ID   FNBA_STAAS              Reviewed;        1015 AA.
AC   Q6G6H3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Fibronectin-binding protein A;
DE   Flags: Precursor;
GN   Name=fnbA; OrderedLocusNames=SAS2388;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
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; BX571857; CAG44202.1; -; Genomic_DNA.
DR   RefSeq; WP_000794648.1; NC_002953.3.
DR   AlphaFoldDB; Q6G6H3; -.
DR   SMR; Q6G6H3; -.
DR   KEGG; sas:SAS2388; -.
DR   HOGENOM; CLU_009849_1_0_9; -.
DR   OMA; DANKPGN; -.
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; 3.
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..982
FT                   /note="Fibronectin-binding protein A"
FT                   /id="PRO_0000313886"
FT   PROPEP          983..1015
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000313887"
FT   REPEAT          546..575
FT                   /note="B-1"
FT   REPEAT          576..605
FT                   /note="B-2"
FT   REPEAT          746..783
FT                   /note="D-1"
FT   REPEAT          784..821
FT                   /note="D-2"
FT   REPEAT          822..860
FT                   /note="D-3"
FT   REPEAT          861..875
FT                   /note="D-4; truncated"
FT   REPEAT          876..889
FT                   /note="WR 1"
FT   REPEAT          890..903
FT                   /note="WR 2"
FT   REPEAT          904..917
FT                   /note="WR 3"
FT   REPEAT          918..931
FT                   /note="WR 4"
FT   REPEAT          932..945
FT                   /note="WR 5"
FT   REGION          37..512
FT                   /note="Ligand-binding A region"
FT   REGION          75..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..512
FT                   /note="Fibrinogen/elastin/tropoelastin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          513..873
FT                   /note="Fibronectin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          546..605
FT                   /note="2 X approximate tandem repeats"
FT   REGION          596..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          741..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          746..875
FT                   /note="4 X approximate tandem repeats"
FT   REGION          828..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          876..945
FT                   /note="5 X tandem repeats, Pro-rich (WR)"
FT   REGION          966..992
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           979..983
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        75..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        792..806
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..873
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..933
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         982
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   1015 AA;  111146 MW;  D0F9281BB64D44D2 CRC64;
     MKNNLRYGIR KHKLGAASVF LGTMIVVGMG QDKEAAASEQ KTTTVEENGN SATENKVNET
     QTTTTNVNTI DETQSYSATA TEQPSNATQV TTEEAPKAVQ APQTAQPANL ETVKEEVVKE
     EAKPQVKETT QSQDNSGDQR QVDLTPKKAT QNQVAETQVE VAQPRTASES KPRVTRSADV
     VEAKEASDEK VETGTDVTSK VTVESGSIEA PQGNKVEPHA GQRVVLKYKL KFADGLKRGD
     YFDFTLSNNV NTYGVSTARK VPEIKNGSVV MATGEILGNG NIRYTFTNEI EHKVEVTANL
     EINLFIDPKT VQSNGEQKIT SKLNGEETEK TIPVVYNPGV SNSYTNVNGS IETFNKESNK
     FTHIAYIKPM NGNQSNTVSV TGTLTEGSNL AGGQPTVKVY EYLGKKDELP QSVYANTSDT
     NKFKDVTKEM NGKLSVQDNG SYSLNLDKLD KTYVIHYTGE YLQGSDQVNF RTELYGYPER
     AYKSYYVYGG YRLTWDNGLV LYSNKADGNG KNGQIIQNND FEYKEDTAKG TMSGQYDAKQ
     IIETEENQDN TPLDIDYHTA IDGEGGYVDG YIETIEETDS SAIDIDYHTA VDSEAGHVGG
     YTESSEESNP IDFEESTHEN SKHHADVVEY EEDTNPGGGQ VTTESNLVEF DEESTKGIVT
     GAVSDHTTIE DTKEYTTESN LIELVDELPE EHGQAQGPIE EITENNHHIS HSGLGTENGH
     GNYGVIEEIE ENSHVDIKSE LGYEGGQNSG NQSFEEDTEE DKPKYEQGGN IVDIDFDSVP
     QIQGQNNGNQ SFEEDTEKDK PKYEQGGNII DIDFDSVPQI HGFNKHTEII EEDTNKDKPN
     YQFGGHNSVD FEEDTLPKVS GQNEGQQTIE EDTTPPTPPT PEVPSEPETP TPPTPEVPSE
     PETPTPPTPE VPSEPETPTP PTPEVPAEPG KPVPPAKEEP KKPSKPVEQG KVVTPVIEIN
     EKVKAVAPTK KAQSKKSELP ETGGEESTNK GMLFGGLFSI LGLALLRRNK KNNKA