ID GGT_ECOLI Reviewed; 580 AA. AC P18956; Q2M7B0; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 03-MAY-2023, entry version 183. DE RecName: Full=Glutathione hydrolase proenzyme; DE EC=3.4.19.13 {ECO:0000305|PubMed:2877974}; DE AltName: Full=Gamma-glutamyltranspeptidase proenzyme {ECO:0000303|PubMed:2570061}; DE Short=GGT; DE EC=2.3.2.2 {ECO:0000269|PubMed:1360205}; DE Contains: DE RecName: Full=Glutathione hydrolase large chain; DE Contains: DE RecName: Full=Glutathione hydrolase small chain; DE Flags: Precursor; GN Name=ggt; OrderedLocusNames=b3447, JW3412; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-41 AND RP 391-403. RC STRAIN=K12; RX PubMed=2570061; DOI=10.1128/jb.171.9.5169-5172.1989; RA Suzuki H., Kumagai H., Echigo T., Tochikura T.; RT "DNA sequence of the Escherichia coli K-12 gamma-glutamyltranspeptidase RT gene, ggt."; RL J. Bacteriol. 171:5169-5172(1989). RN [2] 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 [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-362. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=8041620; DOI=10.1093/nar/22.13.2576; RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.; RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region RT from 76.0 to 81.5 minutes."; RL Nucleic Acids Res. 22:2576-2586(1994). RN [5] RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND RP SUBCELLULAR LOCATION. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=2877974; DOI=10.1128/jb.168.3.1325-1331.1986; RA Suzuki H., Kumagai H., Tochikura T.; RT "gamma-Glutamyltranspeptidase from Escherichia coli K-12: purification and RT properties."; RL J. Bacteriol. 168:1325-1331(1986). RN [6] RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF ARG-513 RP AND ARG-571, AND AUTOCATALYTIC CLEAVAGE. RX PubMed=1360205; DOI=10.1016/0006-291x(92)91540-7; RA Hashimoto W., Suzuki H., Nohara S., Kumagai H.; RT "Escherichia coli gamma-glutamyltranspeptidase mutants deficient in RT processing to subunits."; RL Biochem. Biophys. Res. Commun. 189:173-178(1992). RN [7] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=8104180; DOI=10.1128/jb.175.18.6038-6040.1993; RA Suzuki H., Hashimoto W., Kumagai H.; RT "Escherichia coli K-12 can utilize an exogenous gamma-glutamyl peptide as RT an amino acid source, for which gamma-glutamyltranspeptidase is RT essential."; RL J. Bacteriol. 175:6038-6040(1993). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 25-580 IN COMPLEX WITH GLUTAMATE, RP SUBUNIT, ACTIVE SITE, AND AUTOCATALYTIC CLEAVAGE. RX PubMed=16618936; DOI=10.1073/pnas.0511020103; RA Okada T., Suzuki H., Wada K., Kumagai H., Fukuyama K.; RT "Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, RT a key enzyme in glutathione metabolism, and its reaction intermediate."; RL Proc. Natl. Acad. Sci. U.S.A. 103:6471-6476(2006). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 25-580 OF MUTANT ALA-391, RP SUBUNIT, AUTOCATALYTIC CLEAVAGE, AND MUTAGENESIS OF THR-391. RX PubMed=17135273; DOI=10.1074/jbc.m607490200; RA Okada T., Suzuki H., Wada K., Kumagai H., Fukuyama K.; RT "Crystal structure of the gamma-glutamyltranspeptidase precursor protein RT from Escherichia coli. Structural changes upon autocatalytic processing and RT implications for the maturation mechanism."; RL J. Biol. Chem. 282:2433-2439(2007). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 25-580 IN COMPLEXES WITH RP AZASERINE AND ACIVICIN, ACTIVE SITE, SUBUNIT, AND AUTOCATALYTIC CLEAVAGE. RX PubMed=18555071; DOI=10.1016/j.jmb.2008.05.007; RA Wada K., Hiratake J., Irie M., Okada T., Yamada C., Kumagai H., Suzuki H., RA Fukuyama K.; RT "Crystal structures of Escherichia coli gamma-glutamyltranspeptidase in RT complex with azaserine and acivicin: novel mechanistic implication for RT inhibition by glutamine antagonists."; RL J. Mol. Biol. 380:361-372(2008). CC -!- FUNCTION: Cleaves the gamma-glutamyl bond of periplasmic glutathione CC (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl CC compounds. The metabolism of glutathione releases free glutamate and CC the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and CC glycine by dipeptidases; it may function in amino acid uptake/salvage, CC or possibly in peptidoglycan linkage. Catalyzes the hydrolysis and CC transpeptidation of many gamma-glutamyl compounds (including some D- CC gamma-glutamyl substrates), with a preference for basic and aromatic CC amino acids as acceptors (PubMed:2877974). The KM values for gamma- CC glutamyl acceptors are so high that it has been proposed CC transpeptidation is not the physiological role in E.coli CC (PubMed:2877974, PubMed:8104180). {ECO:0000269|PubMed:2877974, CC ECO:0000305|PubMed:8104180}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = CC 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide]; CC Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795, CC ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599, CC ChEBI:CHEBI:78608; EC=2.3.2.2; Evidence={ECO:0000269|PubMed:1360205}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate; CC Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13; CC Evidence={ECO:0000305|PubMed:2877974}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an S-substituted glutathione + H2O = an S-substituted L- CC cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779, CC ChEBI:CHEBI:143103; EC=3.4.19.13; CC Evidence={ECO:0000305|PubMed:2877974}; CC -!- ACTIVITY REGULATION: Transferase and hydrolase activities are inhibited CC by L-Ala and L-Gln, and also by GGT affinity labeling reagents such as CC azaserine and 6-diazo-5-oxo-nor-leucine. {ECO:0000269|PubMed:2877974}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=35 uM for glutathione transfer to glycylglycine (gly-gly) CC {ECO:0000269|PubMed:2877974}; CC KM=35 uM for gamma-glutamyl-p-nitroanilide (gamma-GpNA) transfer to CC gly-gly {ECO:0000269|PubMed:2877974}; CC KM=29 uM for glutathione hydrolysis {ECO:0000269|PubMed:2877974}; CC KM=68 uM for gamma-GpNA hydrolysis {ECO:0000269|PubMed:2877974}; CC pH dependence: CC Optimum pH is 8.73 for transfer of p-nitroanilide from gamma-GpNA to CC gly-gly and 9.25 for hydrolysis of gamma-GpNA. CC {ECO:0000269|PubMed:2877974}; CC Temperature dependence: CC Optimum temperature is 50 degrees Celsius for both transferase and CC hydrolase activities. {ECO:0000269|PubMed:2877974}; CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism. CC -!- SUBUNIT: This enzyme consists of two polypeptide chains, which are CC synthesized in precursor form from a single polypeptide. CC {ECO:0000269|PubMed:1360205, ECO:0000269|PubMed:16618936, CC ECO:0000269|PubMed:17135273, ECO:0000269|PubMed:18555071, CC ECO:0000269|PubMed:2877974}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:1360205, CC ECO:0000269|PubMed:2877974}. CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit. CC {ECO:0000269|PubMed:1360205, ECO:0000269|PubMed:16618936, CC ECO:0000269|PubMed:17135273, ECO:0000269|PubMed:18555071, CC ECO:0000269|PubMed:2570061}. CC -!- DISRUPTION PHENOTYPE: Loss of growth using exogenous gamma-glutamyl CC peptides as amino acid sources. {ECO:0000269|PubMed:8104180}. CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family. CC {ECO:0000305}. 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; M28722; AAA23869.1; -; Genomic_DNA. DR EMBL; U18997; AAA58245.1; -; Genomic_DNA. DR EMBL; U00096; AAC76472.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77846.1; -; Genomic_DNA. DR EMBL; U00039; AAB18422.1; -; Genomic_DNA. DR PIR; JV0028; EKECEX. DR RefSeq; NP_417904.1; NC_000913.3. DR RefSeq; WP_000595082.1; NZ_SSZK01000008.1. DR PDB; 2DBU; X-ray; 1.95 A; A/C=25-390, B/D=391-580. DR PDB; 2DBW; X-ray; 1.80 A; A/C=25-390, B/D=391-580. DR PDB; 2DBX; X-ray; 1.70 A; A/C=25-390, B/D=391-580. DR PDB; 2DG5; X-ray; 1.60 A; A/C=25-390, B/D=391-580. DR PDB; 2E0W; X-ray; 2.55 A; A/B=25-580. DR PDB; 2E0X; X-ray; 1.95 A; A/C=25-390, B/D=391-580. DR PDB; 2E0Y; X-ray; 2.02 A; A/C=25-390, B/D=391-580. DR PDB; 2Z8I; X-ray; 1.65 A; A/C=25-390, B/D=391-580. DR PDB; 2Z8J; X-ray; 2.05 A; A/C=25-390, B/D=391-580. DR PDB; 2Z8K; X-ray; 1.65 A; A/C=25-390, B/D=391-580. DR PDB; 5B5T; X-ray; 1.70 A; A/C=25-390, B/D=391-580. DR PDBsum; 2DBU; -. DR PDBsum; 2DBW; -. DR PDBsum; 2DBX; -. DR PDBsum; 2DG5; -. DR PDBsum; 2E0W; -. DR PDBsum; 2E0X; -. DR PDBsum; 2E0Y; -. DR PDBsum; 2Z8I; -. DR PDBsum; 2Z8J; -. DR PDBsum; 2Z8K; -. DR PDBsum; 5B5T; -. DR AlphaFoldDB; P18956; -. DR SMR; P18956; -. DR BioGRID; 4261666; 434. DR DIP; DIP-9758N; -. DR IntAct; P18956; 1. DR STRING; 511145.b3447; -. DR MEROPS; T03.001; -. DR jPOST; P18956; -. DR PaxDb; P18956; -. DR EnsemblBacteria; AAC76472; AAC76472; b3447. DR EnsemblBacteria; BAE77846; BAE77846; BAE77846. DR GeneID; 947947; -. DR KEGG; ecj:JW3412; -. DR KEGG; eco:b3447; -. DR PATRIC; fig|511145.12.peg.3544; -. DR EchoBASE; EB0369; -. DR eggNOG; COG0405; Bacteria. DR HOGENOM; CLU_014813_0_3_6; -. DR InParanoid; P18956; -. DR OMA; KATKNMF; -. DR OrthoDB; 5297205at2; -. DR PhylomeDB; P18956; -. DR BioCyc; EcoCyc:EG10374-MON; -. DR BioCyc; MetaCyc:EG10374-MON; -. DR BRENDA; 2.3.2.2; 2026. DR BRENDA; 3.4.19.13; 2026. DR SABIO-RK; P18956; -. DR UniPathway; UPA00204; -. DR EvolutionaryTrace; P18956; -. DR PRO; PR:P18956; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc. DR GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki. DR GO; GO:0034722; F:gamma-glutamyl-peptidase activity; IDA:EcoCyc. DR GO; GO:0036374; F:glutathione hydrolase activity; IDA:EcoCyc. DR GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC. DR GO; GO:0043102; P:amino acid salvage; IMP:EcoCyc. DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006751; P:glutathione catabolic process; IEA:InterPro. DR GO; GO:0097264; P:self proteolysis; IDA:EcoCyc. DR Gene3D; 1.10.246.130; -; 1. DR Gene3D; 3.60.20.40; -; 1. DR InterPro; IPR043138; GGT_lsub_C. DR InterPro; IPR000101; GGT_peptidase. DR InterPro; IPR043137; GGT_ssub. DR InterPro; IPR029055; Ntn_hydrolases_N. DR PANTHER; PTHR43199; GLUTATHIONE HYDROLASE; 1. DR PANTHER; PTHR43199:SF1; GLUTATHIONE HYDROLASE PROENZYME; 1. DR Pfam; PF01019; G_glu_transpept; 1. DR PRINTS; PR01210; GGTRANSPTASE. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. DR TIGRFAMs; TIGR00066; g_glut_trans; 1. DR PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Direct protein sequencing; KW Glutathione biosynthesis; Hydrolase; Periplasm; Protease; KW Reference proteome; Signal; Transferase; Zymogen. FT SIGNAL 1..25 FT /evidence="ECO:0000269|PubMed:2570061" FT CHAIN 26..390 FT /note="Glutathione hydrolase large chain" FT /id="PRO_0000011052" FT CHAIN 391..580 FT /note="Glutathione hydrolase small chain" FT /id="PRO_0000011053" FT REGION 561..580 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 391 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:16618936, FT ECO:0000269|PubMed:18555071" FT BINDING 114 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:16618936" FT BINDING 409 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:16618936" FT BINDING 411 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:16618936" FT BINDING 430 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:16618936" FT BINDING 433 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:16618936" FT BINDING 462..463 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT BINDING 483..484 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT MUTAGEN 391 FT /note="T->A: Abolishes autocatalytic cleavage, loss of FT enzymatic activity." FT /evidence="ECO:0000269|PubMed:17135273" FT MUTAGEN 513 FT /note="R->A: Not processed into its subunits, loss of FT enzymatic activity." FT /evidence="ECO:0000269|PubMed:1360205" FT MUTAGEN 571 FT /note="R->G: Not processed into its subunits, loss of FT enzymatic activity." FT /evidence="ECO:0000269|PubMed:1360205" FT STRAND 39..41 FT /evidence="ECO:0007829|PDB:2DBU" FT STRAND 44..48 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 56..67 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 72..86 FT /evidence="ECO:0007829|PDB:2DG5" FT TURN 88..90 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 93..102 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 108..113 FT /evidence="ECO:0007829|PDB:2DG5" FT TURN 123..126 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 129..131 FT /evidence="ECO:0007829|PDB:2E0Y" FT HELIX 135..139 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 142..144 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 150..161 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 166..179 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 185..193 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 199..201 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 203..209 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 225..237 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 240..243 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 246..257 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 264..269 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 273..275 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 278..282 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 285..289 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 296..307 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 312..315 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 320..340 FT /evidence="ECO:0007829|PDB:2DG5" FT TURN 344..346 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 351..354 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 357..364 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 375..377 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 384..386 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 392..397 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 403..409 FT /evidence="ECO:0007829|PDB:2DG5" FT TURN 413..416 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 421..423 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 430..433 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 434..437 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 467..471 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 474..479 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 484..486 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 487..499 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 505..510 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 518..520 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 523..525 FT /evidence="ECO:0007829|PDB:2DG5" FT HELIX 531..539 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 544..546 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 554..558 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 564..568 FT /evidence="ECO:0007829|PDB:2DG5" FT STRAND 576..579 FT /evidence="ECO:0007829|PDB:2DG5" SQ SEQUENCE 580 AA; 61768 MW; 772F652EBA2A5F00 CRC64; MIKPTFLRRV AIAALLSGSC FSAAAAPPAP PVSYGVEEDV FHPVRAKQGM VASVDATATQ VGVDILKEGG NAVDAAVAVG YALAVTHPQA GNLGGGGFML IRSKNGNTTA IDFREMAPAK ATRDMFLDDQ GNPDSKKSLT SHLASGTPGT VAGFSLALDK YGTMPLNKVV QPAFKLARDG FIVNDALADD LKTYGSEVLP NHENSKAIFW KEGEPLKKGD TLVQANLAKS LEMIAENGPD EFYKGTIAEQ IAQEMQKNGG LITKEDLAAY KAVERTPISG DYRGYQVYSM PPPSSGGIHI VQILNILENF DMKKYGFGSA DAMQIMAEAE KYAYADRSEY LGDPDFVKVP WQALTNKAYA KSIADQIDIN KAKPSSEIRP GKLAPYESNQ TTHYSVVDKD GNAVAVTYTL NTTFGTGIVA GESGILLNNQ MDDFSAKPGV PNVYGLVGGD ANAVGPNKRP LSSMSPTIVV KDGKTWLVTG SPGGSRIITT VLQMVVNSID YGLNVAEATN APRFHHQWLP DELRVEKGFS PDTLKLLEAK GQKVALKEAM GSTQSIMVGP DGELYGASDP RSVDDLTAGY //