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Protein

Fibronectin-binding protein A

Gene

fnbA

Organism
Staphylococcus aureus (strain NCTC 8325)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.8 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Virulence

Enzyme and pathway databases

BioCyciSAUR93061:GIWJ-2730-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibronectin-binding protein A
Gene namesi
Name:fnbA
Ordered Locus Names:SAOUHSC_02803
OrganismiStaphylococcus aureus (strain NCTC 8325)
Taxonomic identifieri93061 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000008816 Componenti: Chromosome

Subcellular locationi

  • Secretedcell wall PROSITE-ProRule annotation; Peptidoglycan-anchor PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi222 – 2221G → A: No change in elastin or fibrinogen binding. 1 Publication
Mutagenesisi224 – 2241R → A: Significant reduction in fibrinogen and elastin binding. 1 Publication
Mutagenesisi304 – 3041N → A: Significant reduction in fibrinogen and elastin binding. 1 Publication
Mutagenesisi306 – 3061F → A: Significant reduction in fibrinogen and elastin binding. 1 Publication
Mutagenesisi354 – 3541T → A: Small reduction in fibrinogen binding and greater reduction in elastin binding; when associated with G-356. 1 Publication
Mutagenesisi355 – 3551F → A: No reduction in elastin binding. Significant reduction in fibrinogen binding. 1 Publication
Mutagenesisi356 – 3561N → G: Small reduction in fibrinogen binding and greater reduction in elastin binding; when associated with A-354. 1 Publication
Mutagenesisi357 – 3571K → A: No reduction in elastin binding. Significant reduction in fibrinogen binding. 1 Publication
Mutagenesisi415 – 4151A → G: Significant reduction in fibrinogen and elastin binding; when associated with A-417. 1 Publication
Mutagenesisi417 – 4171T → A: Significant reduction in fibrinogen and elastin binding; when associated with G-415. 1 Publication
Mutagenesisi484 – 51128Missing : Abolishes interaction with elastin and fibrinogen. 1 PublicationAdd
BLAST
Mutagenesisi497 – 4971G → A: Significant reduction in fibrinogen and elastin binding. 1 Publication
Mutagenesisi498 – 4981L → A: Significant reduction in fibrinogen and elastin binding. 1 Publication
Mutagenesisi499 – 51113Missing : Abolishes interaction with elastin and fibrinogen. 1 PublicationAdd
BLAST
Mutagenesisi510 – 5112Missing : No change in elastin binding. Impairs fibrinogen binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3636Add
BLAST
Chaini37 – 985949Fibronectin-binding protein APRO_0000005605Add
BLAST
Propeptidei986 – 101833Removed by sortasePROSITE-ProRule annotationPRO_0000005606Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei985 – 9851Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation

Keywords - PTMi

Peptidoglycan-anchor

Expressioni

Inductioni

Expressed predominantly on cells from early exponential phase of growth. Up-regulated by sigma-B factor during early growth stages but not in later stages, although this positive effect on transcription is most probably indirect. Up-regulated by SarA. Down-regulated by Agr.3 Publications

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
FN1P0275118EBI-8398157,EBI-1220319From a different organism.

Protein-protein interaction databases

DIPiDIP-46263N.
IntActiP14738. 1 interaction.
MINTiMINT-7991198.
STRINGi93061.SAOUHSC_02803.

Structurei

Secondary structure

1
1018
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi198 – 2003Combined sources
Beta strandi201 – 2099Combined sources
Helixi211 – 2133Combined sources
Beta strandi214 – 2174Combined sources
Helixi219 – 2213Combined sources
Beta strandi225 – 2339Combined sources
Beta strandi242 – 2476Combined sources
Beta strandi251 – 2533Combined sources
Beta strandi265 – 2673Combined sources
Beta strandi270 – 2778Combined sources
Beta strandi282 – 2876Combined sources
Helixi289 – 2913Combined sources
Beta strandi298 – 30710Combined sources
Turni309 – 3113Combined sources
Beta strandi314 – 32411Combined sources
Beta strandi327 – 3359Combined sources
Beta strandi344 – 35613Combined sources
Turni357 – 3604Combined sources
Beta strandi361 – 37010Combined sources
Beta strandi375 – 38612Combined sources
Beta strandi396 – 4027Combined sources
Helixi406 – 4083Combined sources
Turni420 – 4223Combined sources
Beta strandi423 – 4253Combined sources
Helixi427 – 4293Combined sources
Helixi431 – 4333Combined sources
Beta strandi434 – 4363Combined sources
Beta strandi442 – 4487Combined sources
Beta strandi453 – 4608Combined sources
Beta strandi469 – 47810Combined sources
Beta strandi490 – 50112Combined sources
Beta strandi514 – 5196Combined sources
Beta strandi521 – 5244Combined sources
Beta strandi531 – 5333Combined sources
Beta strandi542 – 5454Combined sources
Beta strandi640 – 65112Combined sources
Beta strandi658 – 6603Combined sources
Beta strandi666 – 6694Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RKYX-ray1.80B/D508-530[»]
2RKZX-ray2.00M/N/O/P/Q/R529-549[»]
2RL0X-ray2.00C/E/G/H/J/L638-655[»]
3CALX-ray1.70B/D655-672[»]
4B5ZX-ray2.20A189-505[»]
4B60X-ray1.83A/B189-505[»]
DisProtiDP00025.
ProteinModelPortaliP14738.
SMRiP14738. Positions 194-503.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14738.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati545 – 57430B-1Add
BLAST
Repeati575 – 60430B-2Add
BLAST
Repeati745 – 78238D-1Add
BLAST
Repeati783 – 82038D-2Add
BLAST
Repeati821 – 85939D-3Add
BLAST
Repeati860 – 87819D-4; truncatedAdd
BLAST
Repeati879 – 89214WR 1Add
BLAST
Repeati893 – 90614WR 2Add
BLAST
Repeati907 – 92014WR 3Add
BLAST
Repeati921 – 93414WR 4Add
BLAST
Repeati935 – 94814WR 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 511475Ligand-binding A regionAdd
BLAST
Regioni194 – 511318Fibrinogen/elastin/tropoelastin-bindingAdd
BLAST
Regioni512 – 872361Fibronectin-bindingAdd
BLAST
Regioni545 – 604602 X approximate tandem repeatsAdd
BLAST
Regioni745 – 8781344 X approximate tandem repeats, D-3 repeat has more fibronectin-binding activityAdd
BLAST
Regioni879 – 948705 X tandem repeats, Pro-rich (WR)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi982 – 9865LPXTG sorting signalPROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG41078HS. Bacteria.
ENOG410XV8D. LUCA.
HOGENOMiHOG000280272.
KOiK13732.
OrthoDBiEOG69D37T.

Family and domain databases

Gene3Di2.60.40.1280. 1 hit.
2.60.40.1290. 1 hit.
InterProiIPR011266. Adhesin_Fg-bd_dom_2.
IPR008966. Adhesion_dom.
IPR011252. Fibrogen-bd_dom1.
IPR004237. Fibron_repeat-bd.
IPR019948. Gram-positive_anchor.
IPR019931. LPXTG_anchor.
IPR005877. YSIRK_signal_dom.
[Graphical view]
PfamiPF02986. Fn_bind. 3 hits.
PF00746. Gram_pos_anchor. 1 hit.
PF10425. SdrG_C_C. 1 hit.
PF04650. YSIRK_signal. 1 hit.
[Graphical view]
SUPFAMiSSF49401. SSF49401. 2 hits.
TIGRFAMsiTIGR01167. LPXTG_anchor. 1 hit.
TIGR01168. YSIRK_signal. 1 hit.
PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14738-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNNLRYGIR KHKLGAASVF LGTMIVVGMG QDKEAAASEQ KTTTVEENGN
60 70 80 90 100
SATDNKTSET QTTATNVNHI EETQSYNATV TEQPSNATQV TTEEAPKAVQ
110 120 130 140 150
APQTAQPANI ETVKEEVVKE EAKPQVKETT QSQDNSGDQR QVDLTPKKAT
160 170 180 190 200
QNQVAETQVE VAQPRTASES KPRVTRSADV AEAKEASNAK VETGTDVTSK
210 220 230 240 250
VTVEIGSIEG HNNTNKVEPH AGQRAVLKYK LKFENGLHQG DYFDFTLSNN
260 270 280 290 300
VNTHGVSTAR KVPEIKNGSV VMATGEVLEG GKIRYTFTND IEDKVDVTAE
310 320 330 340 350
LEINLFIDPK TVQTNGNQTI TSTLNEEQTS KELDVKYKDG IGNYYANLNG
360 370 380 390 400
SIETFNKANN RFSHVAFIKP NNGKTTSVTV TGTLMKGSNQ NGNQPKVRIF
410 420 430 440 450
EYLGNNEDIA KSVYANTTDT SKFKEVTSNM SGNLNLQNNG SYSLNIENLD
460 470 480 490 500
KTYVVHYDGE YLNGTDEVDF RTQMVGHPEQ LYKYYYDRGY TLTWDNGLVL
510 520 530 540 550
YSNKANGNEK NGPIIQNNKF EYKEDTIKET LTGQYDKNLV TTVEEEYDSS
560 570 580 590 600
TLDIDYHTAI DGGGGYVDGY IETIEETDSS AIDIDYHTAV DSEAGHVGGY
610 620 630 640 650
TESSEESNPI DFEESTHENS KHHADVVEYE EDTNPGGGQV TTESNLVEFD
660 670 680 690 700
EESTKGIVTG AVSDHTTVED TKEYTTESNL IELVDELPEE HGQAQGPVEE
710 720 730 740 750
ITKNNHHISH SGLGTENGHG NYDVIEEIEE NSHVDIKSEL GYEGGQNSGN
760 770 780 790 800
QSFEEDTEED KPKYEQGGNI VDIDFDSVPQ IHGQNKGNQS FEEDTEKDKP
810 820 830 840 850
KYEHGGNIID IDFDSVPHIH GFNKHTEIIE EDTNKDKPSY QFGGHNSVDF
860 870 880 890 900
EEDTLPKVSG QNEGQQTIEE DTTPPIVPPT PPTPEVPSEP ETPTPPTPEV
910 920 930 940 950
PSEPETPTPP TPEVPSEPET PTPPTPEVPA EPGKPVPPAK EEPKKPSKPV
960 970 980 990 1000
EQGKVVTPVI EINEKVKAVA PTKKPQSKKS ELPETGGEES TNKGMLFGGL
1010
FSILGLALLR RNKKNHKA
Length:1,018
Mass (Da):111,780
Last modified:April 1, 1990 - v1
Checksum:i58175E0020E81F1F
GO

Sequence cautioni

The sequence ABD31806.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04151 Genomic DNA. Translation: AAA26632.1.
CP000253 Genomic DNA. Translation: ABD31806.1. Different initiation.
RefSeqiWP_011447070.1. NC_007795.1.
YP_501262.1. NC_007795.1.

Genome annotation databases

EnsemblBacteriaiABD31806; ABD31806; SAOUHSC_02803.
GeneIDi3921457.
KEGGisao:SAOUHSC_02803.
PATRICi19582861. VBIStaAur99865_2536.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04151 Genomic DNA. Translation: AAA26632.1.
CP000253 Genomic DNA. Translation: ABD31806.1. Different initiation.
RefSeqiWP_011447070.1. NC_007795.1.
YP_501262.1. NC_007795.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RKYX-ray1.80B/D508-530[»]
2RKZX-ray2.00M/N/O/P/Q/R529-549[»]
2RL0X-ray2.00C/E/G/H/J/L638-655[»]
3CALX-ray1.70B/D655-672[»]
4B5ZX-ray2.20A189-505[»]
4B60X-ray1.83A/B189-505[»]
DisProtiDP00025.
ProteinModelPortaliP14738.
SMRiP14738. Positions 194-503.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46263N.
IntActiP14738. 1 interaction.
MINTiMINT-7991198.
STRINGi93061.SAOUHSC_02803.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD31806; ABD31806; SAOUHSC_02803.
GeneIDi3921457.
KEGGisao:SAOUHSC_02803.
PATRICi19582861. VBIStaAur99865_2536.

Phylogenomic databases

eggNOGiENOG41078HS. Bacteria.
ENOG410XV8D. LUCA.
HOGENOMiHOG000280272.
KOiK13732.
OrthoDBiEOG69D37T.

Enzyme and pathway databases

BioCyciSAUR93061:GIWJ-2730-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP14738.
PROiP14738.

Family and domain databases

Gene3Di2.60.40.1280. 1 hit.
2.60.40.1290. 1 hit.
InterProiIPR011266. Adhesin_Fg-bd_dom_2.
IPR008966. Adhesion_dom.
IPR011252. Fibrogen-bd_dom1.
IPR004237. Fibron_repeat-bd.
IPR019948. Gram-positive_anchor.
IPR019931. LPXTG_anchor.
IPR005877. YSIRK_signal_dom.
[Graphical view]
PfamiPF02986. Fn_bind. 3 hits.
PF00746. Gram_pos_anchor. 1 hit.
PF10425. SdrG_C_C. 1 hit.
PF04650. YSIRK_signal. 1 hit.
[Graphical view]
SUPFAMiSSF49401. SSF49401. 2 hits.
TIGRFAMsiTIGR01167. LPXTG_anchor. 1 hit.
TIGR01168. YSIRK_signal. 1 hit.
PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the gene for a fibronectin-binding protein from Staphylococcus aureus: use of this peptide sequence in the synthesis of biologically active peptides."
    Signaes C., Raucci G., Joensson K., Lindgren P.-E., Anantharamaiah G.M., Hoeoek M., Lindberg M.
    Proc. Natl. Acad. Sci. U.S.A. 86:699-703(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN FIBRONECTIN BINDING.
  2. "The Staphylococcus aureus NCTC 8325 genome."
    Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
    (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.); Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C. (2006)
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCTC 8325.
  3. "Transcription of Staphylococcus aureus fibronectin binding protein genes is negatively regulated by agr and an agr-independent mechanism."
    Saravia-Otten P., Mueller H.-P., Arvidson S.
    J. Bacteriol. 179:5259-5263(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY AGR.
  4. "The fibronectin-binding MSCRAMM fnbpA of Staphylococcus aureus is a bifunctional protein that also binds to fibrinogen."
    Wann E.R., Gurusiddappa S., Hoeoek M.
    J. Biol. Chem. 275:13863-13871(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FIBRINOGEN BINDING, REGULATION.
  5. "Fibronectin-binding protein A of Staphylococcus aureus has multiple, substituting, binding regions that mediate adherence to fibronectin and invasion of endothelial cells."
    Massey R.C., Kantzanou M.N., Fowler T., Day N.P.J., Schofield K., Wann E.R., Berendt A.R., Hoeoek M., Peacock S.J.
    Cell. Microbiol. 3:839-851(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FIBRONECTIN BINDING.
  6. "Reassessing the role of Staphylococcus aureus clumping factor and fibronectin-binding protein by expression in Lactococcus lactis."
    Que Y.-A., Francois P., Haefliger J.-A., Entenza J.-M., Vaudaux P., Moreillon P.
    Infect. Immun. 69:6296-6302(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FIBRONECTIN AND FIBRINOGEN BINDING, ROLE IN ENDOVASCULAR INFECTION.
  7. "Transcription profiling-based identification of Staphylococcus aureus genes regulated by the agr and/or sarA loci."
    Dunman P.M., Murphy E., Haney S., Palacios D., Tucker-Kellogg G., Wu S., Brown E.L., Zagursky R.J., Shlaes D., Projan S.J.
    J. Bacteriol. 183:7341-7353(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY SARA.
  8. "The N-terminal A domain of fibronectin-binding proteins A and B promotes adhesion of Staphylococcus aureus to elastin."
    Roche F.M., Downer R., Keane F., Speziale P., Park P.W., Foster T.J.
    J. Biol. Chem. 279:38433-38440(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ELASTIN BINDING.
  9. "Staphylococcus aureus fibronectin-binding protein (fnbp)-mediated adherence to platelets, and aggregation of platelets induced by fnbpA but not by fnbpB."
    Heilmann C., Niemann S., Sinha B., Herrmann M., Kehrel B.E., Peters G.
    J. Infect. Dis. 190:321-329(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PLATELET AGGREGATION.
  10. "Role of sigmaB in the expression of Staphylococcus aureus cell wall adhesins clfA and fnbA and contribution to infectivity in a rat model of experimental endocarditis."
    Entenza J.-M., Moreillon P., Senn M.M., Kormanec J., Dunman P.M., Berger-Baechi B., Projan S., Bischoff M.
    Infect. Immun. 73:990-998(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY SIGMA-B.
  11. "Fibrinogen and fibronectin binding cooperate for valve infection and invasion in Staphylococcus aureus experimental endocarditis."
    Que Y.-A., Haefliger J.-A., Piroth L., Francois P., Widmer E., Entenza J.M., Sinha B., Herrmann M., Francioli P., Vaudaux P., Moreillon P.
    J. Exp. Med. 201:1627-1635(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN EXPERIMENTAL ENDOCARDITIS.
  12. "Staphylococcus aureus fibronectin binding protein-A induces motile attachment sites and complex actin remodeling in living endothelial cells."
    Schroeder A., Schroeder B., Roppenser B., Linder S., Sinha B., Faessler R., Aepfelbacher M.
    Mol. Biol. Cell 17:5198-5210(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: MECHANISM OF INVASION.
  13. "The N-terminal A domain of Staphylococcus aureus fibronectin-binding protein A binds to tropoelastin."
    Keane F.M., Clarke A.W., Foster T.J., Weiss A.S.
    Biochemistry 46:7226-7232(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TROPOELASTIN BINDING.
  14. "Fibrinogen and elastin bind to the same region within the A domain of fibronectin binding protein A, an MSCRAMM of Staphylococcus aureus."
    Keane F.M., Loughman A., Valtulina V., Brennan M., Speziale P., Foster T.J.
    Mol. Microbiol. 63:711-723(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF FIBRINOGEN AND ELASTIN-BINDING DOMAINS, MUTAGENESIS OF GLY-222; ARG-224; ASN-304; PHE-306; THR-354; PHE-355; ASN-356; LYS-357; ALA-415; THR-417; 484-TYR--ASN-511; GLY-497; LEU-498; 499-VAL--ASN-511 AND 510-LYS-ASN-511.

Entry informationi

Entry nameiFNBA_STAA8
AccessioniPrimary (citable) accession number: P14738
Secondary accession number(s): Q2G1T8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 11, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Fg-binding activity is not regulated by the divalent cations Ca2+, Mn2+ or Mg2+.
Deletion of the Fg-binding domain of FnbA abrogates the ability to promote cardiac valve infection and persistence in vivo.
The mutagenesis studies described in PubMed:17302800 were done with region A alone and not with the entire protein.
Mutants lacking C-terminal residues from the ligand binding A region bind to Fg with a reduced affinity or are unable to bind to both Fg and elastin, depending on the extension of the deletion present in this region. Individual constructs of regions spanning amino acids from 194-336 or 337-511 were unable to bind fibrinogen or elastin.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.