ID CY550_SYNSC Reviewed; 170 AA.
AC Q3AHP7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 97.
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};
GN OrderedLocusNames=Syncc9605_2146;
OS Synechococcus sp. (strain CC9605).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=110662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9605;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9605.";
RL Submitted (JUL-2005) 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: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, PsbZ, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ),
CC PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
CC {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB35885.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000110; ABB35885.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041435140.1; NC_007516.1.
DR AlphaFoldDB; Q3AHP7; -.
DR SMR; Q3AHP7; -.
DR STRING; 110662.Syncc9605_2146; -.
DR KEGG; syd:Syncc9605_2146; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_104149_1_0_3; -.
DR OrthoDB; 486949at2; -.
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; 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_5000102440"
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; 18280 MW; 0F6949BC6AAD5990 CRC64;
MASVFSSLRR SLKGLLVLIP VLIGLAVTSP AQAAQWDAET LTVPADPSGT EVTFSDREID
SGRKVFNTSC GTCHAGGITK TNHNVGLDPE TLALATPARD NVEALVDYMK DPTSYDGEYS
IADLHPSMRD AELYPAMRDL DDEDLRLMAG YILVSPKVQG SAWGGGKIYF
//