AC MF_01378; DC Protein; auto TR HAMAP; MF_01378; -; 1; level=0 XX Names: PSII_Cyt550 XX ID CY550 case DE RecName: Full=Photosystem II extrinsic protein V; DE Short=PsbV; DE AltName: Full=Cytochrome c-550; DE AltName: Full=Cytochrome c550; DE AltName: Full=Low-potential cytochrome c; DE Flags: Precursor; else case DE RecName: Full=Photosystem II extrinsic protein V; DE Short=PsbV; DE AltName: Full=Cytochrome c-550; DE AltName: Full=Cytochrome c550; DE Flags: Precursor; end case GN Name=psbV; XX CC -!- FUNCTION: One of the extrinsic, lumenal subunits of photosystem II CC (PSII). PSII is a light-driven water plastoquinone oxidoreductase, CC using light energy to abstract electrons from H(2)O, generating a CC proton gradient subsequently used for ATP formation. The extrinsic CC proteins stabilize the structure of photosystem II oxygen-evolving CC complex (OEC), the ion environment of oxygen evolution and protect the CC OEC against heat-induced inactivation. Low-potential cytochrome c that CC plays a role in the OEC of PSII. CC -!- COFACTOR: CC Name=heme c; Xref=ChEBI:CHEBI:61717; CC Note=Binds 1 heme c group covalently per subunit.; case 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 PsbY, PsbZ, Psb30/Ycf12, at least 3 peripheral proteins of the oxygen- CC evolving complex and a large number of cofactors. It forms dimeric CC complexes. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; CC Peripheral membrane protein; Lumenal side. Note=Associated with CC photosystem II at the lumenal side of the thylakoid membrane. else case 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, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ), PsbU, PsbV CC and a large number of cofactors. It forms dimeric complexes. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; CC Periplasmic side. Note=Associated with photosystem II at the CC periplasmic side side of the thylakoid membrane. else 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, PsbZ, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ), CC PsbU, PsbV and a large number of cofactors. It forms dimeric complexes. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane CC protein; Lumenal side. Note=Associated with photosystem II at the CC lumenal side of the thylakoid membrane. end case CC -!- SIMILARITY: Belongs to the cytochrome c family. PsbV subfamily. XX DR PROSITE; PS51007; CYTC; 1; trigger=no DR Pfam; PF00034; Cytochrom_C; 1; trigger=no DR NCBIfam; TIGR03045; PS_II_C550; 1; trigger=no DR General; Signal; -; 1; trigger=yes XX KW Electron transport KW Heme KW Iron KW Metal-binding KW Photosynthesis KW Photosystem II case KW Cell membrane KW Cell inner membrane else KW Thylakoid end case KW Membrane KW Transport XX GO GO:0019684; P:photosynthesis, light reaction GO GO:0018063; P:cytochrome c-heme linkage case GO GO:0009535; C:chloroplast thylakoid membrane else case GO GO:0005886; C:plasma membrane else GO GO:0042651; C:thylakoid membrane end case XX FT From: CY550_THEVB (P0A386) FT BINDING 67 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 118 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 63 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT Condition: C FT BINDING 66 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT Condition: C XX Size: 129-186; Related: None; Template: P0A386; Q55013; Q76FB0; Scope: Bacteria; Cyanobacteriota Plastid Fusion: Nter: None Cter: None Duplicate: in GLOVI, THEVB, SYNJA, SYNJB, SYNVU, TRIEI Plasmid: None Comments: In land plants cytochrome c-550 and the 12 kDa protein (PsbU) are replaced by PsbP and PsbQ. The oxygen-evolving complex in Cyanidium caldarium is composed of 4 proteins (PsbO, PsbQ, PsbU and cytochrome c- 550); other algae may be similar. For a review see: PubMed=17200881; DOI=10.1007/s11120-006-9117-1; Roose J.L., Wegener K.M., Pakrasi H.B.; "The extrinsic proteins of Photosystem II."; Photosyn. Res. 92:369-387(2007). XX # Revision 1.31 2023/08/02 //