FNBA_STAAR
ID FNBA_STAAR Reviewed; 965 AA.
AC Q6GDU5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Fibronectin-binding protein A;
DE Flags: Precursor;
GN Name=fnbA; OrderedLocusNames=SAR2580;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- FUNCTION: Promotes bacterial attachment to multiple substrates, such as
CC fibronectin (Fn), fibrinogen (Fg), elastin peptides and tropoelastin.
CC This confers to S.aureus the ability to invade endothelial cells.
CC Promotes adherence to and aggregation of activated platelets (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}. Note=Anchored to the cell wall by sortase A (By
CC similarity). {ECO:0000250|UniProtKB:P14738}.
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DR EMBL; BX571856; CAG41560.1; -; Genomic_DNA.
DR RefSeq; WP_000794580.1; NC_002952.2.
DR AlphaFoldDB; Q6GDU5; -.
DR SMR; Q6GDU5; -.
DR KEGG; sar:SAR2580; -.
DR HOGENOM; CLU_009849_1_0_9; -.
DR OMA; DANKPGN; -.
DR OrthoDB; 117608at2; -.
DR PRO; PR:Q6GDU5; -.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1280; -; 1.
DR InterPro; IPR011266; Adhesin_Fg-bd_dom_2.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR011252; Fibrogen-bd_dom1.
DR InterPro; IPR004237; Fibron_repeat-bd.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR041171; SDR_Ig.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF17961; Big_8; 1.
DR Pfam; PF02986; Fn_bind; 2.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF10425; SdrG_C_C; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SUPFAM; SSF49401; SSF49401; 2.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 3: Inferred from homology;
KW Cell adhesion; Cell wall; Peptidoglycan-anchor; Repeat; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..932
FT /note="Fibronectin-binding protein A"
FT /id="PRO_0000313884"
FT PROPEP 933..965
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000313885"
FT REPEAT 548..577
FT /note="B-1"
FT REPEAT 578..607
FT /note="B-2"
FT REPEAT 748..770
FT /note="D-1; truncated"
FT REPEAT 771..785
FT /note="D-2; truncated"
FT REPEAT 786..824
FT /note="D-3"
FT REPEAT 825..839
FT /note="D-4; truncated"
FT REPEAT 840..853
FT /note="WR 1"
FT REPEAT 854..867
FT /note="WR 2"
FT REPEAT 868..881
FT /note="WR 3"
FT REPEAT 882..895
FT /note="WR 4"
FT REGION 37..514
FT /note="Ligand-binding A region"
FT REGION 37..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..514
FT /note="Fibrinogen/elastin/tropoelastin-binding"
FT /evidence="ECO:0000250"
FT REGION 515..837
FT /note="Fibronectin-binding"
FT /evidence="ECO:0000250"
FT REGION 548..607
FT /note="2 X approximate tandem repeats"
FT REGION 598..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..839
FT /note="4 X approximate tandem repeats"
FT REGION 794..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..895
FT /note="4 X tandem repeats, Pro-rich (WR)"
FT REGION 916..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 7..18
FT /note="YSIRK-G/S signaling motif"
FT /evidence="ECO:0000250|UniProtKB:P14738"
FT MOTIF 929..933
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 37..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..883
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 932
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 965 AA; 105691 MW; 2982E132164D0551 CRC64;
MKNNLRYGIR KHKLGAASVF LGTMIVIGMG QDKEAAASEQ KTTTVEENGN SATDNKVSET
QTTTTNVNTI DETQSYSATA TEQPSNATQV TTEEAPKAVQ APQTAQPANV ETVKEEVVKE
EANPQVKETT QSQDNSGDQR QVDLTPKKAT QNQVAETQVE VAQPRTALES KPRVTRSTDV
AEAKEASDAK VETGTDVTSK VTVEDESKIE APKGNNVQPH EGQRVVLKYK LKFQDGLKTG
DYFDFTLSNN VNTHGVATTR KVPDIKNGSL VMAKGQVLDN GRIRYTFTDY IKDKVNVTAN
LEINLFIDPK TVQSNGQQTI TSKLNGKETS GTMQITYKDG VKNQYTNVNG SIETFDKEKN
KFTHVAYIKP INGNNSDSVT VTGMLTQGSN ENGTQPNVKI YEYVGVENGL PQSVYANTVD
STQLKDVTNQ MGDKLKVQNN GSYSLNFDKL DKTYVIHYTG DYLNGTSEVN FRTQLTGYPE
NRYKTYYYYN NGYTLTWDNG LVLYSNKANG DGKYGPIVDS NNFEFSEDSG NGSISGQYDA
KQIIETEENQ DNTPLDIDYH TAIDGEGGYV DGYIETIEET DSSAIDIDYH TAVDSEAGHV
GGYTESSEES NPIDFEESTH ENSKHHADVV EYEEDTNPGG GQVTTESNLV EFDEESTKGI
VTGAVSDHTT VEDTKEYTTE SNLIELVDEL PEEHGQAQGP VEEITENNHH ISHSGLGTEN
GHGNYGVIEE IEENSHVDIK SELGYEGGQN SGNQSFEEDT EEDKPKYEQG GNIIDIDFDS
VPQIHGFNKH NEIIEEDTNK DKPNYQFGGH NSVDFEEDTL PKVSGQNEGQ QTIEEDTTPP
TPPTPEVPSE PGTPTPPTPE VPSEPGKPTP PTPEVPAEPG KPVPPAKEEP KKPSKPVEQG
KVVTPVIEIN EKVKAVAPTK QKQAKKSELP ETGGEESTNK GMLFGGLFSI LGLALLRRNK
KNHKA
