GenomeNet

Database: UniProt
Entry: Q3AHP7
LinkDB: Q3AHP7
Original site: Q3AHP7 
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system