HAMAP rule MF_01378
General rule information
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| Accession | MF_01378 |
| Dates | 28-JUN-2007 (Created)
2-AUG-2023 (Last updated, Version 31) |
| Name | PSII_Cyt550 |
| Scope(s) |
Bacteria Cyanobacteriota Plastid |
| Template(s) | P0A386 (CY550_THEVB); Q55013 (CY550_SYNY3); Q76FB0 (C550B_CYACA); [ Recover all ] |
| Triggered by |
HAMAP; MF_01378 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | CY550 |
| case <OC:Cyanobacteriota> | |
| Protein name | RecName: Full=Photosystem II extrinsic protein V; Short=PsbV; AltName: Full=Cytochrome c-550; AltName: Full=Cytochrome c550; AltName: Full=Low-potential cytochrome c; Flags: Precursor; |
| else case <OG:Chloroplast> | |
| Protein name | RecName: Full=Photosystem II extrinsic protein V; Short=PsbV; AltName: Full=Cytochrome c-550; AltName: Full=Cytochrome c550; Flags: Precursor; |
| end case | |
| Gene name | Name=psbV; |
Comments
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| FUNCTION | One of the extrinsic, lumenal subunits of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. The extrinsic proteins stabilize the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protect the OEC against heat-induced inactivation. Low-potential cytochrome c that plays a role in the OEC of PSII. |
| COFACTOR | Name=heme c; Xref=ChEBI:CHEBI:61717; Note=Binds 1 heme c group covalently per subunit.; |
| case <OG:Chloroplast> | |
| SUBUNIT | PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbY, PsbZ, Psb30/Ycf12, at least 3 peripheral proteins of the oxygen- evolving complex and a large number of cofactors. It forms dimeric complexes. |
| SUBCELLULAR LOCATION | Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side. Note=Associated with photosystem II at the lumenal side of the thylakoid membrane. |
| else case <OC:Gloeobacter> | |
| SUBUNIT | PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ), PsbU, PsbV and a large number of cofactors. It forms dimeric complexes. |
| SUBCELLULAR LOCATION | Cell inner membrane; Peripheral membrane protein; Periplasmic side. Note=Associated with photosystem II at the periplasmic side side of the thylakoid membrane. |
| else | |
| SUBUNIT | PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ), PsbU, PsbV and a large number of cofactors. It forms dimeric complexes. |
| SUBCELLULAR LOCATION | Cellular thylakoid membrane; Peripheral membrane protein; Lumenal side. Note=Associated with photosystem II at the lumenal side of the thylakoid membrane. |
| end case | |
| SIMILARITY | Belongs to the cytochrome c family. PsbV subfamily. |
Keywords
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| Electron transport | |
| Heme | |
| Iron | |
| Metal-binding | |
| Photosynthesis | |
| Photosystem II | |
| case <OC:Gloeobacter> | |
| Cell membrane | |
| Cell inner membrane | |
| else | |
| Thylakoid | |
| end case | |
| Membrane | |
| Transport | |
Gene Ontology
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| GO:0019684; Biological process:photosynthesis, light reaction | |
| GO:0018063; Biological process:cytochrome c-heme linkage | |
| case <OG:Chloroplast> | |
| GO:0009535; Cellular component:chloroplast thylakoid membrane | |
| else case <OCellular component:Gloeobacter> | |
| GO:0005886; Cellular component:plasma membrane | |
| else; https://www.ebi.ac.uk/QuickGO/term/else | |
| GO:0042651; Cellular component:thylakoid membrane | |
| end case | |
Cross-references
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| PROSITE | PS51007; CYTC; 1; |
| Pfam | PF00034; Cytochrom_C; 1; |
| NCBIfam | TIGR03045; PS_II_C550; 1; |
| General | Signal; -; 1; |
Features
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| From: CY550_THEVB (P0A386) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 67 | 67 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| BINDING | 118 | 118 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /ligand_part="Fe" /ligand_part_id="ChEBI:CHEBI:18248" /note="axial binding residue" |
H | ||||||||
| BINDING | 63 | 63 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /note="covalent" |
C | ||||||||
| BINDING | 66 | 66 | /ligand="heme c" /ligand_id="ChEBI:CHEBI:61717" /note="covalent" |
C | ||||||||
Additional information
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| Size range | 129-186 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: 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). |