SPIKE_CVHNL
ID SPIKE_CVHNL Reviewed; 1356 AA.
AC Q6Q1S2; Q5DIX7; Q5DIX8; Q5DIX9; Q5DIY0; Q6R1L7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04200};
DE Short=S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04200};
DE AltName: Full=E2 {ECO:0000255|HAMAP-Rule:MF_04200};
DE AltName: Full=Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04200};
DE Flags: Precursor;
GN Name=S {ECO:0000255|HAMAP-Rule:MF_04200}; ORFNames=2;
OS Human coronavirus NL63 (HCoV-NL63).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Setracovirus.
OX NCBI_TaxID=277944;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15034574; DOI=10.1038/nm1024;
RA Van Der Hoek L., Pyrc K., Jebbink M.F., Vermeulen-Oost W., Berkhout R.J.,
RA Wolthers K.C., Wertheim-Van Dillen P.M., Kaandorp J., Spaargaren J.,
RA Berkhout B.;
RT "Identification of a new human coronavirus.";
RL Nat. Med. 10:368-373(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA van der Hoek L., Pyrc K., Jebbink M.F., Vermeulen-Oost W., Berkhout R.J.M.,
RA Wolthers K.C., Wertheim-van Dillen P.M.E., Kaandorp J., Spaargaren J.,
RA Berkhout B.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate NL;
RX PubMed=15073334; DOI=10.1073/pnas.0400762101;
RA Fouchier R.A., Hartwig N.G., Bestebroer T.M., Niemeyer B., De Jong J.C.,
RA Simon J.H., Osterhaus A.D.;
RT "A previously undescribed coronavirus associated with respiratory disease
RT in humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:6212-6216(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate NL;
RA Fouchier R.A.M., Bestebroer T.M., de Jong J.C., Niemeyer B., Simon J.H.,
RA Osterhaus A.D.M.E.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-193.
RC STRAIN=Isolate BE03-1153, Isolate BE03-21596, Isolate BE03-40001, and
RC Isolate BE03-64880;
RA Moes E., Vijgen L., Keyaerts E., Zlateva K., Meurs M., Pyrc K.,
RA Berkhout B., van der Hoek L., Van Ranst M.;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND INTERACTION WITH HUMAN ACE2.
RX PubMed=15897467; DOI=10.1073/pnas.0409465102;
RA Hofmann H., Pyrc K., van der Hoek L., Geier M., Berkhout B., Poehlmann S.;
RT "Human coronavirus NL63 employs the severe acute respiratory syndrome
RT coronavirus receptor for cellular entry.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7988-7993(2005).
RN [7]
RP FUNCTION.
RX PubMed=29142129; DOI=10.1128/jvi.01933-17;
RA Milewska A., Nowak P., Owczarek K., Szczepanski A., Zarebski M., Hoang A.,
RA Berniak K., Wojarski J., Zeglen S., Baster Z., Rajfur Z., Pyrc K.;
RT "Entry of Human Coronavirus NL63 into the Cell.";
RL J. Virol. 92:0-0(2018).
RN [8] {ECO:0007744|PDB:2IEQ}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 981-1038 AND 1242-1283.
RX PubMed=17176042; DOI=10.1021/bi061686w;
RA Zheng Q., Deng Y., Liu J., van der Hoek L., Berkhout B., Lu M.;
RT "Core structure of S2 from the human coronavirus NL63 spike glycoprotein.";
RL Biochemistry 45:15205-15215(2006).
RN [9] {ECO:0007744|PDB:3KBH}
RP X-RAY CRYSTALLOGRAPHY (3.31 ANGSTROMS) OF 481-616, GLYCOSYLATION AT ASN-486
RP AND ASN-512, INTERACTION WITH HUMAN ACE2, FUNCTION, AND DISULFIDE BOND.
RX PubMed=19901337; DOI=10.1073/pnas.0908837106;
RA Wu K., Li W., Peng G., Li F.;
RT "Crystal structure of NL63 respiratory coronavirus receptor-binding domain
RT complexed with its human receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19970-19974(2009).
RN [10] {ECO:0007744|PDB:5SZS}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF 16-1291, DISULFIDE
RP BOND, AND GLYCOSYLATION AT ASN-35; ASN-52; ASN-98; ASN-155; ASN-187;
RP ASN-193; ASN-240; ASN-276; ASN-301; ASN-330; ASN-354; ASN-358; ASN-403;
RP ASN-426; ASN-486; ASN-506; ASN-512; ASN-626; ASN-645; ASN-666; ASN-699;
RP ASN-723; ASN-749; ASN-762; ASN-768; ASN-1111; ASN-1196; ASN-1201; ASN-1218;
RP ASN-1242; ASN-1247 AND ASN-1277.
RX PubMed=27617430; DOI=10.1038/nsmb.3293;
RA Walls A.C., Tortorici M.A., Frenz B., Snijder J., Li W., Rey F.A.,
RA DiMaio F., Bosch B.J., Veesler D.;
RT "Glycan shield and epitope masking of a coronavirus spike protein observed
RT by cryo-electron microscopy.";
RL Nat. Struct. Mol. Biol. 23:899-905(2016).
CC -!- FUNCTION: S1 region attaches the virion to the cell membrane by
CC interacting with host ACE2, initiating the infection (PubMed:15897467,
CC PubMed:29142129, PubMed:19901337). Binding to the receptor probably
CC induces conformational changes in the S glycoprotein unmasking the
CC fusion peptide and activating membranes fusion. S2 region belongs to
CC the class I viral fusion protein. Under the current model, the protein
CC has at least 3 conformational states: pre-fusion native state, pre-
CC hairpin intermediate state, and post-fusion hairpin state. During viral
CC and target cell membrane fusion, the coiled coil regions (heptad
CC repeats) regions assume a trimer-of-hairpins structure, positioning the
CC fusion peptide in close proximity to the C-terminal region of the
CC ectodomain. The formation of this structure appears to drive apposition
CC and subsequent fusion of viral and target cell membranes.
CC {ECO:0000255|HAMAP-Rule:MF_04200, ECO:0000269|PubMed:15897467,
CC ECO:0000269|PubMed:19901337, ECO:0000269|PubMed:29142129}.
CC -!- SUBUNIT: Homotrimer. During virus morphogenesis, found in a complex
CC with M proteins (By similarity). Interacts with host
CC ACE2(PubMed:15897467). {ECO:0000255|HAMAP-Rule:MF_04200,
CC ECO:0000269|PubMed:15897467}.
CC -!- INTERACTION:
CC Q6Q1S2; Q9BYF1: ACE2; Xeno; NbExp=9; IntAct=EBI-15814420, EBI-7730807;
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04200}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04200}. Host endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000255|HAMAP-Rule:MF_04200}; Single-pass
CC type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04200}.
CC Note=Accumulates in the endoplasmic reticulum-Golgi intermediate
CC compartment, where it participates in virus particle assembly.
CC {ECO:0000255|HAMAP-Rule:MF_04200}.
CC -!- DOMAIN: The KxHxx motif seems to function as an ER retrieval signal.
CC {ECO:0000255|HAMAP-Rule:MF_04200}.
CC -!- PTM: Glycosylated by host with heterogeneous N-linked glycans
CC protruding from the trimer surface (PubMed:19901337, PubMed:27617430).
CC Highly glycosylated by host, occluding many regions across the surface
CC of the protein (PubMed:27617430). {ECO:0000269|PubMed:19901337,
CC ECO:0000269|PubMed:27617430}.
CC -!- SIMILARITY: Belongs to the alphacoronaviruses spike protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04200}.
CC -!- CAUTION: In contrast to beta- and gammacoronaviruses, S glycoprotein is
CC not cleaved into S1 and S2. {ECO:0000255|HAMAP-Rule:MF_04200}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY567487; AAS58177.1; -; Genomic_RNA.
DR EMBL; AY518894; AAS89767.1; -; Genomic_RNA.
DR EMBL; AY758297; AAW66968.1; ALT_TERM; Genomic_RNA.
DR EMBL; AY758298; AAW66969.1; ALT_TERM; Genomic_RNA.
DR EMBL; AY758300; AAW66970.1; ALT_TERM; Genomic_RNA.
DR EMBL; AY758301; AAW66971.1; ALT_TERM; Genomic_RNA.
DR RefSeq; YP_003767.1; NC_005831.2.
DR PDB; 2IEQ; X-ray; 1.75 A; A/B/C=981-1037, A/B/C=1242-1283.
DR PDB; 3KBH; X-ray; 3.31 A; E/F/G/H=481-616.
DR PDB; 5SZS; EM; 3.40 A; A/B/C=16-1291.
DR PDB; 7FC3; X-ray; 3.19 A; E=481-611.
DR PDB; 7KIP; EM; 3.39 A; A/B/C=1-1356.
DR PDBsum; 2IEQ; -.
DR PDBsum; 3KBH; -.
DR PDBsum; 5SZS; -.
DR PDBsum; 7FC3; -.
DR PDBsum; 7KIP; -.
DR SMR; Q6Q1S2; -.
DR DIP; DIP-49012N; -.
DR IntAct; Q6Q1S2; 2.
DR DNASU; 2943499; -.
DR GeneID; 2943499; -.
DR KEGG; vg:2943499; -.
DR SABIO-RK; Q6Q1S2; -.
DR EvolutionaryTrace; Q6Q1S2; -.
DR Proteomes; UP000008573; Genome.
DR Proteomes; UP000161757; Genome.
DR GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046789; F:host cell surface receptor binding; IPI:BHF-UCL.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IDA:BHF-UCL.
DR HAMAP; MF_04200; ALPHA_CORONA_SPIKE; 1.
DR InterPro; IPR042552; ALPHA_CORONA_SPIKE.
DR InterPro; IPR043607; CoV_S1_C.
DR InterPro; IPR043473; S2_sf_CoV.
DR InterPro; IPR002551; Spike_S1_CoV.
DR InterPro; IPR002552; Spike_S2_CoV.
DR InterPro; IPR043614; Spike_S2_CoV_C.
DR InterPro; IPR044873; Spike_S2_CoV_HR1.
DR InterPro; IPR044874; Spike_S2_CoV_HR2.
DR Pfam; PF01600; CoV_S1; 1.
DR Pfam; PF19209; CoV_S1_C; 1.
DR Pfam; PF01601; CoV_S2; 1.
DR Pfam; PF19214; CoV_S2_C; 1.
DR SUPFAM; SSF111474; SSF111474; 2.
DR PROSITE; PS51923; COV_S2_HR1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Disulfide bond; Glycoprotein; Host membrane;
KW Host-virus interaction; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Virion; Virulence; Virus entry into host cell.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT CHAIN 19..1356
FT /note="Spike glycoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT /id="PRO_0000037204"
FT TOPO_DOM 19..1296
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TRANSMEM 1297..1316
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT TOPO_DOM 1317..1356
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 16..717
FT /note="S1"
FT REGION 19..717
FT /note="S1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 598..728
FT /note="Interaction with host ANPEP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 718..1356
FT /note="S2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 934..954
FT /note="Fusion peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT REGION 948..1067
FT /note="Heptad repeat 1 (HR1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01271"
FT REGION 1212..1308
FT /note="Heptad repeat 2 (HR2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01272"
FT COILED 1015..1059
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT COILED 1244..1286
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT MOTIF 1352..1356
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04200"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:19901337,
FT ECO:0000269|PubMed:27617430"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:19901337,
FT ECO:0000269|PubMed:27617430"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 699
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 723
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 762
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 768
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 1111
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 1196
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 1201
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 1218
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 1242
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 1247
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT CARBOHYD 1277
FT /note="N-linked (GlcNAc) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:27617430"
FT DISULFID 106..126
FT /evidence="ECO:0000269|PubMed:27617430"
FT DISULFID 175..181
FT /evidence="ECO:0000269|PubMed:27617430"
FT DISULFID 207..210
FT /evidence="ECO:0000269|PubMed:27617430"
FT DISULFID 259..284
FT /evidence="ECO:0000269|PubMed:27617430"
FT DISULFID 328..351
FT /evidence="ECO:0000269|PubMed:27617430"
FT DISULFID 438..447
FT /evidence="ECO:0000269|PubMed:27617430"
FT DISULFID 497..500
FT /evidence="ECO:0000269|PubMed:19901337"
FT DISULFID 516..567
FT /evidence="ECO:0000269|PubMed:19901337,
FT ECO:0000269|PubMed:27617430"
FT DISULFID 550..577
FT /evidence="ECO:0000269|PubMed:19901337,
FT ECO:0000269|PubMed:27617430"
FT DISULFID 627..678
FT /evidence="ECO:0000269|PubMed:27617430"
FT DISULFID 724..737
FT /evidence="ECO:0000269|PubMed:27617430"
FT DISULFID 789..811
FT /evidence="ECO:0000269|PubMed:27617430"
FT DISULFID 794..800
FT /evidence="ECO:0000269|PubMed:27617430"
FT DISULFID 896..907
FT /evidence="ECO:0000269|PubMed:27617430"
FT DISULFID 1098..1109
FT /evidence="ECO:0000269|PubMed:27617430"
FT VARIANT 9
FT /note="V -> I (in strain: Isolate BE03-40001 and Isolate
FT NL)"
FT VARIANT 13
FT /note="A -> V (in strain: Isolate BE03-40001 and Isolate
FT NL)"
FT VARIANT 17
FT /note="F -> S (in strain: Isolate BE03-40001 and Isolate
FT NL)"
FT VARIANT 24..25
FT /note="NL -> SI (in strain: Isolate BE03-40001 and Isolate
FT NL)"
FT VARIANT 46
FT /note="T -> V (in strain: Isolate BE03-40001 and Isolate
FT NL)"
FT VARIANT 49
FT /note="F -> I (in strain: Isolate BE03-1153, Isolate BE03-
FT 40001, Isolate BE03-64880 and Isolate NL)"
FT VARIANT 57..59
FT /note="VYS -> SYP (in strain: Isolate BE03-40001 and
FT Isolate NL)"
FT VARIANT 70
FT /note="N -> K (in strain: Isolate BE03-40001 and Isolate
FT NL)"
FT VARIANT 79
FT /note="T -> S (in strain: Isolate BE03-40001 and Isolate
FT NL)"
FT VARIANT 84
FT /note="A -> V (in strain: Isolate BE03-1153 and Isolate
FT BE03-64880)"
FT VARIANT 91
FT /note="V -> L (in strain: Isolate BE03-40001 and Isolate
FT NL)"
FT VARIANT 94..96
FT /note="EIG -> KIH (in strain: Isolate BE03-40001 and
FT Isolate NL)"
FT VARIANT 100
FT /note="S -> P (in strain: Isolate BE03-40001 and Isolate
FT NL)"
FT VARIANT 109..110
FT /note="SR -> GI (in strain: Isolate BE03-1153 and Isolate
FT BE03-64880 and Isolate NL)"
FT VARIANT 109
FT /note="S -> G (in strain: Isolate BE03-40001 and Isolate
FT NL)"
FT VARIANT 110
FT /note="Missing (in strain: Isolate BE03-40001 and Isolate
FT NL)"
FT VARIANT 113
FT /note="T -> S (in strain: Isolate BE03-40001 and Isolate
FT NL)"
FT VARIANT 120..124
FT /note="ASSSF -> VSTSH (in strain: Isolate BE03-40001 and
FT Isolate NL)"
FT VARIANT 125
FT /note="D -> H (in strain: Isolate BE03-40001)"
FT VARIANT 130
FT /note="L -> S (in strain: Isolate BE03-40001)"
FT VARIANT 131
FT /note="L -> S (in strain: Isolate BE03-40001 and Isolate
FT NL)"
FT VARIANT 138
FT /note="A -> V (in strain: Isolate BE03-40001 and Isolate
FT NL)"
FT VARIANT 156
FT /note="V -> A (in strain: Isolate BE03-40001 and Isolate
FT NL)"
FT VARIANT 178..179
FT /note="NY -> SE (in strain: Isolate BE03-40001 and Isolate
FT NL)"
FT VARIANT 190
FT /note="V -> I (in strain: Isolate NL)"
FT VARIANT 197
FT /note="H -> L (in strain: Isolate NL)"
FT VARIANT 201
FT /note="V -> I (in strain: Isolate NL)"
FT VARIANT 293
FT /note="V -> A (in strain: Isolate NL)"
FT VARIANT 302
FT /note="F -> L (in strain: Isolate NL)"
FT VARIANT 307
FT /note="L -> V (in strain: Isolate NL)"
FT VARIANT 503
FT /note="H -> R (in strain: Isolate NL)"
FT VARIANT 730
FT /note="T -> I (in strain: Isolate NL)"
FT VARIANT 863
FT /note="R -> H (in strain: Isolate NL)"
FT VARIANT 999
FT /note="Q -> H (in strain: Isolate NL)"
FT VARIANT 1044
FT /note="Q -> H (in strain: Isolate NL)"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 88..108
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 123..134
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 246..263
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 310..318
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 323..332
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 350..357
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 360..368
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 398..404
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 412..428
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 431..437
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 441..449
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 471..474
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 482..492
FT /evidence="ECO:0007829|PDB:7FC3"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:7FC3"
FT TURN 498..500
FT /evidence="ECO:0007829|PDB:7FC3"
FT STRAND 503..509
FT /evidence="ECO:0007829|PDB:7FC3"
FT STRAND 512..516
FT /evidence="ECO:0007829|PDB:7FC3"
FT STRAND 519..530
FT /evidence="ECO:0007829|PDB:7FC3"
FT TURN 536..539
FT /evidence="ECO:0007829|PDB:7FC3"
FT STRAND 540..545
FT /evidence="ECO:0007829|PDB:7FC3"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:7FC3"
FT HELIX 554..557
FT /evidence="ECO:0007829|PDB:7FC3"
FT TURN 558..560
FT /evidence="ECO:0007829|PDB:7FC3"
FT STRAND 562..571
FT /evidence="ECO:0007829|PDB:7FC3"
FT STRAND 577..585
FT /evidence="ECO:0007829|PDB:7FC3"
FT STRAND 588..608
FT /evidence="ECO:0007829|PDB:7FC3"
FT STRAND 628..632
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 635..644
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 652..655
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 661..665
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 672..676
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 682..687
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 690..700
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 707..711
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 714..719
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 727..731
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 734..737
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 742..744
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 758..779
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 785..787
FT /evidence="ECO:0007829|PDB:5SZS"
FT TURN 789..793
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 800..803
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 804..807
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 808..832
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 837..842
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 845..847
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 849..851
FT /evidence="ECO:0007829|PDB:5SZS"
FT TURN 854..856
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 863..865
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 872..881
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 893..897
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 905..910
FT /evidence="ECO:0007829|PDB:5SZS"
FT TURN 911..913
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 914..916
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 923..935
FT /evidence="ECO:0007829|PDB:5SZS"
FT TURN 936..938
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 941..943
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 950..959
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 983..1029
FT /evidence="ECO:0007829|PDB:2IEQ"
FT HELIX 1031..1033
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 1037..1039
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 1043..1047
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 1052..1098
FT /evidence="ECO:0007829|PDB:5SZS"
FT TURN 1099..1101
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 1108..1122
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 1125..1145
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 1147..1149
FT /evidence="ECO:0007829|PDB:5SZS"
FT TURN 1150..1152
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 1153..1159
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 1162..1167
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 1170..1178
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 1186..1188
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 1189..1191
FT /evidence="ECO:0007829|PDB:5SZS"
FT STRAND 1197..1202
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 1206..1209
FT /evidence="ECO:0007829|PDB:5SZS"
FT HELIX 1217..1223
FT /evidence="ECO:0007829|PDB:5SZS"
SQ SEQUENCE 1356 AA; 149850 MW; 8699E079BB0D54B7 CRC64;
MKLFLILLVL PLASCFFTCN SNANLSMLQL GVPDNSSTIV TGLLPTHWFC ANQSTSVYSA
NGFFYIDVGN HRSAFALHTG YYDANQYYIY VTNEIGLNAS VTLKICKFSR NTTFDFLSNA
SSSFDCIVNL LFTEQLGAPL GITISGETVR LHLYNVTRTF YVPAAYKLTK LSVKCYFNYS
CVFSVVNATV TVNVTTHNGR VVNYTVCDDC NGYTDNIFSV QQDGRIPNGF PFNNWFLLTN
GSTLVDGVSR LYQPLRLTCL WPVPGLKSST GFVYFNATGS DVNCNGYQHN SVVDVMRYNL
NFSANSLDNL KSGVIVFKTL QYDVLFYCSN SSSGVLDTTI PFGPSSQPYY CFINSTINTT
HVSTFVGILP PTVREIVVAR TGQFYINGFK YFDLGFIEAV NFNVTTASAT DFWTVAFATF
VDVLVNVSAT NIQNLLYCDS PFEKLQCEHL QFGLQDGFYS ANFLDDNVLP ETYVALPIYY
QHTDINFTAT ASFGGSCYVC KPHQVNISLN GNTSVCVRTS HFSIRYIYNR VKSGSPGDSS
WHIYLKSGTC PFSFSKLNNF QKFKTICFST VEVPGSCNFP LEATWHYTSY TIVGALYVTW
SEGNSITGVP YPVSGIREFS NLVLNNCTKY NIYDYVGTGI IRSSNQSLAG GITYVSNSGN
LLGFKNVSTG NIFIVTPCNQ PDQVAVYQQS IIGAMTAVNE SRYGLQNLLQ LPNFYYVSNG
GNNCTTAVMT YSNFGICADG SLIPVRPRNS SDNGISAIIT ANLSIPSNWT TSVQVEYLQI
TSTPIVVDCA TYVCNGNPRC KNLLKQYTSA CKTIEDALRL SAHLETNDVS SMLTFDSNAF
SLANVTSFGD YNLSSVLPQR NIRSSRIAGR SALEDLLFSK VVTSGLGTVD VDYKSCTKGL
SIADLACAQY YNGIMVLPGV ADAERMAMYT GSLIGGMVLG GLTSAAAIPF SLALQARLNY
VALQTDVLQE NQKILAASFN KAINNIVASF SSVNDAITQT AEAIHTVTIA LNKIQDVVNQ
QGSALNHLTS QLRHNFQAIS NSIQAIYDRL DSIQADQQVD RLITGRLAAL NAFVSQVLNK
YTEVRGSRRL AQQKINECVK SQSNRYGFCG NGTHIFSIVN SAPDGLLFLH TVLLPTDYKN
VKAWSGICVD GIYGYVLRQP NLVLYSDNGV FRVTSRVMFQ PRLPVLSDFV QIYNCNVTFV
NISRVELHTV IPDYVDVNKT LQEFAQNLPK YVKPNFDLTP FNLTYLNLSS ELKQLEAKTA
SLFQTTVELQ GLIDQINSTY VDLKLLNRFE NYIKWPWWVW LIISVVFVVL LSLLVFCCLS
TGCCGCCNCL TSSMRGCCDC GSTKLPYYEF EKVHVQ
