CY550_THEVL
ID CY550_THEVL Reviewed; 163 AA.
AC P0A387; P56150; Q9ETF4;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Cytochrome c-550 {ECO:0000255|HAMAP-Rule:MF_01378};
DE AltName: Full=Cytochrome c550 {ECO:0000255|HAMAP-Rule:MF_01378};
DE AltName: Full=Low-potential cytochrome c {ECO:0000255|HAMAP-Rule:MF_01378};
DE Flags: Precursor;
GN Name=psbV {ECO:0000255|HAMAP-Rule:MF_01378};
OS Thermostichus vulcanus (Synechococcus vulcanus).
OC Bacteria; Cyanobacteria; Thermostichales; Thermostichaceae; Thermostichus.
OX NCBI_TaxID=32053;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11427679; DOI=10.1093/pcp/pce074;
RA Katoh H., Itoh S., Shen J.-R., Ikeuchi M.;
RT "Functional analysis of psbV and a novel c-type cytochrome gene psbV2 of
RT the thermophilic cyanobacterium Thermosynechococcus elongatus strain BP-
RT 1.";
RL Plant Cell Physiol. 42:599-607(2001).
RN [2]
RP PROTEIN SEQUENCE OF 27-62, SUGGESTION OF FUNCTION IN OXYGEN-EVOLUTION,
RP ASSOCIATION WITH PHOTOSYSTEM II, AND SUBUNIT.
RX PubMed=1314738; DOI=10.1016/0014-5793(92)81235-e;
RA Shen J.-R., Ikeuchi M., Inoue Y.;
RT "Stoichiometric association of extrinsic cytochrome c550 and 12 kDa protein
RT with a highly purified oxygen-evolving photosystem II core complex from
RT Synechococcus vulcanus.";
RL FEBS Lett. 301:145-149(1992).
RN [3]
RP PROTEIN SEQUENCE OF 27-39, COMPOSITION OF PHOTOSYSTEM II, AND SUBUNIT.
RX PubMed=12461137; DOI=10.1093/pcp/pcf168;
RA Kashino Y., Koike H., Yoshio M., Egashira H., Ikeuchi M., Pakrasi H.B.,
RA Satoh K.;
RT "Low-molecular-mass polypeptide components of a photosystem II preparation
RT from the thermophilic cyanobacterium Thermosynechococcus vulcanus.";
RL Plant Cell Physiol. 43:1366-1373(2002).
RN [4]
RP FUNCTION IN OXYGEN-EVOLVING COMPLEX.
RX PubMed=8382523; DOI=10.1021/bi00058a017;
RA Shen J.-R., Inoue Y.;
RT "Binding and functional properties of two new extrinsic components,
RT cytochrome c-550 and a 12-kDa protein, in cyanobacterial photosystem II.";
RL Biochemistry 32:1825-1832(1993).
RN [5]
RP TIGHT ASSOCIATION WITH PHOTOSYSTEM II, COFACTOR, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=8397205; DOI=10.1016/s0021-9258(20)80743-1;
RA Shen J.-R., Inoue Y.;
RT "Cellular localization of cytochrome c550. Its specific association with
RT cyanobacterial photosystem II.";
RL J. Biol. Chem. 268:20408-20413(1993).
RN [6]
RP RECONSTITUTION EXPERIMENTS.
RX PubMed=12941874; DOI=10.1093/pcp/pcg106;
RA Enami I., Iwai M., Akiyama A., Suzuki T., Okumura A., Katoh T., Tada O.,
RA Ohta H., Shen J.-R.;
RT "Comparison of binding and functional properties of two extrinsic
RT components, cyt c550 and a 12 kDa protein, in cyanobacterial PSII with
RT those in red algal PSII.";
RL Plant Cell Physiol. 44:820-827(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12518057; DOI=10.1073/pnas.0135651100;
RA Kamiya N., Shen J.-R.;
RT "Crystal structure of oxygen-evolving photosystem II from
RT Thermosynechococcus vulcanus at 3.7-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:98-103(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II,
RP FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19433803; DOI=10.1073/pnas.0812797106;
RA Kawakami K., Umena Y., Kamiya N., Shen J.R.;
RT "Location of chloride and its possible functions in oxygen-evolving
RT photosystem II revealed by X-ray crystallography.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8567-8572(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH HEME IN PHOTOSYSTEM
RP II, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=21499260; DOI=10.1038/nature09913;
RA Umena Y., Kawakami K., Shen J.R., Kamiya N.;
RT "Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9
RT A.";
RL Nature 473:55-60(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 27-163 IN COMPLEX WITH HEME IN
RP PHOTOSYSTEM II, FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23426624; DOI=10.1073/pnas.1219922110;
RA Koua F.H., Umena Y., Kawakami K., Shen J.R.;
RT "Structure of Sr-substituted photosystem II at 2.1 A resolution and its
RT implications in the mechanism of water oxidation.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:3889-3894(2013).
CC -!- FUNCTION: Low-potential cytochrome c that plays a role in the oxygen-
CC evolving complex of photosystem II (PSII). Binds to PSII in the absence
CC of other extrinsic proteins; required for binding of the PsbU protein
CC to photosystem II. In PSII particles without oxygen-evolving activity,
CC maximal activity is restored only by binding of cytochrome c550, PsbU
CC and the 33 kDa PsbO protein. PSII is a light-driven water plastoquinone
CC oxidoreductase, using light energy to abstract electrons from H(2)O,
CC generating a proton gradient subsequently used for ATP formation.
CC {ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:1314738,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:23426624,
CC ECO:0000269|PubMed:8382523}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Note=Binds 1 heme c group covalently per subunit. PSII binds multiple
CC chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-
CC Rule:MF_01378, ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC ECO:0000269|PubMed:23426624, ECO:0000269|PubMed:8397205};
CC -!- SUBUNIT: The cyanobacterial oxygen-evolving complex is composed of
CC PsbO, PsbP, PsbQ, PsbV and PsbU (Probable). PsbP and PsbQ are not seen
CC in the crystal structures; however there is biochemical evidence that
CC they are part of the OEC. Cyanobacterial PSII is composed of 1 copy
CC each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH,
CC PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, 3
CC peripheral proteins PsbO, PsbU, PsbV and a large number of cofactors.
CC It forms dimeric complexes. {ECO:0000255|HAMAP-Rule:MF_01378,
CC ECO:0000269|PubMed:12461137, ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:1314738, ECO:0000269|PubMed:19433803,
CC ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624,
CC ECO:0000269|PubMed:8397205}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01378, ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC ECO:0000269|PubMed:23426624}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC ECO:0000269|PubMed:23426624}; Lumenal side {ECO:0000255|HAMAP-
CC Rule:MF_01378, ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC ECO:0000269|PubMed:23426624, ECO:0000269|PubMed:8397205}.
CC Note=Associated with photosystem II at the lumenal side of the
CC thylakoid membrane.
CC -!- SIMILARITY: Belongs to the cytochrome c family. PsbV subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01378}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB052598; BAB20063.1; -; Genomic_DNA.
DR PDB; 1IZL; X-ray; 3.70 A; 0/V=27-163.
DR PDB; 3A0B; X-ray; 3.70 A; V/v=27-163.
DR PDB; 3A0H; X-ray; 4.00 A; V/v=27-163.
DR PDB; 3WU2; X-ray; 1.90 A; V/v=27-163.
DR PDB; 4IL6; X-ray; 2.10 A; V/v=27-163.
DR PDB; 4UB6; X-ray; 1.95 A; V/v=27-163.
DR PDB; 4UB8; X-ray; 1.95 A; V/v=27-163.
DR PDB; 5B5E; X-ray; 1.87 A; V/v=27-163.
DR PDB; 5B66; X-ray; 1.85 A; V/v=27-163.
DR PDB; 5GTH; X-ray; 2.50 A; V/v=27-163.
DR PDB; 5GTI; X-ray; 2.50 A; V/v=27-163.
DR PDB; 5V2C; X-ray; 1.90 A; V/v=27-163.
DR PDB; 5WS5; X-ray; 2.35 A; V/v=27-163.
DR PDB; 5WS6; X-ray; 2.35 A; V/v=27-163.
DR PDB; 6JLJ; X-ray; 2.15 A; V/v=27-163.
DR PDB; 6JLK; X-ray; 2.15 A; V/v=27-163.
DR PDB; 6JLL; X-ray; 2.15 A; V/v=27-163.
DR PDB; 6JLM; X-ray; 2.35 A; V/v=27-163.
DR PDB; 6JLN; X-ray; 2.40 A; V/v=27-163.
DR PDB; 6JLO; X-ray; 2.40 A; V/v=27-163.
DR PDB; 6JLP; X-ray; 2.50 A; V/v=27-163.
DR PDB; 7CJI; X-ray; 2.35 A; V/v=27-163.
DR PDB; 7CJJ; X-ray; 2.40 A; V/v=27-163.
DR PDB; 7COU; X-ray; 2.25 A; V/v=27-163.
DR PDB; 7D1T; EM; 1.95 A; V/v=27-163.
DR PDB; 7D1U; EM; 2.08 A; V/v=27-163.
DR PDB; 7EDA; EM; 2.78 A; V=1-163.
DR PDBsum; 1IZL; -.
DR PDBsum; 3A0B; -.
DR PDBsum; 3A0H; -.
DR PDBsum; 3WU2; -.
DR PDBsum; 4IL6; -.
DR PDBsum; 4UB6; -.
DR PDBsum; 4UB8; -.
DR PDBsum; 5B5E; -.
DR PDBsum; 5B66; -.
DR PDBsum; 5GTH; -.
DR PDBsum; 5GTI; -.
DR PDBsum; 5V2C; -.
DR PDBsum; 5WS5; -.
DR PDBsum; 5WS6; -.
DR PDBsum; 6JLJ; -.
DR PDBsum; 6JLK; -.
DR PDBsum; 6JLL; -.
DR PDBsum; 6JLM; -.
DR PDBsum; 6JLN; -.
DR PDBsum; 6JLO; -.
DR PDBsum; 6JLP; -.
DR PDBsum; 7CJI; -.
DR PDBsum; 7CJJ; -.
DR PDBsum; 7COU; -.
DR PDBsum; 7D1T; -.
DR PDBsum; 7D1U; -.
DR PDBsum; 7EDA; -.
DR AlphaFoldDB; P0A387; -.
DR SMR; P0A387; -.
DR DIP; DIP-48861N; -.
DR IntAct; P0A387; 20.
DR EvolutionaryTrace; P0A387; -.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0018063; P:cytochrome c-heme linkage; IEA:UniProtKB-UniRule.
DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR Gene3D; 1.10.760.10; -; 1.
DR HAMAP; MF_01378; PSII_Cyt550; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR029490; Cytochrom_C550.
DR InterPro; IPR016003; PSII_cyt_c550.
DR InterPro; IPR017851; PSII_PsbV_cyt_c550.
DR Pfam; PF14495; Cytochrom_C550; 1.
DR PIRSF; PIRSF005890; Phot_II_cyt_c550; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR TIGRFAMs; TIGR03045; PS_II_C550; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Photosynthesis; Photosystem II; Signal; Thylakoid;
KW Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01378,
FT ECO:0000269|PubMed:12461137, ECO:0000269|PubMed:1314738"
FT CHAIN 27..163
FT /note="Cytochrome c-550"
FT /id="PRO_0000006519"
FT BINDING 63
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:21499260,
FT ECO:0000269|PubMed:23426624"
FT BINDING 66
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:21499260,
FT ECO:0000269|PubMed:23426624"
FT BINDING 67
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21499260,
FT ECO:0000269|PubMed:23426624, ECO:0000303|PubMed:12518057,
FT ECO:0000303|PubMed:19433803"
FT BINDING 118
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21499260,
FT ECO:0000269|PubMed:23426624, ECO:0000303|PubMed:12518057,
FT ECO:0000303|PubMed:19433803"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:7EDA"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 122..126
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 135..152
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:5B66"
SQ SEQUENCE 163 AA; 18027 MW; DA634C5C4084F676 CRC64;
MLKKCVWLAV ALCLCLWQFT MGTALAAELT PEVLTVPLNS EGKTITLTEK QYLEGKRLFQ
YACASCHVGG ITKTNPSLDL RTETLALATP PRDNIEGLVD YMKNPTTYDG EQEIAEVHPS
LRSADIFPKM RNLTEKDLVA IAGHILVEPK ILGDKWGGGK VYY
