ID   SRAP_STAA3              Reviewed;        2271 AA.
AC   Q2FDK5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 98.
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; OrderedLocusNames=SAUSA300_2589;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
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; CP000255; ABD21900.1; -; Genomic_DNA.
DR   RefSeq; WP_000044529.1; NZ_CP027476.1.
DR   AlphaFoldDB; Q2FDK5; -.
DR   SMR; Q2FDK5; -.
DR   KEGG; saa:SAUSA300_2589; -.
DR   HOGENOM; CLU_002109_0_0_9; -.
DR   OMA; TKYPEDP; -.
DR   Proteomes; UP000001939; 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   CDD; cd01951; lectin_L-type; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 3.10.20.320; Putative peptidoglycan bound protein (lpxtg motif); 1.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR022263; KxYKxGKxW.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   NCBIfam; TIGR03715; KxYKxGKxW; 1.
DR   NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR   PANTHER; PTHR22928; TELOMERE-ASSOCIATED PROTEIN RIF1; 1.
DR   PANTHER; PTHR22928:SF3; TELOMERE-ASSOCIATED PROTEIN RIF1; 1.
DR   Pfam; PF18483; Bact_lectin; 1.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF19258; KxYKxGKxW_sig; 1.
DR   SUPFAM; SSF49313; Cadherin-like; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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_0000273934"
FT   PROPEP          2233..2271
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000273935"
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;  228077 MW;  7E4A545A443EC5EA 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 TMNPIVLTTT
     DNGTGTVTNT VTGLPSGLSY DSATNSIIGT PTKIGQSTVT VVSTDQANNK STTTFTINVV
     DTTAPTVTPI GDQSSEVYSP ISPIKIATQD NSGNAVTNTV TGLPSGLTFD STNNTISGTP
     TNIGTSTISI VSTDASGNKT TTTFKYEVTR NSMSDSVSTS GSTQQSQSVS TSKADSQSAS
     TSTSGSIVVS TSASTSKSTS VSLSDSVSAS KSLSTSESNS VSSSTSTSLV NSQSVSSSMS
     DSASKSTSLS DSISNSSSTE KSESLSTSTS DSLRTSTSLS DSLSMSTSGS LSKSQSLSTS
     ISGSSSTSAS LSDSTSNAIS TSTSLSESAS TSDSISISNS IANSQSASTS KSDSQSTSIS
     LSTSDSKSMS TSESLSDSTS TSGSVSGSLS IAASQSVSTS TSDSMSTSEI VSDSISTSGS
     LSASDSKSMS VSSSMSTSQS GSTSESLSDS QSTSDSDSKS LSQSTSQSGS TSTSTSTSAS
     VRTSESQSTS GSMSASQSDS MSISTSFSDS TSDSKSASTA SSESISQSAF TSTSGSVSTS
     TSLSTSNSER TSTSMSDSTS LSTSESDSIS ESTSTSDSIS EAISASESTF ISLSESNSTS
     DSESQSASAF LSESLSESTS ESTSESVSSS TSESTSLSDS TSESGSTSTS LSNSTSGSTS
     ISTSTSISES TSTFKSESVS TSLSMSTSTS LSDSTSLSTS LSDSTSDSKS DSLSTSMSTS
     DSISTSKSDS ISTSTSLSGS TSESESDSTS SSESKSDSTS MSISMSQSTS GSTSTSTSTS
     LSDSTSTSLS LSASMNQSGV DSNSASQSAS NSTSTSTSES DSQSTSSYTS QSTSQSESTS
     TSTSLSDSTS ISKSTSQSGS VSTSASLSGS ESESDSQSIS TSASESTSES ASTSLSDSTS
     TSNSGSASTS TSLSNSASAS ESDLSSTSLS DSTSASMQSS ESDSQSTSAS LSDSLSTSTS
     NRMSTIASLS TSVSTSESGS TSESTSESDS TSTSLSDSQS TSRSTSASGS ASTSTSTSDS
     RSTSASTSTS MRTSTSDSQS MSLSTSTSTS MSDSTSLSDS VSDSTSDSTS ASTSGSMSVS
     ISLSDSTSTS TSASEVMSAS ISDSQSMSES VNDSESVSES NSESDSKSMS GSTSVSDSGS
     LSVSTSLRKS ESVSESSSLS CSQSMSDSVS TSDSSSLSVS TSLRSSESVS ESDSLSDSKS
     TSGSTSTSTS GSLSTSTSLS GSESVSESTS LSDSISMSDS TSTSDSDSLS GSISLSGSTS
     LSTSDSLSDS KSLSSSQSMS GSESTSTSVS DSQSSSTSNS QFDSMSISAS ESDSMSTSDS
     SSISGSNSTS TSLSTSDSMS GSVSVSTSTS LSDSISGSTS VSDSSSTSTS TSLSDSMSQS
     QSTSTSASGS LSTSISTSMS MSASTSSSQS TSVSTSLSTS DSISDSTSIS ISGSQSTVES
     ESTSDSTSIS DSESLSTSDS DSTSTSTSDS TSGSTSTSIS ESLSTSGSGS TSVSDSTSMS
     ESNSSSVSMS QDKSDSTSIS DSESVSTSTS TSLSTSDSTS TSESLSTSMS GSQSISDSTS
     TSMSGSTSTS ESNSMHPSDS MSMHHTHSTS TSRLSSEATT STSESQSTLS ATSEVTKHNG
     TPAQSEKRLP DTGDSIKQNG LLGGVMTLLV GLGLMKRKKK KDENDQDDSQ A
//