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CY550_TRIEI
ID   CY550_TRIEI             Reviewed;         161 AA.
AC   Q111E9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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}; OrderedLocusNames=Tery_2686;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Low-potential cytochrome c that plays a role in the oxygen-
CC       evolving complex of photosystem II. {ECO:0000255|HAMAP-Rule:MF_01378}.
CC   -!- COFACTOR:
CC       Name=heme c; Xref=ChEBI:CHEBI:61717;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01378};
CC       Note=Binds 1 heme c group covalently per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01378};
CC   -!- SUBUNIT: The cyanobacterial oxygen-evolving complex is composed of
CC       PsbO, PsbP, PsbQ, PsbV and PsbU. {ECO:0000255|HAMAP-Rule:MF_01378}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01378}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01378}; Lumenal side {ECO:0000255|HAMAP-Rule:MF_01378}.
CC       Note=Associated with photosystem II at the lumenal side of the
CC       thylakoid membrane. {ECO:0000255|HAMAP-Rule:MF_01378}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. PsbV subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01378}.
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DR   EMBL; CP000393; ABG51875.1; -; Genomic_DNA.
DR   RefSeq; WP_011612237.1; NC_008312.1.
DR   AlphaFoldDB; Q111E9; -.
DR   SMR; Q111E9; -.
DR   STRING; 203124.Tery_2686; -.
DR   EnsemblBacteria; ABG51875; ABG51875; Tery_2686.
DR   KEGG; ter:Tery_2686; -.
DR   eggNOG; COG2010; Bacteria.
DR   HOGENOM; CLU_104149_1_0_3; -.
DR   OMA; GTCHAGG; -.
DR   OrthoDB; 1553768at2; -.
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   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding; Photosynthesis;
KW   Photosystem II; Signal; Thylakoid; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01378"
FT   CHAIN           26..161
FT                   /note="Cytochrome c-550"
FT                   /id="PRO_5000126970"
FT   BINDING         61
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01378"
FT   BINDING         64
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01378"
FT   BINDING         65
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:0000255|HAMAP-Rule:MF_01378"
FT   BINDING         116
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:0000255|HAMAP-Rule:MF_01378"
SQ   SEQUENCE   161 AA;  18118 MW;  B1F4B3D62BB234F3 CRC64;
     MKKFFISVVF IVLLTFTTFI NSATAAKLDD NVRTLPLNED KEVVLTIKEY TQGKREFTNV
     CSQCHVGGIT KTNPDVSLDP ETLALAYPAR DNIEGLIDYM QNPTTYDGFI EISEFHPSIK
     SADIYPEMRN LTEDDLYAIA GYILVQPKVL GKQWGGGKIF R
 
 
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