PSBZ_THEVB
ID PSBZ_THEVB Reviewed; 62 AA.
AC Q8DHJ2;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Photosystem II reaction center protein Z {ECO:0000255|HAMAP-Rule:MF_00644};
DE Short=PSII-Z {ECO:0000255|HAMAP-Rule:MF_00644};
GN Name=psbZ {ECO:0000255|HAMAP-Rule:MF_00644}; OrderedLocusNames=tsr1967;
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 [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 [2]
RP PROTEIN SEQUENCE OF 1-15, COFACTOR, SUBUNIT, 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 [3]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17967798; DOI=10.1093/pcp/pcm148;
RA Iwai M., Suzuki T., Dohmae N., Inoue Y., Ikeuchi M.;
RT "Absence of the PsbZ subunit prevents association of PsbK and Ycf12 with
RT the PSII complex in the thermophilic cyanobacterium Thermosynechococcus
RT elongatus BP-1.";
RL Plant Cell Physiol. 48:1758-1763(2007).
RN [4] {ECO:0000312|PDB:1S5L}
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP SUBUNIT, 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 (3.00 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP 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) IN PHOTOSYSTEM II, COFACTOR,
RP SUBUNIT, SUBCELLULAR LOCATION, FORMYLATION AT MET-1, MASS SPECTROMETRY, AND
RP TOPOLOGY.
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) IN PHOTOSYSTEM II, FUNCTION,
RP COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, FORMYLATION AT MET-1, AND MASS
RP 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) IN PHOTOSYSTEM II, FUNCTION,
RP 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) IN PHOTOSYSTEM II, COFACTOR,
RP 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) IN PHOTOSYSTEM II, COFACTOR,
RP 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: Controls the interaction of photosystem II (PSII) cores with
CC the light-harvesting antenna. May also aid in binding of PsbK, Ycf12
CC and the oxygen-evolving complex to PSII, at least in vitro. PSII is a
CC light-driven water plastoquinone oxidoreductase, using light energy to
CC abstract electrons from H(2)O, generating a proton gradient
CC subsequently used for ATP formation. {ECO:0000255|HAMAP-Rule:MF_00644,
CC ECO:0000269|PubMed:17967798, ECO:0000269|PubMed:20558739,
CC ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:25006873}.
CC -!- COFACTOR:
CC Note=PSII binds multiple chlorophylls, carotenoids and specific lipids.
CC {ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:17967798,
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: Cyanobacterial PSII is composed of 1 copy each of membrane
CC proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK,
CC PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, 3 peripheral proteins PsbO,
CC PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
CC {ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:17967798,
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 -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00644, ECO:0000269|PubMed:14764885,
CC ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689,
CC ECO:0000269|PubMed:17967798, 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}; Multi-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_00644,
CC ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:17967798,
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 the photosystem II
CC complex.
CC -!- MASS SPECTROMETRY: Mass=6798; Mass_error=5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19219048};
CC -!- MASS SPECTROMETRY: Mass=6793; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20558739};
CC -!- DISRUPTION PHENOTYPE: Cells grow normally under all light regimes
CC tested; it is dispensable for photoautotrophic growth. The deletion
CC strain is more tolerant to photoinhibition, while isolated PSII complex
CC contains less PsbK and Ycf12 than wild-type and also has reduced
CC oxygen-evolving capacity. {ECO:0000269|PubMed:17967798}.
CC -!- SIMILARITY: Belongs to the PsbZ family. {ECO:0000255|HAMAP-
CC Rule:MF_00644}.
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DR EMBL; BA000039; BAC09519.1; -; Genomic_DNA.
DR RefSeq; NP_682757.1; NC_004113.1.
DR RefSeq; WP_011057802.1; NC_004113.1.
DR PDB; 1S5L; X-ray; 3.50 A; Z/z=1-62.
DR PDB; 2AXT; X-ray; 3.00 A; Z/z=1-62.
DR PDB; 3KZI; X-ray; 3.60 A; Z=1-62.
DR PDB; 4FBY; X-ray; 6.56 A; Z/l=1-62.
DR PDB; 4IXQ; X-ray; 5.70 A; Z/z=1-62.
DR PDB; 4IXR; X-ray; 5.90 A; Z/z=1-62.
DR PDB; 4PBU; X-ray; 5.00 A; Z/z=1-62.
DR PDB; 4PJ0; X-ray; 2.44 A; Z/z=1-62.
DR PDB; 4RVY; X-ray; 5.50 A; Z/z=1-62.
DR PDB; 4TNH; X-ray; 4.90 A; Z/z=1-62.
DR PDB; 4TNI; X-ray; 4.60 A; Z/z=1-62.
DR PDB; 4TNJ; X-ray; 4.50 A; Z/z=1-62.
DR PDB; 4TNK; X-ray; 5.20 A; Z/z=1-62.
DR PDB; 4V62; X-ray; 2.90 A; AZ/BZ=1-62.
DR PDB; 4V82; X-ray; 3.20 A; AZ/BZ=1-62.
DR PDB; 5E79; X-ray; 3.50 A; Z/z=1-62.
DR PDB; 5E7C; X-ray; 4.50 A; Z/z=1-62.
DR PDB; 5H2F; X-ray; 2.20 A; Z/z=1-62.
DR PDB; 5KAF; X-ray; 3.00 A; Z/z=1-62.
DR PDB; 5KAI; X-ray; 2.80 A; Z/z=1-62.
DR PDB; 5MX2; X-ray; 2.20 A; Z/z=1-62.
DR PDB; 5TIS; X-ray; 2.25 A; Z/z=1-62.
DR PDB; 5ZZN; X-ray; 2.10 A; Z/z=1-62.
DR PDB; 6DHE; X-ray; 2.05 A; Z/z=1-62.
DR PDB; 6DHF; X-ray; 2.08 A; Z/z=1-62.
DR PDB; 6DHG; X-ray; 2.50 A; Z/z=1-62.
DR PDB; 6DHH; X-ray; 2.20 A; Z/z=1-62.
DR PDB; 6DHO; X-ray; 2.07 A; Z/z=1-62.
DR PDB; 6DHP; X-ray; 2.04 A; Z/z=1-62.
DR PDB; 6W1O; X-ray; 2.08 A; Z/z=1-62.
DR PDB; 6W1P; X-ray; 2.26 A; Z/z=1-62.
DR PDB; 6W1Q; X-ray; 2.27 A; Z/z=1-62.
DR PDB; 6W1R; X-ray; 2.23 A; Z/z=1-62.
DR PDB; 6W1T; X-ray; 2.01 A; Z/z=1-62.
DR PDB; 6W1U; X-ray; 2.09 A; Z/z=1-62.
DR PDB; 6W1V; X-ray; 2.09 A; Z/z=1-62.
DR PDB; 7NHO; EM; 2.66 A; Z=1-62.
DR PDB; 7NHP; EM; 2.72 A; Z=1-62.
DR PDB; 7NHQ; EM; 2.68 A; Z=1-62.
DR PDB; 7RF1; X-ray; 1.89 A; Z/z=1-62.
DR PDB; 7RF2; X-ray; 2.08 A; Z/z=1-62.
DR PDB; 7RF3; X-ray; 2.26 A; Z/z=1-62.
DR PDB; 7RF4; X-ray; 2.27 A; Z/z=1-62.
DR PDB; 7RF5; X-ray; 2.23 A; Z/z=1-62.
DR PDB; 7RF6; X-ray; 2.01 A; Z/z=1-62.
DR PDB; 7RF7; X-ray; 2.09 A; Z/z=1-62.
DR PDB; 7RF8; X-ray; 2.09 A; Z/z=1-62.
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; 7NHO; -.
DR PDBsum; 7NHP; -.
DR PDBsum; 7NHQ; -.
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; Q8DHJ2; -.
DR SMR; Q8DHJ2; -.
DR DIP; DIP-48504N; -.
DR IntAct; Q8DHJ2; 1.
DR STRING; 197221.22295693; -.
DR EnsemblBacteria; BAC09519; BAC09519; BAC09519.
DR KEGG; tel:tsr1967; -.
DR PATRIC; fig|197221.4.peg.2057; -.
DR eggNOG; ENOG5032ZB0; Bacteria.
DR OMA; NWEQSKS; -.
DR OrthoDB; 2012567at2; -.
DR EvolutionaryTrace; Q8DHJ2; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009539; C:photosystem II reaction center; 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 Gene3D; 1.10.287.740; -; 1.
DR HAMAP; MF_00644; PSII_PsbZ; 1.
DR InterPro; IPR002644; PSII_PsbZ.
DR InterPro; IPR036512; PSII_PsbZ_sf.
DR PANTHER; PTHR34971; PTHR34971; 1.
DR Pfam; PF01737; Ycf9; 1.
DR SUPFAM; SSF161055; SSF161055; 1.
DR TIGRFAMs; TIGR03043; PS_II_psbZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Formylation; Membrane;
KW Photosynthesis; Photosystem II; Reaction center; Reference proteome;
KW Thylakoid; Transmembrane; Transmembrane helix.
FT CHAIN 1..62
FT /note="Photosystem II reaction center protein Z"
FT /id="PRO_0000217733"
FT TOPO_DOM 1..10
FT /note="Lumenal"
FT TRANSMEM 11..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00644,
FT ECO:0000269|PubMed:19219048"
FT TOPO_DOM 25..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TRANSMEM 39..53
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00644,
FT ECO:0000269|PubMed:19219048"
FT TOPO_DOM 54..62
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:19219048"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:19219048,
FT ECO:0000269|PubMed:20558739"
FT HELIX 4..27
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:5MX2"
FT HELIX 33..61
FT /evidence="ECO:0007829|PDB:5ZZN"
SQ SEQUENCE 62 AA; 6764 MW; 313A629F73715DD8 CRC64;
MTILFQLALA ALVILSFVMV IGVPVAYASP QDWDRSKQLI FLGSGLWIAL VLVVGVLNFF
VV