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Database: UniProt
Entry: L8LTR2_9CHRO
LinkDB: L8LTR2_9CHRO
Original site: L8LTR2_9CHRO 
ID   L8LTR2_9CHRO            Unreviewed;       163 AA.
AC   L8LTR2;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
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   ORFNames=GLO73106DRAFT_00024180 {ECO:0000313|EMBL:ELR98584.1};
OS   Gloeocapsa sp. PCC 73106.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Chroococcaceae; Gloeocapsa.
OX   NCBI_TaxID=102232 {ECO:0000313|EMBL:ELR98584.1, ECO:0000313|Proteomes:UP000011180};
RN   [1] {ECO:0000313|EMBL:ELR98584.1, ECO:0000313|Proteomes:UP000011180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 73106 {ECO:0000313|EMBL:ELR98584.1,
RC   ECO:0000313|Proteomes:UP000011180};
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       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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELR98584.1}.
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DR   EMBL; ALVY01000177; ELR98584.1; -; Genomic_DNA.
DR   RefSeq; WP_006528597.1; NZ_ALVY01000177.1.
DR   AlphaFoldDB; L8LTR2; -.
DR   STRING; 102232.GLO73106DRAFT_00024180; -.
DR   eggNOG; COG2010; Bacteria.
DR   OrthoDB; 486949at2; -.
DR   Proteomes; UP000011180; 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:UP000011180};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_01378};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01378}.
FT   DOMAIN          50..149
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         63
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                   /note="covalent"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT   BINDING         67
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         118
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   163 AA;  18327 MW;  78F4993251ABE3DA CRC64;
     MLKRLIWVII AVAFFTVHLP LNQAMAVELN EDVRTVKLNP QGQEMVISLQ EAELGKRIFN
     DTCSQCHLGG RTKTNPNVGL RLEALEGAEP PRDNVVALVD YFKYPMTYDG EEEITLLHPN
     TERSDIFAEM RNLTDADLKA LAGYILIQPK VRGVEWGGGK VYN
//
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