLSTS
     TSDSASTSQS VSDSTSNSIS TSESLSESAS TSDSISISNS IANSQSASTS KSDSQSTSIS
     LSTSDSKSMS TSESLSDSTS TSDSVSGSLS IATSQSVSTS SSDSMSTSEM ISDSMSTSGS
     LAASDSKSMS VSSSMSTSQS GSTSESLSDS ISTSDSDSKS LSLSTSQSGS TSTSTSTSSS
     VRTSESQSTS GSMSASQFDS TSISTSFSDS TSDSKSASTA SSESISQSVS TSTSGSTSGS
     TSTSTSESLS MSGSDSTSVS DSTSMSESDS TSVSMSQDKS DSTSISDSES VSTSTSMSLS
     TSDSTSTSES LSTSMSGSQS ISDSTSTSMS NSTSMSNSTS TSMSGSTSTS ESNSMHPSDS
     MSMHHTHSTS TSRSSSEATT STSESQSTLS ATSEVTKHNG TPAQSEKRLP DTGDSIKQNG
     LLGGVMTLLV GLGLMKRKKK KDENDQDDSQ A