PSBU_THEVB
ID PSBU_THEVB Reviewed; 134 AA.
AC Q9F1L5;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Photosystem II 12 kDa extrinsic protein {ECO:0000255|HAMAP-Rule:MF_00589};
DE AltName: Full=PS II complex 12 kDa extrinsic protein {ECO:0000255|HAMAP-Rule:MF_00589};
DE AltName: Full=PSII-U {ECO:0000255|HAMAP-Rule:MF_00589};
DE Flags: Precursor;
GN Name=psbU {ECO:0000255|HAMAP-Rule:MF_00589}; OrderedLocusNames=tll2409;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Katoh H., Ikeuchi M.;
RT "Cloning and disruption of the psbU gene from thermophilic
RT Thermosynechococcus (formerly Synechococcus) elongatus BP-1.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [3]
RP PROTEIN SEQUENCE OF 31-39, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=17935689; DOI=10.1016/j.bbabio.2007.08.008;
RA Kashino Y., Takahashi T., Inoue-Kashino N., Ban A., Ikeda Y., Satoh K.,
RA Sugiura M.;
RT "Ycf12 is a core subunit in the photosystem II complex.";
RL Biochim. Biophys. Acta 1767:1269-1275(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR, SUBUNIT,
RP AND SUBCELLULAR LOCATION.
RX PubMed=14764885; DOI=10.1126/science.1093087;
RA Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S.;
RT "Architecture of the photosynthetic oxygen-evolving center.";
RL Science 303:1831-1838(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 31-134 IN PHOTOSYSTEM II,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=16355230; DOI=10.1038/nature04224;
RA Loll B., Kern J., Saenger W., Zouni A., Biesiadka J.;
RT "Towards complete cofactor arrangement in the 3.0 A resolution structure of
RT photosystem II.";
RL Nature 438:1040-1044(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 31-134 IN PHOTOSYSTEM II,
RP COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=19219048; DOI=10.1038/nsmb.1559;
RA Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.;
RT "Cyanobacterial photosystem II at 2.9-A resolution and the role of
RT quinones, lipids, channels and chloride.";
RL Nat. Struct. Mol. Biol. 16:334-342(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 31-134 IN PHOTOSYSTEM II,
RP FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=20558739; DOI=10.1074/jbc.m110.127589;
RA Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W.,
RA Zouni A.;
RT "Crystal structure of monomeric photosystem II from Thermosynechococcus
RT elongatus at 3.6 A resolution.";
RL J. Biol. Chem. 285:26255-26262(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 31-134 IN PHOTOSYSTEM II,
RP FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=21367867; DOI=10.1074/jbc.m110.215970;
RA Broser M., Glockner C., Gabdulkhakov A., Guskov A., Buchta J., Kern J.,
RA Muh F., Dau H., Saenger W., Zouni A.;
RT "Structural basis of cyanobacterial photosystem II inhibition by the
RT herbicide terbutryn.";
RL J. Biol. Chem. 286:15964-15972(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) OF 31-134 IN PHOTOSYSTEM II,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=22665786; DOI=10.1073/pnas.1204598109;
RA Kern J., Alonso-Mori R., Hellmich J., Tran R., Hattne J., Laksmono H.,
RA Glockner C., Echols N., Sierra R.G., Sellberg J., Lassalle-Kaiser B.,
RA Gildea R.J., Glatzel P., Grosse-Kunstleve R.W., Latimer M.J., McQueen T.A.,
RA DiFiore D., Fry A.R., Messerschmidt M., Miahnahri A., Schafer D.W.,
RA Seibert M.M., Sokaras D., Weng T.C., Zwart P.H., White W.E., Adams P.D.,
RA Bogan M.J., Boutet S., Williams G.J., Messinger J., Sauter N.K., Zouni A.,
RA Bergmann U., Yano J., Yachandra V.K.;
RT "Room temperature femtosecond X-ray diffraction of photosystem II
RT microcrystals.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:9721-9726(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=23413188; DOI=10.1126/science.1234273;
RA Kern J., Alonso-Mori R., Tran R., Hattne J., Gildea R.J., Echols N.,
RA Glockner C., Hellmich J., Laksmono H., Sierra R.G., Lassalle-Kaiser B.,
RA Koroidov S., Lampe A., Han G., Gul S., Difiore D., Milathianaki D.,
RA Fry A.R., Miahnahri A., Schafer D.W., Messerschmidt M., Seibert M.M.,
RA Koglin J.E., Sokaras D., Weng T.C., Sellberg J., Latimer M.J.,
RA Grosse-Kunstleve R.W., Zwart P.H., White W.E., Glatzel P., Adams P.D.,
RA Bogan M.J., Williams G.J., Boutet S., Messinger J., Zouni A., Sauter N.K.,
RA Yachandra V.K., Bergmann U., Yano J.;
RT "Simultaneous femtosecond X-ray spectroscopy and diffraction of photosystem
RT II at room temperature.";
RL Science 340:491-495(2013).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 38-134 IN PHOTOSYSTEM II,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=25043005; DOI=10.1038/nature13453;
RA Kupitz C., Basu S., Grotjohann I., Fromme R., Zatsepin N.A., Rendek K.N.,
RA Hunter M.S., Shoeman R.L., White T.A., Wang D., James D., Yang J.H.,
RA Cobb D.E., Reeder B., Sierra R.G., Liu H., Barty A., Aquila A.L.,
RA Deponte D., Kirian R.A., Bari S., Bergkamp J.J., Beyerlein K.R.,
RA Bogan M.J., Caleman C., Chao T.C., Conrad C.E., Davis K.M.,
RA Fleckenstein H., Galli L., Hau-Riege S.P., Kassemeyer S., Laksmono H.,
RA Liang M., Lomb L., Marchesini S., Martin A.V., Messerschmidt M.,
RA Milathianaki D., Nass K., Ros A., Roy-Chowdhury S., Schmidt K., Seibert M.,
RA Steinbrener J., Stellato F., Yan L., Yoon C., Moore T.A., Moore A.L.,
RA Pushkar Y., Williams G.J., Boutet S., Doak R.B., Weierstall U., Frank M.,
RA Chapman H.N., Spence J.C., Fromme P.;
RT "Serial time-resolved crystallography of photosystem II using a femtosecond
RT X-ray laser.";
RL Nature 513:261-265(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=25006873; DOI=10.1038/ncomms5371;
RA Kern J., Tran R., Alonso-Mori R., Koroidov S., Echols N., Hattne J.,
RA Ibrahim M., Gul S., Laksmono H., Sierra R.G., Gildea R.J., Han G.,
RA Hellmich J., Lassalle-Kaiser B., Chatterjee R., Brewster A.S., Stan C.A.,
RA Gloeckner C., Lampe A., DiFiore D., Milathianaki D., Fry A.R.,
RA Seibert M.M., Koglin J.E., Gallo E., Uhlig J., Sokaras D., Weng T.C.,
RA Zwart P.H., Skinner D.E., Bogan M.J., Messerschmidt M., Glatzel P.,
RA Williams G.J., Boutet S., Adams P.D., Zouni A., Messinger J., Sauter N.K.,
RA Bergmann U., Yano J., Yachandra V.K.;
RT "Taking snapshots of photosynthetic water oxidation using femtosecond X-ray
RT diffraction and spectroscopy.";
RL Nat. Commun. 5:4371-4371(2014).
CC -!- FUNCTION: Stabilizes the structure of photosystem II oxygen-evolving
CC complex (OEC), the ion environment of oxygen evolution and protects the
CC OEC against heat-induced inactivation. PSII is a light-driven water
CC plastoquinone oxidoreductase, using light energy to abstract electrons
CC from H(2)O, generating a proton gradient subsequently used for ATP
CC formation. {ECO:0000255|HAMAP-Rule:MF_00589,
CC ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC ECO:0000269|PubMed:25006873}.
CC -!- COFACTOR:
CC Note=PSII binds multiple chlorophylls, carotenoids and specific lipids.
CC {ECO:0000255|HAMAP-Rule:MF_00589, ECO:0000269|PubMed:14764885,
CC ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689,
CC ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC ECO:0000269|PubMed:25043005};
CC -!- SUBUNIT: The cyanobacterial oxygen-evolving complex is composed of
CC PsbO, PsbP, PsbQ, PsbV and PsbU. PsbP and PsbQ are not seen in the
CC crystal structures; however there is biochemical evidence that they are
CC part of the OEC (By similarity). Cyanobacterial PSII is composed of 1
CC copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF,
CC PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, 3
CC peripheral proteins PsbO, PsbU, PsbV and a large number of cofactors.
CC It forms dimeric complexes. {ECO:0000250, ECO:0000269|PubMed:14764885,
CC ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
CC ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
CC ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00589, ECO:0000269|PubMed:14764885,
CC ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:20558739,
CC ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC ECO:0000269|PubMed:25043005}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00589, ECO:0000269|PubMed:14764885,
CC ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689,
CC ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC ECO:0000269|PubMed:25043005}; Lumenal side {ECO:0000255|HAMAP-
CC Rule:MF_00589, ECO:0000269|PubMed:14764885,
CC ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689,
CC ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC ECO:0000269|PubMed:25043005}. Note=Associated with photosystem II at
CC the lumenal side of the thylakoid membrane.
CC -!- MASS SPECTROMETRY: Mass=11649; Mass_error=8; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19219048};
CC -!- MASS SPECTROMETRY: Mass=11641; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20558739};
CC -!- SIMILARITY: Belongs to the PsbU family. {ECO:0000255|HAMAP-
CC Rule:MF_00589}.
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DR EMBL; AB052848; BAB20625.1; -; Genomic_DNA.
DR EMBL; BA000039; BAC09961.1; -; Genomic_DNA.
DR RefSeq; NP_683199.1; NC_004113.1.
DR RefSeq; WP_011058241.1; NC_004113.1.
DR PDB; 1S5L; X-ray; 3.50 A; U/u=1-134.
DR PDB; 2AXT; X-ray; 3.00 A; U/u=31-134.
DR PDB; 3KZI; X-ray; 3.60 A; U=31-134.
DR PDB; 4FBY; X-ray; 6.56 A; U/h=31-134.
DR PDB; 4IXQ; X-ray; 5.70 A; U/u=1-134.
DR PDB; 4IXR; X-ray; 5.90 A; U/u=1-134.
DR PDB; 4PBU; X-ray; 5.00 A; U/u=38-134.
DR PDB; 4PJ0; X-ray; 2.44 A; U/u=1-134.
DR PDB; 4RVY; X-ray; 5.50 A; U/u=38-134.
DR PDB; 4TNH; X-ray; 4.90 A; U/u=1-134.
DR PDB; 4TNI; X-ray; 4.60 A; U/u=1-134.
DR PDB; 4TNJ; X-ray; 4.50 A; U/u=1-134.
DR PDB; 4TNK; X-ray; 5.20 A; U/u=1-134.
DR PDB; 4V62; X-ray; 2.90 A; AU/BU=31-134.
DR PDB; 4V82; X-ray; 3.20 A; AU/BU=31-134.
DR PDB; 5E79; X-ray; 3.50 A; U/u=38-134.
DR PDB; 5E7C; X-ray; 4.50 A; U/u=38-134.
DR PDB; 5H2F; X-ray; 2.20 A; U/u=38-134.
DR PDB; 5KAF; X-ray; 3.00 A; U/u=1-134.
DR PDB; 5KAI; X-ray; 2.80 A; U/u=1-134.
DR PDB; 5MX2; X-ray; 2.20 A; U/u=1-134.
DR PDB; 5TIS; X-ray; 2.25 A; U/u=1-134.
DR PDB; 5ZZN; X-ray; 2.10 A; U/u=38-134.
DR PDB; 6DHE; X-ray; 2.05 A; U/u=38-134.
DR PDB; 6DHF; X-ray; 2.08 A; U/u=38-134.
DR PDB; 6DHG; X-ray; 2.50 A; U/u=38-134.
DR PDB; 6DHH; X-ray; 2.20 A; U/u=38-134.
DR PDB; 6DHO; X-ray; 2.07 A; U/u=38-134.
DR PDB; 6DHP; X-ray; 2.04 A; U/u=38-134.
DR PDB; 6W1O; X-ray; 2.08 A; U/u=1-134.
DR PDB; 6W1P; X-ray; 2.26 A; U/u=1-134.
DR PDB; 6W1Q; X-ray; 2.27 A; U/u=1-134.
DR PDB; 6W1R; X-ray; 2.23 A; U/u=1-134.
DR PDB; 6W1T; X-ray; 2.01 A; U/u=1-134.
DR PDB; 6W1U; X-ray; 2.09 A; U/u=1-134.
DR PDB; 6W1V; X-ray; 2.09 A; U/u=1-134.
DR PDB; 7RF1; X-ray; 1.89 A; U/u=1-134.
DR PDB; 7RF2; X-ray; 2.08 A; U/u=1-134.
DR PDB; 7RF3; X-ray; 2.26 A; U/u=1-134.
DR PDB; 7RF4; X-ray; 2.27 A; U/u=1-134.
DR PDB; 7RF5; X-ray; 2.23 A; U/u=1-134.
DR PDB; 7RF6; X-ray; 2.01 A; U/u=1-134.
DR PDB; 7RF7; X-ray; 2.09 A; U/u=1-134.
DR PDB; 7RF8; X-ray; 2.09 A; U/u=1-134.
DR PDBsum; 1S5L; -.
DR PDBsum; 2AXT; -.
DR PDBsum; 3KZI; -.
DR PDBsum; 4FBY; -.
DR PDBsum; 4IXQ; -.
DR PDBsum; 4IXR; -.
DR PDBsum; 4PBU; -.
DR PDBsum; 4PJ0; -.
DR PDBsum; 4RVY; -.
DR PDBsum; 4TNH; -.
DR PDBsum; 4TNI; -.
DR PDBsum; 4TNJ; -.
DR PDBsum; 4TNK; -.
DR PDBsum; 4V62; -.
DR PDBsum; 4V82; -.
DR PDBsum; 5E79; -.
DR PDBsum; 5E7C; -.
DR PDBsum; 5H2F; -.
DR PDBsum; 5KAF; -.
DR PDBsum; 5KAI; -.
DR PDBsum; 5MX2; -.
DR PDBsum; 5TIS; -.
DR PDBsum; 5ZZN; -.
DR PDBsum; 6DHE; -.
DR PDBsum; 6DHF; -.
DR PDBsum; 6DHG; -.
DR PDBsum; 6DHH; -.
DR PDBsum; 6DHO; -.
DR PDBsum; 6DHP; -.
DR PDBsum; 6W1O; -.
DR PDBsum; 6W1P; -.
DR PDBsum; 6W1Q; -.
DR PDBsum; 6W1R; -.
DR PDBsum; 6W1T; -.
DR PDBsum; 6W1U; -.
DR PDBsum; 6W1V; -.
DR PDBsum; 7RF1; -.
DR PDBsum; 7RF2; -.
DR PDBsum; 7RF3; -.
DR PDBsum; 7RF4; -.
DR PDBsum; 7RF5; -.
DR PDBsum; 7RF6; -.
DR PDBsum; 7RF7; -.
DR PDBsum; 7RF8; -.
DR AlphaFoldDB; Q9F1L5; -.
DR SMR; Q9F1L5; -.
DR DIP; DIP-48501N; -.
DR IntAct; Q9F1L5; 1.
DR STRING; 197221.22296137; -.
DR EnsemblBacteria; BAC09961; BAC09961; BAC09961.
DR KEGG; tel:tll2409; -.
DR PATRIC; fig|197221.4.peg.2532; -.
DR eggNOG; COG1555; Bacteria.
DR OMA; PTMAGKI; -.
DR OrthoDB; 1626529at2; -.
DR EvolutionaryTrace; Q9F1L5; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0019898; C:extrinsic component of membrane; IEA:InterPro.
DR GO; GO:0009654; C:photosystem II oxygen evolving complex; IEA:InterPro.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR GO; GO:0042549; P:photosystem II stabilization; IEA:InterPro.
DR HAMAP; MF_00589; PSII_PsbU; 1.
DR InterPro; IPR010527; PSII_PsbU.
DR Pfam; PF06514; PsbU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Membrane;
KW Photosynthesis; Photosystem II; Reference proteome; Signal; Thylakoid;
KW Transport.
FT SIGNAL 1..30
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00589,
FT ECO:0000269|PubMed:17935689"
FT CHAIN 31..134
FT /note="Photosystem II 12 kDa extrinsic protein"
FT /id="PRO_0000029602"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:1S5L"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:5ZZN"
SQ SEQUENCE 134 AA; 15018 MW; C75346D2DA75447F CRC64;
MQRLGRWLAL AYFVGVSLLG WINWSAPTLA ATASTEEELV NVVDEKLGTA YGEKIDLNNT
NIAAFIQYRG LYPTLAKLIV KNAPYESVED VLNIPGLTER QKQILRENLE HFTVTEVETA
LVEGGDRYNN GLYK
