ID   PSBA_PROM0              Reviewed;         360 AA.
AC   A3PAU3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Photosystem II protein D1 {ECO:0000255|HAMAP-Rule:MF_01379};
DE            Short=PSII D1 protein {ECO:0000255|HAMAP-Rule:MF_01379};
DE            EC=1.10.3.9 {ECO:0000255|HAMAP-Rule:MF_01379};
DE   AltName: Full=Photosystem II Q(B) protein {ECO:0000255|HAMAP-Rule:MF_01379};
DE   Flags: Precursor;
GN   Name=psbA {ECO:0000255|HAMAP-Rule:MF_01379};
GN   OrderedLocusNames=P9301_02451;
OS   Prochlorococcus marinus (strain MIT 9301).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=167546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9301;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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/PsbD) 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   -!- 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   -!- 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. The PSII complex binds additional
CC       chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-
CC       Rule:MF_01379};
CC   -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC       PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT,
CC       PsbX, PsbY, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ), PsbU,
CC       PsbV and a large number of cofactors. It forms dimeric complexes.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01379}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01379}.
CC   -!- PTM: Tyr-162 forms a radical intermediate that is referred to as redox-
CC       active TyrZ, YZ or Y-Z. {ECO:0000255|HAMAP-Rule:MF_01379}.
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   -!- MISCELLANEOUS: Cyanobacteria usually contain more than 2 copies of the
CC       psbA gene. {ECO:0000255|HAMAP-Rule:MF_01379}.
CC   -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2)
CC       are entirely coordinated by water. {ECO:0000255|HAMAP-Rule:MF_01379}.
CC   -!- MISCELLANEOUS: Herbicides such as atrazine, BNT, diuron or ioxynil bind
CC       in the Q(B) binding site and block subsequent electron transfer.
CC       {ECO:0000255|HAMAP-Rule:MF_01379}.
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; CP000576; ABO16868.1; -; Genomic_DNA.
DR   RefSeq; WP_002805533.1; NC_009091.1.
DR   AlphaFoldDB; A3PAU3; -.
DR   SMR; A3PAU3; -.
DR   STRING; 167546.P9301_02451; -.
DR   KEGG; pmg:P9301_02451; -.
DR   eggNOG; ENOG502Z87P; Bacteria.
DR   HOGENOM; CLU_054206_1_0_3; -.
DR   OrthoDB; 505356at2; -.
DR   Proteomes; UP000001430; Chromosome.
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   Gene3D; 1.20.85.10; Photosystem II protein D1-like; 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   NCBIfam; TIGR01151; psbA; 1.
DR   PANTHER; PTHR33149; PHOTOSYSTEM II PROTEIN D1; 1.
DR   PANTHER; PTHR33149:SF12; PHOTOSYSTEM II PROTEIN D1; 1.
DR   Pfam; PF00124; Photo_RC; 1.
DR   PRINTS; PR00256; REACTNCENTRE.
DR   SUPFAM; SSF81483; Bacterial photosystem II reaction centre, L and M subunits; 1.
DR   PROSITE; PS00244; REACTION_CENTER; 1.
PE   3: Inferred from homology;
KW   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   CHAIN           1..345
FT                   /note="Photosystem II protein D1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT                   /id="PRO_0000316357"
FT   PROPEP          346..360
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT                   /id="PRO_0000316358"
FT   TRANSMEM        30..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   TRANSMEM        119..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   TRANSMEM        143..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   TRANSMEM        198..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   TRANSMEM        275..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         119
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   BINDING         127
FT                   /ligand="pheophytin a"
FT                   /ligand_id="ChEBI:CHEBI:136840"
FT                   /ligand_label="D1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         171
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         190
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         199
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   BINDING         216
FT                   /ligand="a quinone"
FT                   /ligand_id="ChEBI:CHEBI:132124"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         216
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   BINDING         265..266
FT                   /ligand="a quinone"
FT                   /ligand_id="ChEBI:CHEBI:132124"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         273
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   BINDING         333
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         334
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         343
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         345
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   SITE            162
FT                   /note="Tyrosine radical intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   SITE            191
FT                   /note="Stabilizes free radical intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   SITE            345..346
FT                   /note="Cleavage; by CtpA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
SQ   SEQUENCE   360 AA;  39638 MW;  E8389C98C87541E0 CRC64;
     MTTIQQQRSS LLKGWPQFCE WVTSTNNRIY VGWFGVLMIP CLLTAAACFI VAFIAAPPVD
     IDGIREPVAG SFLYGNNIIS GAVVPSSNAI GLHFYPIWEA ATVDEWLYNG GPYQLVIFHF
     LIGISAYMGR QWELSYRLGM RPWICVAYSA PVSAAFAVFL VYPFGQGSFS DGMPLGISGT
     FNFMFVFQAE HNILMHPFHM AGVAGMFGGS LFSAMHGSLV TSSLIRETTE TESQNYGYKF
     GQEEETYNIV AAHGYFGRLI FQYASFNNSR SLHFFLAVFP VVCVWLTSMG ICTMAFNLNG
     FNFNQSVVDA NGKIVPTWGD VLNRANLGME VMHERNAHNF PLDLAAAEST TVALSAPAIG
//