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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

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)DescriptionActionsGraphical viewLength
Mutagenesisi222G → A: No change in elastin or fibrinogen binding. 1 Publication1
Mutagenesisi224R → A: Significant reduction in fibrinogen and elastin binding. 1 Publication1
Mutagenesisi304N → A: Significant reduction in fibrinogen and elastin binding. 1 Publication1
Mutagenesisi306F → A: Significant reduction in fibrinogen and elastin binding. 1 Publication1
Mutagenesisi354T → A: Small reduction in fibrinogen binding and greater reduction in elastin binding; when associated with G-356. 1 Publication1
Mutagenesisi355F → A: No reduction in elastin binding. Significant reduction in fibrinogen binding. 1 Publication1
Mutagenesisi356N → G: Small reduction in fibrinogen binding and greater reduction in elastin binding; when associated with A-354. 1 Publication1
Mutagenesisi357K → A: No reduction in elastin binding. Significant reduction in fibrinogen binding. 1 Publication1
Mutagenesisi415A → G: Significant reduction in fibrinogen and elastin binding; when associated with A-417. 1 Publication1
Mutagenesisi417T → A: Significant reduction in fibrinogen and elastin binding; when associated with G-415. 1 Publication1
Mutagenesisi484 – 511Missing : Abolishes interaction with elastin and fibrinogen. 1 PublicationAdd BLAST28
Mutagenesisi497G → A: Significant reduction in fibrinogen and elastin binding. 1 Publication1
Mutagenesisi498L → A: Significant reduction in fibrinogen and elastin binding. 1 Publication1
Mutagenesisi499 – 511Missing : Abolishes interaction with elastin and fibrinogen. 1 PublicationAdd BLAST13
Mutagenesisi510 – 511Missing : No change in elastin binding. Impairs fibrinogen binding. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 36Add BLAST36
ChainiPRO_000000560537 – 985Fibronectin-binding protein AAdd BLAST949
PropeptideiPRO_0000005606986 – 1018Removed by sortasePROSITE-ProRule annotationAdd BLAST33

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei985Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation1

Keywords - PTMi

Peptidoglycan-anchor

Proteomic databases

PRIDEiP14738.

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 interactor.
MINTiMINT-7991198.
STRINGi93061.SAOUHSC_02803.

Structurei

Secondary structure

11018
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi198 – 200Combined sources3
Beta strandi201 – 209Combined sources9
Helixi211 – 213Combined sources3
Beta strandi214 – 217Combined sources4
Helixi219 – 221Combined sources3
Beta strandi225 – 233Combined sources9
Beta strandi242 – 247Combined sources6
Beta strandi251 – 253Combined sources3
Beta strandi265 – 267Combined sources3
Beta strandi270 – 277Combined sources8
Beta strandi282 – 287Combined sources6
Helixi289 – 291Combined sources3
Beta strandi298 – 307Combined sources10
Turni309 – 311Combined sources3
Beta strandi314 – 324Combined sources11
Beta strandi327 – 335Combined sources9
Beta strandi344 – 356Combined sources13
Turni357 – 360Combined sources4
Beta strandi361 – 370Combined sources10
Beta strandi375 – 386Combined sources12
Beta strandi396 – 402Combined sources7
Helixi406 – 408Combined sources3
Turni420 – 422Combined sources3
Beta strandi423 – 425Combined sources3
Helixi427 – 429Combined sources3
Helixi431 – 433Combined sources3
Beta strandi434 – 436Combined sources3
Beta strandi442 – 448Combined sources7
Beta strandi453 – 460Combined sources8
Beta strandi469 – 478Combined sources10
Beta strandi490 – 501Combined sources12
Beta strandi514 – 519Combined sources6
Beta strandi521 – 524Combined sources4
Beta strandi531 – 533Combined sources3
Beta strandi542 – 545Combined sources4
Beta strandi640 – 651Combined sources12
Beta strandi658 – 660Combined sources3
Beta strandi666 – 669Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14738.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati545 – 574B-1Add BLAST30
Repeati575 – 604B-2Add BLAST30
Repeati745 – 782D-1Add BLAST38
Repeati783 – 820D-2Add BLAST38
Repeati821 – 859D-3Add BLAST39
Repeati860 – 878D-4; truncatedAdd BLAST19
Repeati879 – 892WR 1Add BLAST14
Repeati893 – 906WR 2Add BLAST14
Repeati907 – 920WR 3Add BLAST14
Repeati921 – 934WR 4Add BLAST14
Repeati935 – 948WR 5Add BLAST14

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni37 – 511Ligand-binding A regionAdd BLAST475
Regioni194 – 511Fibrinogen/elastin/tropoelastin-bindingAdd BLAST318
Regioni512 – 872Fibronectin-bindingAdd BLAST361
Regioni545 – 6042 X approximate tandem repeatsAdd BLAST60
Regioni745 – 8784 X approximate tandem repeats, D-3 repeat has more fibronectin-binding activityAdd BLAST134
Regioni879 – 9485 X tandem repeats, Pro-rich (WR)Add BLAST70

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi982 – 986LPXTG sorting signalPROSITE-ProRule annotation5

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

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

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.
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.
TIGRFAMsiTIGR01168. 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 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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PRIDEiP14738.

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.

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.
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.
TIGRFAMsiTIGR01168. YSIRK_signal. 1 hit.
PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 122 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.