CY550_SYNY3
ID CY550_SYNY3 Reviewed; 160 AA.
AC Q55013; Q55333;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Cytochrome c-550 {ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000303|PubMed:7896839};
DE AltName: Full=Cytochrome c549;
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}; Synonyms=petK;
GN OrderedLocusNames=sll0258;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-73, PROBABLE
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=7896839; DOI=10.1074/jbc.270.12.6901;
RA Shen J.-R., Vermaas W., Inoue Y.;
RT "The role of cytochrome c-550 as studied through reverse genetics and
RT mutant characterization in Synechocystis sp. PCC 6803.";
RL J. Biol. Chem. 270:6901-6907(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-160, AND PROTEIN SEQUENCE OF 26-49.
RX PubMed=8181563; DOI=10.1016/0014-5793(94)00341-6;
RA Kang C., Chitnis P.R., Smith S., Krogmann D.W.;
RT "Cloning and sequence analysis of the gene encoding the low potential
RT cytochrome c of Synechocystis PCC 6803.";
RL FEBS Lett. 344:5-9(1994).
RN [4]
RP PROTEIN SEQUENCE OF 26-40.
RX PubMed=9298645; DOI=10.1002/elps.1150180806;
RA Sazuka T., Ohara O.;
RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT PCC6803: linking 130 protein spots with their respective genes.";
RL Electrophoresis 18:1252-1258(1997).
RN [5]
RP PROTEIN SEQUENCE OF 26-39, IDENTIFICATION BY MASS SPECTROMETRY, COFACTOR,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=12069591; DOI=10.1021/bi026012+;
RA Kashino Y., Lauber W.M., Carroll J.A., Wang Q., Whitmarsh J., Satoh K.,
RA Pakrasi H.B.;
RT "Proteomic analysis of a highly active photosystem II preparation from the
RT cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel
RT polypeptides.";
RL Biochemistry 41:8004-8012(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.21 ANGSTROMS) OF 26-160 IN COMPLEX WITH HEME, AND
RP COFACTOR.
RX PubMed=11315568; DOI=10.1007/s007750100208;
RA Frazao C., Enguita F.J., Coelho R., Sheldrick G.M., Navarro J.A.,
RA Hervas M., De la Rosa M.A., Carrondo M.A.;
RT "Crystal structure of low-potential cytochrome c549 from Synechocystis sp.
RT PCC 6803 at 1.21 A resolution.";
RL J. Biol. Inorg. Chem. 6:324-332(2001).
CC -!- FUNCTION: Low-potential cytochrome c that plays a role in the oxygen-
CC evolving complex of photosystem II (PSII). Required for normal function
CC or stabilization of PSII. Extrinsic protein associated with PSII that
CC enhances oxygen evolution. {ECO:0000305}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:11315568, ECO:0000269|PubMed:12069591};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000269|PubMed:11315568, ECO:0000269|PubMed:12069591};
CC -!- SUBUNIT: The cyanobacterial oxygen-evolving complex is composed of
CC PsbO, PsbP, PsbQ, PsbV and PsbU. {ECO:0000255|HAMAP-Rule:MF_01378,
CC ECO:0000269|PubMed:12069591}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000269|PubMed:12069591, ECO:0000305}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12069591, ECO:0000305}; Lumenal side
CC {ECO:0000305|PubMed:7896839}. Note=Associated with photosystem II at
CC the lumenal side of the thylakoid membrane.
CC {ECO:0000305|PubMed:7896839}.
CC -!- DISRUPTION PHENOTYPE: Cells show decreased but not abolished level of
CC PSII and photoautotrophic growth. {ECO:0000269|PubMed:7896839}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. PsbV subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01378}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA19982.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D45178; BAA08124.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA18512.1; -; Genomic_DNA.
DR EMBL; U07021; AAA19982.2; ALT_INIT; Genomic_DNA.
DR PIR; A56189; A56189.
DR PDB; 1E29; X-ray; 1.21 A; A=26-160.
DR PDB; 7N8O; EM; 1.93 A; V/v=1-160.
DR PDB; 7RCV; EM; 2.01 A; V/v=1-160.
DR PDBsum; 1E29; -.
DR PDBsum; 7N8O; -.
DR PDBsum; 7RCV; -.
DR AlphaFoldDB; Q55013; -.
DR SMR; Q55013; -.
DR IntAct; Q55013; 1.
DR STRING; 1148.1653599; -.
DR DrugBank; DB03317; Ferroheme C.
DR PaxDb; Q55013; -.
DR EnsemblBacteria; BAA18512; BAA18512; BAA18512.
DR KEGG; syn:sll0258; -.
DR eggNOG; COG2010; Bacteria.
DR InParanoid; Q55013; -.
DR OMA; GTCHAGG; -.
DR BioCyc; MetaCyc:PSBV-MON; -.
DR EvolutionaryTrace; Q55013; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030096; C:plasma membrane-derived thylakoid photosystem II; IDA:UniProtKB.
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;
KW Reference proteome; Signal; Thylakoid; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01378,
FT ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:7896839,
FT ECO:0000269|PubMed:8181563, ECO:0000269|PubMed:9298645"
FT CHAIN 26..160
FT /note="Cytochrome c-550"
FT /id="PRO_0000006521"
FT BINDING 62
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:11315568"
FT BINDING 65
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:11315568"
FT BINDING 66
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:11315568"
FT BINDING 117
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:11315568"
FT CONFLICT 60
FT /note="D -> T (in Ref. 3; AAA19982)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 90..91
FT /note="RR -> PS (in Ref. 3; AAA19982)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="V -> R (in Ref. 3; AAA19982)"
FT /evidence="ECO:0000305"
FT CONFLICT 138..139
FT /note="FD -> YN (in Ref. 3; AAA19982)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="G -> A (in Ref. 3; AAA19982)"
FT /evidence="ECO:0000305"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:1E29"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:1E29"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1E29"
FT HELIX 48..61
FT /evidence="ECO:0007829|PDB:1E29"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:1E29"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1E29"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1E29"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1E29"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:1E29"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1E29"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:1E29"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:1E29"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1E29"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:1E29"
FT HELIX 134..150
FT /evidence="ECO:0007829|PDB:1E29"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:7N8O"
SQ SEQUENCE 160 AA; 17884 MW; 3DA6F835DB79F665 CRC64;
MKRFFLVAIA SVLFFFNTMV GSANAVELTE STRTIPLDEA GGTTTLTARQ FTNGQKIFVD
TCTQCHLQGK TKTNNNVSLG LADLAGAEPR RDNVLALVEF LKNPKSYDGE DDYSELHPNI
SRPDIYPEMR NYTEDDIFDV AGYTLIAPKL DERWGGTIYF
