CY550_SYNP2
ID CY550_SYNP2 Reviewed; 170 AA.
AC Q55210; B1XLG7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: 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}; Synonyms=cytCLP;
GN OrderedLocusNames=SYNPCC7002_A0112;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-58, SUBCELLULAR
RP LOCATION, AND ASSOCIATION OF THE PROTEIN WITH THYLAKOID MEMBRANES.
RX PubMed=7972498; DOI=10.1104/pp.105.4.1313;
RA Nishiyama Y., Hayashi H., Watanabe T., Murata N.;
RT "Photosynthetic oxygen evolution is stabilized by cytochrome c550 against
RT heat inactivation in Synechococcus sp. PCC 7002.";
RL Plant Physiol. 105:1313-1319(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Low-potential cytochrome c that plays a role in the oxygen-
CC evolving complex of photosystem II. {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: The cyanobacterial oxygen-evolving complex is composed of
CC PsbO, PsbP, PsbQ, PsbV and PsbU. {ECO:0000255|HAMAP-Rule:MF_01378}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01378, ECO:0000269|PubMed:7972498}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:7972498}; Lumenal
CC side {ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:7972498}.
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}.
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DR EMBL; D29788; BAA06173.1; -; Genomic_DNA.
DR EMBL; CP000951; ACA98127.1; -; Genomic_DNA.
DR RefSeq; WP_012305751.1; NC_010475.1.
DR AlphaFoldDB; Q55210; -.
DR SMR; Q55210; -.
DR STRING; 32049.SYNPCC7002_A0112; -.
DR EnsemblBacteria; ACA98127; ACA98127; SYNPCC7002_A0112.
DR KEGG; syp:SYNPCC7002_A0112; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_104149_1_0_3; -.
DR OMA; GTCHAGG; -.
DR Proteomes; UP000001688; 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: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 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Photosynthesis; Photosystem II; Reference proteome; Signal;
KW Thylakoid; Transport.
FT SIGNAL 1..34
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01378,
FT ECO:0000269|PubMed:7972498"
FT CHAIN 35..170
FT /note="Cytochrome c-550"
FT /id="PRO_0000006520"
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"
FT CONFLICT 117
FT /note="G -> V (in Ref. 1; BAA06173)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 170 AA; 18777 MW; B60E4C9A892EA87D CRC64;
MNKILGIDPL KKFIFGISAF VLLFWQLNVG AANATALREV DRTVNLNETE TVVLSDQQVA
KGERIFINTC STCHNSGRTK SNPNVTLSLV DLEGAEPRRD NILAMVDYLK NPTSYDGELD
LSQLHPNTVR ADIWSSMRNL NEEDLQNVSG YVLVQAQVRG VAWGGGKTVN
