FNBA_STAA1
ID FNBA_STAA1 Reviewed; 1038 AA.
AC A7X6I5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Fibronectin-binding protein A;
DE Flags: Precursor;
GN Name=fnbA; OrderedLocusNames=SAHV_2487;
OS Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=418127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu3 / ATCC 700698;
RX PubMed=17954695; DOI=10.1128/aac.00534-07;
RA Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT "Mutated response regulator graR is responsible for phenotypic conversion
RT of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT resistance to vancomycin-intermediate resistance.";
RL Antimicrob. Agents Chemother. 52:45-53(2008).
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; AP009324; BAF79370.1; -; Genomic_DNA.
DR RefSeq; WP_000794614.1; NC_009782.1.
DR AlphaFoldDB; A7X6I5; -.
DR SMR; A7X6I5; -.
DR KEGG; saw:SAHV_2487; -.
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..1005
FT /note="Fibronectin-binding protein A"
FT /id="PRO_0000313872"
FT PROPEP 1006..1038
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000313873"
FT REPEAT 541..570
FT /note="B-1"
FT REPEAT 571..600
FT /note="B-2"
FT REPEAT 741..778
FT /note="D-1"
FT REPEAT 779..816
FT /note="D-2"
FT REPEAT 817..855
FT /note="D-3"
FT REPEAT 856..898
FT /note="D-4"
FT REPEAT 899..912
FT /note="WR 1"
FT REPEAT 913..926
FT /note="WR 2"
FT REPEAT 927..940
FT /note="WR 3"
FT REPEAT 941..954
FT /note="WR 4"
FT REPEAT 955..968
FT /note="WR 5"
FT REGION 37..507
FT /note="Ligand-binding A region"
FT REGION 37..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..507
FT /note="Fibrinogen/elastin/tropoelastin-binding"
FT /evidence="ECO:0000250"
FT REGION 508..868
FT /note="Fibronectin-binding"
FT /evidence="ECO:0000250"
FT REGION 541..600
FT /note="2 X approximate tandem repeats"
FT REGION 736..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..898
FT /note="4 X approximate tandem repeats"
FT REGION 825..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..968
FT /note="5 X tandem repeats, Pro-rich (WR)"
FT REGION 989..1015
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 1002..1006
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..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..956
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1005
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1038 AA; 113618 MW; 666BF6BF2BFBEB12 CRC64;
MKNNLRYGIR KHKLGAASVF LGTMIVVGMG QDKEAAASEQ KTTTVEENGN SATDNKTSET
QTTATNVNHI EETQSYNATV TEQPSNATQV TTEEAPKAVQ APQTAQPANV ETVKEEEKPQ
VKETTQPQDN SGNQRQVDLT PKKVTQNQGT ETQVEVAQPR TASESKPRVT RSADVAEAKE
ASDVSEVKGT DVTSKVTVES GSIEAPQGNK VEPHAGQRVV LKYKLKFADG LKRGDYFDFT
LSNNVNTYGV STARKVPEIK NGSVVMATGE ILGNGNIRYT FTNEIEHKVE VTANLEINLF
IDPKTVQSNG EQKITSKLNG EETEKTIPVV YNPGVSNSYT NVNGSIETFN KESNKFTHIA
YIKPMNGNQS NTVSVTGTLT EGSNLAGGQP TVKVYEYLGK KDELPQSVYA NTSDTNKFKD
VTKEMNGKLS VQDNGSYSLN LDKLDKTYVI HYTGEYLQGS DQVNFRTELY GYPERAYKSY
YVYGGYRLTW DNGLVLYSNK ADGNGKNGQI IQDNDFEYKE DTAKGTMSGQ YDAKQIIETE
ENQDNTPLDI DYHTAIDGEG GYVDGYIETI EETDSSAIDI DYHTAVDSEV GHVGGYTESS
EESNPIDFEE STHENSKHHA DVVEYEEDTN PGGGQVTTES NLVEFDEEST KGIVTGAVSD
HTTIEDTKEY TTESNLIELV DELPEEHGQA QGPIEEITEN NHHISHSGLG TENGHGNYGV
IEEIEENSHV DIKSELGYEG GQNSGNQSFE EDTEEDKPKY EQGGNIVDID FDSVPQIHGQ
NKGDQSFEED TEKDKPKYEH GGNIIDIDFD SVPQIHGFNK HNEIIEEDTN KDKPNYQFGG
HNSVDFEEDT LPKVSGQNEG QQTIEEDTTP PTPPTPEVPS EPETPMPPTP EVPSEPETPT
PPTPEVPSEP ETPTPPTPEV PSEPETPTPP TPEVPSEPET PTPPTPEVPA EPGKPVPPAK
EEPKKPSKPV EQGKVVTPVI EINEKVKAVA PTKKAQSKKS ELPETGGEES TNKGMLFGGL
FSILGLALLR RNKKNNKA
