SRAP_STAA3
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 25-MAY-2022, entry version 92.
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; Firmicutes; 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 EnsemblBacteria; ABD21900; ABD21900; SAUSA300_2589.
DR KEGG; saa:SAUSA300_2589; -.
DR HOGENOM; CLU_002109_0_0_9; -.
DR OMA; SSLYSTX; -.
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 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_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