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Database: UniProt
Entry: Q8DIP0
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ID   PSBE_THEEB              Reviewed;          84 AA.
AC   Q8DIP0;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   07-APR-2021, entry version 130.
DE   RecName: Full=Cytochrome b559 subunit alpha {ECO:0000255|HAMAP-Rule:MF_00642};
DE   AltName: Full=PSII reaction center subunit V {ECO:0000255|HAMAP-Rule:MF_00642};
GN   Name=psbE {ECO:0000255|HAMAP-Rule:MF_00642}; OrderedLocusNames=tsr1541;
OS   Thermosynechococcus elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=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 2-8, CLEAVAGE OF INITIATOR METHIONINE, AND SUBCELLULAR
RP   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   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   DOI=10.1039/B406989G;
RA   Biesiadka J., Loll B., Kern J., Irrgang K.-D., Zouni A.;
RT   "Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a
RT   closer look at the Mn-cluster.";
RL   Phys. Chem. Chem. Phys. 6:4733-4736(2004).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
RP   COFACTOR, 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 (3.2 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=16049768; DOI=10.1007/s11120-004-7077-x;
RA   Kern J., Loll B., Zouni A., Saenger W., Irrgang K.D., Biesiadka J.;
RT   "Cyanobacterial photosystem II at 3.2 A resolution -- the plastoquinone
RT   binding pockets.";
RL   Photosyn. Res. 84:153-159(2005).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=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   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=16172937; DOI=10.1007/s11120-005-4117-0;
RA   Loll B., Kern J., Zouni A., Saenger W., Biesiadka J., Irrgang K.D.;
RT   "The antenna system of photosystem II from Thermosynechococcus elongatus at
RT   3.2 A resolution.";
RL   Photosyn. Res. 86:175-184(2005).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
RP   COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND TOPOLOGY.
RC   STRAIN=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   [9]
RP   X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 2-84 IN PHOTOSYSTEM II WITH HEME,
RP   FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   STRAIN=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   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
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   [11]
RP   X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) OF 2-84 IN PHOTOSYSTEM II WITH HEME,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=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   [12]
RP   X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=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   [13]
RP   X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 4-84 IN PHOTOSYSTEM II WITH HEME,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=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   [14]
RP   X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
RP   FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=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: This b-type cytochrome is tightly associated with the
CC       reaction center of photosystem II (PSII). PSII is a light-driven
CC       water:plastoquinone oxidoreductase that uses light energy to abstract
CC       electrons from H(2)O, generating O(2) and a proton gradient
CC       subsequently used for ATP formation. It consists of a core antenna
CC       complex that captures photons, and an electron transfer chain that
CC       converts photonic excitation into a charge separation.
CC       {ECO:0000255|HAMAP-Rule:MF_00642, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:25006873}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00642,
CC         ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16049768,
CC         ECO:0000269|PubMed:16172937, ECO:0000269|PubMed:16355230,
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, ECO:0000269|Ref.3};
CC       Note=With its partner (PsbF) binds heme. PSII binds additional
CC       chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-
CC       Rule:MF_00642, ECO:0000269|PubMed:14764885,
CC       ECO:0000269|PubMed:16049768, ECO:0000269|PubMed:16172937,
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       ECO:0000269|Ref.3};
CC   -!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit.
CC       Cyanobacterial PSII is composed of 1 copy each of membrane proteins
CC       PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM,
CC       PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins PsbO,
CC       PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
CC       {ECO:0000255|HAMAP-Rule:MF_00642, ECO:0000269|PubMed:14764885,
CC       ECO:0000269|PubMed:16049768, ECO:0000269|PubMed:16172937,
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       ECO:0000269|Ref.3}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00642, ECO:0000269|PubMed:14764885,
CC       ECO:0000269|PubMed:16049768, ECO:0000269|PubMed:16172937,
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, ECO:0000269|Ref.3}; Single-pass membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_00642, ECO:0000269|PubMed:14764885,
CC       ECO:0000269|PubMed:16049768, ECO:0000269|PubMed:16172937,
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, ECO:0000269|Ref.3}.
CC   -!- MASS SPECTROMETRY: Mass=9446; Mass_error=6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19219048};
CC   -!- MASS SPECTROMETRY: Mass=9440; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20558739};
CC   -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00642}.
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DR   EMBL; BA000039; BAC09093.1; -; Genomic_DNA.
DR   RefSeq; NP_682331.1; NC_004113.1.
DR   RefSeq; WP_011057381.1; NC_004113.1.
DR   PDB; 1S5L; X-ray; 3.50 A; E/e=1-84.
DR   PDB; 1W5C; X-ray; 3.20 A; E/K=1-84.
DR   PDB; 2AXT; X-ray; 3.00 A; E/e=1-84.
DR   PDB; 3KZI; X-ray; 3.60 A; E=2-84.
DR   PDB; 4FBY; X-ray; 6.56 A; E/R=2-84.
DR   PDB; 4IXQ; X-ray; 5.70 A; E/e=1-84.
DR   PDB; 4IXR; X-ray; 5.90 A; E/e=1-84.
DR   PDB; 4PBU; X-ray; 5.00 A; E/e=4-84.
DR   PDB; 4PJ0; X-ray; 2.44 A; E/e=1-84.
DR   PDB; 4RVY; X-ray; 5.50 A; E/e=4-84.
DR   PDB; 4TNH; X-ray; 4.90 A; E/e=1-84.
DR   PDB; 4TNI; X-ray; 4.60 A; E/e=1-84.
DR   PDB; 4TNJ; X-ray; 4.50 A; E/e=1-84.
DR   PDB; 4TNK; X-ray; 5.20 A; E/e=1-84.
DR   PDB; 4V62; X-ray; 2.90 A; AE/BE=1-84.
DR   PDB; 4V82; X-ray; 3.20 A; AE/BE=1-84.
DR   PDB; 5E79; X-ray; 3.50 A; E/e=4-84.
DR   PDB; 5E7C; X-ray; 4.50 A; E/e=4-84.
DR   PDB; 5H2F; X-ray; 2.20 A; E/e=5-84.
DR   PDB; 5KAF; X-ray; 3.00 A; E/e=1-84.
DR   PDB; 5KAI; X-ray; 2.80 A; E/e=1-84.
DR   PDB; 5MX2; X-ray; 2.20 A; E/e=1-84.
DR   PDB; 5TIS; X-ray; 2.25 A; E/e=1-84.
DR   PDB; 5ZZN; X-ray; 2.10 A; E/e=4-84.
DR   PDB; 6DHE; X-ray; 2.05 A; E/e=3-84.
DR   PDB; 6DHF; X-ray; 2.08 A; E/e=3-84.
DR   PDB; 6DHG; X-ray; 2.50 A; E/e=3-84.
DR   PDB; 6DHH; X-ray; 2.20 A; E/e=3-84.
DR   PDB; 6DHO; X-ray; 2.07 A; E/e=3-84.
DR   PDB; 6DHP; X-ray; 2.04 A; E/e=3-84.
DR   PDB; 6W1O; X-ray; 2.08 A; E/e=1-84.
DR   PDB; 6W1P; X-ray; 2.26 A; E/e=1-84.
DR   PDB; 6W1Q; X-ray; 2.27 A; E/e=1-84.
DR   PDB; 6W1R; X-ray; 2.23 A; E/e=1-84.
DR   PDB; 6W1T; X-ray; 2.01 A; E/e=1-84.
DR   PDB; 6W1U; X-ray; 2.09 A; E/e=1-84.
DR   PDB; 6W1V; X-ray; 2.09 A; E/e=1-84.
DR   PDBsum; 1S5L; -.
DR   PDBsum; 1W5C; -.
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   SMR; Q8DIP0; -.
DR   DIP; DIP-48491N; -.
DR   IntAct; Q8DIP0; 1.
DR   STRING; 197221.22295266; -.
DR   EnsemblBacteria; BAC09093; BAC09093; BAC09093.
DR   KEGG; tel:tsr1541; -.
DR   PATRIC; fig|197221.4.peg.1617; -.
DR   eggNOG; ENOG5032RR6; Bacteria.
DR   OMA; VRYWVIH; -.
DR   OrthoDB; 1863986at2; -.
DR   EvolutionaryTrace; Q8DIP0; -.
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:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009767; P:photosynthetic electron transport chain; IEA:InterPro.
DR   Gene3D; 1.20.5.860; -; 1.
DR   HAMAP; MF_00642; PSII_PsbE; 1.
DR   InterPro; IPR006217; PSII_cyt_b559_asu.
DR   InterPro; IPR037025; PSII_cyt_b559_asu_sf.
DR   InterPro; IPR006216; PSII_cyt_b559_CS.
DR   InterPro; IPR013081; PSII_cyt_b559_N.
DR   InterPro; IPR013082; PSII_cytb559_asu_lum.
DR   Pfam; PF00283; Cytochrom_B559; 1.
DR   Pfam; PF00284; Cytochrom_B559a; 1.
DR   PIRSF; PIRSF000036; PsbE; 1.
DR   TIGRFAMs; TIGR01332; cyt_b559_alpha; 1.
DR   PROSITE; PS00537; CYTOCHROME_B559; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW   Membrane; Metal-binding; Photosynthesis; Photosystem II;
KW   Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:17935689,
FT                   ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739"
FT   CHAIN           2..84
FT                   /note="Cytochrome b559 subunit alpha"
FT                   /id="PRO_0000200343"
FT   TOPO_DOM        2..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        20..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        36..84
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   METAL           23
FT                   /note="Iron (heme axial ligand); shared with beta subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00642,
FT                   ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
FT                   ECO:0000303|PubMed:14764885, ECO:0000303|PubMed:20558739,
FT                   ECO:0000303|PubMed:21367867, ECO:0000303|PubMed:22665786,
FT                   ECO:0000303|PubMed:23413188, ECO:0000303|PubMed:25006873,
FT                   ECO:0000303|PubMed:25043005, ECO:0000303|Ref.3"
FT   HELIX           10..14
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           17..39
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           42..47
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          54..56
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          69..71
FT                   /evidence="ECO:0007744|PDB:2AXT"
FT   HELIX           72..81
FT                   /evidence="ECO:0007744|PDB:5ZZN"
SQ   SEQUENCE   84 AA;  9573 MW;  19C7A074624D937F CRC64;
     MAGTTGERPF SDIITSVRYW VIHSITIPAL FIAGWLFVST GLAYDVFGTP RPDSYYAQEQ
     RSIPLVTDRF EAKQQVETFL EQLK
//
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