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 29-OCT-2014, entry version 86. DE RecName: Full=Photosystem Q(B) protein {ECO:0000255|HAMAP-Rule:MF_01379}; DE EC=1.10.3.9 {ECO:0000255|HAMAP-Rule:MF_01379}; DE AltName: Full=32 kDa thylakoid membrane protein {ECO:0000255|HAMAP-Rule:MF_01379}; DE AltName: Full=Photosystem II protein D1 {ECO:0000255|HAMAP-Rule:MF_01379}; DE Flags: Precursor; GN Name=psbA {ECO:0000255|HAMAP-Rule:MF_01379}; 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. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2 H(2)O + 2 plastoquinone + 4 light = O(2) + 2 CC plastoquinol. {ECO:0000255|HAMAP-Rule:MF_01379}. 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). {ECO:0000250}. 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). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000255|HAMAP-Rule:MF_01379}; Multi-pass membrane protein CC {ECO:0000255|HAMAP-Rule:MF_01379}. CC -!- MISCELLANEOUS: Herbicides such as atrazine, BNT, diuron or ioxynil CC bind to Q(B) and block electron transport. {ECO:0000255|HAMAP- CC Rule:MF_01379}. CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family. CC {ECO:0000255|HAMAP-Rule:MF_01379}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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-HAMAP. 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: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 {ECO:0000255|HAMAP-Rule:MF_01379}. FT /FTId=PRO_0000316505. FT TRANSMEM 36 56 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT TRANSMEM 109 129 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT TRANSMEM 141 164 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT TRANSMEM 192 218 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT TRANSMEM 269 289 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 170 170 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; calcium. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 170 170 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 1. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 189 189 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 2. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 215 215 Iron; shared with heterodimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_01379}. FT METAL 272 272 Iron; shared with heterodimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_01379}. FT METAL 332 332 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 2; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01379}. FT METAL 333 333 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 1. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 333 333 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 3. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 342 342 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 2. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 342 342 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 4. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 344 344 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; calcium; via carboxylate. FT {ECO:0000255|HAMAP-Rule:MF_01379}. FT METAL 344 344 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 4; via carboxylate. FT {ECO:0000255|HAMAP-Rule:MF_01379}. FT SITE 344 345 Cleavage; by ctpA. {ECO:0000250}. 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 //