ID   SRAP_STAAC              Reviewed;        2261 AA.
AC   Q5HCP3;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=SACOL2676;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW38674.1; -; Genomic_DNA.
DR   RefSeq; WP_000044536.1; NC_002951.2.
DR   AlphaFoldDB; Q5HCP3; -.
DR   SMR; Q5HCP3; -.
DR   EnsemblBacteria; AAW38674; AAW38674; SACOL2676.
DR   KEGG; sac:SACOL2676; -.
DR   HOGENOM; CLU_002109_0_0_9; -.
DR   OMA; SSLYSTX; -.
DR   Proteomes; UP000000530; 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..2222
FT                   /note="Serine-rich adhesin for platelets"
FT                   /id="PRO_0000273920"
FT   PROPEP          2223..2261
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000273921"
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..2222
FT                   /note="Serine-rich repeat region 2, SRR2"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FUW1"
FT   REGION          806..2233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           2219..2223
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        806..2218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2222
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   2261 AA;  227020 MW;  9C405EAC30E0B067 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 SSESISQSAS TSTSGSVSTS
     TSLSTSNSER TSTSMSDSTS LSTSESDSIS ESTSTSDSIS EAISASESTF ISLSESNSTS
     DSESQSASAF LSESLSESTS ESTSESVSSS TSESTSLSDS TSESGSTSTS LSNSTSGSTS
     ISTSTSISES TSTFKSESVS TSLSMSTSTS LSDSTSLSTS LSDSTSDSKS DSLSTSMSTS
     DSISTSKSDS ISTSTSLSGS TSESKSDSTS 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