Reviewed,
UniProtKB/Swiss-Prot P08500 (UCRI_RHOCA)
Last modified
June 16, 2009.
Version 86.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Ubiquinol-cytochrome c reductase iron-sulfur subunit EC=1.10.2.2 Alternative name(s): Rieske iron-sulfur protein Short name=RISP | ||||
| Gene names |
| ||||
| Organism | Rhodobacter capsulatus (Rhodopseudomonas capsulata) | ||||
| Taxonomic identifier | 1061 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter |
Protein attributes
| Sequence length | 191 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. |
| Catalytic activity | QH2 + 2 ferricytochrome c = Q + 2 ferrocytochrome c + 2 H+. |
| Cofactor | Binds 1 2Fe-2S cluster per subunit. |
| Subunit structure | The main subunits of complex b-c1 are: cytochrome b, cytochrome c1 and the Rieske protein. |
| Subcellular location | |
| Miscellaneous | The Rieske protein is a high potential 2Fe-2S protein. |
| Sequence similarities | Contains 1 Rieske domain. |
| Caution | The sequence reported in Ref.2 was thought to originate from R.sphaeroides but was later shown (Ref.3) to be derived from R.capsulatus. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Transport |
| Cellular component | Cell membrane Membrane |
| Domain | Transmembrane |
| Ligand | 2Fe-2S Iron Iron-sulfur Metal-binding |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activityInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW ubiquinol-cytochrome-c reductase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 191 | 191 | Ubiquinol-cytochrome c reductase iron-sulfur subunit | PRO_0000127762 | |||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||
| Transmembrane | 18 – 35 | 18 | Potential | ||||||||||||||||||||||||||||||||||||||||
| Domain | 94 – 189 | 96 | Rieske | ||||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||||
| Metal binding | 133 | 1 | Iron-sulfur (2Fe-2S) | ||||||||||||||||||||||||||||||||||||||||
| Metal binding | 135 | 1 | Iron-sulfur (2Fe-2S); via pros nitrogen | ||||||||||||||||||||||||||||||||||||||||
| Metal binding | 153 | 1 | Iron-sulfur (2Fe-2S) | ||||||||||||||||||||||||||||||||||||||||
| Metal binding | 156 | 1 | Iron-sulfur (2Fe-2S); via pros nitrogen | ||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 138 ↔ 155 | ||||||||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 48 | 1 | A → S in strain: GA. | ||||||||||||||||||||||||||||||||||||||||
| Natural variant | 114 | 1 | T → S in strain: GA. | ||||||||||||||||||||||||||||||||||||||||
| Natural variant | 116 | 1 | P → A in strain: GA. | ||||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 133 | 1 | C → R or S: Photosynthetically incompetent. | ||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 135 | 1 | H → L or P: Photosynthetically incompetent. | ||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 138 | 1 | C → F, R or S: Photosynthetically incompetent. | ||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 153 | 1 | C → R or S: Photosynthetically incompetent. | ||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 155 | 1 | C → D, G or S: Photosynthetically incompetent. | ||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 156 | 1 | H → L, P or F: Photosynthetically incompetent. | ||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 156 | 1 | H → T or Y: Photosynthetically incompetent. | ||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 159 | 1 | H → A or S: Photosynthetically competent. | ||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 12 – 37 | 26 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 43 – 45 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 50 – 52 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 63 – 67 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 70 – 75 | 6 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 79 – 86 | 8 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 90 – 92 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 101 – 103 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 110 – 114 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 119 – 121 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 127 – 129 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 134 – 136 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 146 – 148 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 154 – 156 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 166 – 170 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 179 – 186 | 8 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 188 – 190 | 3 | |||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Primary structure of the bc1 complex of Rhodopseudomonas capsulata. Nucleotide sequence of the pet operon encoding the Rieske cytochrome b, and cytochrome c1 apoproteins." Davidson E., Daldal F. J. Mol. Biol. 195:13-24(1987) [PubMed: 2821268] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 23782 / LMG 2373 / NCIB 11773 / SB1003 / St. Louis. |
| [2] | "Nucleotide sequence and transcription of the fbc operon from Rhodopseudomonas sphaeroides. Evaluation of the deduced amino acid sequences of the FeS protein, cytochrome b and cytochrome c1." Gabellini N., Sebald W. Eur. J. Biochem. 154:569-579(1986) [PubMed: 3004982] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: GA. |
| [3] | "fbc operon, encoding the Rieske Fe-S protein cytochrome b, and cytochrome c1 apoproteins previously described from Rhodopseudomonas sphaeroides, is from Rhodopseudomonas capsulata." Davidson E., Daldal F. J. Mol. Biol. 195:25-29(1987) [PubMed: 2821272] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95, SHOWS THAT SEQUENCE DESCRIBED IN PUBMED:3004982 ORIGINATES FROM RHODOBACTER CAPSULATUS. |
| [4] | "petR, located upstream of the fbcFBC operon encoding the cytochrome bc1 complex, is homologous to bacterial response regulators and necessary for photosynthetic and respiratory growth of Rhodobacter capsulatus." Tokito M.K., Daldal F. Mol. Microbiol. 6:1645-1654(1992) [PubMed: 1323023] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23. Strain: MT1131. |
| [5] | "Potential ligands to the [2Fe-2S] Rieske cluster of the cytochrome bc1 complex of Rhodobacter capsulatus probed by site-directed mutagenesis." Davidson E., Ohnishi T., Atta-Asafo-Adjei E., Daldal F. Biochemistry 31:3342-3351(1992) [PubMed: 1313292] [Abstract] Cited for: MUTAGENESIS. Strain: MT0-404. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| X05630 Genomic DNA. Translation: CAA29116.1. M18576 Genomic DNA. Translation: AAA26151.1. Z12113 Genomic DNA. Translation: CAA78099.1. X03476 Genomic DNA. Translation: CAA27194.1. | |||||||||||||
| PIR | A29336. | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 1.10.2.2. 567. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR017941. Rieske_2Fe-2S. IPR014349. Rieske_Fe-S_prot. IPR006311. Tat. IPR017909. Twin_arg_translocation_Tat. IPR019470. Ubiq_cytC_Rdtase_Fe-S_su_TAT. IPR006317. Ubiquinol_cyt_c_Rdtase_Fe-S-su. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:2.102.10.10. Rieske_reg. 1 hit. | ||||||||||||
| PANTHER | PTHR10134. Rieske. 1 hit. | ||||||||||||
| Pfam | PF00355. Rieske. 1 hit. PF10399. UCR_Fe-S_N. 1 hit. [Graphical view] | ||||||||||||
| TIGRFAMs | TIGR01416. Rieske_proteo. 1 hit. TIGR01409. TAT_signal_seq. 1 hit. | ||||||||||||
| PROSITE | PS51296. RIESKE. 1 hit. PS51318. TAT. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | UCRI_RHOCA | ||||||||
| Accession | Primary (citable) accession number: P08500 Secondary accession number(s): P07055 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


