FTSW_ECOLI
ID FTSW_ECOLI Reviewed; 414 AA.
AC P0ABG4; P16457;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Probable peptidoglycan glycosyltransferase FtsW {ECO:0000250|UniProtKB:P0ABG7, ECO:0000255|HAMAP-Rule:MF_00913};
DE Short=PGT {ECO:0000250|UniProtKB:P0ABG7, ECO:0000255|HAMAP-Rule:MF_00913};
DE EC=2.4.1.129 {ECO:0000250|UniProtKB:P0ABG7, ECO:0000255|HAMAP-Rule:MF_00913};
DE AltName: Full=Cell division protein FtsW {ECO:0000255|HAMAP-Rule:MF_00913, ECO:0000305};
DE AltName: Full=Cell wall polymerase {ECO:0000250|UniProtKB:P0ABG7, ECO:0000255|HAMAP-Rule:MF_00913};
DE AltName: Full=Lipid II flippase FtsW {ECO:0000305};
DE AltName: Full=Peptidoglycan polymerase {ECO:0000250|UniProtKB:P0ABG7, ECO:0000255|HAMAP-Rule:MF_00913};
DE Short=PG polymerase {ECO:0000250|UniProtKB:P0ABG7, ECO:0000255|HAMAP-Rule:MF_00913};
GN Name=ftsW {ECO:0000255|HAMAP-Rule:MF_00913};
GN OrderedLocusNames=b0089, JW0087;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2509435; DOI=10.1128/jb.171.11.6375-6378.1989;
RA Ikeda M., Sato T., Wachi M., Jung H.K., Ishino F., Kobayashi Y.,
RA Matsuhashi M.;
RT "Structural similarity among Escherichia coli FtsW and RodA proteins and
RT Bacillus subtilis SpoVE protein, which function in cell division, cell
RT elongation, and spore formation, respectively.";
RL J. Bacteriol. 171:6375-6378(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-414.
RC STRAIN=K12;
RX PubMed=2197603; DOI=10.1093/nar/18.13.4014;
RA Ikeda M., Wachi M., Jung H.K., Ishino F., Matsuhashi M.;
RT "Nucleotide sequence involving murG and murC in the mra gene cluster region
RT of Escherichia coli.";
RL Nucleic Acids Res. 18:4014-4014(1990).
RN [6]
RP FUNCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9218774; DOI=10.1046/j.1365-2958.1997.4091773.x;
RA Boyle D.S., Khattar M.M., Addinall S.G., Lutkenhaus J., Donachie W.D.;
RT "ftsW is an essential cell-division gene in Escherichia coli.";
RL Mol. Microbiol. 24:1263-1273(1997).
RN [7]
RP VARIANT MUTANT ALLELE FTSW201.
RC STRAIN=K12;
RX PubMed=7961485; DOI=10.1128/jb.176.23.7140-7147.1994;
RA Khattar M.M., Begg K.J., Donachie W.D.;
RT "Identification of FtsW and characterization of a new ftsW division mutant
RT of Escherichia coli.";
RL J. Bacteriol. 176:7140-7147(1994).
RN [8]
RP VARIANTS MUTANT ALLELES FTSW263 AND FTSW1640.
RC STRAIN=K12;
RX PubMed=9006034; DOI=10.1128/jb.179.3.784-793.1997;
RA Khattar M.M., Addinall S.G., Stedul K.H., Boyle D.S., Lutkenhaus J.,
RA Donachie W.D.;
RT "Two polypeptide products of the Escherichia coli cell division gene ftsW
RT and a possible role for FtsW in FtsZ function.";
RL J. Bacteriol. 179:784-793(1997).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=9603865; DOI=10.1128/jb.180.11.2810-2816.1998;
RA Wang L., Khattar M.K., Donachie W.D., Lutkenhaus J.;
RT "FtsI and FtsW are localized to the septum in Escherichia coli.";
RL J. Bacteriol. 180:2810-2816(1998).
RN [10]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=12423747; DOI=10.1111/j.1574-6968.2002.tb11409.x;
RA Lara B., Ayala J.A.;
RT "Topological characterization of the essential Escherichia coli cell
RT division protein FtsW.";
RL FEMS Microbiol. Lett. 216:23-32(2002).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=11807049; DOI=10.1128/jb.184.4.904-912.2002;
RA Mercer K.L., Weiss D.S.;
RT "The Escherichia coli cell division protein FtsW is required to recruit its
RT cognate transpeptidase, FtsI (PBP3), to the division site.";
RL J. Bacteriol. 184:904-912(2002).
RN [12]
RP DOMAIN, AND MUTAGENESIS OF ARG-172; ARG-243; GLY-311; PRO-368; PRO-375 AND
RP ARG-402.
RX PubMed=15576787; DOI=10.1128/jb.186.24.8370-8379.2004;
RA Pastoret S., Fraipont C., den Blaauwen T., Wolf B., Aarsman M.E.,
RA Piette A., Thomas A., Brasseur R., Nguyen-Disteche M.;
RT "Functional analysis of the cell division protein FtsW of Escherichia
RT coli.";
RL J. Bacteriol. 186:8370-8379(2004).
RN [13]
RP INTERACTION WITH FTSI; FTSL; FTSQ AND FTSN.
RC STRAIN=K12;
RX PubMed=15774864; DOI=10.1128/jb.187.7.2233-2243.2005;
RA Karimova G., Dautin N., Ladant D.;
RT "Interaction network among Escherichia coli membrane proteins involved in
RT cell division as revealed by bacterial two-hybrid analysis.";
RL J. Bacteriol. 187:2233-2243(2005).
RN [14]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [15]
RP INTERACTION WITH FTSQ.
RC STRAIN=K12;
RX PubMed=17185541; DOI=10.1099/mic.0.2006/000265-0;
RA D'Ulisse V., Fagioli M., Ghelardini P., Paolozzi L.;
RT "Three functional subdomains of the Escherichia coli FtsQ protein are
RT involved in its interaction with the other division proteins.";
RL Microbiology 153:124-138(2007).
RN [16]
RP INTERACTION WITH FTSN.
RX PubMed=20497333; DOI=10.1111/j.1365-2958.2010.07211.x;
RA Alexeeva S., Gadella T.W. Jr., Verheul J., Verhoeven G.S., den Blaauwen T.;
RT "Direct interactions of early and late assembling division proteins in
RT Escherichia coli cells resolved by FRET.";
RL Mol. Microbiol. 77:384-398(2010).
RN [17]
RP PROPOSED FUNCTION AS A FLIPPASE.
RX PubMed=21386816; DOI=10.1038/emboj.2011.61;
RA Mohammadi T., van Dam V., Sijbrandi R., Vernet T., Zapun A., Bouhss A.,
RA Diepeveen-de Bruin M., Nguyen-Disteche M., de Kruijff B., Breukink E.;
RT "Identification of FtsW as a transporter of lipid-linked cell wall
RT precursors across the membrane.";
RL EMBO J. 30:1425-1432(2011).
RN [18]
RP INTERACTION WITH FTSI.
RX PubMed=20847002; DOI=10.1099/mic.0.040071-0;
RA Fraipont C., Alexeeva S., Wolf B., van der Ploeg R., Schloesser M.,
RA den Blaauwen T., Nguyen-Disteche M.;
RT "The integral membrane FtsW protein and peptidoglycan synthase PBP3 form a
RT subcomplex in Escherichia coli.";
RL Microbiology 157:251-259(2011).
RN [19]
RP PROPOSED FUNCTION AS A FLIPPASE, AND MUTAGENESIS OF ARG-145;
RP 150-GLU--THR-152; LYS-153 AND 154-LEU--LEU-156.
RX PubMed=24711460; DOI=10.1074/jbc.m114.557371;
RA Mohammadi T., Sijbrandi R., Lutters M., Verheul J., Martin N.,
RA den Blaauwen T., de Kruijff B., Breukink E.;
RT "Specificity of the transport of lipid II by FtsW in Escherichia coli.";
RL J. Biol. Chem. 289:14707-14718(2014).
RN [20]
RP PROPOSED FUNCTION AS A PEPTIDOGLYCAN POLYMERASE.
RX PubMed=27643381; DOI=10.1038/nmicrobiol.2016.172;
RA Cho H., Wivagg C.N., Kapoor M., Barry Z., Rohs P.D., Suh H., Marto J.A.,
RA Garner E.C., Bernhardt T.G.;
RT "Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase
RT families functioning semi-autonomously.";
RL Nat. Microbiol. 2016:16172-16172(2016).
CC -!- FUNCTION: Peptidoglycan polymerase that is essential for cell division
CC (Probable). Functions probably in conjunction with the penicillin-
CC binding protein 3 (ftsI) (PubMed:9603865, PubMed:11807049). Required
CC for localization of FtsI (PubMed:11807049).
CC {ECO:0000269|PubMed:11807049, ECO:0000269|PubMed:9603865,
CC ECO:0000305|PubMed:27643381, ECO:0000305|PubMed:9218774}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00913};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00913}.
CC -!- SUBUNIT: Forms a complex with FtsI. Interacts also with FtsL, FtsQ and
CC FtsN. {ECO:0000269|PubMed:15774864, ECO:0000269|PubMed:17185541,
CC ECO:0000269|PubMed:20497333, ECO:0000269|PubMed:20847002}.
CC -!- INTERACTION:
CC P0ABG4; P0AD68: ftsI; NbExp=7; IntAct=EBI-1214767, EBI-548564;
CC P0ABG4; P29131: ftsN; NbExp=3; IntAct=EBI-1214767, EBI-1134233;
CC P0ABG4; P06136: ftsQ; NbExp=4; IntAct=EBI-1214767, EBI-1130157;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00913, ECO:0000269|PubMed:11807049,
CC ECO:0000269|PubMed:12423747, ECO:0000269|PubMed:9603865}; Multi-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_00913,
CC ECO:0000269|PubMed:11807049, ECO:0000269|PubMed:12423747,
CC ECO:0000269|PubMed:9603865}. Note=Localizes to the division septum.
CC Localization requires FtsZ, FtsA, FtsQ and FtsL, but not FtsI.
CC -!- DOMAIN: The periplasmic loop between transmembrane domains 7 and 8 is
CC essential for activity and the loop between transmembrane domains 9 and
CC 10 is involved in the recruitment of FtsI at the division site.
CC {ECO:0000269|PubMed:15576787}.
CC -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00913, ECO:0000305}.
CC -!- CAUTION: Has previously been proposed to be a lipid II flippase that
CC transports lipid-linked peptidoglycan precursors from the inner to the
CC outer leaflet of the cytoplasmic membrane (PubMed:21386816,
CC PubMed:24711460), but recent evidence suggests that FtsW may function
CC as a peptidoglycan polymerase (PubMed:27643381). The identity of the
CC lipid II flippase is still controversial with conflicting in vivo and
CC in vitro results, but MurJ (AC P0AF16) is probably the lipid II
CC flippase. {ECO:0000305}.
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DR EMBL; M30807; AAA83859.1; -; Genomic_DNA.
DR EMBL; X55034; CAA38866.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73200.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96657.1; -; Genomic_DNA.
DR EMBL; X52644; CAA36866.1; -; Genomic_DNA.
DR PIR; A32581; CEECFW.
DR RefSeq; NP_414631.1; NC_000913.3.
DR RefSeq; WP_001295532.1; NZ_STEB01000010.1.
DR AlphaFoldDB; P0ABG4; -.
DR SMR; P0ABG4; -.
DR BioGRID; 4261096; 505.
DR ComplexPortal; CPX-1936; Divisome complex.
DR DIP; DIP-47989N; -.
DR IntAct; P0ABG4; 14.
DR MINT; P0ABG4; -.
DR STRING; 511145.b0089; -.
DR TCDB; 2.A.103.1.1; the bacterial murein precursor exporter (mpe) family.
DR jPOST; P0ABG4; -.
DR PaxDb; P0ABG4; -.
DR PRIDE; P0ABG4; -.
DR EnsemblBacteria; AAC73200; AAC73200; b0089.
DR EnsemblBacteria; BAB96657; BAB96657; BAB96657.
DR GeneID; 66671621; -.
DR GeneID; 946322; -.
DR KEGG; ecj:JW0087; -.
DR KEGG; eco:b0089; -.
DR PATRIC; fig|1411691.4.peg.2191; -.
DR EchoBASE; EB0340; -.
DR eggNOG; COG0772; Bacteria.
DR HOGENOM; CLU_029243_1_1_6; -.
DR InParanoid; P0ABG4; -.
DR OMA; KLWWSNL; -.
DR PhylomeDB; P0ABG4; -.
DR BioCyc; EcoCyc:EG10344-MON; -.
DR BioCyc; MetaCyc:EG10344-MON; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:P0ABG4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoliWiki.
DR GO; GO:1990586; C:divisome complex; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IDA:EcoCyc.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051301; P:cell division; IMP:EcoliWiki.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000917; P:division septum assembly; IC:ComplexPortal.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IC:ComplexPortal.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IMP:EcoliWiki.
DR HAMAP; MF_00913; PGT_FtsW_proteobact; 1.
DR InterPro; IPR018365; Cell_cycle_FtsW-rel_CS.
DR InterPro; IPR013437; FtsW.
DR InterPro; IPR001182; FtsW/RodA.
DR PANTHER; PTHR30474; PTHR30474; 1.
DR Pfam; PF01098; FTSW_RODA_SPOVE; 1.
DR TIGRFAMs; TIGR02614; ftsW; 1.
DR PROSITE; PS00428; FTSW_RODA_SPOVE; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW Peptidoglycan synthesis; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..414
FT /note="Probable peptidoglycan glycosyltransferase FtsW"
FT /id="PRO_0000062700"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 34..47
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 69..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 108..111
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 133..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..194
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 195..197
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..217
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 218..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..244
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 245..301
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 323..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 364..373
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00913"
FT TOPO_DOM 395..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 145
FT /note="R->A: Loss of flippase activity. Does not affect
FT localization at the division site."
FT /evidence="ECO:0000269|PubMed:24711460"
FT MUTAGEN 150..152
FT /note="ELT->AAA: Does not affect flippase activity."
FT /evidence="ECO:0000269|PubMed:24711460"
FT MUTAGEN 153
FT /note="K->N: Loss of flippase activity. Does not affect
FT localization at the division site."
FT /evidence="ECO:0000269|PubMed:24711460"
FT MUTAGEN 154..156
FT /note="LSL->AAA: Does not affect flippase activity."
FT /evidence="ECO:0000269|PubMed:24711460"
FT MUTAGEN 170
FT /note="E->K: In ftsW201; TS; blocks division at the
FT initiation stage."
FT MUTAGEN 172
FT /note="R->S: Does not affect localization, but affects its
FT thermosensitivity."
FT /evidence="ECO:0000269|PubMed:15576787"
FT MUTAGEN 181
FT /note="P->L: In ftsW1640; TS; blocks division at a late
FT stage."
FT MUTAGEN 243
FT /note="R->Q: Lack of activity."
FT /evidence="ECO:0000269|PubMed:15576787"
FT MUTAGEN 253
FT /note="P->L: In ftsW263; TS; blocks division at the
FT initiation stage."
FT MUTAGEN 311
FT /note="G->D: Thermosensitive. Fails to localize to the
FT division site at 42 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:15576787"
FT MUTAGEN 368
FT /note="P->A: Cannot recruit FtsI at the division site; when
FT associated with A-375."
FT /evidence="ECO:0000269|PubMed:15576787"
FT MUTAGEN 375
FT /note="P->A: Cannot recruit FtsI at the division site; when
FT associated with A-368."
FT /evidence="ECO:0000269|PubMed:15576787"
FT MUTAGEN 402
FT /note="R->Q: Does not affect localization and activity."
FT /evidence="ECO:0000269|PubMed:15576787"
SQ SEQUENCE 414 AA; 45987 MW; 7935EC952AD9A1F3 CRC64;
MRLSLPRLKM PRLPGFSILV WISTALKGWV MGSREKDTDS LIMYDRTLLW LTFGLAAIGF
IMVTSASMPI GQRLTNDPFF FAKRDGVYLI LAFILAIITL RLPMEFWQRY SATMLLGSII
LLMIVLVVGS SVKGASRWID LGLLRIQPAE LTKLSLFCYI ANYLVRKGDE VRNNLRGFLK
PMGVILVLAV LLLAQPDLGT VVVLFVTTLA MLFLAGAKLW QFIAIIGMGI SAVVLLILAE
PYRIRRVTAF WNPWEDPFGS GYQLTQSLMA FGRGELWGQG LGNSVQKLEY LPEAHTDFIF
AIIGEELGYV GVVLALLMVF FVAFRAMSIG RKALEIDHRF SGFLACSIGI WFSFQALVNV
GAAAGMLPTK GLTLPLISYG GSSLLIMSTA IMMLLRIDYE TRLEKAQAFV RGSR
