FNBA_STAA8
ID FNBA_STAA8 Reviewed; 1018 AA.
AC P14738; Q2G1T8;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Fibronectin-binding protein A;
DE Short=FnbpA;
DE Flags: Precursor;
GN Name=fnbA; OrderedLocusNames=SAOUHSC_02803;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN FIBRONECTIN BINDING.
RX PubMed=2521391; DOI=10.1073/pnas.86.2.699;
RA Signaes C., Raucci G., Joensson K., Lindgren P.-E., Anantharamaiah G.M.,
RA Hoeoek M., Lindberg M.;
RT "Nucleotide sequence of the gene for a fibronectin-binding protein from
RT Staphylococcus aureus: use of this peptide sequence in the synthesis of
RT biologically active peptides.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:699-703(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP INDUCTION BY AGR.
RX PubMed=9286974; DOI=10.1128/jb.179.17.5259-5263.1997;
RA Saravia-Otten P., Mueller H.-P., Arvidson S.;
RT "Transcription of Staphylococcus aureus fibronectin binding protein genes
RT is negatively regulated by agr and an agr-independent mechanism.";
RL J. Bacteriol. 179:5259-5263(1997).
RN [4]
RP FUNCTION IN FIBRINOGEN BINDING, AND REGULATION.
RX PubMed=10788510; DOI=10.1074/jbc.275.18.13863;
RA Wann E.R., Gurusiddappa S., Hoeoek M.;
RT "The fibronectin-binding MSCRAMM fnbpA of Staphylococcus aureus is a
RT bifunctional protein that also binds to fibrinogen.";
RL J. Biol. Chem. 275:13863-13871(2000).
RN [5]
RP FUNCTION IN FIBRONECTIN BINDING.
RX PubMed=11736995; DOI=10.1046/j.1462-5822.2001.00157.x;
RA Massey R.C., Kantzanou M.N., Fowler T., Day N.P.J., Schofield K.,
RA Wann E.R., Berendt A.R., Hoeoek M., Peacock S.J.;
RT "Fibronectin-binding protein A of Staphylococcus aureus has multiple,
RT substituting, binding regions that mediate adherence to fibronectin and
RT invasion of endothelial cells.";
RL Cell. Microbiol. 3:839-851(2001).
RN [6]
RP FUNCTION IN FIBRONECTIN AND FIBRINOGEN BINDING, AND ROLE IN ENDOVASCULAR
RP INFECTION.
RX PubMed=11553573; DOI=10.1128/iai.69.10.6296-6302.2001;
RA Que Y.-A., Francois P., Haefliger J.-A., Entenza J.-M., Vaudaux P.,
RA Moreillon P.;
RT "Reassessing the role of Staphylococcus aureus clumping factor and
RT fibronectin-binding protein by expression in Lactococcus lactis.";
RL Infect. Immun. 69:6296-6302(2001).
RN [7]
RP INDUCTION BY SARA.
RX PubMed=11717293; DOI=10.1128/jb.183.24.7341-7353.2001;
RA Dunman P.M., Murphy E., Haney S., Palacios D., Tucker-Kellogg G., Wu S.,
RA Brown E.L., Zagursky R.J., Shlaes D., Projan S.J.;
RT "Transcription profiling-based identification of Staphylococcus aureus
RT genes regulated by the agr and/or sarA loci.";
RL J. Bacteriol. 183:7341-7353(2001).
RN [8]
RP SUBCELLULAR LOCATION, AND PROCESSING BY SORTASE A.
RC STRAIN=RN4220;
RX PubMed=11830639; DOI=10.1073/pnas.032523999;
RA Mazmanian S.K., Ton-That H., Su K., Schneewind O.;
RT "An iron-regulated sortase anchors a class of surface protein during
RT Staphylococcus aureus pathogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2293-2298(2002).
RN [9]
RP PROBABLE CELL WALL ANCHORING.
RC STRAIN=Newman;
RX PubMed=14769030; DOI=10.1021/bi035920j;
RA Kruger R.G., Otvos B., Frankel B.A., Bentley M., Dostal P.,
RA McCafferty D.G.;
RT "Analysis of the substrate specificity of the Staphylococcus aureus sortase
RT transpeptidase SrtA.";
RL Biochemistry 43:1541-1551(2004).
RN [10]
RP FUNCTION IN ELASTIN BINDING.
RX PubMed=15234962; DOI=10.1074/jbc.m402122200;
RA Roche F.M., Downer R., Keane F., Speziale P., Park P.W., Foster T.J.;
RT "The N-terminal A domain of fibronectin-binding proteins A and B promotes
RT adhesion of Staphylococcus aureus to elastin.";
RL J. Biol. Chem. 279:38433-38440(2004).
RN [11]
RP FUNCTION IN PLATELET AGGREGATION.
RX PubMed=15216468; DOI=10.1086/421914;
RA Heilmann C., Niemann S., Sinha B., Herrmann M., Kehrel B.E., Peters G.;
RT "Staphylococcus aureus fibronectin-binding protein (fnbp)-mediated
RT adherence to platelets, and aggregation of platelets induced by fnbpA but
RT not by fnbpB.";
RL J. Infect. Dis. 190:321-329(2004).
RN [12]
RP INDUCTION BY SIGMA-B.
RX PubMed=15664942; DOI=10.1128/iai.73.2.990-998.2005;
RA Entenza J.-M., Moreillon P., Senn M.M., Kormanec J., Dunman P.M.,
RA Berger-Baechi B., Projan S., Bischoff M.;
RT "Role of sigmaB in the expression of Staphylococcus aureus cell wall
RT adhesins clfA and fnbA and contribution to infectivity in a rat model of
RT experimental endocarditis.";
RL Infect. Immun. 73:990-998(2005).
RN [13]
RP ROLE IN EXPERIMENTAL ENDOCARDITIS.
RX PubMed=15897276; DOI=10.1084/jem.20050125;
RA Que Y.-A., Haefliger J.-A., Piroth L., Francois P., Widmer E.,
RA Entenza J.M., Sinha B., Herrmann M., Francioli P., Vaudaux P.,
RA Moreillon P.;
RT "Fibrinogen and fibronectin binding cooperate for valve infection and
RT invasion in Staphylococcus aureus experimental endocarditis.";
RL J. Exp. Med. 201:1627-1635(2005).
RN [14]
RP MECHANISM OF INVASION.
RX PubMed=17021255; DOI=10.1091/mbc.e06-05-0463;
RA Schroeder A., Schroeder B., Roppenser B., Linder S., Sinha B., Faessler R.,
RA Aepfelbacher M.;
RT "Staphylococcus aureus fibronectin binding protein-A induces motile
RT attachment sites and complex actin remodeling in living endothelial
RT cells.";
RL Mol. Biol. Cell 17:5198-5210(2006).
RN [15]
RP FUNCTION IN TROPOELASTIN BINDING.
RX PubMed=17516661; DOI=10.1021/bi700454x;
RA Keane F.M., Clarke A.W., Foster T.J., Weiss A.S.;
RT "The N-terminal A domain of Staphylococcus aureus fibronectin-binding
RT protein A binds to tropoelastin.";
RL Biochemistry 46:7226-7232(2007).
RN [16]
RP CHARACTERIZATION OF FIBRINOGEN AND ELASTIN-BINDING DOMAINS, AND MUTAGENESIS
RP OF GLY-222; ARG-224; ASN-304; PHE-306; THR-354; PHE-355; ASN-356; LYS-357;
RP ALA-415; THR-417; 484-TYR--ASN-511; GLY-497; LEU-498; 499-VAL--ASN-511 AND
RP 510-LYS-ASN-511.
RX PubMed=17302800; DOI=10.1111/j.1365-2958.2006.05552.x;
RA Keane F.M., Loughman A., Valtulina V., Brennan M., Speziale P.,
RA Foster T.J.;
RT "Fibrinogen and elastin bind to the same region within the A domain of
RT fibronectin binding protein A, an MSCRAMM of Staphylococcus aureus.";
RL Mol. Microbiol. 63:711-723(2007).
CC -!- FUNCTION: Possesses multiple, substituting fibronectin (Fn) binding
CC regions, each capable of conferring adherence to both soluble and
CC immobilized forms of Fn. This confers to S.aureus the ability to invade
CC endothelial cells both in vivo and in vitro, without requiring
CC additional factors, although in a slow and inefficient way through
CC actin rearrangements in host cells. This invasion process is mediated
CC by integrin alpha-5/beta-1. Promotes bacterial attachment to both
CC soluble and immobilized forms of fibrinogen (Fg) by means of a unique
CC binding site localized within the 17 C-terminal residues of the gamma-
CC chain of human Fg. Both plasma proteins (Fn and Fg) function as a
CC bridge between bacterium and host cell. Promotes attachment to
CC immobilized elastin peptides in a dose-dependent and saturable manner.
CC Promotes attachment to both full-length and segments of immobilized
CC human tropoelastin at multiple sites in a dose and pH-dependent manner.
CC Promotes adherence to and aggregation of activated platelets
CC independently of other S.aureus surface molecules. Is a critical
CC mediator implicated in the induction of experimental endocarditis in
CC rats with catheter-induced aortic vegetations, promoting both
CC colonization and persistence of the bacterium into the host.
CC {ECO:0000269|PubMed:10788510, ECO:0000269|PubMed:11553573,
CC ECO:0000269|PubMed:11736995, ECO:0000269|PubMed:15216468,
CC ECO:0000269|PubMed:15234962, ECO:0000269|PubMed:15897276,
CC ECO:0000269|PubMed:17516661, ECO:0000269|PubMed:2521391}.
CC -!- INTERACTION:
CC P14738; P02751: FN1; Xeno; NbExp=23; IntAct=EBI-8398157, EBI-1220319;
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477, ECO:0000305|PubMed:11830639}; Peptidoglycan-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000305|PubMed:11830639,
CC ECO:0000305|PubMed:14769030}. Note=Anchored to the cell wall by sortase
CC A. {ECO:0000305|PubMed:11830639, ECO:0000305|PubMed:14769030}.
CC -!- INDUCTION: Expressed predominantly on cells from early exponential
CC phase of growth. Up-regulated by sigma-B factor during early growth
CC stages but not in later stages, although this positive effect on
CC transcription is most probably indirect. Up-regulated by SarA. Down-
CC regulated by Agr. {ECO:0000269|PubMed:11717293,
CC ECO:0000269|PubMed:15664942, ECO:0000269|PubMed:9286974}.
CC -!- MISCELLANEOUS: Fg-binding activity is not regulated by the divalent
CC cations Ca(2+), Mn(2+) or Mg(2+).
CC -!- MISCELLANEOUS: Deletion of the Fg-binding domain of FnbA abrogates the
CC ability to promote cardiac valve infection and persistence in vivo.
CC -!- MISCELLANEOUS: The mutagenesis studies described in PubMed:17302800
CC were done with region A alone and not with the entire protein.
CC -!- MISCELLANEOUS: Mutants lacking C-terminal residues from the ligand
CC binding A region bind to Fg with a reduced affinity or are unable to
CC bind to both Fg and elastin, depending on the extension of the deletion
CC present in this region. Individual constructs of regions spanning amino
CC acids from 194-336 or 337-511 were unable to bind fibrinogen or
CC elastin.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD31806.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J04151; AAA26632.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD31806.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000794582.1; NZ_LS483365.1.
DR RefSeq; YP_501262.1; NC_007795.1.
DR PDB; 2RKY; X-ray; 1.80 A; B/D=508-530.
DR PDB; 2RKZ; X-ray; 2.00 A; M/N/O/P/Q/R=529-549.
DR PDB; 2RL0; X-ray; 2.00 A; C/E/G/H/J/L=638-655.
DR PDB; 3CAL; X-ray; 1.70 A; B/D=655-672.
DR PDB; 4B5Z; X-ray; 2.20 A; A=189-505.
DR PDB; 4B60; X-ray; 1.83 A; A/B=189-505.
DR PDBsum; 2RKY; -.
DR PDBsum; 2RKZ; -.
DR PDBsum; 2RL0; -.
DR PDBsum; 3CAL; -.
DR PDBsum; 4B5Z; -.
DR PDBsum; 4B60; -.
DR AlphaFoldDB; P14738; -.
DR SMR; P14738; -.
DR DIP; DIP-46263N; -.
DR IntAct; P14738; 1.
DR MINT; P14738; -.
DR STRING; 1280.SAXN108_2750; -.
DR PRIDE; P14738; -.
DR EnsemblBacteria; ABD31806; ABD31806; SAOUHSC_02803.
DR GeneID; 3921457; -.
DR KEGG; sao:SAOUHSC_02803; -.
DR PATRIC; fig|93061.5.peg.2536; -.
DR eggNOG; COG4932; Bacteria.
DR HOGENOM; CLU_009849_1_0_9; -.
DR EvolutionaryTrace; P14738; -.
DR PRO; PR:P14738; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0070051; F:fibrinogen binding; IMP:CAFA.
DR GO; GO:0001968; F:fibronectin binding; IPI:CAFA.
DR GO; GO:0098630; P:aggregation of unicellular organisms; IMP:CAFA.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR DisProt; DP00025; -.
DR Gene3D; 2.60.40.1280; -; 1.
DR InterPro; IPR011266; Adhesin_Fg-bd_dom_2.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR011252; Fibrogen-bd_dom1.
DR InterPro; IPR004237; Fibron_repeat-bd.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR041171; SDR_Ig.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF17961; Big_8; 1.
DR Pfam; PF02986; Fn_bind; 3.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF10425; SdrG_C_C; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SUPFAM; SSF49401; SSF49401; 2.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell wall; Peptidoglycan-anchor;
KW Reference proteome; Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..36
FT CHAIN 37..985
FT /note="Fibronectin-binding protein A"
FT /id="PRO_0000005605"
FT PROPEP 986..1018
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000305|PubMed:11830639, ECO:0000305|PubMed:14769030"
FT /id="PRO_0000005606"
FT REPEAT 545..574
FT /note="B-1"
FT REPEAT 575..604
FT /note="B-2"
FT REPEAT 745..782
FT /note="D-1"
FT REPEAT 783..820
FT /note="D-2"
FT REPEAT 821..859
FT /note="D-3"
FT REPEAT 860..878
FT /note="D-4; truncated"
FT REPEAT 879..892
FT /note="WR 1"
FT REPEAT 893..906
FT /note="WR 2"
FT REPEAT 907..920
FT /note="WR 3"
FT REPEAT 921..934
FT /note="WR 4"
FT REPEAT 935..948
FT /note="WR 5"
FT REGION 37..511
FT /note="Ligand-binding A region"
FT REGION 38..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..511
FT /note="Fibrinogen/elastin/tropoelastin-binding"
FT REGION 512..872
FT /note="Fibronectin-binding"
FT REGION 545..604
FT /note="2 X approximate tandem repeats"
FT REGION 595..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..878
FT /note="4 X approximate tandem repeats, D-3 repeat has more
FT fibronectin-binding activity"
FT REGION 827..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..948
FT /note="5 X tandem repeats, Pro-rich (WR)"
FT MOTIF 7..18
FT /note="YSIRK-G/S signaling motif"
FT /evidence="ECO:0000305"
FT MOTIF 982..986
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 78..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..936
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 985
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT MUTAGEN 222
FT /note="G->A: No change in elastin or fibrinogen binding."
FT /evidence="ECO:0000269|PubMed:17302800"
FT MUTAGEN 224
FT /note="R->A: Significant reduction in fibrinogen and
FT elastin binding."
FT /evidence="ECO:0000269|PubMed:17302800"
FT MUTAGEN 304
FT /note="N->A: Significant reduction in fibrinogen and
FT elastin binding."
FT /evidence="ECO:0000269|PubMed:17302800"
FT MUTAGEN 306
FT /note="F->A: Significant reduction in fibrinogen and
FT elastin binding."
FT /evidence="ECO:0000269|PubMed:17302800"
FT MUTAGEN 354
FT /note="T->A: Small reduction in fibrinogen binding and
FT greater reduction in elastin binding; when associated with
FT G-356."
FT /evidence="ECO:0000269|PubMed:17302800"
FT MUTAGEN 355
FT /note="F->A: No reduction in elastin binding. Significant
FT reduction in fibrinogen binding."
FT /evidence="ECO:0000269|PubMed:17302800"
FT MUTAGEN 356
FT /note="N->G: Small reduction in fibrinogen binding and
FT greater reduction in elastin binding; when associated with
FT A-354."
FT /evidence="ECO:0000269|PubMed:17302800"
FT MUTAGEN 357
FT /note="K->A: No reduction in elastin binding. Significant
FT reduction in fibrinogen binding."
FT /evidence="ECO:0000269|PubMed:17302800"
FT MUTAGEN 415
FT /note="A->G: Significant reduction in fibrinogen and
FT elastin binding; when associated with A-417."
FT /evidence="ECO:0000269|PubMed:17302800"
FT MUTAGEN 417
FT /note="T->A: Significant reduction in fibrinogen and
FT elastin binding; when associated with G-415."
FT /evidence="ECO:0000269|PubMed:17302800"
FT MUTAGEN 484..511
FT /note="Missing: Abolishes interaction with elastin and
FT fibrinogen."
FT /evidence="ECO:0000269|PubMed:17302800"
FT MUTAGEN 497
FT /note="G->A: Significant reduction in fibrinogen and
FT elastin binding."
FT /evidence="ECO:0000269|PubMed:17302800"
FT MUTAGEN 498
FT /note="L->A: Significant reduction in fibrinogen and
FT elastin binding."
FT /evidence="ECO:0000269|PubMed:17302800"
FT MUTAGEN 499..511
FT /note="Missing: Abolishes interaction with elastin and
FT fibrinogen."
FT /evidence="ECO:0000269|PubMed:17302800"
FT MUTAGEN 510..511
FT /note="Missing: No change in elastin binding. Impairs
FT fibrinogen binding."
FT /evidence="ECO:0000269|PubMed:17302800"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 201..209
FT /evidence="ECO:0007829|PDB:4B60"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:4B60"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:4B5Z"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:4B60"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 298..307
FT /evidence="ECO:0007829|PDB:4B60"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 314..324
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 327..335
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 344..356
FT /evidence="ECO:0007829|PDB:4B60"
FT TURN 357..360
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 361..370
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 375..386
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:4B60"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:4B60"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:4B60"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:4B60"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:4B5Z"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 442..448
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 453..460
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 469..478
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 490..501
FT /evidence="ECO:0007829|PDB:4B60"
FT STRAND 514..519
FT /evidence="ECO:0007829|PDB:2RKY"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:2RKY"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:2RKZ"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:2RKZ"
FT STRAND 640..651
FT /evidence="ECO:0007829|PDB:2RL0"
FT STRAND 658..660
FT /evidence="ECO:0007829|PDB:3CAL"
FT STRAND 666..669
FT /evidence="ECO:0007829|PDB:3CAL"
SQ 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
