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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   12-AUG-2020, entry version 37.
DE   RecName: 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; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Chroococcaceae; Gloeocapsa; unclassified 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: Low-potential cytochrome c that plays a role in the oxygen-
CC       evolving complex of photosystem II. {ECO:0000256|HAMAP-Rule:MF_01378}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01378};
CC       Note=Binds 1 heme group covalently per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01378};
CC   -!- SUBUNIT: The cyanobacterial oxygen-evolving complex is composed of
CC       PsbO, PsbP, PsbQ, PsbV and PsbU. {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   STRING; 102232.GLO73106DRAFT_00024180; -.
DR   EnsemblBacteria; ELR98584; ELR98584; GLO73106DRAFT_00024180.
DR   eggNOG; COG2010; Bacteria.
DR   OrthoDB; 1553768at2; -.
DR   BioCyc; GSP102232:G1HEF-1710-MONOMER; -.
DR   Proteomes; UP000011180; Unassembled WGS sequence.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0042651; C: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:0018063; P:cytochrome c-heme linkage; IEA:UniProtKB-UniRule.
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; -; 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; IPR016003; PSII_cyt_c550.
DR   InterPro; IPR017851; PSII_PsbV_cyt_c550.
DR   Pfam; PF14495; Cytochrom_C550; 1.
DR   PIRSF; PIRSF005890; Phot_II_cyt_c550; 1.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   TIGRFAMs; TIGR03045; PS_II_C550; 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   ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01378,
KW   ECO:0000256|PROSITE-ProRule:PRU00433};
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, ECO:0000256|PROSITE-ProRule:PRU00433};
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   METAL           67
FT                   /note="Iron (heme axial ligand)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT   METAL           118
FT                   /note="Iron (heme axial ligand)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT   BINDING         63
FT                   /note="Heme (covalent)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01378"
FT   BINDING         66
FT                   /note="Heme (covalent)"
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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