ID K9Z6S3_CYAAP Unreviewed; 162 AA.
AC K9Z6S3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 05-FEB-2025, entry version 56.
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};
DE Flags: Precursor;
GN Name=psbV {ECO:0000256|HAMAP-Rule:MF_01378};
GN OrderedLocusNames=Cyan10605_2004 {ECO:0000313|EMBL:AFZ54098.1};
OS Cyanobacterium aponinum (strain PCC 10605).
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Cyanobacterium.
OX NCBI_TaxID=755178 {ECO:0000313|EMBL:AFZ54098.1, ECO:0000313|Proteomes:UP000010480};
RN [1] {ECO:0000313|Proteomes:UP000010480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 10605 {ECO:0000313|Proteomes:UP000010480};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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 Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Note=Associated with photosystem II at
CC the lumenal side of the thylakoid membrane. {ECO:0000256|HAMAP-
CC 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; CP003947; AFZ54098.1; -; Genomic_DNA.
DR AlphaFoldDB; K9Z6S3; -.
DR SMR; K9Z6S3; -.
DR STRING; 755178.Cyan10605_2004; -.
DR KEGG; can:Cyan10605_2004; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_104149_1_0_3; -.
DR Proteomes; UP000010480; 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 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|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW 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:UP000010480};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_01378};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01378}.
FT DOMAIN 49..148
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 62
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT BINDING 65
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
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:0000256|HAMAP-Rule:MF_01378"
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:0000256|HAMAP-Rule:MF_01378"
SQ SEQUENCE 162 AA; 17955 MW; 41561B358D46BFF4 CRC64;
MKKFVLIFIV GVIFAWQSFV GSANALSLSE EIRTIPLNES GETITLSNQE ALKGSRLFVS
NCAQCHIQGK TKTNPNVSLS KEALANALPA RDNLVGLMDY IEHPTSYDGE EDLTLLHVNT
ERPDLWPEIR NYSEDDIKAV AGHILIQAFS DPKWGNLSLI DN
//
