Cytochrome c-550 precursor - Thermosynechococcus vulcanus

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P0A387 (CY550_THEVL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 55. 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 c-550

Alternative name(s):
Cytochrome c550
Low-potential cytochrome c

Gene names

Name:

psbV

Organism

Thermosynechococcus vulcanus (Synechococcus vulcanus)

Taxonomic identifier

32053 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Thermosynechococcus

Protein attributes

Sequence length	163 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). Binds to PSII in the absence of other extrinsic proteins; required for binding of the PsbU protein to photosystem II. In PSII particles without oxygen-evolving activity, maximal activity is restored only by binding of cytochrome c550, PsbU and the 33 kDa PsbO protein. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H₂O, generating a proton gradient subsequently used for ATP formation. Ref.2 Ref.4
Cofactor	Binds 1 heme group covalently per subunit.
Subunit structure	The cyanobacterial oxygen-evolving complex is composed of PsbO, PsbP, PsbQ, PsbV and PsbU Probable. PsbP and PsbQ are not seen in the crystal structures; however there is biochemical evidence that they are part of the OEC. Cyanobacterial PSII is composed of one copy of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, 3 peripheral proteins PsbO, 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. HAMAP-Rule MF_01378
Sequence similarities	Belongs to the cytochrome c family. PsbV subfamily.

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 Direct protein sequencing
Gene Ontology (GO)
Biological_process	cytochrome c-heme linkage Inferred from electronic annotation. Source: HAMAP photosynthesis, light reaction Inferred from electronic annotation. Source: HAMAP respiratory electron transport chain Inferred from electronic annotation. Source: InterPro
Cellular_component	photosystem II Inferred from electronic annotation. Source: UniProtKB-KW thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred 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 – 26

Ref.2 Ref.3

Chain

27 – 163

137

Cytochrome c-550 HAMAP-Rule MF_01378

PRO_0000006519

Sites

Metal binding

Iron (heme axial ligand)

Metal binding

118

Iron (heme axial ligand)

Binding site

Heme (covalent)

Binding site

Heme (covalent)

Secondary structure

163

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A387 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: DA634C5C4084F676
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FASTA

163

18,027

        10         20         30         40         50         60 
MLKKCVWLAV ALCLCLWQFT MGTALAAELT PEVLTVPLNS EGKTITLTEK QYLEGKRLFQ 

        70         80         90        100        110        120 
YACASCHVGG ITKTNPSLDL RTETLALATP PRDNIEGLVD YMKNPTTYDG EQEIAEVHPS 

       130        140        150        160 
LRSADIFPKM RNLTEKDLVA IAGHILVEPK ILGDKWGGGK VYY

« Hide

References

[1]	"Functional analysis of psbV and a novel c-type cytochrome gene psbV2 of the thermophilic cyanobacterium Thermosynechococcus elongatus strain BP-1." Katoh H., Itoh S., Shen J.-R., Ikeuchi M. Plant Cell Physiol. 42:599-607(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Stoichiometric association of extrinsic cytochrome c550 and 12 kDa protein with a highly purified oxygen-evolving photosystem II core complex from Synechococcus vulcanus." Shen J.-R., Ikeuchi M., Inoue Y. FEBS Lett. 301:145-149(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-62, ASSOCIATION WITH PHOTOSYSTEM II, SUGGESTION OF ROLE IN OXYGEN-EVOLUTION.
[3]	"Low-molecular-mass polypeptide components of a photosystem II preparation from the thermophilic cyanobacterium Thermosynechococcus vulcanus." Kashino Y., Koike H., Yoshio M., Egashira H., Ikeuchi M., Pakrasi H.B., Satoh K. Plant Cell Physiol. 43:1366-1373(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-39, COMPOSITION OF PHOTOSYSTEM II.
[4]	"Binding and functional properties of two new extrinsic components, cytochrome c-550 and a 12-kDa protein, in cyanobacterial photosystem II." Shen J.-R., Inoue Y. Biochemistry 32:1825-1832(1993) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, FUNCTION IN OXYGEN-EVOLVING COMPLEX.
[5]	"Cellular localization of cytochrome c550. Its specific association with cyanobacterial photosystem II." Shen J.-R., Inoue Y. J. Biol. Chem. 268:20408-20413(1993) [PubMed] [Europe PMC] [Abstract] Cited for: TIGHT ASSOCIATION WITH PHOTOSYSTEM II.
[6]	"Comparison of binding and functional properties of two extrinsic components, cyt c550 and a 12 kDa protein, in cyanobacterial PSII with those in red algal PSII." Enami I., Iwai M., Akiyama A., Suzuki T., Okumura A., Katoh T., Tada O., Ohta H., Shen J.-R. Plant Cell Physiol. 44:820-827(2003) [PubMed] [Europe PMC] [Abstract] Cited for: RECONSTITUTION EXPERIMENTS.
[7]	"Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-A resolution." Kamiya N., Shen J.-R. Proc. Natl. Acad. Sci. U.S.A. 100:98-103(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 27-163, SUBUNIT, SUBCELLULAR LOCATION.
[8]	"Location of chloride and its possible functions in oxygen-evolving photosystem II revealed by X-ray crystallography." Kawakami K., Umena Y., Kamiya N., Shen J.R. Proc. Natl. Acad. Sci. U.S.A. 106:8567-8572(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 27-163, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
[9]	"Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 A." Umena Y., Kawakami K., Shen J.R., Kamiya N. Nature 473:55-60(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[10]	"Structure of Sr-substituted photosystem II at 2.1 A resolution and its implications in the mechanism of water oxidation." Koua F.H., Umena Y., Kawakami K., Shen J.R. Proc. Natl. Acad. Sci. U.S.A. 110:3889-3894(2013) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 27-163.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB052598 Genomic DNA. Translation: BAB20063.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IZL	X-ray	3.70	0/V	27-163	[»]
3A0B	X-ray	3.70	V/v	27-163	[»]
3A0H	X-ray	4.00	V/v	27-163	[»]
3ARC	X-ray	1.90	V/v	27-163	[»]
4IL6	X-ray	2.10	V/v	27-163	[»]

ProteinModelPortal

P0A387.

SMR

P0A387. Positions 27-163.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48861N.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

HAMAP

MF_01378. PSII_Cyt550.

InterPro

IPR009056. Cyt_c_dom.
IPR003088. Cyt_c_I.
IPR016003. PSII_cyt_c550.
IPR017851. PSII_PsbV_cyt_c550.
[Graphical view]

Pfam

PF00034. Cytochrom_C. 1 hit.
[Graphical view]

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...

Other

EvolutionaryTrace

P0A387.

Entry information

Entry name

CY550_THEVL

Accession

Primary (citable) accession number: P0A387
Secondary accession number(s): P56150, Q9ETF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	May 29, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Family and domain databases

Other

Entry information

Relevant documents