Q55013 (CY550_SYNY3) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 100.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Cytochrome c-550 Alternative name(s): Cytochrome c549 Cytochrome c550 Low-potential cytochrome c | ||||||
| Gene names |
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| Organism | Synechocystis sp. (strain PCC 6803 / Kazusa) | ||||||
| Taxonomic identifier | 1111708 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Chroococcales › Synechocystis |
Protein attributes
| Sequence length | 160 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II (PSII). Required for normal function or stabilization of PSII. Extrinsic protein associated with PSII that enhances oxygen evolution. HAMAP MF_01378 |
| Cofactor | Binds 1 heme group covalently per subunit. |
| Subunit structure | The cyanobacterial oxygen-evolving complex is composed of psbO, psbP, psbQ, psbV and psbU Potential. |
| Subcellular location | Cellular thylakoid membrane; Peripheral membrane protein; Lumenal side Probable. Note: Associated with photosystem II at the lumenal side of the thylakoid membrane Probable. Ref.1 |
| Disruption phenotype | Cells show decreased but not abolished level of PSII and photoautotrophic growth. Ref.1 |
| Sequence similarities | Belongs to the cytochrome c family. PsbV subfamily. |
| Sequence caution | The sequence AAA19982.2 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Photosynthesis Transport |
| Cellular component | Membrane Photosystem II Thylakoid |
| Domain | Signal |
| Ligand | Heme Iron Metal-binding |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | photosynthesis Inferred from electronic annotation. Source: UniProtKB-KW respiratory electron transport chainInferred from electronic annotation. Source: InterPro transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | plasma membrane-derived thylakoid photosystem II Inferred from direct assay. Source: UniProtKB thylakoid membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | electron carrier activity Inferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 25 | 25 | Ref.1 Ref.3 Ref.4 | |||||||||||||||||||||||||||||||||
| Chain | 26 – 160 | 135 | Cytochrome c-550 HAMAP MF_01378 | PRO_0000006521 | ||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||
| Metal binding | 66 | 1 | Iron (heme axial ligand) | |||||||||||||||||||||||||||||||||
| Metal binding | 117 | 1 | Iron (heme axial ligand) | |||||||||||||||||||||||||||||||||
| Binding site | 62 | 1 | Heme (covalent) | |||||||||||||||||||||||||||||||||
| Binding site | 65 | 1 | Heme (covalent) | |||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||
| Sequence conflict | 60 | 1 | D → T in AAA19982. Ref.3 | |||||||||||||||||||||||||||||||||
| Sequence conflict | 71 | 1 | Missing AA sequence Ref.1 | |||||||||||||||||||||||||||||||||
| Sequence conflict | 90 – 91 | 2 | RR → PS in AAA19982. Ref.3 | |||||||||||||||||||||||||||||||||
| Sequence conflict | 94 | 1 | V → R in AAA19982. Ref.3 | |||||||||||||||||||||||||||||||||
| Sequence conflict | 138 – 139 | 2 | FD → YN in AAA19982. Ref.3 | |||||||||||||||||||||||||||||||||
| Sequence conflict | 142 | 1 | G → A in AAA19982. Ref.3 | |||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||
| Turn | 30 – 33 | 4 | ||||||||||||||||||||||||||||||||||
| Beta strand | 34 – 41 | 8 | ||||||||||||||||||||||||||||||||||
| Beta strand | 43 – 45 | 3 | ||||||||||||||||||||||||||||||||||
| Helix | 48 – 61 | 14 | ||||||||||||||||||||||||||||||||||
| Helix | 63 – 66 | 4 | ||||||||||||||||||||||||||||||||||
| Helix | 67 – 69 | 3 | ||||||||||||||||||||||||||||||||||
| Beta strand | 71 – 76 | 6 | ||||||||||||||||||||||||||||||||||
| Beta strand | 78 – 80 | 3 | ||||||||||||||||||||||||||||||||||
| Helix | 81 – 85 | 5 | ||||||||||||||||||||||||||||||||||
| Beta strand | 87 – 89 | 3 | ||||||||||||||||||||||||||||||||||
| Helix | 94 – 102 | 9 | ||||||||||||||||||||||||||||||||||
| Turn | 114 – 116 | 3 | ||||||||||||||||||||||||||||||||||
| Turn | 123 – 125 | 3 | ||||||||||||||||||||||||||||||||||
| Helix | 127 – 129 | 3 | ||||||||||||||||||||||||||||||||||
| Helix | 134 – 150 | 17 | ||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The role of cytochrome c-550 as studied through reverse genetics and mutant characterization in Synechocystis sp. PCC 6803." Shen J.-R., Vermaas W., Inoue Y. J. Biol. Chem. 270:6901-6907(1995) [PubMed: 7896839] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-73, PROBABLE SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. |
| [2] | "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. Tabata S.DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27184 / PCC 6803 / N-1. |
| [3] | "Cloning and sequence analysis of the gene encoding the low potential cytochrome c of Synechocystis PCC 6803." Kang C., Chitnis P.R., Smith S., Krogmann D.W. FEBS Lett. 344:5-9(1994) [PubMed: 8181563] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-160, PROTEIN SEQUENCE OF 26-49. |
| [4] | "Towards a proteome project of cyanobacterium Synechocystis sp. strain PCC6803: linking 130 protein spots with their respective genes." Sazuka T., Ohara O. Electrophoresis 18:1252-1258(1997) [PubMed: 9298645] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-40. |
| [5] | "Crystal structure of low-potential cytochrome c549 from Synechocystis sp. PCC 6803 at 1.21 A resolution." Frazao C., Enguita F.J., Coelho R., Sheldrick G.M., Navarro J.A., Hervas M., De la Rosa M.A., Carrondo M.A. J. Biol. Inorg. Chem. 6:324-332(2001) [PubMed: 11315568] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.21 ANGSTROMS) OF 26-160. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | D45178 Genomic DNA. Translation: BAA08124.1. BA000022 Genomic DNA. Translation: BAA18512.1. U07021 Genomic DNA. Translation: AAA19982.2. Different initiation. | ||||||||||||
| PIR | A56189. | ||||||||||||
| RefSeq | NP_441834.1. NC_000911.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | Q55013. | ||||||||||||
| SMR | Q55013. Positions 26-160. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q55013. 1 interaction. | ||||||||||||
| STRING | Q55013. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 954270. | ||||||||||||
| GenomeReviews | Gene locus sll0258 in contig BA000022_GR. | ||||||||||||
| KEGG | syn:sll0258. | ||||||||||||
| NMPDR | fig|1148.1.peg.1935. | ||||||||||||
| PATRIC | 23841184. VBISynSp132158_2143. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | NOG13404. | ||||||||||||
| HOGENOM | HBG285698. | ||||||||||||
| OMA | WGGGKIY. | ||||||||||||
| PhylomeDB | Q55013. | ||||||||||||
| ProtClustDB | PRK13619. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | MetaCyc:PSBV-MONOMER. SSP1148:SLL0258-MONOMER. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_01378. PSII_Cyt550. [Tree] | ||||||||||||
| InterPro | IPR009056. Cyt_c_dom. IPR016003. PSII_cyt_c550. IPR017851. PSII_PsbV_cyt_c550. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:1.10.760.10. Cytochrome_c_R. 1 hit. | ||||||||||||
| KO | K02720. | ||||||||||||
| PIRSF | PIRSF005890. Phot_II_cyt_c550. 1 hit. | ||||||||||||
| SUPFAM | SSF46626. Cytochrome_c. 1 hit. | ||||||||||||
| TIGRFAMs | TIGR03045. PS_II_C550. 1 hit. | ||||||||||||
| PROSITE | PS51007. CYTC. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | CY550_SYNY3 | ||||||||
| Accession | Primary (citable) accession number: Q55013 Secondary accession number(s): Q55333 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Synechocystis PCC 6803 Synechocystis (strain PCC 6803): entries and gene names |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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