ID B4VPE5_9CYAN Unreviewed; 177 AA.
AC B4VPE5;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Photosystem II extrinsic protein V {ECO:0000256|HAMAP-Rule:MF_01378};
DE Short=PsbV {ECO:0000256|HAMAP-Rule:MF_01378};
DE AltName: Full=Cytochrome c-550 {ECO:0000256|HAMAP-Rule:MF_01378};
DE AltName: Full=Cytochrome c550 {ECO:0000256|HAMAP-Rule:MF_01378};
DE AltName: Full=Low-potential cytochrome c {ECO:0000256|HAMAP-Rule:MF_01378};
GN Name=psbV {ECO:0000256|HAMAP-Rule:MF_01378};
GN ORFNames=MC7420_5475 {ECO:0000313|EMBL:EDX76041.1};
OS Coleofasciculus chthonoplastes PCC 7420.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Coleofasciculus.
OX NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX76041.1, ECO:0000313|Proteomes:UP000003835};
RN [1] {ECO:0000313|EMBL:EDX76041.1, ECO:0000313|Proteomes:UP000003835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX76041.1,
RC ECO:0000313|Proteomes:UP000003835};
RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01378}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01378};
CC Note=Binds 1 heme c group covalently per subunit. {ECO:0000256|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, PsbZ, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ),
CC PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
CC {ECO:0000256|HAMAP-Rule:MF_01378}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_01378}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01378}; Lumenal side {ECO:0000256|HAMAP-Rule:MF_01378}.
CC Note=Associated with photosystem II at the lumenal side of the
CC thylakoid membrane. {ECO:0000256|HAMAP-Rule:MF_01378}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. PsbV subfamily.
CC {ECO:0000256|ARBA:ARBA00010433, ECO:0000256|HAMAP-Rule:MF_01378}.
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DR EMBL; DS989847; EDX76041.1; -; Genomic_DNA.
DR AlphaFoldDB; B4VPE5; -.
DR STRING; 118168.MC7420_5475; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_104149_1_0_3; -.
DR Proteomes; UP000003835; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_01378};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_01378};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01378};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01378};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01378};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW Rule:MF_01378};
KW Photosystem II {ECO:0000256|ARBA:ARBA00023276, ECO:0000256|HAMAP-
KW Rule:MF_01378}; Reference proteome {ECO:0000313|Proteomes:UP000003835};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_01378};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01378}.
FT DOMAIN 64..163
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 77
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT BINDING 80
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT BINDING 81
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:0000256|HAMAP-Rule:MF_01378"
FT BINDING 132
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:0000256|HAMAP-Rule:MF_01378"
SQ SEQUENCE 177 AA; 19913 MW; A7F719CF4236CC66 CRC64;
MHLKRMSQIF QGEPRMKRLI LLAVAMVFFV FQIAVSSATA LELSEDIRTV PVNEQGNTTV
LSLEEVAKGK RLFNDSCSQC HIGGRTKTNP NVTLRLEDLK LAFPPRDNIA ALVDYMKNPT
TYDGFTEIYE FHPSTRSADI FPEMRNLTED DLKAIAGYIL VQPKVQGIMW GGGKVYN
//
