General information | DisProt: | DP00025 | Name: | Fibronectin-binding protein A | Synonym(s): | FNBA_STAA8
FNBP
Fibronectin-binding protein
| First appeared in release: | Release 1.0 (08/01/2003) | UniProt: | P14738 | UniGene: | | SwissProt: | FNBA_STAA8 | TrEMBL: | | NCBI (GI): | 120457 | Source organism: | Staphylococcus aureus (strain NCTC 8325) | Sequence length: | 1018 | Percent disordered: | 13% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MKNNLRYGIR KHKLGAASVF LGTMIVVGMG QDKEAAASEQ KTTTVEENGN SATDNKTSET - 60 QTTATNVNHI EETQSYNATV TEQPSNATQV TTEEAPKAVQ APQTAQPANI ETVKEEVVKE - 120 EAKPQVKETT QSQDNSGDQR QVDLTPKKAT QNQVAETQVE VAQPRTASES KPRVTRSADV - 180 AEAKEASNAK VETGTDVTSK VTVEIGSIEG HNNTNKVEPH AGQRAVLKYK LKFENGLHQG - 240 DYFDFTLSNN VNTHGVSTAR KVPEIKNGSV VMATGEVLEG GKIRYTFTND IEDKVDVTAE - 300 LEINLFIDPK TVQTNGNQTI TSTLNEEQTS KELDVKYKDG IGNYYANLNG SIETFNKANN - 360 RFSHVAFIKP NNGKTTSVTV TGTLMKGSNQ NGNQPKVRIF EYLGNNEDIA KSVYANTTDT - 420 SKFKEVTSNM SGNLNLQNNG SYSLNIENLD KTYVVHYDGE YLNGTDEVDF RTQMVGHPEQ - 480 LYKYYYDRGY TLTWDNGLVL YSNKANGNEK NGPIIQNNKF EYKEDTIKET LTGQYDKNLV - 540 TTVEEEYDSS TLDIDYHTAI DGGGGYVDGY IETIEETDSS AIDIDYHTAV DSEAGHVGGY - 600 TESSEESNPI DFEESTHENS KHHADVVEYE EDTNPGGGQV TTESNLVEFD EESTKGIVTG - 660 AVSDHTTVED TKEYTTESNL IELVDELPEE HGQAQGPVEE ITKNNHHISH SGLGTENGHG - 720 NYDVIEEIEE NSHVDIKSEL GYEGGQNSGN QSFEEDTEED KPKYEQGGNI VDIDFDSVPQ - 780 IHGQNKGNQS FEEDTEKDKP KYEHGGNIID IDFDSVPHIH GFNKHTEIIE EDTNKDKPSY - 840 QFGGHNSVDF EEDTLPKVSG QNEGQQTIEE DTTPPIVPPT PPTPEVPSEP ETPTPPTPEV - 900 PSEPETPTPP TPEVPSEPET PTPPTPEVPA EPGKPVPPAK EEPKKPSKPV EQGKVVTPVI - 960 EINEKVKAVA PTKKPQSKKS ELPETGGEES TNKGMLFGGL FSILGLALLR RNKKNHKA
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Functional narrative |
Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding site localized within the 17 C-terminal residues of the gamma-chain of human Fg. Both plasma proteins (Fn and Fg) function as a bridge between bacterium and host cell. Promotes attachment to immobilized elastin peptides in a dose-dependent and saturable manner. Promotes attachment to both full-length and segments of immobilized human tropoelastin at multiple sites in a dose and pH-dependent manner. Promotes adherence to and aggregation of activated platelets independently of other S.aureus surface molecules. Is a critical mediator implicated in the induction of experimental endocarditis in rats with catheter-induced aortic vegetations, promoting both colonization and persistence of the bacterium into the host. Ref.1 Ref.4 Ref.5 Ref.6 Ref.8 Ref.9 Ref.11 Ref.13
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Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | D1-D4 | Location: | 745 - 874 | Length: | 130 | Region sequence: |
GQNSGNQSFEEDTEEDKPKYEQGGNIVDIDFDSVPQIHGQNKGDQSFEEDTEKDKPKYEH GGNIIDIDFDSVPHIHGFNKHTEIIEEDTNKDKPNYQFGGHNSVDFEEDTLPQVSGHNEG QQTIEEDTTT | Modification type: | Fragment
Natural variant
| PDB: | | Structural/functional type: | | Functional classes: | | Functional subclasses: | Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (278 K; pH: 6; protein (sample) 1 mM; spectrometer 750 MHz)
| References:
- Penkett CJ, Redfield C, Dodd I, Hubbard J, McBay DL, Mossakowska DE, Smith RA, Dobson CM, Smith LJ. "NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein." J Mol Biol. 1997; 274(2): 152-9. PubMed: 9398523
| Comments:
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References |
- Penkett CJ, Redfield C, Dodd I, Hubbard J, McBay DL, Mossakowska DE, Smith RA, Dobson CM, Smith LJ. "NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein." J Mol Biol. 1997; 274(2): 152-9. PubMed: 9398523
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Comments |
AV (6-17-2010) PubMed: 9398523
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