PGLB_CAMLR
ID PGLB_CAMLR Reviewed; 712 AA.
AC B9KDD4;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Undecaprenyl-diphosphooligosaccharide--protein glycotransferase;
DE EC=2.4.99.19;
DE AltName: Full=Protein glycosylation B;
GN Name=pglB; OrderedLocusNames=Cla_1253;
OS Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=306263;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM2100 / D67 / ATCC BAA-1060;
RX PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT "The complete genome sequence and analysis of the human pathogen
RT Campylobacter lari.";
RL Foodborne Pathog. Dis. 5:371-386(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23382388; DOI=10.1074/jbc.m112.445940;
RA Gerber S., Lizak C., Michaud G., Bucher M., Darbre T., Aebi M.,
RA Reymond J.L., Locher K.P.;
RT "Mechanism of bacterial oligosaccharyltransferase: in vitro quantification
RT of sequon binding and catalysis.";
RL J. Biol. Chem. 288:8849-8861(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24149797; DOI=10.1038/ncomms3627;
RA Lizak C., Gerber S., Michaud G., Schubert M., Fan Y.Y., Bucher M.,
RA Darbre T., Aebi M., Reymond J.L., Locher K.P.;
RT "Unexpected reactivity and mechanism of carboxamide activation in bacterial
RT N-linked protein glycosylation.";
RL Nat. Commun. 4:2627-2627(2013).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 3-712 IN COMPLEX WITH MAGNESIUM
RP AND AN ACCEPTOR PEPTIDE, COFACTOR, FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF ASP-56; ASP-154 AND GLU-319, AND GLYCOSYLATION AT ASN-535
RP AND ASN-556.
RX PubMed=21677752; DOI=10.1038/nature10151;
RA Lizak C., Gerber S., Numao S., Aebi M., Locher K.P.;
RT "X-ray structure of a bacterial oligosaccharyltransferase.";
RL Nature 474:350-355(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH MANGANESE;
RP LIPID-LINKED OLIGOSACCHARIDE AND AN ACCEPTOR PEPTIDE, AND MUTAGENESIS OF
RP TYR-196 AND TYR-468.
RX PubMed=29058712; DOI=10.1038/nsmb.3491;
RA Napiorkowska M., Boilevin J., Sovdat T., Darbre T., Reymond J.L., Aebi M.,
RA Locher K.P.;
RT "Molecular basis of lipid-linked oligosaccharide recognition and processing
RT by bacterial oligosaccharyltransferase.";
RL Nat. Struct. Mol. Biol. 24:1100-1106(2017).
CC -!- FUNCTION: Oligosaccharyl transferase (OST) that catalyzes the initial
CC transfer of a defined glycan (GalNAc(2)GlcGalNAc(3)Bac(NAc)(2) in
CC eubacteria, where Bac(NAc)(2) is di-N-acetyl bacillosamine) from the
CC lipid carrier undecaprenol-pyrophosphate to an asparagine residue
CC within an Asp/Glu-Asn-X-Ser/Thr consensus motif in nascent polypeptide
CC chains, the first step in protein N-glycosylation.
CC {ECO:0000269|PubMed:21677752, ECO:0000269|PubMed:24149797}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tritrans,heptacis-undecaprenyl diphosphooligosaccharide +
CC [protein]-L-asparagine = tritrans,heptacis-undecaprenyl diphosphate +
CC a glycoprotein with the oligosaccharide chain attached by N-beta-D-
CC glycosyl linkage to protein L-asparagine.; EC=2.4.99.19;
CC Evidence={ECO:0000269|PubMed:21677752, ECO:0000269|PubMed:24149797};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21677752};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:21677752, ECO:0000269|PubMed:29058712};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 uM for an Asp-Gln-Asn-Ala-Thr pentapeptide
CC {ECO:0000269|PubMed:23382388};
CC Note=Glycosylates at a rate of 1.55 peptides per second per OST.
CC {ECO:0000269|PubMed:23382388};
CC pH dependence:
CC Optimum pH is 6.8. {ECO:0000269|PubMed:24149797};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:23382388}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:21677752}.
CC -!- DOMAIN: Despite low primary sequence conservation between eukaryotic
CC catalytic subunits and bacterial and archaeal single subunit OSTs
CC (ssOST), structural comparison revealed several common motifs at
CC spatially equivalent positions, like the DXD motif 1 on the external
CC loop 1 and the DXD motif 2 on the external loop 2 involved in binding
CC of the metal ion cofactor and the carboxamide group of the acceptor
CC asparagine, the conserved Glu residue of the TIXE/SVSE motif on the
CC external loop 5 involved in catalysis, as well as the WWDYG and the
CC DK/MI motifs in the globular domain that define the binding pocket for
CC the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg
CC residue was found to interact with a negatively charged side chain at
CC the -2 position of the sequon. This Arg is conserved in bacterial
CC enzymes and correlates with an extended sequon requirement (Asp-X-Asn-
CC X-Ser/Thr) for bacterial N-glycosylation.
CC {ECO:0000305|PubMed:29058712}.
CC -!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
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DR EMBL; CP000932; ACM64573.1; -; Genomic_DNA.
DR RefSeq; WP_012661956.1; NC_012039.1.
DR PDB; 3RCE; X-ray; 3.40 A; A=1-712.
DR PDB; 5OGL; X-ray; 2.70 A; A=1-712.
DR PDB; 6GXC; X-ray; 3.40 A; A=1-712.
DR PDBsum; 3RCE; -.
DR PDBsum; 5OGL; -.
DR PDBsum; 6GXC; -.
DR AlphaFoldDB; B9KDD4; -.
DR SMR; B9KDD4; -.
DR DIP; DIP-59188N; -.
DR STRING; 306263.Cla_1253; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR TCDB; 9.B.142.3.11; the integral membrane glycosyltransferase family 39 (gt39) family.
DR iPTMnet; B9KDD4; -.
DR EnsemblBacteria; ACM64573; ACM64573; CLA_1253.
DR GeneID; 7410986; -.
DR KEGG; cla:CLA_1253; -.
DR PATRIC; fig|306263.5.peg.1240; -.
DR eggNOG; COG1287; Bacteria.
DR HOGENOM; CLU_024679_0_0_7; -.
DR OMA; GYPIRYY; -.
DR OrthoDB; 702825at2; -.
DR BRENDA; 2.4.99.19; 13108.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000007727; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004576; F:oligosaccharyl transferase activity; IEA:InterPro.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
DR DisProt; DP01199; -.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR InterPro; IPR041563; STT3_PglB_C.
DR PANTHER; PTHR13872; PTHR13872; 1.
DR Pfam; PF02516; STT3; 1.
DR Pfam; PF18527; STT3_PglB_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Glycoprotein;
KW Glycosyltransferase; Magnesium; Manganese; Membrane; Metal-binding;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..712
FT /note="Undecaprenyl-diphosphooligosaccharide--protein
FT glycotransferase"
FT /id="PRO_0000422589"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21677752"
FT TRANSMEM 13..37
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21677752"
FT TOPO_DOM 38..98
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:21677752"
FT TRANSMEM 99..124
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21677752"
FT TOPO_DOM 125..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21677752"
FT TRANSMEM 128..146
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21677752"
FT TOPO_DOM 147..154
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:21677752"
FT TRANSMEM 155..176
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21677752"
FT TOPO_DOM 177..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21677752"
FT TRANSMEM 179..194
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21677752"
FT TOPO_DOM 195..199
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:21677752"
FT TRANSMEM 200..217
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21677752"
FT TOPO_DOM 218..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21677752"
FT TRANSMEM 223..235
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21677752"
FT TOPO_DOM 236..239
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:21677752"
FT TRANSMEM 240..256
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21677752"
FT TOPO_DOM 257..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21677752"
FT TRANSMEM 263..280
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21677752"
FT TOPO_DOM 281..327
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:21677752"
FT TRANSMEM 328..350
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21677752"
FT TOPO_DOM 351..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21677752"
FT TRANSMEM 356..372
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21677752"
FT TOPO_DOM 373..376
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:21677752"
FT TRANSMEM 377..399
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21677752"
FT TOPO_DOM 400..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21677752"
FT TRANSMEM 408..432
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21677752"
FT TOPO_DOM 433..712
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:21677752"
FT REGION 463..465
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000269|PubMed:21677752"
FT MOTIF 54..56
FT /note="DXD motif 1"
FT /evidence="ECO:0000255"
FT MOTIF 154..156
FT /note="DXD motif 2"
FT /evidence="ECO:0000305|PubMed:21677752"
FT MOTIF 316..319
FT /note="TIXE motif"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 463..467
FT /note="WWDYG motif"
FT /evidence="ECO:0000250|UniProtKB:O29918"
FT MOTIF 569..576
FT /note="MI motif"
FT /evidence="ECO:0000250|UniProtKB:O29918"
FT BINDING 56
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:21677752"
FT BINDING 154
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:21677752"
FT BINDING 196..198
FT /ligand="[alpha-D-GalNAc-(1->4)]2-[beta-D-Glc-(1->3)]-
FT [alpha-D-GalNAc-(1->4)]2-alpha-D-GalNAc-(1->3)-alpha-D-
FT diNAcBac-tri-trans,hepta-cis-undecaprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:68654"
FT /evidence="ECO:0000269|PubMed:29058712"
FT BINDING 293
FT /ligand="[alpha-D-GalNAc-(1->4)]2-[beta-D-Glc-(1->3)]-
FT [alpha-D-GalNAc-(1->4)]2-alpha-D-GalNAc-(1->3)-alpha-D-
FT diNAcBac-tri-trans,hepta-cis-undecaprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:68654"
FT /evidence="ECO:0000269|PubMed:29058712"
FT BINDING 319
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:21677752"
FT BINDING 375
FT /ligand="[alpha-D-GalNAc-(1->4)]2-[beta-D-Glc-(1->3)]-
FT [alpha-D-GalNAc-(1->4)]2-alpha-D-GalNAc-(1->3)-alpha-D-
FT diNAcBac-tri-trans,hepta-cis-undecaprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:68654"
FT /evidence="ECO:0000269|PubMed:29058712"
FT BINDING 468
FT /ligand="[alpha-D-GalNAc-(1->4)]2-[beta-D-Glc-(1->3)]-
FT [alpha-D-GalNAc-(1->4)]2-alpha-D-GalNAc-(1->3)-alpha-D-
FT diNAcBac-tri-trans,hepta-cis-undecaprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:68654"
FT /evidence="ECO:0000269|PubMed:29058712"
FT SITE 56
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000269|PubMed:21677752"
FT SITE 147
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305|PubMed:21677752"
FT SITE 319
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000269|PubMed:21677752"
FT SITE 331
FT /note="Interacts with target acceptor peptide in protein
FT substrate; important for extended sequon recognition"
FT /evidence="ECO:0000269|PubMed:21677752"
FT SITE 572
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000269|PubMed:21677752"
FT CARBOHYD 535
FT /note="N-linked (DATDGlc) asparagine"
FT /evidence="ECO:0000269|PubMed:21677752"
FT CARBOHYD 556
FT /note="N-linked (DATDGlc) asparagine"
FT /evidence="ECO:0000269|PubMed:21677752"
FT MUTAGEN 56
FT /note="D->A: Strongly reduced catalytic activity. Abolished
FT catalytic activity; when associated with A-319."
FT /evidence="ECO:0000269|PubMed:21677752"
FT MUTAGEN 154
FT /note="D->A: Reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:21677752"
FT MUTAGEN 196
FT /note="Y->A,F: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:29058712"
FT MUTAGEN 319
FT /note="E->A: Strongly reduced catalytic activity. Abolished
FT catalytic activity; when associated with A-56."
FT /evidence="ECO:0000269|PubMed:21677752"
FT MUTAGEN 468
FT /note="Y->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:29058712"
FT MUTAGEN 468
FT /note="Y->F: Reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:29058712"
FT HELIX 13..38
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:5OGL"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6GXC"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 161..176
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 181..195
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 200..217
FT /evidence="ECO:0007829|PDB:5OGL"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 240..256
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 263..279
FT /evidence="ECO:0007829|PDB:5OGL"
FT TURN 280..283
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 284..293
FT /evidence="ECO:0007829|PDB:5OGL"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 336..350
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 354..359
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 360..372
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 381..401
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 408..432
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 441..453
FT /evidence="ECO:0007829|PDB:5OGL"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 467..474
FT /evidence="ECO:0007829|PDB:5OGL"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:5OGL"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:3RCE"
FT HELIX 487..498
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 501..521
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 526..531
FT /evidence="ECO:0007829|PDB:5OGL"
FT TURN 532..535
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 539..545
FT /evidence="ECO:0007829|PDB:5OGL"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:3RCE"
FT STRAND 561..566
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 567..572
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 573..580
FT /evidence="ECO:0007829|PDB:5OGL"
FT TURN 584..586
FT /evidence="ECO:0007829|PDB:5OGL"
FT STRAND 595..598
FT /evidence="ECO:0007829|PDB:5OGL"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:3RCE"
FT STRAND 610..612
FT /evidence="ECO:0007829|PDB:3RCE"
FT TURN 613..615
FT /evidence="ECO:0007829|PDB:3RCE"
FT STRAND 616..619
FT /evidence="ECO:0007829|PDB:3RCE"
FT STRAND 622..627
FT /evidence="ECO:0007829|PDB:5OGL"
FT STRAND 630..642
FT /evidence="ECO:0007829|PDB:5OGL"
FT TURN 643..646
FT /evidence="ECO:0007829|PDB:5OGL"
FT STRAND 647..652
FT /evidence="ECO:0007829|PDB:5OGL"
FT STRAND 659..664
FT /evidence="ECO:0007829|PDB:5OGL"
FT TURN 665..668
FT /evidence="ECO:0007829|PDB:5OGL"
FT STRAND 669..674
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 675..678
FT /evidence="ECO:0007829|PDB:5OGL"
FT HELIX 681..685
FT /evidence="ECO:0007829|PDB:5OGL"
FT TURN 693..695
FT /evidence="ECO:0007829|PDB:5OGL"
FT STRAND 696..702
FT /evidence="ECO:0007829|PDB:5OGL"
FT STRAND 705..710
FT /evidence="ECO:0007829|PDB:5OGL"
SQ SEQUENCE 712 AA; 82729 MW; A04C959507F3C581 CRC64;
MKLQQNFTDN NSIKYTCILI LIAFAFSVLC RLYWVAWASE FYEFFFNDQL MITTNDGYAF
AEGARDMIAG FHQPNDLSYF GSSLSTLTYW LYSILPFSFE SIILYMSAFF ASLIVVPIIL
IAREYKLTTY GFIAALLGSI ANSYYNRTMS GYYDTDMLVL VLPMLILLTF IRLTINKDIF
TLLLSPVFIM IYLWWYPSSY SLNFAMIGLF GLYTLVFHRK EKIFYLTIAL MIIALSMLAW
QYKLALIVLL FAIFAFKEEK INFYMIWALI FISILILHLS GGLDPVLYQL KFYVFKASDV
QNLKDAAFMY FNVNETIMEV NTIDPEVFMQ RISSSVLVFI LSFIGFILLC KDHKSMLLAL
PMLALGFMAL RAGLRFTIYA VPVMALGFGY FLYAFFNFLE KKQIKLSLRN KNILLILIAF
FSISPALMHI YYYKSSTVFT SYEASILNDL KNKAQREDYV VAWWDYGYPI RYYSDVKTLI
DGGKHLGKDN FFSSFVLSKE QIPAANMARL SVEYTEKSFK ENYPDVLKAM VKDYNKTSAK
DFLESLNDKD FKFDTNKTRD VYIYMPYRML RIMPVVAQFA NTNPDNGEQE KSLFFSQANA
IAQDKTTGSV MLDNGVEIIN DFRALKVEGA SIPLKAFVDI ESITNGKFYY NEIDSKAQIY
LLFLREYKSF VILDESLYNS SYIQMFLLNQ YDQDLFEQIT NDTRAKIYRL KR
