FNBA_STAAC
ID FNBA_STAAC Reviewed; 1018 AA.
AC Q5HD51;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Fibronectin-binding protein A;
DE Flags: Precursor;
GN Name=fnbA; OrderedLocusNames=SACOL2511;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW37290.1; -; Genomic_DNA.
DR RefSeq; WP_000794589.1; NC_002951.2.
DR AlphaFoldDB; Q5HD51; -.
DR SMR; Q5HD51; -.
DR EnsemblBacteria; AAW37290; AAW37290; SACOL2511.
DR KEGG; sac:SACOL2511; -.
DR HOGENOM; CLU_009849_1_0_9; -.
DR OMA; DANKPGN; -.
DR Proteomes; UP000000530; 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; 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..985
FT /note="Fibronectin-binding protein A"
FT /id="PRO_0000313878"
FT PROPEP 986..1018
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000313879"
FT REPEAT 545..574
FT /note="B-1"
FT REPEAT 575..604
FT /note="B-2"
FT REPEAT 745..782
FT /note="D-1"
FT REPEAT 783..820
FT /note="D-2"
FT REPEAT 821..859
FT /note="D-3"
FT REPEAT 860..878
FT /note="D-4; truncated"
FT REPEAT 879..892
FT /note="WR 1"
FT REPEAT 893..906
FT /note="WR 2"
FT REPEAT 907..920
FT /note="WR 3"
FT REPEAT 921..934
FT /note="WR 4"
FT REPEAT 935..948
FT /note="WR 5"
FT REGION 37..511
FT /note="Ligand-binding A region"
FT REGION 38..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..195
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..872
FT /note="Fibronectin-binding"
FT /evidence="ECO:0000250"
FT REGION 545..604
FT /note="2 X approximate tandem repeats"
FT REGION 595..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..878
FT /note="4 X approximate tandem repeats"
FT REGION 827..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..948
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 982..986
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 78..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 789..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..936
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 985
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1018 AA; 111709 MW; 9B215B90035EEA6E CRC64;
MKNNLRYGIR KHKLGAASVF LGTMIVVGMG QDKEAAASEQ KTTTVEENGN SATDNKTSET
QTTATNVNHI EETQSYNATV TEQPSNATQV TTEEAPKAVQ APQTAQPANI ETVKEEVVKE
EAKPQVKETT QSQDNSGDQR QVDLTPKKAT QNQVAETQVE VAQPRTASES KPRVTRSADV
AEAKEASNAK VETGTDVTSK VTVEIGSIEG HNNTNKVEPH AGQRAVLKYK LKFENGLHQG
DYFDFTLSNN VNTHGVSTAR KVPEIKNGSV VMATGEVLEG GKIRYTFTND IEDKVDVTAE
LEINLFIDPK TVQTNGNQTI TSTLNEEQTS KELDVKYKDG IGNYYANLNG SIETFNKANN
RFSHVAFIKP NNGKTTSVTV TGTLMKGSNQ NGNQPKVRIF EYLGNNEDIA KSVYANTTDT
SKFKEVTSNM SGNLNLQNNG SYSLNIENLD KTYVVHYDGE YLNGTDEVDF RTQMVGHPEQ
LYKYYYDRGY TLTWDNGLVL YSNKANGNGK NGPIIQNNKF EYKEDTIKET LTGQYDKNLV
TTVEEEYDSS TLDIDYHTAI DGGGGYVDGY IETIEETDSS AIDIDYHTAV DSEAGHVGGY
TESSEESNPI DFEESTHENS KHHADVVEYE EDTNPGGGQV TTESNLVEFD EESTKGIVTG
AVSDHTTVED TKEYTTESNL IELVDELPEE HGQAQGPVEE ITENNHHISH SGLGTENGHG
NYDVIEEIEE NSHVDIKSEL GYEGGQNSGN QSFEEDTEED KPKYEQGGNI VDIDFDSVPQ
IHGQNKGNQS FEEDTEKDKP KYEHGGNIID IDFDSVPHIH GFNKHTEIIE EDTNKDKPSY
QFGGHNSVDF EEDTLPKVSG QNEGQQTIEE DTTPPIVPPT PPTPEVPSEP ETPTPPTPEV
PSEPETPTPP TPEVPSEPET PTPPTPEVPA EPGKPVPPAK EEPKKPSKPV EQGKVVTPVI
EINEKVKAVA PTKKPQSKKS ELPETGGEES TNKGMLFGGL FSILGLALLR RNKKNHKA
