Annotations for this protein have been verified by the authors of the corresponding papers



DP00025: Fibronectin-binding protein AFASTA viewXML view

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



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

Region 1: 745-874

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.


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:
  1. Nuclear magnetic resonance (NMR) (278 K; pH: 6; protein (sample) 1 mM; spectrometer 750 MHz)

References:
  1. 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:
 



References

  1. 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


AV (6-17-2010) PubMed: 9398523


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