PSBA1_THEVB
ID PSBA1_THEVB Reviewed; 360 AA.
AC P0A444; P35876;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
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 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 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=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 1-344 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 1-344 IN PHOTOSYSTEM II,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
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 1-344 IN PHOTOSYSTEM II IN
RP COMPLEX WITH HERBICIDE, FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / 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=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 11-344 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) OF 1-344 IN PHOTOSYSTEM II,
RP FUNCTION, CATALYTIC ACTIVITY, 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).
RN [13] {ECO:0007744|PDB:5OJ5, ECO:0007744|PDB:5OJR}
RP X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) OF 335-344 IN COMPLEX WITH YCF48,
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 335-352 IN COMPLEX WITH YCF48,
RP AND INTERACTION WITH YCF48.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=30061392; DOI=10.1073/pnas.1800609115;
RA Yu J., Knoppova J., Michoux F., Bialek W., Cota E., Shukla M.K.,
RA Straskova A., Pascual Aznar G., Sobotka R., Komenda J., Murray J.W.,
RA Nixon P.J.;
RT "Ycf48 involved in the biogenesis of the oxygen-evolving photosystem II
RT complex is a seven-bladed beta-propeller protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E7824-E7833(2018).
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 (By similarity) (PubMed:14764885, PubMed:16355230,
CC PubMed:19219048, PubMed:20558739, PubMed:21367867, PubMed:22665786,
CC PubMed:23413188, PubMed:25006873, PubMed:25043005, Ref.3). Precursor
CC protein interacts with Ycf48 (PubMed:30061392). {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|PubMed:30061392, 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; 5OJR; X-ray; 1.96 A; E/F=335-352.
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 PDB; 7NHO; EM; 2.66 A; A=1-360.
DR PDB; 7NHP; EM; 2.72 A; A=1-360.
DR PDB; 7NHQ; EM; 2.68 A; A=1-360.
DR PDB; 7RF1; X-ray; 1.89 A; A/a=1-344.
DR PDB; 7RF2; X-ray; 2.08 A; A/a=1-344.
DR PDB; 7RF3; X-ray; 2.26 A; A/a=1-344.
DR PDB; 7RF4; X-ray; 2.27 A; A/a=1-344.
DR PDB; 7RF5; X-ray; 2.23 A; A/a=1-344.
DR PDB; 7RF6; X-ray; 2.01 A; A/a=1-344.
DR PDB; 7RF7; X-ray; 2.09 A; A/a=1-344.
DR PDB; 7RF8; 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; 5OJR; -.
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; P0A444; -.
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; ASCYMGR; -.
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:UniProtKB-EC.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
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 BINDING 118
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="ChlzD1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
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 BINDING 126
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="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 /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="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 /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="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 170
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
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 BINDING 189
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
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 BINDING 198
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="PD1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
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 BINDING 215
FT /ligand="a quinone"
FT /ligand_id="ChEBI:CHEBI:132124"
FT /ligand_label="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 BINDING 215
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared with heterodimeric partner"
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 264..265
FT /ligand="a quinone"
FT /ligand_id="ChEBI:CHEBI:132124"
FT /ligand_label="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 BINDING 272
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared with heterodimeric partner"
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 332
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
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 BINDING 333
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
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 BINDING 342
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
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 BINDING 344
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
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 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:0007829|PDB:5ZZN"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 31..54
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 87..91
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 110..137
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 143..158
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 176..190
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 196..221
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:7NHO"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:5MX2"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:7NHQ"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 268..293
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:7NHO"
FT HELIX 317..331
FT /evidence="ECO:0007829|PDB:5ZZN"
FT TURN 332..336
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 339..341
FT /evidence="ECO:0007829|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
