C550B_CYACA
ID C550B_CYACA Reviewed; 155 AA.
AC Q76FB0;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Cytochrome c-550 {ECO:0000255|HAMAP-Rule:MF_01378};
DE AltName: Full=Cytochrome c550 {ECO:0000255|HAMAP-Rule:MF_01378};
DE Flags: Precursor;
GN Name=psbV {ECO:0000255|HAMAP-Rule:MF_01378};
OS Cyanidium caldarium (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX NCBI_TaxID=2771;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, AND RECONSTITUTION EXPERIMENTS.
RC STRAIN=RK-1;
RX PubMed=12941874; DOI=10.1093/pcp/pcg106;
RA Enami I., Iwai M., Akiyama A., Suzuki T., Okumura A., Katoh T., Tada O.,
RA Ohta H., Shen J.-R.;
RT "Comparison of binding and functional properties of two extrinsic
RT components, cyt c550 and a 12 kDa protein, in cyanobacterial PSII with
RT those in red algal PSII.";
RL Plant Cell Physiol. 44:820-827(2003).
RN [2]
RP PROTEIN SEQUENCE OF 21-54, SUBCELLULAR LOCATION, AND ASSOCIATION WITH
RP PHOTOSYSTEM II.
RC STRAIN=Geitler;
RX PubMed=8534673; DOI=10.1016/0005-2728(95)00122-0;
RA Enami I., Murayama H., Ohta H., Kamo M., Nakazato K., Shen J.-R.;
RT "Isolation and characterization of a Photosystem II complex from the red
RT alga Cyanidium caldarium: association of cytochrome c-550 and a 12 kDa
RT protein with the complex.";
RL Biochim. Biophys. Acta 1232:208-216(1995).
CC -!- FUNCTION: Low-potential cytochrome c that plays a role in the oxygen-
CC evolving complex of photosystem II (PSII). Unlike Synechococcus
CC vulcanus it does not bind by itself to PSII, but requires all extrinsic
CC members of the OEC.
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 oxygen-evolving complex in red algae is composed of psbO
CC (OEC33), psbQ', cytochrome c-550 and psbU.
CC {ECO:0000269|PubMed:12941874}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:8534673};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01378,
CC ECO:0000269|PubMed:8534673}; Lumenal side {ECO:0000255|HAMAP-
CC Rule:MF_01378, ECO:0000269|PubMed:8534673}. Note=Associated with
CC photosystem II at the lumenal side of the thylakoid membrane.
CC -!- SIMILARITY: Belongs to the cytochrome c family. PsbV subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01378}.
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; AB105371; BAC84949.1; -; mRNA.
DR PDB; 4YUU; X-ray; 2.77 A; V1/V2/v1/v2=1-155.
DR PDBsum; 4YUU; -.
DR AlphaFoldDB; Q76FB0; -.
DR SMR; Q76FB0; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
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 3D-structure; Chloroplast; Direct protein sequencing; Electron transport;
KW Heme; Iron; Membrane; Metal-binding; Photosynthesis; Photosystem II;
KW Plastid; Signal; Thylakoid; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01378,
FT ECO:0000269|PubMed:8534673"
FT CHAIN 21..155
FT /note="Cytochrome c-550"
FT /id="PRO_0000295612"
FT BINDING 50
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01378"
FT BINDING 53
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01378"
FT BINDING 54
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 105
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 52
FT /note="S -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 155 AA; 17221 MW; 9704B6B2335B1571 CRC64;
MFVKMIGWLV LFLFAHQTWA IEVAKDTNGG ILNIAPEQLK RGKRLFNSHC SSCHVGGITK
TNPNIGLDLE SLSLATPPRN NLDALVDYMK NPTTYDGSES IAQIHPSIAS SDIFPKMRDL
SEDDLYAIAA HILTQPQIQA EKWGGGKIYY TKRSM
