ID CY550_PROMM Reviewed; 170 AA.
AC Q7V5W0;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 05-FEB-2025, entry version 113.
DE RecName: Full=Photosystem II extrinsic protein V {ECO:0000255|HAMAP-Rule:MF_01378};
DE Short=PsbV {ECO:0000255|HAMAP-Rule:MF_01378};
DE AltName: 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=PMT_1427;
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=74547;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
CC -!- FUNCTION: One of the extrinsic, lumenal subunits of photosystem II
CC (PSII). PSII is a light-driven water plastoquinone oxidoreductase,
CC using light energy to abstract electrons from H(2)O, generating a
CC proton gradient subsequently used for ATP formation. The extrinsic
CC proteins stabilize the structure of photosystem II oxygen-evolving
CC complex (OEC), the ion environment of oxygen evolution and protect the
CC OEC against heat-induced inactivation. Low-potential cytochrome c that
CC plays a role in the OEC of PSII. {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: PSII is composed of 1 copy each of membrane proteins PsbA,
CC PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT,
CC PsbX, PsbY, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ), PsbU,
CC PsbV and a large number of cofactors. It forms dimeric complexes.
CC {ECO:0000305}.
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; BX548175; CAE21602.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7V5W0; -.
DR SMR; Q7V5W0; -.
DR KEGG; pmt:PMT_1427; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_104149_1_0_3; -.
DR OrthoDB; 486949at2; -.
DR Proteomes; UP000001423; Chromosome.
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: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; Cytochrome c-like domain; 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; IPR017851; PsbV_cyt_c550.
DR InterPro; IPR016003; PsbV_cyt_c550-like.
DR NCBIfam; TIGR03045; PS_II_C550; 1.
DR Pfam; PF14495; Cytochrom_C550; 1.
DR PIRSF; PIRSF005890; Phot_II_cyt_c550; 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Photosynthesis;
KW Photosystem II; Reference proteome; Signal; Thylakoid; Transport.
FT SIGNAL 1..33
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01378"
FT CHAIN 34..170
FT /note="Photosystem II extrinsic protein V"
FT /id="PRO_5000096803"
FT BINDING 70
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01378"
FT BINDING 73
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01378"
FT BINDING 74
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 125
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 170 AA; 18174 MW; 0F1C1260905C6E0C CRC64;
MASLFASLGR SLIKLLIVLP VIIGLSISSP AMAAQWDAET LTVPAGSGGQ QVTFTESEIK
SASKLFKSNC ATCHNQGVTK TNQNVGLDLE ALSLASPARD NVDGLVEFLK NPMSYDGEYS
IADTHPGISS SDVYVQMRTL NDEDLRLIAG YILTAEKVQG DQWGGGKIYF
//
