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Fibronectin-binding protein A

 FNBA_STAA8              Reviewed;        1018 AA.
P14738; Q2G1T8;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
10-OCT-2018, entry version 131.
RecName: Full=Fibronectin-binding protein A;
Short=FnbpA;
Flags: Precursor;
Name=fnbA; OrderedLocusNames=SAOUHSC_02803;
Staphylococcus aureus (strain NCTC 8325).
Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
Staphylococcus.
NCBI_TaxID=93061;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN FIBRONECTIN
BINDING.
PubMed=2521391; DOI=10.1073/pnas.86.2.699;
Signaes C., Raucci G., Joensson K., Lindgren P.-E.,
Anantharamaiah G.M., Hoeoek M., Lindberg M.;
"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.";
Proc. Natl. Acad. Sci. U.S.A. 86:699-703(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NCTC 8325;
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W.,
Iandolo J.J.;
"The Staphylococcus aureus NCTC 8325 genome.";
(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).
[3]
INDUCTION BY AGR.
PubMed=9286974; DOI=10.1128/jb.179.17.5259-5263.1997;
Saravia-Otten P., Mueller H.-P., Arvidson S.;
"Transcription of Staphylococcus aureus fibronectin binding protein
genes is negatively regulated by agr and an agr-independent
mechanism.";
J. Bacteriol. 179:5259-5263(1997).
[4]
FUNCTION IN FIBRINOGEN BINDING, AND REGULATION.
PubMed=10788510; DOI=10.1074/jbc.275.18.13863;
Wann E.R., Gurusiddappa S., Hoeoek M.;
"The fibronectin-binding MSCRAMM fnbpA of Staphylococcus aureus is a
bifunctional protein that also binds to fibrinogen.";
J. Biol. Chem. 275:13863-13871(2000).
[5]
FUNCTION IN FIBRONECTIN BINDING.
PubMed=11736995; DOI=10.1046/j.1462-5822.2001.00157.x;
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.;
"Fibronectin-binding protein A of Staphylococcus aureus has multiple,
substituting, binding regions that mediate adherence to fibronectin
and invasion of endothelial cells.";
Cell. Microbiol. 3:839-851(2001).
[6]
FUNCTION IN FIBRONECTIN AND FIBRINOGEN BINDING, AND ROLE IN
ENDOVASCULAR INFECTION.
PubMed=11553573; DOI=10.1128/IAI.69.10.6296-6302.2001;
Que Y.-A., Francois P., Haefliger J.-A., Entenza J.-M., Vaudaux P.,
Moreillon P.;
"Reassessing the role of Staphylococcus aureus clumping factor and
fibronectin-binding protein by expression in Lactococcus lactis.";
Infect. Immun. 69:6296-6302(2001).
[7]
INDUCTION BY SARA.
PubMed=11717293; DOI=10.1128/JB.183.24.7341-7353.2001;
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.;
"Transcription profiling-based identification of Staphylococcus aureus
genes regulated by the agr and/or sarA loci.";
J. Bacteriol. 183:7341-7353(2001).
[8]
SUBCELLULAR LOCATION, AND PROCESSING BY SORTASE A.
STRAIN=RN4220;
PubMed=11830639; DOI=10.1073/pnas.032523999;
Mazmanian S.K., Ton-That H., Su K., Schneewind O.;
"An iron-regulated sortase anchors a class of surface protein during
Staphylococcus aureus pathogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 99:2293-2298(2002).
[9]
PROBABLE CELL WALL ANCHORING.
STRAIN=Newman;
PubMed=14769030; DOI=10.1021/bi035920j;
Kruger R.G., Otvos B., Frankel B.A., Bentley M., Dostal P.,
McCafferty D.G.;
"Analysis of the substrate specificity of the Staphylococcus aureus
sortase transpeptidase SrtA.";
Biochemistry 43:1541-1551(2004).
[10]
FUNCTION IN ELASTIN BINDING.
PubMed=15234962; DOI=10.1074/jbc.M402122200;
Roche F.M., Downer R., Keane F., Speziale P., Park P.W., Foster T.J.;
"The N-terminal A domain of fibronectin-binding proteins A and B
promotes adhesion of Staphylococcus aureus to elastin.";
J. Biol. Chem. 279:38433-38440(2004).
[11]
FUNCTION IN PLATELET AGGREGATION.
PubMed=15216468; DOI=10.1086/421914;
Heilmann C., Niemann S., Sinha B., Herrmann M., Kehrel B.E.,
Peters G.;
"Staphylococcus aureus fibronectin-binding protein (fnbp)-mediated
adherence to platelets, and aggregation of platelets induced by fnbpA
but not by fnbpB.";
J. Infect. Dis. 190:321-329(2004).
[12]
INDUCTION BY SIGMA-B.
PubMed=15664942; DOI=10.1128/IAI.73.2.990-998.2005;
Entenza J.-M., Moreillon P., Senn M.M., Kormanec J., Dunman P.M.,
Berger-Baechi B., Projan S., Bischoff M.;
"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.";
Infect. Immun. 73:990-998(2005).
[13]
ROLE IN EXPERIMENTAL ENDOCARDITIS.
PubMed=15897276; DOI=10.1084/jem.20050125;
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.;
"Fibrinogen and fibronectin binding cooperate for valve infection and
invasion in Staphylococcus aureus experimental endocarditis.";
J. Exp. Med. 201:1627-1635(2005).
[14]
MECHANISM OF INVASION.
PubMed=17021255; DOI=10.1091/mbc.E06-05-0463;
Schroeder A., Schroeder B., Roppenser B., Linder S., Sinha B.,
Faessler R., Aepfelbacher M.;
"Staphylococcus aureus fibronectin binding protein-A induces motile
attachment sites and complex actin remodeling in living endothelial
cells.";
Mol. Biol. Cell 17:5198-5210(2006).
[15]
FUNCTION IN TROPOELASTIN BINDING.
PubMed=17516661; DOI=10.1021/bi700454x;
Keane F.M., Clarke A.W., Foster T.J., Weiss A.S.;
"The N-terminal A domain of Staphylococcus aureus fibronectin-binding
protein A binds to tropoelastin.";
Biochemistry 46:7226-7232(2007).
[16]
CHARACTERIZATION OF FIBRINOGEN AND ELASTIN-BINDING DOMAINS, AND
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.
PubMed=17302800; DOI=10.1111/j.1365-2958.2006.05552.x;
Keane F.M., Loughman A., Valtulina V., Brennan M., Speziale P.,
Foster T.J.;
"Fibrinogen and elastin bind to the same region within the A domain of
fibronectin binding protein A, an MSCRAMM of Staphylococcus aureus.";
Mol. Microbiol. 63:711-723(2007).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:10788510, ECO:0000269|PubMed:11553573,
ECO:0000269|PubMed:11736995, ECO:0000269|PubMed:15216468,
ECO:0000269|PubMed:15234962, ECO:0000269|PubMed:15897276,
ECO:0000269|PubMed:17516661, ECO:0000269|PubMed:2521391}.
-!- INTERACTION:
P02751:FN1 (xeno); NbExp=20; IntAct=EBI-8398157, EBI-1220319;
-!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
ProRule:PRU00477, ECO:0000305|PubMed:11830639}; Peptidoglycan-
anchor {ECO:0000255|PROSITE-ProRule:PRU00477,
ECO:0000305|PubMed:11830639, ECO:0000305|PubMed:14769030}.
Note=Anchored to the cell wall by sortase A.
{ECO:0000305|PubMed:11830639, ECO:0000305|PubMed:14769030}.
-!- INDUCTION: 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. {ECO:0000269|PubMed:11717293,
ECO:0000269|PubMed:15664942, ECO:0000269|PubMed:9286974}.
-!- MISCELLANEOUS: Fg-binding activity is not regulated by the
divalent cations Ca(2+), Mn(2+) or Mg(2+).
-!- MISCELLANEOUS: Deletion of the Fg-binding domain of FnbA abrogates
the ability to promote cardiac valve infection and persistence in
vivo.
-!- MISCELLANEOUS: The mutagenesis studies described in
PubMed:17302800 were done with region A alone and not with the
entire protein.
-!- MISCELLANEOUS: 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.
-!- SEQUENCE CAUTION:
Sequence=ABD31806.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; J04151; AAA26632.1; -; Genomic_DNA.
EMBL; CP000253; ABD31806.1; ALT_INIT; Genomic_DNA.
RefSeq; WP_000794582.1; NZ_LS483365.1.
RefSeq; YP_501262.1; NC_007795.1.
PDB; 2RKY; X-ray; 1.80 A; B/D=508-530.
PDB; 2RKZ; X-ray; 2.00 A; M/N/O/P/Q/R=529-549.
PDB; 2RL0; X-ray; 2.00 A; C/E/G/H/J/L=638-655.
PDB; 3CAL; X-ray; 1.70 A; B/D=655-672.
PDB; 4B5Z; X-ray; 2.20 A; A=189-505.
PDB; 4B60; X-ray; 1.83 A; A/B=189-505.
PDBsum; 2RKY; -.
PDBsum; 2RKZ; -.
PDBsum; 2RL0; -.
PDBsum; 3CAL; -.
PDBsum; 4B5Z; -.
PDBsum; 4B60; -.
DisProt; DP00025; -.
ProteinModelPortal; P14738; -.
SMR; P14738; -.
DIP; DIP-46263N; -.
IntAct; P14738; 1.
MINT; P14738; -.
STRING; 93061.SAOUHSC_02803; -.
PRIDE; P14738; -.
EnsemblBacteria; ABD31806; ABD31806; SAOUHSC_02803.
GeneID; 3921457; -.
KEGG; sao:SAOUHSC_02803; -.
PATRIC; fig|93061.5.peg.2536; -.
eggNOG; ENOG41078HS; Bacteria.
eggNOG; ENOG410XV8D; LUCA.
HOGENOM; HOG000280272; -.
KO; K13732; -.
EvolutionaryTrace; P14738; -.
PRO; PR:P14738; -.
Proteomes; UP000008816; Chromosome.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0070051; F:fibrinogen binding; IMP:CAFA.
GO; GO:0001968; F:fibronectin binding; IPI:CAFA.
GO; GO:0098630; P:aggregation of unicellular organisms; IMP:CAFA.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
Gene3D; 2.60.40.1280; -; 1.
InterPro; IPR011266; Adhesin_Fg-bd_dom_2.
InterPro; IPR008966; Adhesion_dom_sf.
InterPro; IPR011252; Fibrogen-bd_dom1.
InterPro; IPR004237; Fibron_repeat-bd.
InterPro; IPR019948; Gram-positive_anchor.
InterPro; IPR005877; YSIRK_signal_dom.
Pfam; PF02986; Fn_bind; 3.
Pfam; PF00746; Gram_pos_anchor; 1.
Pfam; PF10425; SdrG_C_C; 1.
Pfam; PF04650; YSIRK_signal; 1.
SUPFAM; SSF49401; SSF49401; 2.
TIGRFAMs; TIGR01168; YSIRK_signal; 1.
PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
1: Evidence at protein level;
3D-structure; Cell adhesion; Cell wall; Complete proteome;
Peptidoglycan-anchor; Reference proteome; Repeat; Secreted; Signal;
Virulence.
SIGNAL 1 36
CHAIN 37 985 Fibronectin-binding protein A.
/FTId=PRO_0000005605.
PROPEP 986 1018 Removed by sortase. {ECO:0000255|PROSITE-
ProRule:PRU00477,
ECO:0000305|PubMed:11830639,
ECO:0000305|PubMed:14769030}.
/FTId=PRO_0000005606.
REPEAT 545 574 B-1.
REPEAT 575 604 B-2.
REPEAT 745 782 D-1.
REPEAT 783 820 D-2.
REPEAT 821 859 D-3.
REPEAT 860 878 D-4; truncated.
REPEAT 879 892 WR 1.
REPEAT 893 906 WR 2.
REPEAT 907 920 WR 3.
REPEAT 921 934 WR 4.
REPEAT 935 948 WR 5.
REGION 37 511 Ligand-binding A region.
REGION 194 511 Fibrinogen/elastin/tropoelastin-binding.
REGION 512 872 Fibronectin-binding.
REGION 545 604 2 X approximate tandem repeats.
REGION 745 878 4 X approximate tandem repeats, D-3
repeat has more fibronectin-binding
activity.
REGION 879 948 5 X tandem repeats, Pro-rich (WR).
MOTIF 7 18 YSIRK-G/S signaling motif. {ECO:0000305}.
MOTIF 982 986 LPXTG sorting signal.
{ECO:0000255|PROSITE-ProRule:PRU00477}.
MOD_RES 985 985 Pentaglycyl murein peptidoglycan amidated
threonine. {ECO:0000255|PROSITE-
ProRule:PRU00477}.
MUTAGEN 222 222 G->A: No change in elastin or fibrinogen
binding. {ECO:0000269|PubMed:17302800}.
MUTAGEN 224 224 R->A: Significant reduction in fibrinogen
and elastin binding.
{ECO:0000269|PubMed:17302800}.
MUTAGEN 304 304 N->A: Significant reduction in fibrinogen
and elastin binding.
{ECO:0000269|PubMed:17302800}.
MUTAGEN 306 306 F->A: Significant reduction in fibrinogen
and elastin binding.
{ECO:0000269|PubMed:17302800}.
MUTAGEN 354 354 T->A: Small reduction in fibrinogen
binding and greater reduction in elastin
binding; when associated with G-356.
{ECO:0000269|PubMed:17302800}.
MUTAGEN 355 355 F->A: No reduction in elastin binding.
Significant reduction in fibrinogen
binding. {ECO:0000269|PubMed:17302800}.
MUTAGEN 356 356 N->G: Small reduction in fibrinogen
binding and greater reduction in elastin
binding; when associated with A-354.
{ECO:0000269|PubMed:17302800}.
MUTAGEN 357 357 K->A: No reduction in elastin binding.
Significant reduction in fibrinogen
binding. {ECO:0000269|PubMed:17302800}.
MUTAGEN 415 415 A->G: Significant reduction in fibrinogen
and elastin binding; when associated with
A-417. {ECO:0000269|PubMed:17302800}.
MUTAGEN 417 417 T->A: Significant reduction in fibrinogen
and elastin binding; when associated with
G-415. {ECO:0000269|PubMed:17302800}.
MUTAGEN 484 511 Missing: Abolishes interaction with
elastin and fibrinogen.
{ECO:0000269|PubMed:17302800}.
MUTAGEN 497 497 G->A: Significant reduction in fibrinogen
and elastin binding.
{ECO:0000269|PubMed:17302800}.
MUTAGEN 498 498 L->A: Significant reduction in fibrinogen
and elastin binding.
{ECO:0000269|PubMed:17302800}.
MUTAGEN 499 511 Missing: Abolishes interaction with
elastin and fibrinogen.
{ECO:0000269|PubMed:17302800}.
MUTAGEN 510 511 Missing: No change in elastin binding.
Impairs fibrinogen binding.
{ECO:0000269|PubMed:17302800}.
HELIX 198 200 {ECO:0000244|PDB:4B60}.
STRAND 201 209 {ECO:0000244|PDB:4B60}.
HELIX 211 213 {ECO:0000244|PDB:4B60}.
STRAND 214 217 {ECO:0000244|PDB:4B60}.
HELIX 219 221 {ECO:0000244|PDB:4B5Z}.
STRAND 225 233 {ECO:0000244|PDB:4B60}.
STRAND 242 247 {ECO:0000244|PDB:4B60}.
STRAND 251 253 {ECO:0000244|PDB:4B60}.
STRAND 265 267 {ECO:0000244|PDB:4B60}.
STRAND 270 277 {ECO:0000244|PDB:4B60}.
STRAND 282 287 {ECO:0000244|PDB:4B60}.
HELIX 289 291 {ECO:0000244|PDB:4B60}.
STRAND 298 307 {ECO:0000244|PDB:4B60}.
TURN 309 311 {ECO:0000244|PDB:4B60}.
STRAND 314 324 {ECO:0000244|PDB:4B60}.
STRAND 327 335 {ECO:0000244|PDB:4B60}.
STRAND 344 356 {ECO:0000244|PDB:4B60}.
TURN 357 360 {ECO:0000244|PDB:4B60}.
STRAND 361 370 {ECO:0000244|PDB:4B60}.
STRAND 375 386 {ECO:0000244|PDB:4B60}.
STRAND 396 402 {ECO:0000244|PDB:4B60}.
HELIX 406 408 {ECO:0000244|PDB:4B60}.
TURN 420 422 {ECO:0000244|PDB:4B60}.
STRAND 423 425 {ECO:0000244|PDB:4B60}.
HELIX 427 429 {ECO:0000244|PDB:4B60}.
HELIX 431 433 {ECO:0000244|PDB:4B5Z}.
STRAND 434 436 {ECO:0000244|PDB:4B60}.
STRAND 442 448 {ECO:0000244|PDB:4B60}.
STRAND 453 460 {ECO:0000244|PDB:4B60}.
STRAND 469 478 {ECO:0000244|PDB:4B60}.
STRAND 490 501 {ECO:0000244|PDB:4B60}.
STRAND 514 519 {ECO:0000244|PDB:2RKY}.
STRAND 521 524 {ECO:0000244|PDB:2RKY}.
STRAND 531 533 {ECO:0000244|PDB:2RKZ}.
STRAND 542 545 {ECO:0000244|PDB:2RKZ}.
STRAND 640 651 {ECO:0000244|PDB:2RL0}.
STRAND 658 660 {ECO:0000244|PDB:3CAL}.
STRAND 666 669 {ECO:0000244|PDB:3CAL}.
SEQUENCE 1018 AA; 111780 MW; 58175E0020E81F1F CRC64;
MKNNLRYGIR KHKLGAASVF LGTMIVVGMG QDKEAAASEQ KTTTVEENGN SATDNKTSET
QTTATNVNHI EETQSYNATV TEQPSNATQV TTEEAPKAVQ APQTAQPANI ETVKEEVVKE
EAKPQVKETT QSQDNSGDQR QVDLTPKKAT QNQVAETQVE VAQPRTASES KPRVTRSADV
AEAKEASNAK VETGTDVTSK VTVEIGSIEG HNNTNKVEPH AGQRAVLKYK LKFENGLHQG
DYFDFTLSNN VNTHGVSTAR KVPEIKNGSV VMATGEVLEG GKIRYTFTND IEDKVDVTAE
LEINLFIDPK TVQTNGNQTI TSTLNEEQTS KELDVKYKDG IGNYYANLNG SIETFNKANN
RFSHVAFIKP NNGKTTSVTV TGTLMKGSNQ NGNQPKVRIF EYLGNNEDIA KSVYANTTDT
SKFKEVTSNM SGNLNLQNNG SYSLNIENLD KTYVVHYDGE YLNGTDEVDF RTQMVGHPEQ
LYKYYYDRGY TLTWDNGLVL YSNKANGNEK NGPIIQNNKF EYKEDTIKET LTGQYDKNLV
TTVEEEYDSS TLDIDYHTAI DGGGGYVDGY IETIEETDSS AIDIDYHTAV DSEAGHVGGY
TESSEESNPI DFEESTHENS KHHADVVEYE EDTNPGGGQV TTESNLVEFD EESTKGIVTG
AVSDHTTVED TKEYTTESNL IELVDELPEE HGQAQGPVEE ITKNNHHISH SGLGTENGHG
NYDVIEEIEE NSHVDIKSEL GYEGGQNSGN QSFEEDTEED KPKYEQGGNI VDIDFDSVPQ
IHGQNKGNQS FEEDTEKDKP KYEHGGNIID IDFDSVPHIH GFNKHTEIIE EDTNKDKPSY
QFGGHNSVDF EEDTLPKVSG QNEGQQTIEE DTTPPIVPPT PPTPEVPSEP ETPTPPTPEV
PSEPETPTPP TPEVPSEPET PTPPTPEVPA EPGKPVPPAK EEPKKPSKPV EQGKVVTPVI
EINEKVKAVA PTKKPQSKKS ELPETGGEES TNKGMLFGGL FSILGLALLR RNKKNHKA


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