SRAP_STAA8
ID SRAP_STAA8 Reviewed; 2271 AA.
AC Q2FUW1;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Serine-rich adhesin for platelets;
DE AltName: Full=Adhesin SraP {ECO:0000305};
DE AltName: Full=Staphylococcus aureus surface protein A {ECO:0000303|PubMed:12634333};
DE Short=SasA {ECO:0000303|PubMed:12634333};
DE Flags: Precursor;
GN Name=sraP {ECO:0000303|PubMed:15784571};
GN Synonyms=sasA {ECO:0000303|PubMed:12634333};
GN OrderedLocusNames=SAOUHSC_02990;
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 [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 [2]
RP SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=12634333; DOI=10.1099/mic.0.25996-0;
RA Roche F.M., Massey R., Peacock S.J., Day N.P.J., Visai L., Speziale P.,
RA Lam A., Pallen M., Foster T.J.;
RT "Characterization of novel LPXTG-containing proteins of Staphylococcus
RT aureus identified from genome sequences.";
RL Microbiology 149:643-654(2003).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND GLYCOSYLATION.
RC STRAIN=ISP479C;
RX PubMed=15784571; DOI=10.1128/iai.73.4.2273-2280.2005;
RA Siboo I.R., Chambers H.F., Sullam P.M.;
RT "Role of SraP, a serine-rich surface protein of Staphylococcus aureus, in
RT binding to human platelets.";
RL Infect. Immun. 73:2273-2280(2005).
RN [4]
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 [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=RN4220;
RX PubMed=18800056; DOI=10.1038/emboj.2008.185;
RA DeDent A., Bae T., Missiakas D.M., Schneewind O.;
RT "Signal peptides direct surface proteins to two distinct envelope locations
RT of Staphylococcus aureus.";
RL EMBO J. 27:2656-2668(2008).
RN [6]
RP SUBCELLULAR LOCATION, AND EXPORT VIA THE ACCESSORY SECA2/SECY2 SYSTEM.
RC STRAIN=ISP479C;
RX PubMed=18621893; DOI=10.1128/jb.00300-08;
RA Siboo I.R., Chaffin D.O., Rubens C.E., Sullam P.M.;
RT "Characterization of the accessory Sec system of Staphylococcus aureus.";
RL J. Bacteriol. 190:6188-6196(2008).
RN [7]
RP DISCUSSION OF SEQUENCE.
RX PubMed=19202081; DOI=10.1099/mic.0.025221-0;
RA Zhou M., Wu H.;
RT "Glycosylation and biogenesis of a family of serine-rich bacterial
RT adhesins.";
RL Microbiology 155:317-327(2009).
RN [8]
RP INDUCTION.
RC STRAIN=RN4220;
RX PubMed=20472795; DOI=10.1128/jb.01452-09;
RA Sibbald M.J., Winter T., van der Kooi-Pol M.M., Buist G., Tsompanidou E.,
RA Bosma T., Schafer T., Ohlsen K., Hecker M., Antelmann H., Engelmann S.,
RA van Dijl J.M.;
RT "Synthetic effects of secG and secY2 mutations on exoproteome biogenesis in
RT Staphylococcus aureus.";
RL J. Bacteriol. 192:3788-3800(2010).
RN [9]
RP FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=ISP479C;
RX PubMed=20714350; DOI=10.1371/journal.ppat.1001044;
RA Sanchez C.J., Shivshankar P., Stol K., Trakhtenbroit S., Sullam P.M.,
RA Sauer K., Hermans P.W., Orihuela C.J.;
RT "The pneumococcal serine-rich repeat protein is an intra-species bacterial
RT adhesin that promotes bacterial aggregation in vivo and in biofilms.";
RL PLoS Pathog. 6:E1001044-E1001044(2010).
RN [10] {ECO:0007744|PDB:4M00, ECO:0007744|PDB:4M01, ECO:0007744|PDB:4M02, ECO:0007744|PDB:4M03}
RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 494-663 IN COMPLEX WITH CALCIUM,
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 245-751 (NON-REPEAT REGION) IN
RP COMPLEX WITH CALCIUM, FUNCTION, IDENTIFICATION OF HOST RECEPTOR, DOMAIN,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TYR-367.
RC STRAIN=NCTC 8325 / PS 47;
RX PubMed=24901708; DOI=10.1371/journal.ppat.1004169;
RA Yang Y.H., Jiang Y.L., Zhang J., Wang L., Bai X.H., Zhang S.J., Ren Y.M.,
RA Li N., Zhang Y.H., Zhang Z., Gong Q., Mei Y., Xue T., Zhang J.R., Chen Y.,
RA Zhou C.Z.;
RT "Structural insights into SraP-mediated Staphylococcus aureus adhesion to
RT host cells.";
RL PLoS Pathog. 10:e1004169-e1004169(2014).
CC -!- FUNCTION: Mediates binding to human platelets, possibly through a
CC receptor-ligand interaction. Probably associated with virulence in
CC endovascular infection (PubMed:15784571). Plays a positive role in
CC biofilm formation, possibly by self-association via the non-repeat
CC region (NRR or binding region, BR) (PubMed:20714350). Binds to and
CC plays a role in human lung epithelial cell invasion via the L-lectin
CC module of its NRR domain; N-acetylneuraminic acid (Neu5Ac) inhibits
CC binding. Treatment of host cells with neuraminidase decreases adherence
CC of S.aureus cells, suggesting SraP recognizes a host terminal Neu5Ac
CC moiety as a receptor (PubMed:24901708). {ECO:0000269|PubMed:15784571,
CC ECO:0000269|PubMed:20714350, ECO:0000269|PubMed:24901708}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477, ECO:0000269|PubMed:12634333,
CC ECO:0000269|PubMed:15784571, ECO:0000269|PubMed:18621893,
CC ECO:0000269|PubMed:18800056, ECO:0000305|PubMed:11830639};
CC Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477,
CC ECO:0000269|PubMed:12634333, ECO:0000269|PubMed:15784571,
CC ECO:0000269|PubMed:18621893, ECO:0000305|PubMed:11830639}.
CC Note=Primarily exported by the accessory SecA2/SecY2 protein
CC translocation apparatus (PubMed:18621893). Distributed in a discrete,
CC punctate pattern with up to 3 loci per cell over the surface
CC (PubMed:18800056). Anchored to the cell wall by sortase A (Probable).
CC {ECO:0000269|PubMed:18621893, ECO:0000269|PubMed:18800056,
CC ECO:0000305|PubMed:11830639}.
CC -!- INDUCTION: Most highly expressed in the transient phase between
CC exponential and stationary growth. A further 2-fold induction occurs in
CC secG or secG/secY2 disruption mutants. {ECO:0000269|PubMed:20472795}.
CC -!- DOMAIN: The non-repeat region (NRR, also called binding region, BR)
CC binds to whole cell lysates of wild-type but not bacteria deleted of
CC this gene; it also recognizes whole cell lysates of S.gordonii strain
CC M99 probably via GspB, but not lysates of S.pneumoniae TIGR4
CC (PubMed:20714350). The NRR is acidic, with a predicted pI of 5.69 in
CC strain ISP479C (PubMed:19202081). The NRR has 4 discrete modules that
CC align end-to-end to form a slightly bent rod. The first is an L-lectin
CC module which binds 1 Ca(2+) ion and N-acetylneuraminic acid (Neu5Ac),
CC and mediates adhesion to human lung epithelial cells (A549 cell line),
CC probably via sialylated receptors. Neu5Ac inhibits binding of A549
CC cells by the NRR domain. The second beta-grasp module adopts a
CC ubiquitin-like beta-grasp fold which resembles the Ig-binding
CC superfamily, while the 2 other modules resemble cadherins; the
CC cadherin-like modules each bind a Ca(2+). Ca(2+) binding rigidifies the
CC cadherin-like modules and extends the molecule (PubMed:24901708).
CC {ECO:0000269|PubMed:20714350, ECO:0000269|PubMed:24901708,
CC ECO:0000303|PubMed:19202081}.
CC -!- PTM: Proteolytically cleaved by a metalloprotease.
CC {ECO:0000269|PubMed:12634333}.
CC -!- PTM: Glycosylated (PubMed:15784571). It is probable that most of the
CC Ser residues in SSR1 and SSR2 are O-GlcNAcylated. Sequential
CC glycosylation by sugar transferases are able to generate complex sugar
CC polymorphisms (By similarity). {ECO:0000250|UniProtKB:A0A0H2URK1,
CC ECO:0000269|PubMed:15784571}.
CC -!- DISRUPTION PHENOTYPE: Decrease in early biofilm formation
CC (PubMed:20714350). About 40% reduction in adhesion to human lung
CC epithelial cells and about 50% reduction in host cell invasion. No
CC significant reduction in biofilm formation or bacterial aggregation
CC (PubMed:24901708). {ECO:0000269|PubMed:20714350,
CC ECO:0000269|PubMed:24901708}.
CC -!- SIMILARITY: Belongs to the serine-rich repeat protein (SRRP) family.
CC {ECO:0000305}.
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DR EMBL; CP000253; ABD31977.1; -; Genomic_DNA.
DR RefSeq; WP_000044531.1; NC_007795.1.
DR RefSeq; YP_501439.1; NC_007795.1.
DR PDB; 4M00; X-ray; 2.05 A; A=245-751.
DR PDB; 4M01; X-ray; 2.10 A; A/B/C/D=245-575.
DR PDB; 4M02; X-ray; 1.59 A; A=494-663.
DR PDB; 4M03; X-ray; 2.24 A; A=576-751.
DR PDBsum; 4M00; -.
DR PDBsum; 4M01; -.
DR PDBsum; 4M02; -.
DR PDBsum; 4M03; -.
DR AlphaFoldDB; Q2FUW1; -.
DR SMR; Q2FUW1; -.
DR STRING; 1280.SAXN108_2926; -.
DR EnsemblBacteria; ABD31977; ABD31977; SAOUHSC_02990.
DR GeneID; 3921472; -.
DR KEGG; sao:SAOUHSC_02990; -.
DR PATRIC; fig|93061.5.peg.2697; -.
DR eggNOG; COG5492; Bacteria.
DR eggNOG; COG5604; Bacteria.
DR HOGENOM; CLU_002109_0_0_9; -.
DR OMA; SSLYSTX; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR022263; KxYKxGKxW.
DR InterPro; IPR019931; LPXTG_anchor.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF19258; KxYKxGKxW_sig; 1.
DR SUPFAM; SSF49313; SSF49313; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR TIGRFAMs; TIGR03715; KxYKxGKxW; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell wall; Glycoprotein;
KW Metal-binding; Peptidoglycan-anchor; Reference proteome; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..89
FT /evidence="ECO:0000305|PubMed:15784571"
FT CHAIN 90..2232
FT /note="Serine-rich adhesin for platelets"
FT /id="PRO_0000273932"
FT PROPEP 2233..2271
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000305|PubMed:11830639"
FT /id="PRO_0000273933"
FT REGION 90..230
FT /note="Serine-rich repeat region 1, SRR1"
FT /evidence="ECO:0000303|PubMed:15784571,
FT ECO:0000303|PubMed:19202081"
FT REGION 100..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..751
FT /note="Non-repeat region (NRR)"
FT /evidence="ECO:0000303|PubMed:15784571,
FT ECO:0000303|PubMed:19202081"
FT REGION 245..491
FT /note="L-lectin module"
FT /evidence="ECO:0000305|PubMed:24901708"
FT REGION 492..571
FT /note="beta-grasp module"
FT /evidence="ECO:0000305|PubMed:24901708"
FT REGION 572..659
FT /note="Cadherin-like module-1"
FT /evidence="ECO:0000305|PubMed:24901708"
FT REGION 660..751
FT /note="Cadherin-like module-2"
FT /evidence="ECO:0000305|PubMed:24901708"
FT REGION 751..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..2232
FT /note="Serine-rich repeat region 2, SRR2"
FT /evidence="ECO:0000303|PubMed:15784571,
FT ECO:0000303|PubMed:19202081"
FT REGION 806..2242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2229..2233
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 806..2228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24901708,
FT ECO:0007744|PDB:4M00, ECO:0007744|PDB:4M01"
FT BINDING 367
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24901708,
FT ECO:0007744|PDB:4M00, ECO:0007744|PDB:4M01"
FT BINDING 369
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24901708,
FT ECO:0007744|PDB:4M00, ECO:0007744|PDB:4M01"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24901708,
FT ECO:0007744|PDB:4M00, ECO:0007744|PDB:4M01"
FT BINDING 573
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24901708,
FT ECO:0007744|PDB:4M00, ECO:0007744|PDB:4M02"
FT BINDING 575
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24901708,
FT ECO:0007744|PDB:4M00, ECO:0007744|PDB:4M02"
FT BINDING 601
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24901708,
FT ECO:0007744|PDB:4M00, ECO:0007744|PDB:4M02"
FT BINDING 602
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24901708,
FT ECO:0007744|PDB:4M00, ECO:0007744|PDB:4M02"
FT BINDING 645
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24901708,
FT ECO:0007744|PDB:4M00, ECO:0007744|PDB:4M02"
FT BINDING 661
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24901708,
FT ECO:0007744|PDB:4M00, ECO:0007744|PDB:4M03"
FT BINDING 663
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24901708,
FT ECO:0007744|PDB:4M00, ECO:0007744|PDB:4M03"
FT BINDING 690
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24901708,
FT ECO:0007744|PDB:4M00, ECO:0007744|PDB:4M03"
FT BINDING 691
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24901708,
FT ECO:0007744|PDB:4M00, ECO:0007744|PDB:4M03"
FT BINDING 734
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24901708,
FT ECO:0007744|PDB:4M00, ECO:0007744|PDB:4M03"
FT MOD_RES 2232
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT MUTAGEN 367
FT /note="Y->G: NRR region no longer binds to host cells."
FT /evidence="ECO:0000269|PubMed:24901708"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:4M00"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:4M00"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:4M00"
FT TURN 280..283
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:4M01"
FT STRAND 295..305
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 310..317
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 331..339
FT /evidence="ECO:0007829|PDB:4M00"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:4M00"
FT TURN 351..355
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:4M00"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:4M00"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 392..398
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:4M00"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:4M00"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:4M00"
FT HELIX 456..461
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 465..474
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 496..503
FT /evidence="ECO:0007829|PDB:4M02"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:4M02"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:4M02"
FT STRAND 514..517
FT /evidence="ECO:0007829|PDB:4M02"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:4M02"
FT HELIX 530..535
FT /evidence="ECO:0007829|PDB:4M02"
FT STRAND 538..547
FT /evidence="ECO:0007829|PDB:4M02"
FT TURN 553..556
FT /evidence="ECO:0007829|PDB:4M02"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:4M02"
FT STRAND 565..573
FT /evidence="ECO:0007829|PDB:4M02"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:4M02"
FT STRAND 584..587
FT /evidence="ECO:0007829|PDB:4M02"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:4M02"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:4M02"
FT STRAND 607..612
FT /evidence="ECO:0007829|PDB:4M02"
FT STRAND 618..621
FT /evidence="ECO:0007829|PDB:4M02"
FT TURN 622..625
FT /evidence="ECO:0007829|PDB:4M02"
FT STRAND 626..629
FT /evidence="ECO:0007829|PDB:4M02"
FT STRAND 635..645
FT /evidence="ECO:0007829|PDB:4M02"
FT STRAND 650..660
FT /evidence="ECO:0007829|PDB:4M02"
FT STRAND 673..676
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 691..694
FT /evidence="ECO:0007829|PDB:4M03"
FT STRAND 697..701
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 707..710
FT /evidence="ECO:0007829|PDB:4M00"
FT TURN 711..714
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 715..718
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 724..733
FT /evidence="ECO:0007829|PDB:4M00"
FT STRAND 739..749
FT /evidence="ECO:0007829|PDB:4M00"
SQ SEQUENCE 2271 AA; 228044 MW; C1813D70A03F8E35 CRC64;
MSKRQKAFHD SLANEKTRVR LYKSGKNWVK SGIKEIEMFK IMGLPFISHS LVSQDNQSIS
KKMTGYGLKT TAVIGGAFTV NMLHDQQAFA ASDAPLTSEL NTQSETVGNQ NSTTIEASTS
TADSTSVTKN SSSVQTSNSD TVSSEKSEKV TSTTNSTSNQ QEKLTSTSES TSSKNTTSSS
DTKSVASTSS TEQPINTSTN QSTASNNTSQ STTPSSVNLN KTSTTSTSTA PVKLRTFSRL
AMSTFASAAT TTAVTANTIT VNKDNLKQYM TTSGNATYDQ STGIVTLTQD AYSQKGAITL
GTRIDSNKSF HFSGKVNLGN KYEGHGNGGD GIGFAFSPGV LGETGLNGAA VGIGGLSNAF
GFKLDTYHNT SKPNSAAKAN ADPSNVAGGG AFGAFVTTDS YGVATTYTSS STADNAAKLN
VQPTNNTFQD FDINYNGDTK VMTVKYAGQT WTRNISDWIA KSGTTNFSLS MTASTGGATN
LQQVQFGTFE YTESAVTQVR YVDVTTGKDI IPPKTYSGNV DQVVTIDNQQ SALTAKGYNY
TSVDSSYAST YNDTNKTVKM TNAGQSVTYY FTDVKAPTVT VGNQTIEVGK TMNPIVLTTT
DNGTGTVTNT VTGLPSGLSY DSATNSIIGT PTKIGQSTVT VVSTDQANNK STTTFTINVV
DTTAPTVTPI GDQSSEVYSP ISPIKIATQD NSGNAVTNTV TGLPSGLTFD STNNTISGTP
TNIGTSTISI VSTDASGNKT TTTFKYEVTR NSMSDSVSTS GSTQQSQSVS TSKADSQSAS
TSTSGSIVVS TSASTSKSTS VSLSDSVSAS KSLSTSESNS VSSSTSTSLV NSQSVSSSMS
DSASKSTSLS DSISNSSSTE KSESLSTSTS DSLRTSTSLS DSLSMSTSGS LSKSQSLSTS
ISGSSSTSAS LSDSTSNAIS TSTSLSESAS TSDSISISNS IANSQSASTS KSDSQSTSIS
LSTSDSKSMS TSESLSDSTS TSGSVSGSLS IAASQSVSTS TSDSMSTSEI VSDSISTSGS
LSASDSKSMS VSSSMSTSQS GSTSESLSDS QSTSDSDSKS LSQSTSQSGS TSTSTSTSAS
VRTSESQSTS GSMSASQSDS MSISTSFSDS TSDSKSASTA SSESISQSAS TSTSGSVSTS
TSLSTSNSER TSTSMSDSTS LSTSESDSIS ESTSTSDSIS EAISASESTF ISLSESNSTS
DSESQSASAF LSESLSESTS ESTSESVSSS TSESTSLSDS TSESGSTSTS LSNSTSGSTS
ISTSTSISES TSTFKSESVS TSLSMSTSTS LSDSTSLSTS LSDSTSDSKS DSLSTSMSTS
DSISTSKSDS ISTSTSLSGS TSESESDSTS SSESKSDSTS MSISMSQSTS GSTSTSTSTS
LSDSTSTSLS LSASMNQSGV DSNSASQSAS NSTSTSTSES DSQSTSSYTS QSTSQSESTS
TSTSLSDSTS ISKSTSQSGS VSTSASLSGS ESESDSQSIS TSASESTSES ASTSLSDSTS
TSNSGSASTS TSLNNSASAS ESDLSSTSLS DSTSASMQSS ESDSQSTSAS LSDSLSTSTS
NRMSTIASLS TSVSTSESGS TSESTSESDS TSTSLSDSQS TSRSTSASGS ASTSTSTSDS
RSTSASTSTS MRTSTSDSQS MSLSTSTSTS MSDSTSLSDS VSDSTSDSTS ASTSGSMSVS
ISLSDSTSTS TSASEVMSAS ISDSQSMSES VNDSESVSES NSESDSKSMS GSTSVSDSGS
LSVSTSLRKS ESVSESSSLS CSQSMSDSVS TSDSSSLSVS TSLRSSESVS ESDSLSDSKS
TSGSTSTSTS GSLSTSTSLS GSESVSESTS LSDSISMSDS TSTSDSDSLS GSISLSGSTS
LSTSDSLSDS KSLSSSQSMS GSESTSTSVS DSQSSSTSNS QFDSMSISAS ESDSMSTSDS
SSISGSNSTS TSLSTSDSMS GSVSVSTSTS LSDSISGSTS VSDSSSTSTS TSLSDSMSQS
QSTSTSASGS LSTSISTSMS MSASTSSSQS TSVSTSLSTS DSISDSTSIS ISGSQSTVES
ESTSDSTSIS DSESLSTSDS DSTSTSTSDS TSGSTSTSIS ESLSTSGSGS TSVSDSTSMS
ESNSSSVSMS QDKSDSTSIS DSESVSTSTS TSLSTSDSTS TSESLSTSMS GSQSISDSTS
TSMSGSTSTS ESNSMHPSDS MSMHHTHSTS TSRLSSEATT STSESQSTLS ATSEVTKHNG
TPAQSEKRLP DTGDSIKQNG LLGGVMTLLV GLGLMKRKKK KDENDQDDSQ A
