FNBA_STAAB
ID FNBA_STAAB Reviewed; 990 AA.
AC Q2YW62;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Fibronectin-binding protein A;
DE Flags: Precursor;
GN Name=fnbA; OrderedLocusNames=SAB2375c;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI82063.1; -; Genomic_DNA.
DR RefSeq; WP_000794654.1; NC_007622.1.
DR AlphaFoldDB; Q2YW62; -.
DR SMR; Q2YW62; -.
DR KEGG; sab:SAB2375c; -.
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 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..35
FT /evidence="ECO:0000255"
FT CHAIN 36..957
FT /note="Fibronectin-binding protein A"
FT /id="PRO_0000313876"
FT PROPEP 958..990
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000313877"
FT REPEAT 545..574
FT /note="B-1"
FT REPEAT 575..604
FT /note="B-2"
FT REPEAT 707..744
FT /note="D-1"
FT REPEAT 745..782
FT /note="D-2"
FT REPEAT 783..821
FT /note="D-3"
FT REPEAT 822..850
FT /note="D-4; truncated"
FT REPEAT 851..864
FT /note="WR 1"
FT REPEAT 865..878
FT /note="WR 2"
FT REPEAT 879..892
FT /note="WR 3"
FT REPEAT 893..906
FT /note="WR 4"
FT REPEAT 907..920
FT /note="WR 5"
FT REGION 33..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..511
FT /note="Ligand-binding A region"
FT REGION 96..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..511
FT /note="Fibrinogen/elastin/tropoelastin-binding"
FT /evidence="ECO:0000250"
FT REGION 512..834
FT /note="Fibronectin-binding"
FT /evidence="ECO:0000250"
FT REGION 545..604
FT /note="2 X approximate tandem repeats"
FT REGION 702..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..850
FT /note="4 X approximate tandem repeats"
FT REGION 851..920
FT /note="5 X tandem repeats, Pro-rich (WR)"
FT MOTIF 7..18
FT /note="YSIRK-G/S signaling motif"
FT /evidence="ECO:0000250|UniProtKB:P14738"
FT MOTIF 954..958
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 35..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..173
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 753..767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..908
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 957
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 990 AA; 108925 MW; 03796A945C115538 CRC64;
MKNNLRYGIR KHKLGAASVF LGTMIVVGMG QDKEAATSEQ KTTTVEENGN SATDNKVSET
QTTTTNVNTI DETQSYSATA TEQPSNATQV ITEEAPKAVQ APQTAQPANL ETVKEEVVKE
EEKPQVKETT QSQDNSGDQR QVDLTPKKAT QNQAAETQVE VAQPRTVSES KPRVTRSADV
AEAKEASDVT EVKGTDVTSK VTVTESSIEG HNNTNKVEPH AGQRAVLKYK LKFEDGLHQG
DYFDFTLSNN VNTHGVSTAR KVPEIKNGSV VMATGKILED GKIRYTFTND VEHKVEVTAN
LEINLFIDPK TFQSNGEEKV TSSLNGSKTE KNLQIEYKNG VGTYYANVNG SIETFDKEKN
KFTHVAYVKP LNQFKLGTVT VSGTVTQGSN PNGEKPTVKI YEVTNDGKDL PQSVYLDASD
KNKYKDVTNE MQSKLTVQEN GNYTLNLDTL DKSYVIHYSG EYLNGTNEVN FRTQMFGYPE
QRYGYYYNSY QLTWDNGLVL YSNKADGNGK NGQIIQNNDF EYKEDTLTET VTGQYDEKQI
IETEENQDNT PLDIDYHTAI DGEGGYADGY IETIEETDSS AIDIDYHTAV DSEAGHVGGY
TESSEESNPI DFEESTKGIV TGAVSDHTTV EDTKEYTTES NLIELVDELP EEHGQAQGPI
EEITENNHHI SHSGLGTENG HGNYGVIEEI EENSHVDIKS ELGYEGGQNS GNQSFEEDTE
EDKPKYEQGG NIVDIDFDSV PQIQGQNNGN QSFEEDTEKD KPKYEQGGNI IDIDFDSVPQ
IHGFNKHNEI IEEDTNKDKP NYQFGGHNSV DFEEDTLPKV SGQNEGQQTI EEDTTPPTPP
TPEVPSEPET PTPPTPEVPS EPETPTPPTP EVPSEPETPT PPTPEVPSEP ETPTPPTPEV
PAEPGKPVPP AEEEPKKPSK PVEQGKVVTP VIEINEKVKA VAPTKQKQSK KSELPETGGE
ESTNKGMLFG GLFSILGLAL LRRNKKNHKA
