P07173 (CYCR_RHOVI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Photosynthetic reaction center cytochrome c subunit

Alternative name(s):
Cytochrome c558/c559

Gene names

Name:	pufC
Synonyms:	cytC

Organism

Rhodopseudomonas viridis

Taxonomic identifier

1079 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Hyphomicrobiaceae › Blastochloris

Protein attributes

Sequence length	356 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	The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor.
Subcellular location	Cell membrane; Lipid-anchor.
Post-translational modification	Binds 4 heme groups per subunit. After the signal sequence is removed, the N-terminal cysteine is modified to form a diacylglyceride thioether, but the alpha-amino group is free and is not N-palmitoylated.

Ontologies

Keywords
Biological process	Electron transport Photosynthesis Transport
Cellular component	Cell membrane Membrane Reaction center
Domain	Repeat Signal
Ligand	Heme Iron Metal-binding
PTM	Lipoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW photosynthesis, light reaction Inferred from electronic annotation. Source: InterPro
Cellular_component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane light-harvesting complex Inferred from electronic annotation. Source: InterPro
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 – 20

20

Chain

21 – 356

336

Photosynthetic reaction center cytochrome c subunit

PRO_0000006551

Sites

Metal binding

94

1

Iron (heme 1 axial ligand)

Metal binding

111

1

Iron (heme 1 axial ligand)

Metal binding

130

1

Iron (heme 2 axial ligand)

Metal binding

144

1

Iron (heme 4 axial ligand)

Metal binding

156

1

Iron (heme 2 axial ligand)

Metal binding

253

1

Iron (heme 3 axial ligand)

Metal binding

268

1

Iron (heme 3 axial ligand)

Metal binding

329

1

Iron (heme 4 axial ligand)

Binding site

107

1

Heme 1 (covalent)

Binding site

110

1

Heme 1 (covalent)

Binding site

152

1

Heme 2 (covalent)

Binding site

155

1

Heme 2 (covalent)

Binding site

264

1

Heme 3 (covalent)

Binding site

267

1

Heme 3 (covalent)

Binding site

325

1

Heme 4 (covalent)

Binding site

328

1

Heme 4 (covalent)

Site

21

1

Not N-palmitoylated

Amino acid modifications

Lipidation

21

1

S-diacylglycerol cysteine

Secondary structure

1

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356

Helix Strand Turn

Details...

Helix

45 – 55

11

Beta strand

69 – 71

3

Helix

72 – 75

4

Beta strand

76 – 78

3

Beta strand

80 – 82

3

Helix

87 – 101

15

Turn

103 – 105

3

Helix

106 – 109

4

Helix

122 – 140

19

Helix

142 – 145

4

Turn

146 – 148

3

Helix

152 – 156

5

Beta strand

159 – 161

3

Beta strand

172 – 175

4

Turn

182 – 184

3

Helix

189 – 191

3

Helix

192 – 197

6

Turn

198 – 202

5

Helix

209 – 213

5

Beta strand

215 – 217

3

Beta strand

226 – 229

4

Beta strand

234 – 236

3

Helix

237 – 239

3

Helix

244 – 260

17

Helix

264 – 266

3

Helix

270 – 272

3

Helix

282 – 300

19

Helix

303 – 307

5

Helix

311 – 313

3

Helix

325 – 329

5

Beta strand

332 – 334

3

Helix

335 – 338

4

Helix

342 – 344

3

Helix

346 – 348

3

Sequences

	Sequence		Length	Mass (Da)
	P07173 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: ECE3D64F1BB0877A	FASTA	356	39,371
	10 20 30 40 50 60 MKQLIVNSVA TVALASLVAG CFEPPPATTT QTGFRGLSMG EVLHPATVKA KKERDAQYPP 70 80 90 100 110 120 ALAAVKAEGP PVSQVYKNVK VLGNLTEAEF LRTMTAITEW VSPQEGCTYC HDENNLASEA 130 140 150 160 170 180 KYPYVVARRM LEMTRAINTN WTQHVAQTGV TCYTCHRGTP LPPYVRYLEP TLPLNNRETP 190 200 210 220 230 240 THVERVETRS GYVVRLAKYT AYSALNYDPF TMFLANDKRQ VRVVPQTALP LVGVSRGKER 250 260 270 280 290 300 RPLSDAYATF ALMMSISDSL GTNCTFCHNA QTFESWGKKS TPQRAIAWWG IRMVRDLNMN 310 320 330 340 350 YLAPLNASLP ASRLGRQGEA PQADCRTCHQ GVTKPLFGAS RLKDYPELGP IKAAAK

References

[1]	"Amino acid sequence of the cytochrome subunit of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis." Weyer K.A., Lottspeich F., Lang F., Oesterhelt D., Michel H. EMBO J. 6:2197-2202(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE. Strain: DSM 133.
[2]	"The cytochrome subunit of the photosynthetic reaction center from Rhodopseudomonas viridis is a lipoprotein." Weyer K.A., Schaefer W., Lottspeich F., Michel H. Biochemistry 26:2909-2914(1987) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46.
[3]	"Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3-A resolution." Deisenhofer J., Epp O., Miki K., Huber R., Michel H. Nature 318:618-624(1985) Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
[4]	"X-ray structure analysis of a membrane protein complex. Electron density map at 3-A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis." Deisenhofer J., Epp O., Miki K., Huber R., Michel H. J. Mol. Biol. 180:385-398(1984) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
[5]	"The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB." Lancaster C.R.D., Michel H. Structure 5:1339-1359(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS). Strain: DSM 133.
[6]	"Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid." Lancaster C.R.D., Michel H. J. Mol. Biol. 286:883-898(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS). Strain: DSM 133.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X05768 Genomic DNA. Translation: CAA29223.1.
M16317 Genomic DNA. Translation: AAA26093.1.

PIR

S00139.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DXR	X-ray	2.00	C	21-356	[»]
1PRC	X-ray	2.30	C	21-356	[»]
1R2C	X-ray	2.86	C	21-356	[»]
1VRN	X-ray	2.20	C	21-352	[»]
2I5N	X-ray	1.96	C	21-356	[»]
2JBL	X-ray	2.40	C	1-356	[»]
2PRC	X-ray	2.45	C	21-356	[»]
2WJM	X-ray	1.95	C	21-356	[»]
2WJN	X-ray	1.86	C	21-356	[»]
2X5U	X-ray	3.00	C	21-356	[»]
2X5V	X-ray	3.00	C	21-356	[»]
3D38	X-ray	3.21	C	21-356	[»]
3G7F	X-ray	2.50	C	21-356	[»]
3PRC	X-ray	2.40	C	21-356	[»]
3T6D	X-ray	1.95	C	1-356	[»]
3T6E	X-ray	1.92	C	1-356	[»]
4AC5	X-ray	8.20	C	21-356	[»]
5PRC	X-ray	2.35	C	21-356	[»]
6PRC	X-ray	2.30	C	21-356	[»]
7PRC	X-ray	2.65	C	21-356	[»]

ProteinModelPortal

P07173.

SMR

P07173. Positions 21-352.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.10.468.10. 2 hits.

InterPro

IPR011031. Multihaem_cyt.
IPR023119. Multihaem_cyt_PRC_cyt_su-like.
IPR003158. Photosyn_RC_cyt_c-su.
[Graphical view]

Pfam

PF02276. CytoC_RC. 1 hit.
[Graphical view]

PIRSF

PIRSF000017. RC_cytochrome. 1 hit.

PROSITE

PS51008. MULTIHEME_CYTC. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P07173.

Entry information

Entry name

CYCR_RHOVI

Accession

Primary (citable) accession number: P07173

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	April 3, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program