SRAP_STAAW
ID SRAP_STAAW Reviewed; 2275 AA.
AC Q8NUJ3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Serine-rich adhesin for platelets;
DE AltName: Full=Adhesin SraP {ECO:0000305};
DE AltName: Full=Staphylococcus aureus surface protein A;
DE Short=SasA {ECO:0000303|PubMed:23439307};
DE Flags: Precursor;
GN Name=sraP; Synonyms=sasA {ECO:0000303|PubMed:23439307};
GN OrderedLocusNames=MW2575;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
RN [2]
RP INTERACTION WITH HOST DMBT1, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=MW2;
RX PubMed=23439307; DOI=10.1128/iai.00011-13;
RA Kukita K., Kawada-Matsuo M., Oho T., Nagatomo M., Oogai Y., Hashimoto M.,
RA Suda Y., Tanaka T., Komatsuzawa H.;
RT "Staphylococcus aureus SasA is responsible for binding to the salivary
RT agglutinin gp340, derived from human saliva.";
RL Infect. Immun. 81:1870-1879(2013).
CC -!- FUNCTION: Mediates binding to human platelets, possibly through a
CC receptor-ligand interaction. Probably associated with virulence in
CC endovascular infection (By similarity). Interacts with host (human) gp-
CC 340 via the non-repeat region (NRR or binding region). Binding is
CC inhibited by N-acetylneuraminic acid (NeuAc) (PubMed:23439307).
CC {ECO:0000250|UniProtKB:Q2FUW1, ECO:0000269|PubMed:23439307}.
CC -!- SUBUNIT: Interacts with human gp-340 (DMBT1).
CC {ECO:0000269|PubMed:23439307}.
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 -!- DOMAIN: The non-repeat region (NRR, also called binding region, BR)
CC binds to human gp-340; binding is prevented by N-acetylneuraminic acid
CC (NeuAc). {ECO:0000269|PubMed:23439307}.
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 -!- DISRUPTION PHENOTYPE: Significantly decreased binding to human
CC saliva- and gp340-coated resins (DMBT1). {ECO:0000269|PubMed:23439307}.
CC -!- SIMILARITY: Belongs to the serine-rich repeat protein (SRRP) family.
CC {ECO:0000305}.
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DR EMBL; BA000033; BAB96440.1; -; Genomic_DNA.
DR RefSeq; WP_000044592.1; NC_003923.1.
DR AlphaFoldDB; Q8NUJ3; -.
DR SMR; Q8NUJ3; -.
DR EnsemblBacteria; BAB96440; BAB96440; BAB96440.
DR KEGG; sam:MW2575; -.
DR HOGENOM; CLU_002109_0_0_9; -.
DR OMA; SSLYSTX; -.
DR Proteomes; UP000000418; 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 1: Evidence at protein level;
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..2236
FT /note="Serine-rich adhesin for platelets"
FT /id="PRO_0000273928"
FT PROPEP 2237..2275
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000273929"
FT REGION 90..264
FT /note="Serine-rich repeat region 1, SRR1"
FT /evidence="ECO:0000305|PubMed:23439307"
FT REGION 100..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..751
FT /note="Non-repeat region (NRR)"
FT /evidence="ECO:0000305|PubMed:23439307"
FT REGION 751..2247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..2236
FT /note="Serine-rich repeat region 2, SRR2"
FT /evidence="ECO:0000305|PubMed:23439307"
FT MOTIF 2233..2237
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 751..2232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2236
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 2275 AA; 228407 MW; E676B6BB9E60CE2E CRC64;
MSKRQKEFHD 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 KYEGNGNGGD GIGFAFSPGV LGETGLNGAA VGIGGLSNAF
GFKLDTYHNT SKPNSAAKAN ADPSNVAGGG AFGAFVTTDS YGVATTYTSS STADNAAKLK
VQPTNNTFQD FDINYNGDTK VMTVTYAGQT 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
TNIGTSTITI VSTDASGNKT TTTFKYEVTR NSMSDSVSTS GSTQQSQSVS TSKADSQSAS
TSTSGSIVVS TSASTSKSTS VSLSDSVSAS KSLSTSESNS VSSSTSTSLV NSQSVSSSMS
DSASKSTSLS DSISNSSSTE KSESLSTSTS DSLRTSTSLS DSLSMSTSGS LSKSQSLSTS
TSESSSTSAS LSDSTSNAIS TSESLSESAS TSDSISISNS IANSQSASTS KSDSQSTSIS
LSTSDSKSMS TSESLSDSTS TSGSVSGSLS IAASQSVSTS TSDSMSTSEI VSDSISTSGS
LSASDSKSMS VSSSMSTSQS GSTSESLSDS QSTSDSDSKS LSLSTSQSGS TSTSTSTSAS
VRTSESQSTS GSMSASQSDS MSISTSFSDS TSDSKSASTA SSESISQSAS TSTSGSVSTS
TSLSTSNSER TSTSMSDSTS LSTSESDSIS ESTSTSDSIS EAISASESTF ISLSESNSTS
DSESQSASAF LSESLSESTS ESTSESVSSS TSESTSLSDS TSESGSTSTS LSNSTSGSAS
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 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
SSISGSNSTS TSLSTSDSMS GSVSVSTSTS LSDSISGSTS LSDSSSTSTS TSLSDSMSQS
QSTSTSASGS LSTSISTSMS MSASTSSSQS TSVSTSLSTS DSISDSTSIS ISGSQSTVES
ESTSDSTSIS DSESLSTSDS DSTSTSTSDS TSGSTSTSIS ESLSTSGSGS TSVSDSTSMS
ESDSTSVSMS QSMSGSTYNS TSVSDSESVS TSTSTSLSTS DSTSTSESLS TSMSGSQSIS
DSTSTSMSGS TSTSESNSMH PSDSMSMHHT HSTSTSRLSS EATTSTSESQ STLSATSEVT
KHNGTPAQSE KRLPDTGDSI KQNGLLGGVM TLLVGLGLMK RKKKKDENDQ DDSQA
