PPK1_ECOLI
ID PPK1_ECOLI Reviewed; 688 AA.
AC P0A7B1; P28688; Q47549;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Polyphosphate kinase {ECO:0000255|HAMAP-Rule:MF_00347};
DE EC=2.7.4.1 {ECO:0000255|HAMAP-Rule:MF_00347, ECO:0000269|PubMed:10660553, ECO:0000269|PubMed:1331061, ECO:0000269|PubMed:8962061};
DE AltName: Full=ATP-polyphosphate phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00347};
DE AltName: Full=Polyphosphoric acid kinase {ECO:0000255|HAMAP-Rule:MF_00347};
GN Name=ppk {ECO:0000255|HAMAP-Rule:MF_00347};
GN OrderedLocusNames=b2501, JW2486;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC
RP ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=1331061; DOI=10.1016/s0021-9258(18)41708-5;
RA Akiyama M., Crooke E., Kornberg A.;
RT "The polyphosphate kinase gene of Escherichia coli. Isolation and sequence
RT of the ppk gene and membrane location of the protein.";
RL J. Biol. Chem. 267:22556-22561(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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 1-91.
RC STRAIN=K12;
RX PubMed=3301838; DOI=10.1016/s0021-9258(18)60999-8;
RA Smith J.M., Daum H.A. III;
RT "Identification and nucleotide sequence of a gene encoding 5'-
RT phosphoribosylglycinamide transformylase in Escherichia coli K12.";
RL J. Biol. Chem. 262:10565-10569(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 679-688.
RC STRAIN=K12;
RX PubMed=8380170; DOI=10.1016/s0021-9258(18)54198-3;
RA Akiyama M., Crooke E., Kornberg A.;
RT "An exopolyphosphatase of Escherichia coli. The enzyme and its ppx gene in
RT a polyphosphate operon.";
RL J. Biol. Chem. 268:633-639(1993).
RN [7]
RP PROTEIN SEQUENCE OF 434-437, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE,
RP PHOSPHORYLATION, AND MUTAGENESIS OF HIS-424; HIS-435; HIS-454 AND HIS-592.
RX PubMed=8962061; DOI=10.1073/pnas.93.25.14391;
RA Kumble K.D., Ahn K., Kornberg A.;
RT "Phosphohistidyl active sites in polyphosphate kinase of Escherichia
RT coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14391-14395(1996).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, AND MUTAGENESIS OF
RP ARG-375; SER-380; PHE-488; PRO-507; ARG-564; ARG-621 AND GLN-674.
RX PubMed=10660553; DOI=10.1074/jbc.275.6.3977;
RA Tzeng C.M., Kornberg A.;
RT "The multiple activities of polyphosphate kinase of Escherichia coli and
RT their subunit structure determined by radiation target analysis.";
RL J. Biol. Chem. 275:3977-3983(2000).
RN [9] {ECO:0007744|PDB:1XDO, ECO:0007744|PDB:1XDP}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND
RP MAGNESIUM, SUBUNIT, AND ACTIVE SITE.
RX PubMed=15947782; DOI=10.1038/sj.embor.7400448;
RA Zhu Y., Huang W., Lee S.S., Xu W.;
RT "Crystal structure of a polyphosphate kinase and its implications for
RT polyphosphate synthesis.";
RL EMBO Rep. 6:681-687(2005).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC of ATP to form a long-chain polyphosphate (polyP). Can form linear
CC polymers of orthophosphate with chain lengths up to 1000 or more. Can
CC use GTP instead of ATP, but the efficiency of GTP is 5% that of ATP.
CC Also exhibits several other enzymatic activities, which include: ATP
CC synthesis from polyP in the presence of excess ADP, general nucleoside-
CC diphosphate kinase activity, linear guanosine 5'-tetraphosphate (ppppG)
CC synthesis and autophosphorylation. {ECO:0000269|PubMed:10660553,
CC ECO:0000269|PubMed:8962061}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphate](n) + ATP = [phosphate](n+1) + ADP;
CC Xref=Rhea:RHEA:19573, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC ChEBI:CHEBI:16838, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.4.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00347,
CC ECO:0000269|PubMed:10660553, ECO:0000269|PubMed:1331061,
CC ECO:0000269|PubMed:8962061};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00347,
CC ECO:0000269|PubMed:10660553};
CC -!- SUBUNIT: Homotetramer (PubMed:1331061). Dimer of dimers
CC (PubMed:10660553, PubMed:15947782). The diverse functions of this
CC enzyme involve different subunit organizations and conformations
CC (PubMed:10660553). {ECO:0000269|PubMed:10660553,
CC ECO:0000269|PubMed:1331061, ECO:0000269|PubMed:15947782}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1331061};
CC Peripheral membrane protein {ECO:0000269|PubMed:1331061}.
CC Note=Associated with the outer membrane in overproducing cells.
CC {ECO:0000269|PubMed:1331061}.
CC -!- PTM: An intermediate of this reaction is the autophosphorylated ppk in
CC which a phosphate is covalently linked to a histidine residue through a
CC N-P bond. {ECO:0000255|HAMAP-Rule:MF_00347,
CC ECO:0000269|PubMed:8962061}.
CC -!- SIMILARITY: Belongs to the polyphosphate kinase 1 (PPK1) family.
CC {ECO:0000255|HAMAP-Rule:MF_00347}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA83900.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L03719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00096; AAC75554.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16389.1; -; Genomic_DNA.
DR EMBL; M13747; AAA83900.1; ALT_INIT; Genomic_DNA.
DR EMBL; L06129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A44306; A44306.
DR RefSeq; NP_416996.1; NC_000913.3.
DR RefSeq; WP_000529576.1; NZ_STEB01000011.1.
DR PDB; 1XDO; X-ray; 3.00 A; A/B=2-688.
DR PDB; 1XDP; X-ray; 2.50 A; A/B=2-688.
DR PDBsum; 1XDO; -.
DR PDBsum; 1XDP; -.
DR AlphaFoldDB; P0A7B1; -.
DR SMR; P0A7B1; -.
DR BioGRID; 4261066; 64.
DR BioGRID; 851310; 6.
DR DIP; DIP-36218N; -.
DR IntAct; P0A7B1; 29.
DR STRING; 511145.b2501; -.
DR jPOST; P0A7B1; -.
DR PaxDb; P0A7B1; -.
DR PRIDE; P0A7B1; -.
DR EnsemblBacteria; AAC75554; AAC75554; b2501.
DR EnsemblBacteria; BAA16389; BAA16389; BAA16389.
DR GeneID; 66673634; -.
DR GeneID; 946971; -.
DR KEGG; ecj:JW2486; -.
DR KEGG; eco:b2501; -.
DR PATRIC; fig|1411691.4.peg.4237; -.
DR EchoBASE; EB1472; -.
DR eggNOG; COG0855; Bacteria.
DR HOGENOM; CLU_009678_6_1_6; -.
DR InParanoid; P0A7B1; -.
DR OMA; NIKWARK; -.
DR PhylomeDB; P0A7B1; -.
DR BioCyc; EcoCyc:PPK-MON; -.
DR BioCyc; MetaCyc:PPK-MON; -.
DR BRENDA; 2.7.4.1; 2026.
DR EvolutionaryTrace; P0A7B1; -.
DR PRO; PR:P0A7B1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0031241; C:periplasmic side of cell outer membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009358; C:polyphosphate kinase complex; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016778; F:diphosphotransferase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016776; F:phosphotransferase activity, phosphate group as acceptor; IDA:EcoCyc.
DR GO; GO:0008976; F:polyphosphate kinase activity; IDA:EcoCyc.
DR GO; GO:0043751; F:polyphosphate:AMP phosphotransferase activity; IMP:EcoCyc.
DR GO; GO:0006757; P:ATP generation from ADP; IDA:EcoCyc.
DR GO; GO:0006799; P:polyphosphate biosynthetic process; IDA:EcoCyc.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR Gene3D; 3.30.1840.10; -; 1.
DR HAMAP; MF_00347; Polyphosphate_kinase; 1.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR003414; PP_kinase.
DR InterPro; IPR041108; PP_kinase_C_1.
DR InterPro; IPR024953; PP_kinase_middle.
DR InterPro; IPR036830; PP_kinase_middle_dom_sf.
DR InterPro; IPR025200; PPK_C_dom2.
DR InterPro; IPR025198; PPK_N_dom.
DR InterPro; IPR036832; PPK_N_dom_sf.
DR PANTHER; PTHR30218; PTHR30218; 1.
DR Pfam; PF02503; PP_kinase; 1.
DR Pfam; PF13090; PP_kinase_C; 1.
DR Pfam; PF17941; PP_kinase_C_1; 1.
DR Pfam; PF13089; PP_kinase_N; 1.
DR PIRSF; PIRSF015589; PP_kinase; 1.
DR SUPFAM; SSF140356; SSF140356; 1.
DR TIGRFAMs; TIGR03705; poly_P_kin; 1.
DR PROSITE; PS50035; PLD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Direct protein sequencing;
KW Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..688
FT /note="Polyphosphate kinase"
FT /id="PRO_0000128640"
FT DOMAIN 430..464
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT ACT_SITE 435
FT /note="Phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347,
FT ECO:0000269|PubMed:8962061, ECO:0000305|PubMed:15947782"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347,
FT ECO:0007744|PDB:1XDP"
FT BINDING 375
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347,
FT ECO:0007744|PDB:1XDP"
FT BINDING 405
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347,
FT ECO:0007744|PDB:1XDP"
FT BINDING 468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347,
FT ECO:0007744|PDB:1XDP"
FT BINDING 564
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347,
FT ECO:0007744|PDB:1XDP"
FT BINDING 592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347,
FT ECO:0007744|PDB:1XDP"
FT MUTAGEN 375
FT /note="R->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:10660553"
FT MUTAGEN 380
FT /note="S->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:10660553"
FT MUTAGEN 424
FT /note="H->Q: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:8962061"
FT MUTAGEN 435
FT /note="H->A,Q: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:8962061"
FT MUTAGEN 454
FT /note="H->A,Q: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:8962061"
FT MUTAGEN 488
FT /note="F->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:10660553"
FT MUTAGEN 507
FT /note="P->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:10660553"
FT MUTAGEN 564
FT /note="R->A: Loss of enzyme activity, but retains low
FT autophosphorylation activity."
FT /evidence="ECO:0000269|PubMed:10660553"
FT MUTAGEN 592
FT /note="H->Q: Slightly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:8962061"
FT MUTAGEN 621
FT /note="R->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:10660553"
FT MUTAGEN 674
FT /note="Q->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:10660553"
FT HELIX 10..26
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 32..51
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 73..103
FT /evidence="ECO:0007829|PDB:1XDP"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1XDP"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:1XDP"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 199..211
FT /evidence="ECO:0007829|PDB:1XDP"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 218..229
FT /evidence="ECO:0007829|PDB:1XDP"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:1XDP"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 284..290
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 297..302
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 332..338
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 351..362
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 366..375
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 381..391
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:1XDP"
FT TURN 407..415
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 416..420
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 437..445
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 448..458
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 468..475
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 478..492
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 510..526
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 533..538
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 543..554
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 559..565
FT /evidence="ECO:0007829|PDB:1XDP"
FT TURN 574..576
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 580..585
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 587..591
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 595..598
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 600..602
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 605..610
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 615..619
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 620..627
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 631..645
FT /evidence="ECO:0007829|PDB:1XDP"
FT STRAND 649..653
FT /evidence="ECO:0007829|PDB:1XDP"
FT HELIX 673..684
FT /evidence="ECO:0007829|PDB:1XDP"
SQ SEQUENCE 688 AA; 80432 MW; E1EA6C53432E6935 CRC64;
MGQEKLYIEK ELSWLSFNER VLQEAADKSN PLIERMRFLG IYSNNLDEFY KVRFAELKRR
IIISEEQGSN SHSRHLLGKI QSRVLKADQE FDGLYNELLL EMARNQIFLI NERQLSVNQQ
NWLRHYFKQY LRQHITPILI NPDTDLVQFL KDDYTYLAVE IIRGDTIRYA LLEIPSDKVP
RFVNLPPEAP RRRKPMILLD NILRYCLDDI FKGFFDYDAL NAYSMKMTRD AEYDLVHEME
ASLMELMSSS LKQRLTAEPV RFVYQRDMPN ALVEVLREKL TISRYDSIVP GGRYHNFKDF
INFPNVGKAN LVNKPLPRLR HIWFDKAQFR NGFDAIRERD VLLYYPYHTF EHVLELLRQA
SFDPSVLAIK INIYRVAKDS RIIDSMIHAA HNGKKVTVVV ELQARFDEEA NIHWAKRLTE
AGVHVIFSAP GLKIHAKLFL ISRKENGEVV RYAHIGTGNF NEKTARLYTD YSLLTADARI
TNEVRRVFNF IENPYRPVTF DYLMVSPQNS RRLLYEMVDR EIANAQQGLP SGITLKLNNL
VDKGLVDRLY AASSSGVPVN LLVRGMCSLI PNLEGISDNI RAISIVDRYL EHDRVYIFEN
GGDKKVYLSS ADWMTRNIDY RIEVATPLLD PRLKQRVLDI IDILFSDTVK ARYIDKELSN
RYVPRGNRRK VRAQLAIYDY IKSLEQPE
