ID   PSBA_ANTSP              Reviewed;         360 AA.
AC   P24625;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   16-OCT-2013, entry version 83.
DE   RecName: Full=Photosystem Q(B) protein;
DE            EC=1.10.3.9;
DE   AltName: Full=32 kDa thylakoid membrane protein;
DE   AltName: Full=Photosystem II protein D1;
DE   Flags: Precursor;
GN   Name=psbA;
OS   Antithamnion sp.
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Florideophyceae; Ceramiales; Ceramiaceae;
OC   Antithamnion.
OX   NCBI_TaxID=2767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LB 95.79;
RX   PubMed=1934114; DOI=10.1007/BF00312783;
RA   Winhauer T., Jaeger S., Valentin K.-U., Zetsche K.;
RT   "Structural similarities between psbA genes from red and brown
RT   algae.";
RL   Curr. Genet. 20:177-180(1991).
CC   -!- FUNCTION: This is one of the two reaction center proteins of
CC       photosystem II (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O + 2 plastoquinone + 4 light = O(2) + 2
CC       plastoquinol.
CC   -!- COFACTOR: The psbA/B heterodimer binds P680, the primary electron
CC       donor of PSII. It shares a non-heme iron and each subunit binds
CC       additional chlorophylls and pheophytin. PsbA provides most of the
CC       ligands for the Mn-cluster of the oxygen-evolving complex (By
CC       similarity).
CC   -!- SUBUNIT: The psbA/B heterodimer binds the P680 chlorophylls and
CC       subsequent electron acceptors. PSII consists of a core antenna
CC       complex that captures photons, and an electron transfer chain that
CC       converts photonic excitation into a charge separation. PSII forms
CC       dimeric complexes (By similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC       Multi-pass membrane protein (By similarity).
CC   -!- MISCELLANEOUS: Herbicides such as atrazine, BNT, diuron or ioxynil
CC       bind to Q(B) and block electron transport (By similarity).
CC   -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
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DR   EMBL; X55364; CAA39049.1; -; Genomic_DNA.
DR   PIR; S32577; S32577.
DR   ProteinModelPortal; P24625; -.
DR   SMR; P24625; 10-344.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
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-HAMAP.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; -; 1.
DR   HAMAP; MF_01379; PSII_PsbA_D1; 1; -.
DR   InterPro; IPR000484; Photo_RC_L/M.
DR   InterPro; IPR005867; PSII_D1.
DR   Pfam; PF00124; Photo_RC; 1.
DR   PRINTS; PR00256; REACTNCENTRE.
DR   SUPFAM; SSF81483; SSF81483; 1.
DR   TIGRFAMs; TIGR01151; psbA; 1.
DR   PROSITE; PS00244; REACTION_CENTER; 1.
PE   3: Inferred from homology;
KW   Calcium; Chloroplast; Electron transport; Herbicide resistance; Iron;
KW   Manganese; Membrane; Metal-binding; Oxidoreductase; Photosynthesis;
KW   Photosystem II; Plastid; Thylakoid; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    344       Photosystem Q(B) protein.
FT                                /FTId=PRO_0000090424.
FT   PROPEP      345    360       Potential.
FT                                /FTId=PRO_0000316505.
FT   TRANSMEM     36     56       Helical; (Potential).
FT   TRANSMEM    109    129       Helical; (Potential).
FT   TRANSMEM    141    164       Helical; (Potential).
FT   TRANSMEM    192    218       Helical; (Potential).
FT   TRANSMEM    269    289       Helical; (Potential).
FT   METAL       170    170       Calcium-manganese-oxide cluster [Ca-4Mn-
FT                                5O]; calcium (By similarity).
FT   METAL       170    170       Calcium-manganese-oxide cluster [Ca-4Mn-
FT                                5O]; manganese 1 (By similarity).
FT   METAL       189    189       Calcium-manganese-oxide cluster [Ca-4Mn-
FT                                5O]; manganese 2 (By similarity).
FT   METAL       215    215       Iron; shared with heterodimeric partner
FT                                (By similarity).
FT   METAL       272    272       Iron; shared with heterodimeric partner
FT                                (By similarity).
FT   METAL       332    332       Calcium-manganese-oxide cluster [Ca-4Mn-
FT                                5O]; manganese 2; via tele nitrogen (By
FT                                similarity).
FT   METAL       333    333       Calcium-manganese-oxide cluster [Ca-4Mn-
FT                                5O]; manganese 1 (By similarity).
FT   METAL       333    333       Calcium-manganese-oxide cluster [Ca-4Mn-
FT                                5O]; manganese 3 (By similarity).
FT   METAL       342    342       Calcium-manganese-oxide cluster [Ca-4Mn-
FT                                5O]; manganese 2 (By similarity).
FT   METAL       342    342       Calcium-manganese-oxide cluster [Ca-4Mn-
FT                                5O]; manganese 4 (By similarity).
FT   METAL       344    344       Calcium-manganese-oxide cluster [Ca-4Mn-
FT                                5O]; calcium; via carboxylate (By
FT                                similarity).
FT   METAL       344    344       Calcium-manganese-oxide cluster [Ca-4Mn-
FT                                5O]; manganese 4; via carboxylate (By
FT                                similarity).
FT   SITE        344    345       Cleavage; by ctpA (By similarity).
SQ   SEQUENCE   360 AA;  39681 MW;  288EDE4685061F5F CRC64;
     MTATLERRES ASLWARFCTW ITMNENRLYI GWFGVVMIPT LLTATSVFII ACFAAPPVDI
     DGIREPVAGS LLYGNNIISG AIIPSSAAIG IHFYPIWEAA SLDEWLYNGG PYQLIVLHFL
     LGVCCYIGRE WEFSYRLGMR PWISVAFTAP VVAASAVFLV YPIGQGSFSD GMPLGISGTF
     NFMLVFQAEH NILMHPLHQL GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESANNGYKFG
     QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLGLWPV VGIWFTSMSV STMAFNLNGF
     NFNQSVVDSQ GRVINTWADI LNRANLGMEV MHERNAHNFP LDLASNESLP LALVAPAING
//