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Database: UniProt
Entry: CY550_SYNY3
LinkDB: CY550_SYNY3
Original site: 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   02-DEC-2020, entry version 156.
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; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000269|PubMed:11315568, ECO:0000269|PubMed:12069591};
CC       Note=Binds 1 heme 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   PDBsum; 1E29; -.
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; DYMKDPT; -.
DR   BioCyc; MetaCyc:PSBV-MONOMER; -.
DR   EvolutionaryTrace; Q55013; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0030096; C:plasma membrane-derived thylakoid photosystem II; IDA:UniProtKB.
DR   GO; GO:0042651; C: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;
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   METAL           66
FT                   /note="Iron (heme axial ligand); via tele nitrogen"
FT                   /evidence="ECO:0000269|PubMed:11315568"
FT   METAL           117
FT                   /note="Iron (heme axial ligand); via tele nitrogen"
FT                   /evidence="ECO:0000269|PubMed:11315568"
FT   BINDING         62
FT                   /note="Heme (covalent)"
FT                   /evidence="ECO:0000269|PubMed:11315568"
FT   BINDING         65
FT                   /note="Heme (covalent)"
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:0000244|PDB:1E29"
FT   STRAND          34..41
FT                   /evidence="ECO:0000244|PDB:1E29"
FT   STRAND          43..45
FT                   /evidence="ECO:0000244|PDB:1E29"
FT   HELIX           48..61
FT                   /evidence="ECO:0000244|PDB:1E29"
FT   HELIX           63..66
FT                   /evidence="ECO:0000244|PDB:1E29"
FT   HELIX           67..69
FT                   /evidence="ECO:0000244|PDB:1E29"
FT   STRAND          71..76
FT                   /evidence="ECO:0000244|PDB:1E29"
FT   STRAND          78..80
FT                   /evidence="ECO:0000244|PDB:1E29"
FT   HELIX           81..85
FT                   /evidence="ECO:0000244|PDB:1E29"
FT   STRAND          87..89
FT                   /evidence="ECO:0000244|PDB:1E29"
FT   HELIX           94..102
FT                   /evidence="ECO:0000244|PDB:1E29"
FT   TURN            114..116
FT                   /evidence="ECO:0000244|PDB:1E29"
FT   TURN            123..125
FT                   /evidence="ECO:0000244|PDB:1E29"
FT   HELIX           127..129
FT                   /evidence="ECO:0000244|PDB:1E29"
FT   HELIX           134..150
FT                   /evidence="ECO:0000244|PDB:1E29"
SQ   SEQUENCE   160 AA;  17884 MW;  3DA6F835DB79F665 CRC64;
     MKRFFLVAIA SVLFFFNTMV GSANAVELTE STRTIPLDEA GGTTTLTARQ FTNGQKIFVD
     TCTQCHLQGK TKTNNNVSLG LADLAGAEPR RDNVLALVEF LKNPKSYDGE DDYSELHPNI
     SRPDIYPEMR NYTEDDIFDV AGYTLIAPKL DERWGGTIYF
//
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