ID   SRAP_STAAM              Reviewed;        2271 AA.
AC   Q99QY4;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
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; Synonyms=sasA; OrderedLocusNames=SAV2654;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000017; BAB58816.1; -; Genomic_DNA.
DR   RefSeq; WP_000044547.1; NC_002758.2.
DR   AlphaFoldDB; Q99QY4; -.
DR   SMR; Q99QY4; -.
DR   PaxDb; Q99QY4; -.
DR   EnsemblBacteria; BAB58816; BAB58816; SAV2654.
DR   KEGG; sav:SAV2654; -.
DR   HOGENOM; CLU_002109_0_0_9; -.
DR   OMA; SSLYSTX; -.
DR   BioCyc; SAUR158878:SAV_RS14500-MON; -.
DR   Proteomes; UP000002481; 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   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..2232
FT                   /note="Serine-rich adhesin for platelets"
FT                   /id="PRO_0000273926"
FT   PROPEP          2233..2271
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000273927"
FT   REGION          90..230
FT                   /note="Serine-rich repeat region 1, SRR1"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FUW1"
FT   REGION          100..229
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..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..2232
FT                   /note="Serine-rich repeat region 2, SRR2"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FUW1"
FT   REGION          806..2243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           2229..2233
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        806..2228
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2232
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   2271 AA;  227848 MW;  7C2A7040D6C8289D CRC64;
     MSKRQKAFHD SLANEKTRVR LYKSGKNWVK SGIKEIEMFK IMGLPFISHS LVSQDNQSIS
     KKMTGYGLKT TAVIGGAFTV NMLHDQQAFA ASDAPLTSEL NTQSETVGNQ NSTTIEASTS
     TADSTSVTKN SSSVQTSNSD TVSSEKSEKV TSTTNSTSNQ QEKLTSTSES TSSKNTTSSS
     DTKSVASTSS TEQPINTSTN QSTASNNTSQ STTPSSVNLN KTSTTSTSTA PVKLRTFSRL
     AMSTFASAAT TTAVTANTIT VNKDNLKQYM TTSGNATYDQ STGIVTLTQD AYSQKGAITL
     GTRIDSNKSF HFSGKVNLGN KYEGHGNGGD GIGFAFSPGV LGETGLNGAA VGIGGLSNAF
     GFKLDTYHNT SKPNSAAKAN ADPSNVAGGG AFGAFVTTDS YGVATTYTSS STADNAAKLN
     VQPTNNTFQD FDINYNGDTK VMTVKYAGQT WTRNISDWIA KSGTTNFSLS MTASTGGATN
     LQQVQFGTFE YTESAVTQVR YVDVTTGKDI IPPKTYSGNV DQVVTIDNQQ SALTAKGYNY
     TSVDSSYAST YNDTNKTVKM TNAGQSVTYY FTDVKAPTVT VGNQTIEVGK TMNPVVLTTT
     DNGTGTVTNT VTGLPSGLSY DSATNSIIGT PTKIGQSTVT VVSTDQANNK STTTFTINVV
     DTTAPTVTPI GDQSSEVYSP ISPIKIATQD NSGNAVTNTV TGLPSGLTFD STNNTISGTP
     TNIGTSTISI VSTDASGNKT TTTFKYEVTR NSMSDSVSTS GSTQQSQSVS TSKADSQSAS
     TSTSGSIVVS TSASTSKSTS VSLSDSVSAS KSLSTSESNS VSSSTSTSLV NSQSVSSSMS
     GSVSKSTSLS DSISNSNSTE KSESLSTSTS DSLRTSTSLS DSLSMSTSGS LSKSQSLSTS
     ISGSSSTSAS LSDSTSNAIS TSTSLSESAS TSDSISISNS IANSQSASTS KSDSQSTSIS
     LSTSDSKSMS TSESLSDSTS TSGSVSGSLS IAASQSVSTS TSDSMSTSEI VSDSISTSGS
     LSASDSKSMS VSSSMSTSQS GSTSESLSDS QSTSDSDSKS LSLSTSQSGS TSTSTSTSAS
     VRTSESQSTS GSMSASQSDS MSISTSFSDS TSDSKSASTA SSESISQSAS TSTSGSVSTS
     TSLSTSNSER TSTSVSDSTS LSTSESDSIS ESTSTSDSIS EAISASESTS ISLSESNSTS
     DSESQSASAF LSESLSESTS ESTSESVSSS TSESTSLSDS TSESGSTSTS LSNSTSGSAS
     ISTSTSISES TSTFKSESVS TSLSMSTSTS LSNSTSLSTS LSDSTSDSKS DSLSTSMSTS
     DSISTSKSDS ISTSTSLSGS TSESESDSTS SSESKSDSTS MSISMSQSTS GSTSTSTSTS
     LSDSTSTSLS LSASMNQSGV DSNSASQSAS NSTSTSTSES DSQSTSTYTS QSTSQSESTS
     TSTSLSDSTS ISKSTSQSGS TSTSASLSGS ESESDSQSIS TSASESTSES ASTSLSDSTS
     TSNSGSASTS TSLSNSASAS ESDSSSTSLS DSTSASMQSS ESDSQSTSAS LSDSLSTSTS
     NRMSTIASLS TSVSTSESGS TSESTSESDS TSTSLSDSQS TSRSTSASGS ASTSTSTSDS
     RSTSASTSTS MRTSTSDSQS MSLSTSTSTS MSDSTSLSDS VSDSTSDSTS ASTSGSMSVS
     ISLSDSTSTS TSASEVMSAS ISDSQSMSES VNDSESVSES NSESDSKSMS GSTSVSDSGS
     LSVSTSLRKS ESVSESSSLS GSQSMSDSVS TSDSSSLSVS TSLRSSESVS ESDSLSDSKS
     TSGSTSTSTS GSLSTSTSLS GSESVSESTS LSDSISMSDS TSTSDSDSLS GSISLSGSTS
     LSTSDSLSDS KSLSSSQSMS GSESTSTSVS DSQSSSTSNS QFDSMSISAS ESDSMSTSDS
     SNISGSNSTS TSLSTSDSMS GSVSVSTSTS LSDSISGSTS VSDSSSTSTS TSLSDSMSQS
     QSTSTSASGS LSTSISTSMS MSASTSSSQS TSVSTSLSTS DSISDSTSIS ISGSQSTVES
     ESTSDSTSIS DSESLSTSDS DSTSTSTSDS TSGSTSTSIS ESLSTSGSGS TSVSDSTSMS
     ESDSTSVSMS QDKSDSTSIS DSESVSTSTS TSLSTSDSTS TSESLSTSMS GSQSISDSTS
     TSMSGSTSTS ESNSMHPSDS MSMHHTHSTS TSRLSSEATT STSESQSTLS ATSEVTKHNG
     TPAQSEKRLP DTGDSIKQNG LLGGVMTLLV GLGLMKRKKK KDENDQDDSQ A