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Entry: P0A444
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ID   PSBA1_THEEB             Reviewed;         360 AA.
AC   P0A444; P35876;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   07-APR-2021, entry version 122.
DE   RecName: Full=Photosystem II protein D1 1 {ECO:0000255|HAMAP-Rule:MF_01379};
DE            Short=PSII D1 protein 1 {ECO:0000255|HAMAP-Rule:MF_01379};
DE            EC=1.10.3.9 {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:25006873};
DE   AltName: Full=Photosystem II Q(B) protein 1 {ECO:0000255|HAMAP-Rule:MF_01379};
DE   Flags: Precursor;
GN   Name=psbA1 {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305}; Synonyms=psbA-1;
GN   OrderedLocusNames=tlr1843;
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   X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 1-360.
RX   PubMed=11217865; DOI=10.1038/35055589;
RA   Zouni A., Witt H.T., Kern J., Fromme P., Krauss N., Saenger W., Orth P.;
RT   "Crystal structure of photosystem II from Synechococcus elongatus at 3.8 A
RT   resolution.";
RL   Nature 409:739-743(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   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) OF 1-344 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 (3.0 ANGSTROMS) OF 1-344 IN PHOTOSYSTEM II, COFACTOR,
RP   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   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-344 IN PHOTOSYSTEM II,
RP   COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
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   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 1-344 IN PHOTOSYSTEM II,
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
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   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1-344 IN PHOTOSYSTEM II IN
RP   COMPLEX WITH HERBICIDE, FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=BP-1;
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 1-344 IN PHOTOSYSTEM II,
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   [10]
RP   X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   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   [11]
RP   X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 11-344 IN PHOTOSYSTEM II,
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   [12]
RP   X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) OF 1-344 IN PHOTOSYSTEM II,
RP   FUNCTION, CATALYTIC ACTIVITY, 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: Photosystem II (PSII) is a light-driven water:plastoquinone
CC       oxidoreductase that uses light energy to abstract electrons from H(2)O,
CC       generating O(2) and a proton gradient subsequently used for ATP
CC       formation. It consists of a core antenna complex that captures photons,
CC       and an electron transfer chain that converts photonic excitation into a
CC       charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer
CC       binds P680, the primary electron donor of PSII as well as several
CC       subsequent electron acceptors. {ECO:0000255|HAMAP-Rule:MF_01379,
CC       ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC       ECO:0000269|PubMed:25006873}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2;
CC         Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757,
CC         ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01379,
CC         ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:25006873};
CC   -!- COFACTOR:
CC       Note=The D1/D2 heterodimer binds P680, chlorophylls that are the
CC       primary electron donor of PSII, and subsequent electron acceptors. It
CC       shares a non-heme iron and each subunit binds pheophytin, quinone,
CC       additional chlorophylls, carotenoids and lipids. D1 provides most of
CC       the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex
CC       (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is
CC       required for oxygen evolution (PubMed:19219048, PubMed:21367867). PSII
CC       binds additional chlorophylls, carotenoids and specific lipids.
CC       {ECO:0000255|HAMAP-Rule:MF_01379, 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       ECO:0000269|Ref.3};
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, at least 3 peripheral
CC       proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms
CC       dimeric complexes. {ECO:0000255|HAMAP-Rule:MF_01379,
CC       ECO:0000269|PubMed:14764885, 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   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01379, 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       ECO:0000269|Ref.3}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01379, 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       ECO:0000269|Ref.3}.
CC   -!- PTM: C-terminally processed by CtpA; processing is essential to allow
CC       assembly of the oxygen-evolving complex and thus photosynthetic growth.
CC       {ECO:0000255|HAMAP-Rule:MF_01379}.
CC   -!- PTM: Tyr-161 forms a radical intermediate that is referred to as redox-
CC       active TyrZ, YZ or Y-Z. {ECO:0000255|HAMAP-Rule:MF_01379,
CC       ECO:0000303|PubMed:11217865, ECO:0000303|PubMed:14764885,
CC       ECO:0000303|PubMed:19219048, ECO:0000303|PubMed:21367867,
CC       ECO:0000303|Ref.3}.
CC   -!- MASS SPECTROMETRY: Mass=38144; Mass_error=224; Method=MALDI; Note=Mass
CC       for C-terminally truncated D1. The measured protein is probably a
CC       mixture of the products of the 3 psbA genes.;
CC       Evidence={ECO:0000269|PubMed:19219048};
CC   -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2)
CC       are entirely coordinated by water. {ECO:0000255|HAMAP-Rule:MF_01379,
CC       ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048}.
CC   -!- MISCELLANEOUS: Herbicides such as terbutryn, atrazine, BNT, diuron or
CC       ioxynil bind in the Q(B) binding site and block subsequent electron
CC       transfer. {ECO:0000255|HAMAP-Rule:MF_01379,
CC       ECO:0000269|PubMed:21367867}.
CC   -!- MISCELLANEOUS: Cyanobacteria usually contain more than 2 copies of the
CC       psbA gene; this strain encodes 3. {ECO:0000255|HAMAP-Rule:MF_01379,
CC       ECO:0000269|PubMed:12240834}.
CC   -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC       {ECO:0000255|HAMAP-Rule:MF_01379}.
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DR   EMBL; BA000039; BAC09395.1; -; Genomic_DNA.
DR   RefSeq; NP_682633.1; NC_004113.1.
DR   RefSeq; WP_011057680.1; NC_004113.1.
DR   PDB; 1S5L; X-ray; 3.50 A; A/a=1-344.
DR   PDB; 1W5C; X-ray; 3.20 A; A/G=1-360.
DR   PDB; 2AXT; X-ray; 3.00 A; A/a=1-344.
DR   PDB; 3KZI; X-ray; 3.60 A; A=1-344.
DR   PDB; 4FBY; X-ray; 6.56 A; A/G=1-344.
DR   PDB; 4IXQ; X-ray; 5.70 A; A/a=1-360.
DR   PDB; 4IXR; X-ray; 5.90 A; A/a=1-360.
DR   PDB; 4PBU; X-ray; 5.00 A; A/a=11-344.
DR   PDB; 4PJ0; X-ray; 2.44 A; A/a=1-344.
DR   PDB; 4RVY; X-ray; 5.50 A; A/a=11-344.
DR   PDB; 4TNH; X-ray; 4.90 A; A/a=1-344.
DR   PDB; 4TNI; X-ray; 4.60 A; A/a=1-344.
DR   PDB; 4TNJ; X-ray; 4.50 A; A/a=1-344.
DR   PDB; 4TNK; X-ray; 5.20 A; A/a=1-344.
DR   PDB; 4V62; X-ray; 2.90 A; AA/BA=1-344.
DR   PDB; 4V82; X-ray; 3.20 A; AA/BA=1-344.
DR   PDB; 5E79; X-ray; 3.50 A; A/a=11-344.
DR   PDB; 5E7C; X-ray; 4.50 A; A/a=11-344.
DR   PDB; 5H2F; X-ray; 2.20 A; A/a=11-344.
DR   PDB; 5KAF; X-ray; 3.00 A; A/a=1-344.
DR   PDB; 5KAI; X-ray; 2.80 A; A/a=1-344.
DR   PDB; 5MX2; X-ray; 2.20 A; A/a=1-344.
DR   PDB; 5OJ5; X-ray; 1.08 A; B=335-344.
DR   PDB; 5TIS; X-ray; 2.25 A; A/a=1-344.
DR   PDB; 5ZZN; X-ray; 2.10 A; A/a=11-344.
DR   PDB; 6DHE; X-ray; 2.05 A; A/a=11-344.
DR   PDB; 6DHF; X-ray; 2.08 A; A/a=11-344.
DR   PDB; 6DHG; X-ray; 2.50 A; A/a=11-344.
DR   PDB; 6DHH; X-ray; 2.20 A; A/a=11-344.
DR   PDB; 6DHO; X-ray; 2.07 A; A/a=11-344.
DR   PDB; 6DHP; X-ray; 2.04 A; A/a=11-344.
DR   PDB; 6W1O; X-ray; 2.08 A; A/a=11-344.
DR   PDB; 6W1P; X-ray; 2.26 A; A/a=11-344.
DR   PDB; 6W1Q; X-ray; 2.27 A; A/a=1-344.
DR   PDB; 6W1R; X-ray; 2.23 A; A/a=1-344.
DR   PDB; 6W1T; X-ray; 2.01 A; A/a=1-344.
DR   PDB; 6W1U; X-ray; 2.09 A; A/a=1-344.
DR   PDB; 6W1V; X-ray; 2.09 A; A/a=1-344.
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; 5OJ5; -.
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; P0A444; -.
DR   DIP; DIP-48487N; -.
DR   IntAct; P0A444; 1.
DR   STRING; 197221.22295569; -.
DR   DrugBank; DB04735; MONOGALACTOSYL-DIACYLGLYCEROL.
DR   EnsemblBacteria; BAC09395; BAC09395; BAC09395.
DR   KEGG; tel:tlr1843; -.
DR   PATRIC; fig|197221.4.peg.1926; -.
DR   eggNOG; ENOG502Z87P; Bacteria.
DR   OMA; FLIGCAC; -.
DR   OrthoDB; 382342at2; -.
DR   BRENDA; 1.10.3.9; 7763.
DR   EvolutionaryTrace; P0A444; -.
DR   Proteomes; UP000000440; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0010242; F:oxygen evolving activity; IEA:RHEA.
DR   GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR   CDD; cd09289; Photosystem-II_D1; 1.
DR   Gene3D; 1.20.85.10; -; 1.
DR   HAMAP; MF_01379; PSII_PsbA_D1; 1.
DR   InterPro; IPR036854; Photo_II_D1/D2_sf.
DR   InterPro; IPR000484; Photo_RC_L/M.
DR   InterPro; IPR005867; PSII_D1.
DR   PANTHER; PTHR33149; PTHR33149; 1.
DR   Pfam; PF00124; Photo_RC; 1.
DR   SUPFAM; SSF81483; SSF81483; 1.
DR   TIGRFAMs; TIGR01151; psbA; 1.
DR   PROSITE; PS00244; REACTION_CENTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Chlorophyll; Chromophore; Electron transport;
KW   Herbicide resistance; Iron; Magnesium; Manganese; Membrane; Metal-binding;
KW   Oxidoreductase; Photosynthesis; Photosystem II; Reference proteome;
KW   Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   CHAIN           2..344
FT                   /note="Photosystem II protein D1 1"
FT                   /id="PRO_0000090485"
FT   PROPEP          345..360
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT                   /id="PRO_0000316376"
FT   TOPO_DOM        2..31
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        32..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        50..114
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        115..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        131..143
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        144..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        157..196
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        197..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        215..273
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        274..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        289..344
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   REGION          264..265
FT                   /note="Quinone (B)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
FT                   ECO:0000303|PubMed:14764885, ECO:0000303|PubMed:22665786,
FT                   ECO:0000303|PubMed:23413188, ECO:0000303|PubMed:25006873,
FT                   ECO:0000303|PubMed:25043005"
FT   METAL           118
FT                   /note="Magnesium (chlorophyll-a ChlzD1 axial ligand); via
FT                   tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
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:25043005,
FT                   ECO:0000303|Ref.3"
FT   METAL           170
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; calcium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:19219048, 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"
FT   METAL           170
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:19219048, ECO:0000303|PubMed:14764885,
FT                   ECO:0000303|PubMed:16355230, 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"
FT   METAL           189
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; calcium"
FT                   /evidence="ECO:0000269|PubMed:19219048,
FT                   ECO:0000303|PubMed:20558739, ECO:0000303|PubMed:21367867,
FT                   ECO:0000303|PubMed:22665786, ECO:0000303|PubMed:23413188,
FT                   ECO:0000303|PubMed:25006873"
FT   METAL           189
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:19219048, ECO:0000303|PubMed:14764885,
FT                   ECO:0000303|PubMed:16355230, 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"
FT   METAL           198
FT                   /note="Magnesium (chlorophyll-a PD1 axial ligand); via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
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:25043005,
FT                   ECO:0000303|Ref.3"
FT   METAL           215
FT                   /note="Iron; shared with heterodimeric partner; via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
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   METAL           272
FT                   /note="Iron; shared with heterodimeric partner; via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
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   METAL           332
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2;
FT                   via tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:19219048, ECO:0000303|PubMed:14764885,
FT                   ECO:0000303|PubMed:16355230, 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"
FT   METAL           333
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:19219048, ECO:0000303|PubMed:14764885,
FT                   ECO:0000303|PubMed:16355230, 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"
FT   METAL           333
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000303|PubMed:14764885, ECO:0000303|PubMed:16355230,
FT                   ECO:0000303|PubMed:19219048, 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"
FT   METAL           342
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:19219048, ECO:0000303|PubMed:14764885,
FT                   ECO:0000303|PubMed:16355230, ECO:0000303|PubMed:20558739,
FT                   ECO:0000303|PubMed:21367867, ECO:0000303|PubMed:23413188,
FT                   ECO:0000303|PubMed:25006873, ECO:0000303|PubMed:25043005"
FT   METAL           342
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:19219048, ECO:0000303|PubMed:16355230,
FT                   ECO:0000303|PubMed:20558739, ECO:0000303|PubMed:21367867,
FT                   ECO:0000303|PubMed:22665786, ECO:0000303|PubMed:23413188,
FT                   ECO:0000303|PubMed:25006873, ECO:0000303|PubMed:25043005"
FT   METAL           344
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; calcium; via
FT                   carboxylate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:19219048, ECO:0000303|PubMed:14764885,
FT                   ECO:0000303|PubMed:16355230, ECO:0000303|PubMed:20558739,
FT                   ECO:0000303|PubMed:21367867, ECO:0000303|PubMed:23413188,
FT                   ECO:0000303|PubMed:25043005"
FT   METAL           344
FT                   /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4;
FT                   via carboxylate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:19219048, ECO:0000303|PubMed:16355230,
FT                   ECO:0000303|PubMed:20558739, ECO:0000303|PubMed:21367867,
FT                   ECO:0000303|PubMed:22665786, ECO:0000303|PubMed:23413188,
FT                   ECO:0000303|PubMed:25006873, ECO:0000303|PubMed:25043005"
FT   BINDING         126
FT                   /note="Pheophytin D1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
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   BINDING         130
FT                   /note="Pheophytin D1"
FT                   /evidence="ECO:0000269|PubMed:16355230,
FT                   ECO:0000269|PubMed:19219048, ECO:0000303|PubMed:14764885,
FT                   ECO:0000303|PubMed:20558739, ECO:0000303|PubMed:21367867,
FT                   ECO:0000303|PubMed:22665786, ECO:0000303|PubMed:23413188,
FT                   ECO:0000303|PubMed:25006873, ECO:0000303|PubMed:25043005,
FT                   ECO:0000303|Ref.3"
FT   BINDING         147
FT                   /note="Pheophytin D1"
FT                   /evidence="ECO:0000269|PubMed:16355230,
FT                   ECO:0000269|PubMed:19219048, ECO:0000303|PubMed:14764885,
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   BINDING         215
FT                   /note="Quinone (B)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
FT                   ECO:0000303|PubMed:14764885, ECO:0000303|PubMed:22665786,
FT                   ECO:0000303|PubMed:23413188, ECO:0000303|PubMed:25006873,
FT                   ECO:0000303|PubMed:25043005"
FT   SITE            161
FT                   /note="Tyrosine radical intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000303|PubMed:11217865, ECO:0000303|PubMed:14764885,
FT                   ECO:0000303|PubMed:19219048, ECO:0000303|PubMed:21367867,
FT                   ECO:0000303|Ref.3"
FT   SITE            190
FT                   /note="Stabilizes free radical intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   SITE            344..345
FT                   /note="Cleavage; by CtpA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   HELIX           13..21
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          26..28
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           31..54
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          62..64
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           71..73
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   TURN            77..79
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   TURN            87..91
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           96..98
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          99..101
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           102..107
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           110..137
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           143..158
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           160..165
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           168..170
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           176..190
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           192..194
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           196..221
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          229..231
FT                   /evidence="ECO:0007744|PDB:5MX2"
FT   HELIX           233..236
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           248..258
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           261..263
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           268..293
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   TURN            294..296
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          297..299
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          309..311
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   HELIX           317..331
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   TURN            332..336
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          339..341
FT                   /evidence="ECO:0007744|PDB:5MX2"
SQ   SEQUENCE   360 AA;  39737 MW;  D4B45833FA46A4D4 CRC64;
     MTTTLQRRES ANLWERFCNW VTSTDNRLYV GWFGVIMIPT LLAATICFVI AFIAAPPVDI
     DGIREPVSGS LLYGNNIITG AVVPSSNAIG LHFYPIWEAA SLDEWLYNGG PYQLIIFHFL
     LGASCYMGRQ WELSYRLGMR PWICVAYSAP LASAFAVFLI YPIGQGSFSD GMPLGISGTF
     NFMIVFQAEH NILMHPFHQL GVAGVFGGAL FCAMHGSLVT SSLIRETTET ESANYGYKFG
     QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV VGVWFTALGI STMAFNLNGF
     NFNHSVIDAK GNVINTWADI INRANLGMEV MHERNAHNFP LDLASAESAP VAMIAPSING
//
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