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 20-MAY-2008, entry version 57. DE Photosystem Q(B) protein precursor (32 kDa thylakoid membrane protein) DE (Photosystem II protein D1). 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 MEDLINE=92035067; 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 -!- COFACTOR: The psbA/B heterodimer shares a non-heme iron and each CC subunit also binds two chlorophylls, a pheophytin and a CC phylloquinone (By 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. 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 HSSP; P02955; 1DOP. DR SMR; P24625; 10-344. DR GO; GO:0005506; F:iron ion binding; IEA:HAMAP. DR HAMAP; MF_01379; -; 1. DR InterPro; IPR000484; Photo_RC_L/M. DR InterPro; IPR005867; PSII_PsbA/D1. DR Gene3D; G3DSA:1.20.85.10; Photo_RC_L/M; 1. DR Pfam; PF00124; Photo_RC; 1. DR PRINTS; PR00256; REACTNCENTRE. DR ProDom; PD000551; Photo_RC; 1. DR TIGRFAMs; TIGR01151; psbA; 1. DR PROSITE; PS00244; REACTION_CENTER; 1. PE 3: Inferred from homology; KW Chloroplast; Electron transport; Herbicide resistance; Iron; Membrane; KW Metal-binding; Photosynthesis; Photosystem II; Plastid; Thylakoid; KW Transmembrane; 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 Potential. FT TRANSMEM 109 129 Potential. FT TRANSMEM 141 164 Potential. FT TRANSMEM 192 218 Potential. FT TRANSMEM 269 289 Potential. FT METAL 215 215 Iron (non heme) (shared with dimeric FT partner) (By similarity). FT METAL 272 272 Iron (non heme) (shared with dimeric FT partner) (By 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 //