OTSA_ECOLI
ID OTSA_ECOLI Reviewed; 474 AA.
AC P31677;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Trehalose-6-phosphate synthase {ECO:0000303|PubMed:3131312};
DE Short=TPS {ECO:0000303|PubMed:3131312};
DE EC=2.4.1.15 {ECO:0000305|PubMed:20077550, ECO:0000305|PubMed:3131312};
DE AltName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] {ECO:0000305};
DE AltName: Full=Osmoregulatory trehalose synthesis protein A {ECO:0000303|PubMed:3131312};
DE Short=OtsA {ECO:0000303|PubMed:3131312};
DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase {ECO:0000305};
GN Name=otsA {ECO:0000303|PubMed:3131312}; OrderedLocusNames=b1896, JW5312;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12 / CSH7;
RX PubMed=8045430; DOI=10.1016/0378-1119(94)90316-6;
RA Kaasen I., McDougall J., Stroem A.R.;
RT "Analysis of the otsBA operon for osmoregulatory trehalose synthesis in
RT Escherichia coli and homology of the OtsA and OtsB proteins to the yeast
RT trehalose-6-phosphate synthase/phosphatase complex.";
RL Gene 145:9-15(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
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 430-474.
RC STRAIN=K12 / EMG2;
RA Estep P., O'Keeffe T., Robison K., Church G.M.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION AS A TREHALOSE-6-PHOSPHATE SYNTHASE, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, DISRUPTION PHENOTYPE, INDUCTION, NOMENCLATURE, AND PATHWAY.
RX PubMed=3131312; DOI=10.1128/jb.170.6.2841-2849.1988;
RA Giaever H.M., Styrvold O.B., Kaasen I., Stroem A.R.;
RT "Biochemical and genetic characterization of osmoregulatory trehalose
RT synthesis in Escherichia coli.";
RL J. Bacteriol. 170:2841-2849(1988).
RN [7]
RP INDUCTION.
RX PubMed=1744047; DOI=10.1128/jb.173.24.7918-7924.1991;
RA Hengge-Aronis R., Klein W., Lange R., Rimmele M., Boos W.;
RT "Trehalose synthesis genes are controlled by the putative sigma factor
RT encoded by rpoS and are involved in stationary-phase thermotolerance in
RT Escherichia coli.";
RL J. Bacteriol. 173:7918-7924(1991).
RN [8]
RP FUNCTION AS A TREHALOSE-6-PHOSPHATE SYNTHASE, AND INDUCTION.
RX PubMed=1310094; DOI=10.1128/jb.174.3.889-898.1992;
RA Kaasen I., Falkenberg P., Styrvold O.B., Strom A.R.;
RT "Molecular cloning and physical mapping of the otsBA genes, which encode
RT the osmoregulatory trehalose pathway of Escherichia coli: evidence that
RT transcription is activated by katF (AppR).";
RL J. Bacteriol. 174:889-898(1992).
RN [9]
RP FUNCTION AS A TREHALOSE-6-PHOSPHATE SYNTHASE, AND INDUCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12105274; DOI=10.1073/pnas.142314099;
RA Kandror O., DeLeon A., Goldberg A.L.;
RT "Trehalose synthesis is induced upon exposure of Escherichia coli to cold
RT and is essential for viability at low temperatures.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9727-9732(2002).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF 1-457 IN COMPLEX WITH SUBSTRATE
RP ANALOG AND GLUCOSE-6-PHOSPHATE, AND SUBUNIT.
RX PubMed=12498887; DOI=10.1016/s1074-5521(02)00292-2;
RA Gibson R.P., Turkenburg J.P., Charnock S.J., Lloyd R., Davies G.J.;
RT "Insights into trehalose synthesis provided by the structure of the
RT retaining glucosyltransferase OtsA.";
RL Chem. Biol. 9:1337-1346(2002).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
RX PubMed=14570926; DOI=10.1074/jbc.m307643200;
RA Gibson R.P., Tarling C.A., Roberts S., Withers S.G., Davies G.J.;
RT "The donor subsite of trehalose-6-phosphate synthase: binary complexes with
RT UDP-glucose and UDP-2-deoxy-2-fluoro-glucose at 2 A resolution.";
RL J. Biol. Chem. 279:1950-1955(2004).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND REACTION MECHANISM.
RX PubMed=20077550; DOI=10.1002/anie.200905096;
RA Errey J.C., Lee S.S., Gibson R.P., Martinez Fleites C., Barry C.S.,
RA Jung P.M., O'Sullivan A.C., Davis B.G., Davies G.J.;
RT "Mechanistic insight into enzymatic glycosyl transfer with retention of
RT configuration through analysis of glycomimetic inhibitors.";
RL Angew. Chem. Int. Ed. Engl. 49:1234-1237(2010).
CC -!- FUNCTION: Catalyzes the transfer of glucose from UDP-alpha-D-glucose
CC (UDP-Glc) to D-glucose 6-phosphate (Glc-6-P) to form trehalose-6-
CC phosphate. Acts with retention of the anomeric configuration of the
CC UDP-sugar donor. Essential for viability of the cells at low
CC temperatures and at elevated osmotic strength.
CC {ECO:0000269|PubMed:12105274, ECO:0000269|PubMed:1310094,
CC ECO:0000269|PubMed:20077550, ECO:0000269|PubMed:3131312}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-
CC trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15;
CC Evidence={ECO:0000305|PubMed:20077550, ECO:0000305|PubMed:3131312};
CC -!- ACTIVITY REGULATION: Activated by potassium and other monovalent
CC cations at 0.25 M, but partially inhibited at greater concentrations
CC (PubMed:3131312). Inhibited by validoxylamine A 6'-O-phosphate
CC (PubMed:20077550). {ECO:0000269|PubMed:20077550,
CC ECO:0000269|PubMed:3131312}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.7 mM for UDP-Glc {ECO:0000269|PubMed:20077550};
CC KM=7.3 mM for Glc-6-P {ECO:0000269|PubMed:20077550};
CC Note=kcat is 34 sec(-1) for glucosyltransferase activity.
CC {ECO:0000269|PubMed:20077550};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC {ECO:0000305|PubMed:3131312}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12498887}.
CC -!- INDUCTION: By cold-shock, osmotic-shock and during the transition to
CC stationary phase. Expression is partially dependent on RpoS.
CC {ECO:0000269|PubMed:12105274, ECO:0000269|PubMed:1310094,
CC ECO:0000269|PubMed:1744047, ECO:0000269|PubMed:3131312}.
CC -!- DISRUPTION PHENOTYPE: Mutants are viable, but osmotically sensitive in
CC minimal media and sensitive to cold shock.
CC {ECO:0000269|PubMed:3131312}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000305}.
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DR EMBL; X69160; CAA48913.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74966.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15717.2; -; Genomic_DNA.
DR EMBL; U27211; AAA68604.1; -; Genomic_DNA.
DR PIR; I83402; I83402.
DR RefSeq; NP_416410.1; NC_000913.3.
DR RefSeq; WP_001295646.1; NZ_STEB01000026.1.
DR PDB; 1GZ5; X-ray; 2.43 A; A/B/C/D=2-457.
DR PDB; 1UQT; X-ray; 2.00 A; A/B=2-474.
DR PDB; 1UQU; X-ray; 2.00 A; A/B=2-474.
DR PDB; 2WTX; X-ray; 2.20 A; A/B/C/D=1-474.
DR PDB; 6JAK; X-ray; 2.41 A; A/B/C/D=2-456.
DR PDBsum; 1GZ5; -.
DR PDBsum; 1UQT; -.
DR PDBsum; 1UQU; -.
DR PDBsum; 2WTX; -.
DR PDBsum; 6JAK; -.
DR AlphaFoldDB; P31677; -.
DR SMR; P31677; -.
DR BioGRID; 4259473; 16.
DR DIP; DIP-10417N; -.
DR IntAct; P31677; 10.
DR STRING; 511145.b1896; -.
DR DrugBank; DB02007; alpha-D-glucose 6-phosphate.
DR DrugBank; DB03366; Imidazole.
DR DrugBank; DB01861; Uridine diphosphate glucose.
DR DrugBank; DB03435; Uridine-5'-Diphosphate.
DR DrugBank; DB03488; Uridine-5'-diphosphate-2-deoxy-2-fluoro-alpha-D-galactose.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR jPOST; P31677; -.
DR PaxDb; P31677; -.
DR PRIDE; P31677; -.
DR EnsemblBacteria; AAC74966; AAC74966; b1896.
DR EnsemblBacteria; BAA15717; BAA15717; BAA15717.
DR GeneID; 58461800; -.
DR GeneID; 946405; -.
DR KEGG; ecj:JW5312; -.
DR KEGG; eco:b1896; -.
DR PATRIC; fig|1411691.4.peg.353; -.
DR EchoBASE; EB1701; -.
DR eggNOG; COG0380; Bacteria.
DR HOGENOM; CLU_002351_7_1_6; -.
DR InParanoid; P31677; -.
DR OMA; YYGFSNR; -.
DR PhylomeDB; P31677; -.
DR BioCyc; EcoCyc:TREHALOSE6PSYN-MON; -.
DR BioCyc; MetaCyc:TREHALOSE6PSYN-MON; -.
DR BRENDA; 2.4.1.15; 2026.
DR BRENDA; 3.1.3.12; 2026.
DR UniPathway; UPA00299; -.
DR EvolutionaryTrace; P31677; -.
DR PRO; PR:P31677; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0006970; P:response to osmotic stress; IMP:EcoCyc.
DR GO; GO:0005992; P:trehalose biosynthetic process; IMP:EcoCyc.
DR GO; GO:0070415; P:trehalose metabolism in response to cold stress; IMP:EcoCyc.
DR CDD; cd03788; GT20_TPS; 1.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR012766; Trehalose_OtsA.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR TIGRFAMs; TIGR02400; trehalose_OtsA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosyltransferase; Potassium;
KW Reference proteome; Stress response; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..474
FT /note="Trehalose-6-phosphate synthase"
FT /id="PRO_0000122489"
FT BINDING 10
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:12498887,
FT ECO:0000269|PubMed:20077550, ECO:0007744|PDB:1GZ5,
FT ECO:0007744|PDB:2WTX"
FT BINDING 22..23
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000305|PubMed:12498887,
FT ECO:0000305|PubMed:14570926, ECO:0000305|PubMed:20077550,
FT ECO:0007744|PDB:1GZ5, ECO:0007744|PDB:2WTX"
FT BINDING 77
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:12498887,
FT ECO:0000269|PubMed:20077550, ECO:0007744|PDB:1GZ5,
FT ECO:0007744|PDB:2WTX"
FT BINDING 131
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:12498887,
FT ECO:0000269|PubMed:20077550, ECO:0007744|PDB:1GZ5,
FT ECO:0007744|PDB:2WTX"
FT BINDING 263
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000305|PubMed:12498887,
FT ECO:0000305|PubMed:14570926, ECO:0000305|PubMed:20077550,
FT ECO:0007744|PDB:1GZ5, ECO:0007744|PDB:1UQT,
FT ECO:0007744|PDB:1UQU, ECO:0007744|PDB:2WTX"
FT BINDING 268
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000305|PubMed:12498887,
FT ECO:0000305|PubMed:14570926, ECO:0000305|PubMed:20077550,
FT ECO:0007744|PDB:1GZ5, ECO:0007744|PDB:1UQT,
FT ECO:0007744|PDB:1UQU, ECO:0007744|PDB:2WTX"
FT BINDING 301
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:12498887,
FT ECO:0000269|PubMed:20077550, ECO:0007744|PDB:1GZ5,
FT ECO:0007744|PDB:2WTX"
FT BINDING 340
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000305|PubMed:12498887,
FT ECO:0000305|PubMed:14570926, ECO:0000305|PubMed:20077550,
FT ECO:0007744|PDB:1GZ5, ECO:0007744|PDB:1UQT,
FT ECO:0007744|PDB:1UQU, ECO:0007744|PDB:2WTX"
FT BINDING 366..370
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000305|PubMed:12498887,
FT ECO:0000305|PubMed:14570926, ECO:0000305|PubMed:20077550,
FT ECO:0007744|PDB:1GZ5, ECO:0007744|PDB:1UQT,
FT ECO:0007744|PDB:1UQU, ECO:0007744|PDB:2WTX"
FT SITE 86
FT /note="Involved in alpha anomer selectivity"
FT /evidence="ECO:0000305|PubMed:12498887"
FT SITE 156
FT /note="Involved in alpha anomer selectivity"
FT /evidence="ECO:0000305|PubMed:12498887"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:1GZ5"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:1UQT"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:1UQT"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:1UQT"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:1UQT"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 100..117
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1UQT"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:1UQT"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:1UQT"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:1UQT"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:1UQT"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:1UQT"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:1UQT"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:1UQT"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:1UQT"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:1UQT"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:1UQT"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 305..325
FT /evidence="ECO:0007829|PDB:1UQT"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 342..351
FT /evidence="ECO:0007829|PDB:1UQT"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:1UQT"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 366..374
FT /evidence="ECO:0007829|PDB:1UQT"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 390..393
FT /evidence="ECO:0007829|PDB:1UQT"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 406..417
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 421..437
FT /evidence="ECO:0007829|PDB:1UQT"
FT HELIX 440..453
FT /evidence="ECO:0007829|PDB:1UQT"
SQ SEQUENCE 474 AA; 53611 MW; 63FFB6F938056F95 CRC64;
MSRLVVVSNR IAPPDEHAAS AGGLAVGILG ALKAAGGLWF GWSGETGNED QPLKKVKKGN
ITWASFNLSE QDLDEYYNQF SNAVLWPAFH YRLDLVQFQR PAWDGYLRVN ALLADKLLPL
LQDDDIIWIH DYHLLPFAHE LRKRGVNNRI GFFLHIPFPT PEIFNALPTY DTLLEQLCDY
DLLGFQTEND RLAFLDCLSN LTRVTTRSAK SHTAWGKAFR TEVYPIGIEP KEIAKQAAGP
LPPKLAQLKA ELKNVQNIFS VERLDYSKGL PERFLAYEAL LEKYPQHHGK IRYTQIAPTS
RGDVQAYQDI RHQLENEAGR INGKYGQLGW TPLYYLNQHF DRKLLMKIFR YSDVGLVTPL
RDGMNLVAKE YVAAQDPANP GVLVLSQFAG AANELTSALI VNPYDRDEVA AALDRALTMS
LAERISRHAE MLDVIVKNDI NHWQECFISD LKQIVPRSAE SQQRDKVATF PKLA
