FNBB_STAA3
ID FNBB_STAA3 Reviewed; 940 AA.
AC A0A0H2XKG3;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Fibronectin-binding protein B;
DE Flags: Precursor;
GN Name=fnbB; OrderedLocusNames=SAUSA300_2440;
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
RN [2]
RP FUNCTION IN ELASTIN BINDING.
RX PubMed=15234962; DOI=10.1074/jbc.m402122200;
RA Roche F.M., Downer R., Keane F., Speziale P., Park P.W., Foster T.J.;
RT "The N-terminal A domain of fibronectin-binding proteins A and B promotes
RT adhesion of Staphylococcus aureus to elastin.";
RL J. Biol. Chem. 279:38433-38440(2004).
RN [3]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF ASN-276 AND PHE-278.
RX PubMed=21569203; DOI=10.1111/j.1742-4658.2011.08159.x;
RA Burke F.M., Di Poto A., Speziale P., Foster T.J.;
RT "The A domain of fibronectin-binding protein B of Staphylococcus aureus
RT contains a novel fibronectin binding site.";
RL FEBS J. 278:2359-2371(2011).
RN [4]
RP FUNCTION.
RC STRAIN=USA300 / LAC;
RX PubMed=24628034; DOI=10.1111/1574-6968.12424;
RA McCourt J., O'Halloran D.P., McCarthy H., O'Gara J.P., Geoghegan J.A.;
RT "Fibronectin-binding proteins are required for biofilm formation by
RT community-associated methicillin-resistant Staphylococcus aureus strain
RT LAC.";
RL FEMS Microbiol. Lett. 353:157-164(2014).
RN [5]
RP FUNCTION, AND INTERACTION WITH HOST PLG AND FIBRONECTIN.
RC STRAIN=USA300 / LAC;
RX PubMed=27387503; DOI=10.1074/jbc.m116.731125;
RA Pietrocola G., Nobile G., Gianotti V., Zapotoczna M., Foster T.J.,
RA Geoghegan J.A., Speziale P.;
RT "Molecular Interactions of human plasminogen with fibronectin-binding
RT Protein B (FnBPB), a fibrinogen/fibronectin-binding protein from
RT Staphylococcus aureus.";
RL J. Biol. Chem. 291:18148-18162(2016).
RN [6]
RP FUNCTION, INTERACTION WITH HISTONES, AND MUTAGENESIS OF ASN-276 AND
RP PHE-278.
RC STRAIN=USA300 / LAC;
RX PubMed=30622139; DOI=10.1074/jbc.ra118.005707;
RA Pietrocola G., Nobile G., Alfeo M.J., Foster T.J., Geoghegan J.A.,
RA De Filippis V., Speziale P.;
RT "Fibronectin-binding protein B (FnBPB) from Staphylococcus aureus protects
RT against the antimicrobial activity of histones.";
RL J. Biol. Chem. 294:3588-3602(2019).
CC -!- FUNCTION: Multifunctional protein which promotes bacterial attachment
CC to fibrinogen, elastin and fibronectin (PubMed:15234962,
CC PubMed:21569203, PubMed:27387503). Promotes also the accumulation phase
CC and the primary attachment phase of biofilm formation
CC (PubMed:24628034). In addition, protects against the antimicrobial
CC activity of histones. Mechanistically, captures histones and prevents
CC them from reaching the bacterial membrane and simultaneously binds
CC plasminogen, thereby promoting its conversion to plasmin to destroy the
CC bound histones (PubMed:30622139, PubMed:27387503).
CC {ECO:0000269|PubMed:15234962, ECO:0000269|PubMed:21569203,
CC ECO:0000269|PubMed:24628034, ECO:0000269|PubMed:27387503,
CC ECO:0000269|PubMed:30622139}.
CC -!- SUBUNIT: Interacts with host PLG; this interaction provides active
CC plasmin on the surface of bacteria cells (PubMed:27387503). Interacts
CC with host histones (PubMed:30622139). {ECO:0000269|PubMed:27387503,
CC ECO:0000269|PubMed:30622139}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}.
CC -!- DOMAIN: The fibrinogen- and elastin-binding sites have been localized
CC to the N-terminal region. {ECO:0000269|PubMed:15234962}.
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DR EMBL; CP000255; ABD22827.1; -; Genomic_DNA.
DR RefSeq; WP_000841422.1; NZ_CP027476.1.
DR AlphaFoldDB; A0A0H2XKG3; -.
DR SMR; A0A0H2XKG3; -.
DR EnsemblBacteria; ABD22827; ABD22827; SAUSA300_2440.
DR KEGG; saa:SAUSA300_2440; -.
DR HOGENOM; CLU_009849_1_0_9; -.
DR OMA; WDNGVAF; -.
DR Proteomes; UP000001939; 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 PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell wall; Peptidoglycan-anchor; Repeat; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..940
FT /note="Fibronectin-binding protein B"
FT /evidence="ECO:0000255"
FT /id="PRO_5002601974"
FT PROPEP 908..940
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000447313"
FT REPEAT 681..718
FT /note="D-1"
FT /evidence="ECO:0000250|UniProtKB:Q2FE03"
FT REPEAT 719..756
FT /note="D-2"
FT /evidence="ECO:0000250|UniProtKB:Q2FE03"
FT REPEAT 757..795
FT /note="D-3"
FT /evidence="ECO:0000250|UniProtKB:Q2FE03"
FT REPEAT 796..814
FT /note="D-4; truncated"
FT /evidence="ECO:0000250|UniProtKB:Q2FE03"
FT REPEAT 815..828
FT /note="WR 1"
FT /evidence="ECO:0000250|UniProtKB:Q2FE03"
FT REPEAT 829..842
FT /note="WR 2"
FT /evidence="ECO:0000250|UniProtKB:Q2FE03"
FT REPEAT 857..870
FT /note="WR 3"
FT /evidence="ECO:0000250|UniProtKB:Q2FE03"
FT REGION 36..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..480
FT /note="Fibrinogen/elastin/tropoelastin-binding"
FT /evidence="ECO:0000269|PubMed:21569203"
FT REGION 676..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 904..908
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 36..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..858
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 907
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT MUTAGEN 276
FT /note="N->A: Loss of fibrinogen and histone binding; when
FT associated with A-278."
FT /evidence="ECO:0000269|PubMed:21569203,
FT ECO:0000269|PubMed:30622139"
FT MUTAGEN 278
FT /note="F->A: Loss of fibrinogen and histone binding; when
FT associated with A-278."
FT /evidence="ECO:0000269|PubMed:21569203"
SQ SEQUENCE 940 AA; 103555 MW; E35FBBCA907AE345 CRC64;
MKSNLRYGIR KHKLGAASVF LGTMIVVGMG QEKEAAASEQ NNTTVEESGS SATESKASET
QTTTNNVNTI DETQSYSATS TEQPSQSTQV TTEEAPKTVQ APKVETSRVD LPSEKVADKE
TTGTQVDIAQ PSNVSEIKPR MKRSTDVTAV AEKEVVEETK ATGTDVTNKV EVEEGSEIVG
HKQDTNVVNP HNAERVTLKY KWKFGEGIKA GDYFDFTLSD NVETHGISTL RKVPEIKSTD
GQVMATGEII GERKVRYTFK EYVQEKKDLT AELSLNLFID PTTVTQKGNQ NVEVKLGETT
VSKIFNIQYL GGVRDNWGVT ANGRIDTLNK VDGKFSHFAY MKPNNQSLSS VTVTGQVTKG
NKPGVNNPTV KVYKHIGSDD LAESVYAKLD DVSKFEDVTD NMSLDFDTNG GYSLNFNNLD
QSKNYVIKYE GYYDSNASNL EFQTHLFGYY NYYYTSNLTW KNGVAFYSNN AQGDGKDKLK
EPIIEHSTPI ELEFKSEPPV EKHELTGTIE ESNDSKPIDF EYHTAVEGAE GHAEGTIETE
EDSIHVDFEE STHENSKHHA DVVEYEEDTN PGGGQVTTES NLVEFDEDST KGIVTGAVSD
HTTIEDTKEY TTESNLIELV DELPEEHGQA QGPIEEITEN NHHISHSGLG TENGHGNYGV
IEEIEENSHV DIKSELGYEG GQNSGNQSFE EDTEEDKPKY EQGGNIVDID FDSVPQIHGQ
NNGNQSFEED TEKDKPKYEQ GGNIIDIDFD SVPHIHGFNK HTEIIEEDTN KDKPNYQFGG
HNSVDFEEDT LPQVSGHNEG QQTIEEDTTP PIVPPTPPTP EVPSEPETPT PPTPEVPSEP
ETPTPPTPEV PTEPGKPIPP AKEEPKKPSK PVEQGKVVTP VIEINEKVKA VVPTKKAQSK
KSELPETGGE ESTNNGMLFG GLFSILGLAL LRRNKKNHKA
