PSBE_THEVB
ID PSBE_THEVB Reviewed; 84 AA.
AC Q8DIP0;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 135.
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 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 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=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 [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=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 [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=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 [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=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 [12]
RP X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
RP COFACTOR, 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 [13]
RP X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 4-84 IN PHOTOSYSTEM II WITH HEME,
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 [14]
RP X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II WITH HEME,
RP FUNCTION, 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: 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 PDB; 7NHO; EM; 2.66 A; E=1-84.
DR PDB; 7NHP; EM; 2.72 A; E=1-84.
DR PDB; 7NHQ; EM; 2.68 A; E=1-84.
DR PDB; 7RF1; X-ray; 1.89 A; E/e=1-84.
DR PDB; 7RF2; X-ray; 2.08 A; E/e=1-84.
DR PDB; 7RF3; X-ray; 2.26 A; E/e=1-84.
DR PDB; 7RF4; X-ray; 2.27 A; E/e=1-84.
DR PDB; 7RF5; X-ray; 2.23 A; E/e=1-84.
DR PDB; 7RF6; X-ray; 2.01 A; E/e=1-84.
DR PDB; 7RF7; X-ray; 2.09 A; E/e=1-84.
DR PDB; 7RF8; 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 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; Q8DIP0; -.
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 BINDING 23
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_note="ligand shared with beta subunit"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
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:0007829|PDB:5ZZN"
FT HELIX 17..39
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:7NHO"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:5ZZN"
SQ SEQUENCE 84 AA; 9573 MW; 19C7A074624D937F CRC64;
MAGTTGERPF SDIITSVRYW VIHSITIPAL FIAGWLFVST GLAYDVFGTP RPDSYYAQEQ
RSIPLVTDRF EAKQQVETFL EQLK
