NOSZ_PSEST
ID NOSZ_PSEST Reviewed; 638 AA.
AC P19573; P19846; Q6LAE4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Nitrous-oxide reductase;
DE EC=1.7.2.4;
DE AltName: Full=N(2)OR;
DE AltName: Full=N2O reductase;
DE Flags: Precursor;
GN Name=nosZ;
OS Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=316;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC 568 / 218 / ZoBell 632;
RX PubMed=3049543; DOI=10.1128/jb.170.10.4658-4668.1988;
RA Viebrock A., Zumft W.G.;
RT "Molecular cloning, heterologous expression, and primary structure of the
RT structural gene for the copper enzyme nitrous oxide reductase from
RT denitrifying Pseudomonas stutzeri.";
RL J. Bacteriol. 170:4658-4668(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC 568 / 218 / ZoBell 632;
RX PubMed=2170125; DOI=10.1111/j.1432-1033.1990.tb19265.x;
RA Zumft W.G., Viebrock-Sambale A., Braun C.;
RT "Nitrous oxide reductase from denitrifying Pseudomonas stutzeri. Genes for
RT copper-processing and properties of the deduced products, including a new
RT member of the family of ATP/GTP-binding proteins.";
RL Eur. J. Biochem. 192:591-599(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RC STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC 568 / 218 / ZoBell 632;
RX PubMed=1644760; DOI=10.1128/jb.174.16.5332-5339.1992;
RA Cuypers H., Viebrock-Sambale A., Zumft W.G.;
RT "NosR, a membrane-bound regulatory component necessary for expression of
RT nitrous oxide reductase in denitrifying Pseudomonas stutzeri.";
RL J. Bacteriol. 174:5332-5339(1992).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND COFACTOR.
RX PubMed=3000778; DOI=10.1111/j.1432-1033.1985.tb09324.x;
RA Coyle C.L., Zumft W.G., Kroneck P.M., Korner H., Jakob W.;
RT "Nitrous oxide reductase from denitrifying Pseudomonas perfectomarina.
RT Purification and properties of a novel multicopper enzyme.";
RL Eur. J. Biochem. 153:459-467(1985).
RN [5]
RP CHARACTERIZATION.
RX PubMed=2542963; DOI=10.1073/pnas.86.11.4082;
RA Scott R.A., Zumft W.G., Coyle C.L., Dooley D.M.;
RT "Pseudomonas stutzeri N2O reductase contains CuA-type sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:4082-4086(1989).
RN [6]
RP CHARACTERIZATION.
RX PubMed=11456570; DOI=10.1021/ja994322i;
RA Alvarez M.L., Ai J., Zumft W.G., Sanders-Loehr J., Dooley D.M.;
RT "Characterization of the copper-sulfur chromophores in nitrous oxide
RT reductase by resonance Raman spectroscopy: evidence for sulfur coordination
RT in the catalytic cluster.";
RL J. Am. Chem. Soc. 123:576-587(2001).
CC -!- FUNCTION: Nitrous-oxide reductase is part of a bacterial respiratory
CC system which is activated under anaerobic conditions in the presence of
CC nitrate or nitrous oxide. {ECO:0000269|PubMed:3000778}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + H2O + N2 = 2 Fe(II)-[cytochrome c]
CC + 2 H(+) + nitrous oxide; Xref=Rhea:RHEA:43108, Rhea:RHEA-COMP:10350,
CC Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17045, ChEBI:CHEBI:17997, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=1.7.2.4; Evidence={ECO:0000269|PubMed:3000778};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:3000778};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000269|PubMed:3000778};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:3000778};
CC Note=Binds 6 Cu cations. Each subunit contains 2 copper centers; Cu(A)
CC (binuclear) and Cu(Z) (tetranuclear). Cu(Z) is thought to be the site
CC of nitrous oxide reduction. {ECO:0000269|PubMed:3000778};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification);
CC dinitrogen from nitrate: step 4/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:3000778}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the NosZ family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the cytochrome c
CC oxidase subunit 2 family. {ECO:0000305}.
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DR EMBL; X53676; CAA37714.2; -; Genomic_DNA.
DR PIR; A31845; A31845.
DR RefSeq; WP_003279971.1; NZ_CP036186.1.
DR PDB; 3SBP; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-638.
DR PDB; 3SBQ; X-ray; 1.70 A; A/B=1-638.
DR PDB; 3SBR; X-ray; 2.24 A; A/B/C/D/E/F/G/H=1-638.
DR PDB; 6RKZ; X-ray; 1.60 A; A/B=1-638.
DR PDB; 6RL0; X-ray; 1.78 A; A/B/C/D=1-638.
DR PDB; 6Y6Y; X-ray; 1.67 A; A/B=1-638.
DR PDB; 6Y71; X-ray; 1.64 A; A/B=1-638.
DR PDB; 6Y72; X-ray; 1.55 A; A/B=1-638.
DR PDB; 6Y77; X-ray; 1.49 A; A/B=1-638.
DR PDB; 6Y7D; X-ray; 1.60 A; A/B=1-638.
DR PDB; 6Y7E; X-ray; 1.60 A; A/B=1-638.
DR PDB; 7APY; X-ray; 1.78 A; A/B=1-638.
DR PDB; 7AQ0; X-ray; 1.58 A; A/B=1-638.
DR PDB; 7AQ2; X-ray; 1.68 A; A/B=1-638.
DR PDB; 7AQ3; X-ray; 1.64 A; A/B=1-638.
DR PDB; 7AQ4; X-ray; 1.71 A; A/B=1-638.
DR PDB; 7AQ5; X-ray; 1.70 A; A/B=1-638.
DR PDB; 7AQ6; X-ray; 1.51 A; A/B=1-638.
DR PDB; 7AQ7; X-ray; 1.61 A; A/B=1-638.
DR PDB; 7AQ8; X-ray; 1.79 A; A/B=1-638.
DR PDB; 7AQ9; X-ray; 1.58 A; A/B=1-638.
DR PDB; 7AQA; X-ray; 1.50 A; A/B=1-638.
DR PDBsum; 3SBP; -.
DR PDBsum; 3SBQ; -.
DR PDBsum; 3SBR; -.
DR PDBsum; 6RKZ; -.
DR PDBsum; 6RL0; -.
DR PDBsum; 6Y6Y; -.
DR PDBsum; 6Y71; -.
DR PDBsum; 6Y72; -.
DR PDBsum; 6Y77; -.
DR PDBsum; 6Y7D; -.
DR PDBsum; 6Y7E; -.
DR PDBsum; 7APY; -.
DR PDBsum; 7AQ0; -.
DR PDBsum; 7AQ2; -.
DR PDBsum; 7AQ3; -.
DR PDBsum; 7AQ4; -.
DR PDBsum; 7AQ5; -.
DR PDBsum; 7AQ6; -.
DR PDBsum; 7AQ7; -.
DR PDBsum; 7AQ8; -.
DR PDBsum; 7AQ9; -.
DR PDBsum; 7AQA; -.
DR AlphaFoldDB; P19573; -.
DR SMR; P19573; -.
DR DIP; DIP-59162N; -.
DR STRING; 32042.PstZobell_01047; -.
DR KEGG; ag:CAA37714; -.
DR eggNOG; COG4263; Bacteria.
DR BioCyc; MetaCyc:MON-243; -.
DR BRENDA; 1.7.2.4; 5158.
DR UniPathway; UPA00652; UER00709.
DR EvolutionaryTrace; P19573; -.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; IDA:CACAO.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0050304; F:nitrous-oxide reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015677; P:copper ion import; IMP:CACAO.
DR GO; GO:0019333; P:denitrification pathway; IEA:UniProtKB-UniPathway.
DR CDD; cd04223; N2OR_C; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR HAMAP; MF_00716; NosZ; 1.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR011045; N2O_reductase_N.
DR InterPro; IPR034205; N2OR_C.
DR InterPro; IPR023644; NO_Rdtase.
DR InterPro; IPR041114; Nos_propeller.
DR InterPro; IPR041142; NOS_propeller_2.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF18764; nos_propeller; 1.
DR Pfam; PF18793; nos_propeller_2; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF50974; SSF50974; 1.
DR TIGRFAMs; TIGR04244; nitrous_NosZ_RR; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Copper; Direct protein sequencing; Metal-binding;
KW Oxidoreductase; Periplasm; Signal.
FT SIGNAL 1..52
FT /note="Tat-type signal"
FT /evidence="ECO:0000255"
FT CHAIN 53..638
FT /note="Nitrous-oxide reductase"
FT /id="PRO_0000019831"
FT REGION 542..638
FT /note="COX2-like"
FT BINDING 129
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z2"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z3"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z2"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z1"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z1"
FT /evidence="ECO:0000250"
FT BINDING 433
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z3"
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 494
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="Z4"
FT /evidence="ECO:0000250"
FT BINDING 583
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT BINDING 618
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT BINDING 618
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 620
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 622
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT BINDING 622
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 626
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 629
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT CONFLICT 14
FT /note="E -> EE (in Ref. 3)"
FT /evidence="ECO:0000305"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:6Y77"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:6Y77"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:6Y77"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:6Y77"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:6Y77"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:6Y77"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 139..149
FT /evidence="ECO:0007829|PDB:6Y77"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:6Y77"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:6Y77"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 228..244
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 246..256
FT /evidence="ECO:0007829|PDB:6Y77"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:7AQA"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:6Y77"
FT HELIX 280..289
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:7AQ7"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:3SBP"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 344..351
FT /evidence="ECO:0007829|PDB:6Y77"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:6Y77"
FT HELIX 355..359
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:7AQ9"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 387..395
FT /evidence="ECO:0007829|PDB:6Y77"
FT TURN 396..399
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:6Y77"
FT HELIX 406..413
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 421..426
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:6Y77"
FT TURN 437..440
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 448..454
FT /evidence="ECO:0007829|PDB:6Y77"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:7AQA"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 482..489
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 496..500
FT /evidence="ECO:0007829|PDB:6Y77"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:6Y77"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:6Y77"
FT HELIX 518..526
FT /evidence="ECO:0007829|PDB:6Y77"
FT TURN 531..533
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 536..540
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 543..551
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 554..556
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 559..563
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 567..574
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 583..587
FT /evidence="ECO:0007829|PDB:6Y77"
FT TURN 588..591
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 592..596
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 601..607
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 612..617
FT /evidence="ECO:0007829|PDB:6Y77"
FT HELIX 626..628
FT /evidence="ECO:0007829|PDB:6Y77"
FT STRAND 630..636
FT /evidence="ECO:0007829|PDB:6Y77"
SQ SEQUENCE 638 AA; 70822 MW; C2CA79CCB556061B CRC64;
MSDKDSKNTP QVPEKLGLSR RGFLGASAVT GAAVAATALG GAVMTRESWA QAVKESKQKI
HVGPGELDDY YGFWSGGHQG EVRVLGVPSM RELMRIPVFN VDSATGWGLT NESRHIMGDS
AKFLNGDCHH PHISMTDGKY DGKYLFINDK ANSRVARIRL DIMKCDKMIT VPNVQAIHGL
RLQKVPHTKY VFANAEFIIP HPNDGKVFDL QDENSYTMYN AIDAETMEMA FQVIVDGNLD
NTDADYTGRF AAATCYNSEK AFDLGGMMRN ERDWVVVFDI HAVEAAVKAG DFITLGDSKT
PVLDGRKKDG KDSKFTRYVP VPKNPHGCNT SSDGKYFIAA GKLSPTCSMI AIDKLPDLFA
GKLADPRDVI VGEPELGLGP LHTTFDGRGN AYTTLFIDSQ VVKWNMEEAV RAYKGEKVNY
IKQKLDVHYQ PGHLHASLCE TNEADGKWLV ALSKFSKDRF LPVGPLHPEN DQLIDISGDE
MKLVHDGPTF AEPHDCIMAR RDQIKTKKIW DRNDPFFAPT VEMAKKDGIN LDTDNKVIRD
GNKVRVYMTS MAPAFGVQEF TVKQGDEVTV TITNIDQIED VSHGFVVVNH GVSMEISPQQ
TSSITFVADK PGLHWYYCSW FCHALHMEMV GRMMVEPA
