Cytochrome b6-f complex iron-sulfur subunit 2 - Synechocystis sp. (strain PCC 6803 / Kazusa)

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P26290 (UCRIB_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cytochrome b6-f complex iron-sulfur subunit 2
EC=1.10.99.1

Alternative name(s):
Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein 2
Short name=ISP 2
Short name=RISP 2
Rieske iron-sulfur protein 2

Gene names

Name:	petC2
Ordered Locus Names:	sll1316

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa)

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

Protein attributes

Sequence length	180 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions By similarity. HAMAP MF_01335
Catalytic activity	Plastoquinol-1 + 2 oxidized plastocyanin = plastoquinone + 2 reduced plastocyanin. HAMAP MF_01335
Cofactor	Binds 1 2Fe-2S cluster per subunit By similarity. HAMAP MF_01335
Subunit structure	The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer By similarity.
Subcellular location	Cellular thylakoid membrane; Single-pass membrane protein By similarity. Note: The transmembrane helix obliquely spans the membrane in one monomer, and its extrinsic C-terminal domain is part of the other monomer By similarity. HAMAP MF_01335
Miscellaneous	The Rieske iron-sulfur protein is a high potential 2Fe-2S protein. HAMAP MF_01335
Sequence similarities	Contains 1 Rieske domain.
Sequence caution	The sequence BAA17628.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA41421.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Membrane Thylakoid
Domain	Transmembrane Transmembrane helix
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW photosynthesis Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW plastoquinol-plastocyanin reductase activity Inferred from electronic annotation. Source: EC ubiquinol-cytochrome-c reductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 180

180

Cytochrome b6-f complex iron-sulfur subunit 2 HAMAP MF_01335

PRO_0000127785

Regions

Transmembrane

21 – 43

Helical; Potential

Domain

66 – 162

Rieske

Sites

Metal binding

108

Iron-sulfur (2Fe-2S) By similarity

Metal binding

110

Iron-sulfur (2Fe-2S); via pros nitrogen By similarity

Metal binding

126

Iron-sulfur (2Fe-2S) By similarity

Metal binding

129

Iron-sulfur (2Fe-2S); via pros nitrogen By similarity

Amino acid modifications

Disulfide bond

113 ↔ 128

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P26290 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 351CB0C7DF892B5C
Show »

FASTA

180

18,996

        10         20         30         40         50         60 
MTQISGSPDV PDLGRRQFMN LLTFGTITGV AAGALYPAVK YLIPPSSGGS GGGVTAKDAL 

        70         80         90        100        110        120 
GNDVKVTEFL ASHNAGDRVL AQGLKGDPTY IVVQGDDTIA NYGINAVCTH LGCVVPWNAS 

       130        140        150        160        170        180 
ENKFMCPCHG SQYNAEGKVV RGPAPLSLAL AHATVTDDDK LVLSTWTETD FRTDEDPWWA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of the psbN-psbH-petC-petA gene cluster of the cyanobacterium Synechocystis PCC 6803." Mayes S.R., Barber J. Plant Mol. Biol. 17:289-293(1991) [PubMed: 1907512] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X58532 Genomic DNA. Translation: CAA41422.1. X58532 Genomic DNA. Translation: CAA41421.1. Different initiation. BA000022 Genomic DNA. Translation: BAA17628.1. Different initiation.
PIR	S16572.
RefSeq	NP_440948.1. NC_000911.1.
3D structure databases
ProteinModelPortal	P26290.
SMR	P26290. Positions 9-179.
ModBase	Search...
Protein-protein interaction databases
STRING	P26290.
Protein family/group databases
TCDB	3.D.3.5.1. proton-translocating quinol:cytochrome c reductase (QCR) superfamily.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	954258.
GenomeReviews	Gene locus sll1316 in contig BA000022_GR.
KEGG	syn:sll1316.
NMPDR	fig\|1148.1.peg.1049.
PATRIC	23839170. VBISynSp132158_1149.
Phylogenomic databases
eggNOG	COG0723.
HOGENOM	HBG668715.
OMA	YPVANYF.
PhylomeDB	P26290.
ProtClustDB	PRK13474.
Enzyme and pathway databases
BioCyc	SSP1148:SLL1316-MONOMER.
Family and domain databases
HAMAP	MF_01335. Cytb6_f_Rieske. [Tree]
InterPro	IPR000595. cNMP-bd_dom. IPR014909. Cyt_b6-f_cplx_Fe-S_su. IPR023960. Cyt_b6_f_Rieske. IPR017941. Rieske_2Fe-2S. IPR014349. Rieske_Fe-S_prot. IPR005805. Rieske_Fe-S_prot_C. [Graphical view]
Gene3D	G3DSA:2.102.10.10. Rieske_reg. 1 hit.
KO	K02636.
PANTHER	PTHR10134. Rieske. 1 hit.
Pfam	PF08802. CytB6-F_Fe-S. 1 hit. PF00355. Rieske. 1 hit. [Graphical view]
PRINTS	PR00162. RIESKE.
SUPFAM	SSF50022. Rieske_dom. 1 hit.
PROSITE	PS51296. RIESKE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UCRIB_SYNY3

Accession

Primary (citable) accession number: P26290

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 93 of the entry and version 2 of the sequence. [Complete history]

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents