SPIKE_CVHOC
ID SPIKE_CVHOC Reviewed; 1353 AA.
AC P36334; Q66199; Q66290; Q66291; Q696Q6; Q6TNF9; Q86623;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
DE Short=S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
DE AltName: Full=E2 {ECO:0000255|HAMAP-Rule:MF_04099};
DE AltName: Full=Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04099};
DE Contains:
DE RecName: Full=Spike protein S1 {ECO:0000255|HAMAP-Rule:MF_04099};
DE Contains:
DE RecName: Full=Spike protein S2 {ECO:0000255|HAMAP-Rule:MF_04099};
DE Contains:
DE RecName: Full=Spike protein S2' {ECO:0000255|HAMAP-Rule:MF_04099};
DE Flags: Precursor;
GN Name=S {ECO:0000255|HAMAP-Rule:MF_04099}; ORFNames=3;
OS Human coronavirus OC43 (HCoV-OC43).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=31631;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8376972; DOI=10.1099/0022-1317-74-9-1981;
RA Mounir S., Talbot P.J.;
RT "Molecular characterization of the S protein gene of human coronavirus
RT OC43.";
RL J. Gen. Virol. 74:1981-1987(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8317096; DOI=10.1006/viro.1993.1360;
RA Kuenkel F., Herrler G.;
RT "Structural and functional analysis of the surface protein of human
RT coronavirus OC43.";
RL Virology 195:195-202(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate AT, Isolate CU, and Isolate VA;
RX PubMed=8712929; DOI=10.1007/bf01718615;
RA Kuenkel F., Herrler G.;
RT "Structural and functional analysis of the S proteins of two human
RT coronavirus OC43 strains adapted to growth in different cells.";
RL Arch. Virol. 141:1123-1131(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate ATCC VR-759;
RX PubMed=15280490; DOI=10.1128/jvi.78.16.8824-8834.2004;
RA St Jean J.R., Jacomy H., Desforges M., Vabret A., Freymuth F., Talbot P.J.;
RT "Human respiratory coronavirus OC43: genetic stability and neuroinvasion.";
RL J. Virol. 78:8824-8834(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate ATCC VR-759;
RX PubMed=15650185; DOI=10.1128/jvi.79.3.1595-1604.2005;
RA Vijgen L., Keyaerts E., Moes E., Thoelen I., Wollants E., Lemey P.,
RA Vandamme A.M., Van Ranst M.;
RT "Complete genomic sequence of human coronavirus OC43: molecular clock
RT analysis suggests a relatively recent zoonotic coronavirus transmission
RT event.";
RL J. Virol. 79:1595-1604(2005).
RN [6]
RP REVIEW.
RX PubMed=11162792; DOI=10.1006/viro.2000.0757;
RA Gallagher T.M., Buchmeier M.J.;
RT "Coronavirus spike proteins in viral entry and pathogenesis.";
RL Virology 279:371-374(2001).
CC -!- FUNCTION: S1 attaches the virion to the cell membrane by interacting
CC with sialic acid-containing cell receptors, initiating the infection.
CC -!- FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane
CC by interacting with host receptor, initiating the infection.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- FUNCTION: [Spike protein S2]: Mediates fusion of the virion and
CC cellular membranes by acting as a class I viral fusion protein. Under
CC the current model, the protein has at least three conformational
CC states: pre-fusion native state, pre-hairpin intermediate state, and
CC post-fusion hairpin state. During viral and target cell membrane
CC fusion, the coiled coil regions (heptad repeats) assume a trimer-of-
CC hairpins structure, positioning the fusion peptide in close proximity
CC to the C-terminal region of the ectodomain. The formation of this
CC structure appears to drive apposition and subsequent fusion of viral
CC and target cell membranes. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- FUNCTION: [Spike protein S2']: Acts as a viral fusion peptide which is
CC unmasked following S2 cleavage occurring upon virus endocytosis.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- SUBUNIT: Homotrimer; each monomer consists of a S1 and a S2 subunit.
CC The resulting peplomers protrude from the virus surface as spikes.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass
CC type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host cell
CC membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_04099}. Note=Accumulates in the
CC endoplasmic reticulum-Golgi intermediate compartment, where it
CC participates in virus particle assembly. Some S oligomers are
CC transported to the host plasma membrane, where they may mediate cell-
CC cell fusion. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- DOMAIN: Fusion peptide 1 (FP1) and fusion peptide 2 (FP2) function
CC cooperatively and have a membrane-ordering effect on lipid headgroups
CC and shallow hydrophobic regions of target bilayers. They are considered
CC as two domains of an extended, bipartite FP. The membrane-ordering
CC activity is calcium-dependent and also dependent on correct folding,
CC which is maintained by an internal disulfide bond in FP2.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC precursor is processed into S1 and S2 by host cell furin or another
CC cellular protease to yield the mature S1 and S2 proteins. Additionally,
CC a second cleavage leads to the release of a fusion peptide after viral
CC attachment to host cell receptor. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike
CC glycoprotein is digested within host endosomes. {ECO:0000255|HAMAP-
CC Rule:MF_04099}.
CC -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB27260.2; Type=Miscellaneous discrepancy; Note=Unknown reason.;
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; L14643; AAA03055.1; -; Genomic_RNA.
DR EMBL; S62886; AAB27260.2; ALT_SEQ; Genomic_RNA.
DR EMBL; Z21849; CAA79896.1; -; Genomic_RNA.
DR EMBL; Z32768; CAA83660.1; -; Genomic_RNA.
DR EMBL; Z32769; CAA83661.1; -; Genomic_RNA.
DR EMBL; AY585228; AAT84354.1; -; Genomic_RNA.
DR EMBL; AY391777; AAR01015.1; -; Genomic_RNA.
DR PIR; A37474; A37474.
DR PIR; JQ2168; JQ2168.
DR PIR; S29998; S29998.
DR PIR; S44240; S44240.
DR PIR; S44241; S44241.
DR PDB; 7M51; X-ray; 1.80 A; A=1232-1246.
DR PDBsum; 7M51; -.
DR SMR; P36334; -.
DR SABIO-RK; P36334; -.
DR Proteomes; UP000007552; Genome.
DR Proteomes; UP000180344; Genome.
DR GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0019031; C:viral envelope; NAS:UniProtKB.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; NAS:UniProtKB.
DR GO; GO:0046789; F:host cell surface receptor binding; TAS:UniProtKB.
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; TAS:UniProtKB.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:UniProtKB-UniRule.
DR CDD; cd21485; HCoV-OC43-like_Spike_S1_RBD; 1.
DR CDD; cd21625; MHV-like_Spike_S1_NTD; 1.
DR Gene3D; 2.60.120.960; -; 1.
DR HAMAP; MF_04099; BETA_CORONA_SPIKE; 1.
DR InterPro; IPR032500; bCoV_S1_N.
DR InterPro; IPR042578; BETA_CORONA_SPIKE.
DR InterPro; IPR043607; CoV_S1_C.
DR InterPro; IPR043473; S2_sf_CoV.
DR InterPro; IPR043002; Spike_N_sf.
DR InterPro; IPR044339; Spike_S1_NTD_MHV-like.
DR InterPro; IPR018548; Spike_S1_RBD_bCoV.
DR InterPro; IPR044372; Spike_S1_RBD_HCoV-OC43-like.
DR InterPro; IPR036326; Spike_S1_RBD_sf_bCoV.
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; PF16451; bCoV_S1_N; 1.
DR Pfam; PF09408; bCoV_S1_RBD; 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 SUPFAM; SSF143587; SSF143587; 1.
DR PROSITE; PS51921; BCOV_S1_CTD; 1.
DR PROSITE; PS51922; BCOV_S1_NTD; 1.
DR PROSITE; PS51923; COV_S2_HR1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW Membrane; Palmitate; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virulence;
KW Virus entry into host cell.
FT SIGNAL 1..13
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CHAIN 14..1353
FT /note="Spike glycoprotein"
FT /id="PRO_0000037205"
FT CHAIN 14..758
FT /note="Spike protein S1"
FT /id="PRO_0000037206"
FT CHAIN 759..1353
FT /note="Spike protein S2"
FT /id="PRO_0000037207"
FT CHAIN 904..1353
FT /note="Spike protein S2'"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000444081"
FT TOPO_DOM 14..1297
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TRANSMEM 1298..1318
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TOPO_DOM 1319..1353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DOMAIN 15..302
FT /note="BetaCoV S1-NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DOMAIN 333..607
FT /note="BetaCoV S1-CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT REGION 904..925
FT /note="Fusion peptide 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 923..943
FT /note="Fusion peptide 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 1004..1054
FT /note="Heptad repeat 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 1248..1286
FT /note="Heptad repeat 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 1033..1077
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 1259..1287
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT MOTIF 1349..1353
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT SITE 758..759
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 903..904
FT /note="Cleavage"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 686
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 704
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 778
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 927
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1184
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1214
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1224
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1243
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1257
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1278
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DISULFID 21..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 164..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 176..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 290..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 335..360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 378..431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 390..605
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 928..939
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT VARIANT 11..13
FT /note="TAF -> MAL (in strain: Isolate VA)"
FT VARIANT 23..25
FT /note="SDN -> TVA (in strain: Isolate VA)"
FT VARIANT 23..25
FT /note="SDN -> TVS (in strain: Isolate CU)"
FT VARIANT 25
FT /note="N -> TSY (in strain: Isolate AT and Isolate ATCC VR-
FT 759)"
FT VARIANT 29
FT /note="K -> I (in strain: Isolate CU)"
FT VARIANT 29
FT /note="K -> V (in strain: Isolate VA)"
FT VARIANT 33..36
FT /note="PPPI -> VPST (in strain: Isolate VA)"
FT VARIANT 33..35
FT /note="PPP -> APS (in strain: Isolate CU)"
FT VARIANT 40
FT /note="T -> I (in strain: Isolate CU and Isolate VA)"
FT VARIANT 62
FT /note="L -> F (in strain: Isolate AT)"
FT VARIANT 63
FT /note="F -> L (in strain: Isolate AT, Isolate CU and
FT Isolate VA)"
FT VARIANT 83..84
FT /note="SV -> TL (in strain: Isolate CU and Isolate VA)"
FT VARIANT 115
FT /note="D -> H (in strain: Isolate VA)"
FT VARIANT 115
FT /note="D -> K (in strain: Isolate CU)"
FT VARIANT 116
FT /note="R -> G (in strain: Isolate AT, Isolate CU and
FT Isolate VA)"
FT VARIANT 143..151
FT /note="RTINSTQDG -> HTTNL (in strain: Isolate CU and
FT Isolate VA)"
FT VARIANT 152
FT /note="D -> Y (in strain: Isolate AT and Isolate ATCC VR-
FT 759)"
FT VARIANT 161
FT /note="V -> I (in strain: Isolate CU and Isolate VA)"
FT VARIANT 167
FT /note="N -> T (in strain: Isolate CU and Isolate VA)"
FT VARIANT 173
FT /note="Q -> H (in strain: Isolate CU)"
FT VARIANT 173
FT /note="Q -> N (in strain: Isolate VA)"
FT VARIANT 183..185
FT /note="HRK -> RRV (in strain: Isolate CU and Isolate VA)"
FT VARIANT 190
FT /note="L -> W (in strain: Isolate CU and Isolate VA)"
FT VARIANT 222
FT /note="T -> I (in strain: Isolate VA)"
FT VARIANT 244..245
FT /note="MA -> TV (in strain: Isolate CU and Isolate VA)"
FT VARIANT 248
FT /note="H -> Y (in strain: Isolate VA)"
FT VARIANT 252
FT /note="M -> L (in strain: Isolate CU)"
FT VARIANT 259..260
FT /note="KL -> AM (in strain: Isolate CU, Isolate ATCC VR-759
FT and Isolate VA)"
FT VARIANT 260
FT /note="L -> VKNGF (in strain: Isolate AT and Isolate ATCC
FT VR-759)"
FT VARIANT 272
FT /note="R -> K (in strain: Isolate CU and Isolate VA)"
FT VARIANT 283
FT /note="I -> V (in strain: Isolate CU and Isolate VA)"
FT VARIANT 288
FT /note="E -> V (in strain: Isolate AT, Isolate ATCC VR-759,
FT Isolate CU and Isolate VA)"
FT VARIANT 291
FT /note="M -> K (in strain: Isolate CU and Isolate VA)"
FT VARIANT 303
FT /note="Q -> L (in strain: Isolate CU and Isolate VA)"
FT VARIANT 308
FT /note="P -> S (in strain: Isolate CU and Isolate VA)"
FT VARIANT 329
FT /note="K -> I (in strain: Isolate CU and Isolate VA)"
FT VARIANT 330
FT /note="P -> L (in strain: Isolate ATCC VR-759)"
FT VARIANT 334
FT /note="N -> D (in strain: Isolate CU and Isolate VA)"
FT VARIANT 451
FT /note="T -> I (in strain: Isolate VA)"
FT VARIANT 454
FT /note="K -> R (in strain: Isolate CU and Isolate VA)"
FT VARIANT 459..461
FT /note="IED -> TEQ (in strain: Isolate CU and Isolate VA)"
FT VARIANT 467
FT /note="R -> Q (in strain: Isolate CU and Isolate VA)"
FT VARIANT 469..474
FT /note="AGVLTN -> VGVFTH (in strain: Isolate CU)"
FT VARIANT 472..474
FT /note="LTN -> FTD (in strain: Isolate VA)"
FT VARIANT 488
FT /note="K -> T (in strain: Isolate CU and Isolate VA)"
FT VARIANT 496
FT /note="N -> D (in strain: Isolate CU and Isolate VA)"
FT VARIANT 499..536
FT /note="CVGSGPGKNNGIGTCPAGTNYLTCDNLCTPDPITFTGT -> LCVGNGPGID
FT AGYKNSGIGTCPAGTNYLTCHNAAQCDCLCTPDPITSKSTGP (in strain:
FT Isolate CU and Isolate VA)"
FT VARIANT 533
FT /note="F -> FKA (in strain: Isolate AT and Isolate ATCC VR-
FT 759)"
FT VARIANT 544
FT /note="S -> Y (in strain: Isolate CU and Isolate VA)"
FT VARIANT 557
FT /note="V -> I (in strain: Isolate CU and Isolate VA)"
FT VARIANT 566
FT /note="S -> P (in strain: Isolate AT, Isolate CU and
FT Isolate VA)"
FT VARIANT 570
FT /note="R -> Q (in strain: Isolate CU and Isolate VA)"
FT VARIANT 579
FT /note="A -> V (in strain: Isolate CU and Isolate VA)"
FT VARIANT 587
FT /note="K -> R (in strain: Isolate CU and Isolate VA)"
FT VARIANT 603
FT /note="L -> T (in strain: Isolate CU and Isolate VA)"
FT VARIANT 612
FT /note="A -> S (in strain: Isolate CU and Isolate VA)"
FT VARIANT 630
FT /note="L -> T (in strain: Isolate CU and Isolate VA)"
FT VARIANT 641
FT /note="T -> P (in strain: Isolate CU and Isolate VA)"
FT VARIANT 664..665
FT /note="II -> LT (in strain: Isolate CU and Isolate VA)"
FT VARIANT 665
FT /note="I -> T (in strain: Isolate AT and Isolate ATCC VR-
FT 759)"
FT VARIANT 694
FT /note="F -> S (in strain: Isolate AT)"
FT VARIANT 700
FT /note="N -> S (in strain: Isolate CU)"
FT VARIANT 706..708
FT /note="SLT -> TLS (in strain: Isolate CU and Isolate VA)"
FT VARIANT 728
FT /note="Y -> D (in strain: Isolate CU and Isolate VA)"
FT VARIANT 732..734
FT /note="AIS -> SSV (in strain: Isolate CU)"
FT VARIANT 733..734
FT /note="IS -> SA (in strain: Isolate VA)"
FT VARIANT 752..753
FT /note="KN -> TK (in strain: Isolate CU and Isolate VA)"
FT VARIANT 758
FT /note="G -> R (in strain: Isolate CU and Isolate VA)"
FT VARIANT 783
FT /note="P -> H (in strain: Isolate VA)"
FT VARIANT 802
FT /note="V -> E (in strain: Isolate AT, Isolate ATCC VR-759,
FT Isolate CU and Isolate VA)"
FT VARIANT 817
FT /note="A -> S (in strain: Isolate CU and Isolate VA)"
FT VARIANT 824
FT /note="Y -> C (in strain: Isolate VA)"
FT VARIANT 833
FT /note="E -> G (in strain: Isolate AT)"
FT VARIANT 884
FT /note="I -> V (in strain: Isolate VA)"
FT VARIANT 896
FT /note="E -> C (in strain: Isolate CU)"
FT VARIANT 898..900
FT /note="SKA -> NKV (in strain: Isolate CU and Isolate VA)"
FT VARIANT 912
FT /note="D -> S (in strain: Isolate CU and Isolate VA)"
FT VARIANT 915
FT /note="K -> R (in strain: Isolate VA)"
FT VARIANT 933
FT /note="E -> G (in strain: Isolate VA)"
FT VARIANT 944
FT /note="K -> N (in strain: Isolate CU and Isolate VA)"
FT VARIANT 955
FT /note="E -> D (in strain: Isolate VA)"
FT VARIANT 955
FT /note="E -> V (in strain: Isolate CU)"
FT VARIANT 969
FT /note="S -> N (in strain: Isolate VA)"
FT VARIANT 973
FT /note="P -> L (in strain: Isolate ATCC VR-759)"
FT VARIANT 975
FT /note="T -> S (in strain: Isolate CU and Isolate VA)"
FT VARIANT 993
FT /note="L -> I (in strain: Isolate CU and Isolate VA)"
FT VARIANT 1012
FT /note="N -> S (in strain: Isolate CU)"
FT VARIANT 1016
FT /note="Y -> D (in strain: Isolate AT, Isolate CU and
FT Isolate VA)"
FT VARIANT 1039
FT /note="N -> D (in strain: Isolate VA)"
FT VARIANT 1058
FT /note="S -> G (in strain: Isolate CU)"
FT VARIANT 1059
FT /note="A -> S (in strain: Isolate CU and Isolate VA)"
FT VARIANT 1074
FT /note="E -> Q (in strain: Isolate CU and Isolate VA)"
FT VARIANT 1089
FT /note="N -> D (in strain: Isolate VA)"
FT VARIANT 1160
FT /note="R -> K (in strain: Isolate CU and Isolate VA)"
FT VARIANT 1189
FT /note="Y -> F (in strain: Isolate CU and Isolate VA)"
FT VARIANT 1193
FT /note="G -> R (in strain: Isolate VA)"
FT VARIANT 1197
FT /note="P -> L (in strain: Isolate AT)"
FT VARIANT 1202
FT /note="E -> G (in strain: Isolate CU and Isolate VA)"
FT VARIANT 1211
FT /note="C -> W (in strain: Isolate AT)"
FT VARIANT 1220
FT /note="Y -> D (in strain: Isolate CU and Isolate VA)"
FT VARIANT 1225..1227
FT /note="TSI -> IST (in strain: Isolate CU and Isolate VA)"
FT VARIANT 1231
FT /note="P -> H (in strain: Isolate CU)"
FT VARIANT 1246
FT /note="S -> L (in strain: Isolate VA)"
FT VARIANT 1265
FT /note="V -> D (in strain: Isolate CU and Isolate VA)"
FT VARIANT 1305..1306
FT /note="CL -> GF (in strain: Isolate CU and Isolate VA)"
FT VARIANT 1331
FT /note="K -> I (in strain: Isolate CU)"
FT VARIANT 1342
FT /note="Y -> H (in strain: Isolate CU and Isolate VA)"
FT VARIANT 1352..1353
FT /note="DD -> EG (in strain: Isolate VA)"
FT HELIX 1233..1241
FT /evidence="ECO:0007829|PDB:7M51"
SQ SEQUENCE 1353 AA; 150089 MW; 7B1CE3CBDB1A902A CRC64;
MFLILLISLP TAFAVIGDLK CTSDNINDKD TGPPPISTDT VDVTNGLGTY YVLDRVYLNT
TLFLNGYYPT SGSTYRNMAL KGSVLLSRLW FKPPFLSDFI NGIFAKVKNT KVIKDRVMYS
EFPAITIGST FVNTSYSVVV QPRTINSTQD GDNKLQGLLE VSVCQYNMCE YPQTICHPNL
GNHRKELWHL DTGVVSCLYK RNFTYDVNAD YLYFHFYQEG GTFYAYFTDT GVVTKFLFNV
YLGMALSHYY VMPLTCNSKL TLEYWVTPLT SRQYLLAFNQ DGIIFNAEDC MSDFMSEIKC
KTQSIAPPTG VYELNGYTVQ PIADVYRRKP NLPNCNIEAW LNDKSVPSPL NWERKTFSNC
NFNMSSLMSF IQADSFTCNN IDAAKIYGMC FSSITIDKFA IPNGRKVDLQ LGNLGYLQSF
NYRIDTTATS CQLYYNLPAA NVSVSRFNPS TWNKRFGFIE DSVFKPRPAG VLTNHDVVYA
QHCFKAPKNF CPCKLNGSCV GSGPGKNNGI GTCPAGTNYL TCDNLCTPDP ITFTGTYKCP
QTKSLVGIGE HCSGLAVKSD YCGGNSCTCR PQAFLGWSAD SCLQGDKCNI FANFILHDVN
SGLTCSTDLQ KANTDIILGV CVNYDLYGIL GQGIFVEVNA TYYNSWQNLL YDSNGNLYGF
RDYIINRTFM IRSCYSGRVS AAFHANSSEP ALLFRNIKCN YVFNNSLTRQ LQPINYFDSY
LGCVVNAYNS TAISVQTCDL TVGSGYCVDY SKNRRSRGAI TTGYRFTNFE PFTVNSVNDS
LEPVGGLYEI QIPSEFTIGN MVEFIQTSSP KVTIDCAAFV CGDYAACKSQ LVEYGSFCDN
INAILTEVNE LLDTTQLQVA NSLMNGVTLS TKLKDGVNFN VDDINFSPVL GCLGSECSKA
SSRSAIEDLL FDKVKLSDVG FVEAYNNCTG GAEIRDLICV QSYKGIKVLP PLLSENQISG
YTLAATSASL FPPWTAAAGV PFYLNVQYRI NGLGVTMDVL SQNQKLIANA FNNALYAIQE
GFDATNSALV KIQAVVNANA EALNNLLQQL SNRFGAISAS LQEILSRLDA LEAEAQIDRL
INGRLTALNA YVSQQLSDST LVKFSAAQAM EKVNECVKSQ SSRINFCGNG NHIISLVQNA
PYGLYFIHFS YVPTKYVTAR VSPGLCIAGD RGIAPKSGYF VNVNNTWMYT GSGYYYPEPI
TENNVVVMST CAVNYTKAPY VMLNTSIPNL PDFKEELDQW FKNQTSVAPD LSLDYINVTF
LDLQVEMNRL QEAIKVLNQS YINLKDIGTY EYYVKWPWYV WLLICLAGVA MLVLLFFICC
CTGCGTSCFK KCGGCCDDYT GYQELVIKTS HDD