CY550_LIMMA
ID CY550_LIMMA Reviewed; 129 AA.
AC P82603;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cytochrome c-550 {ECO:0000255|HAMAP-Rule:MF_01378};
DE AltName: Full=Cytochrome c-549 {ECO:0000303|PubMed:11478889};
DE AltName: Full=Cytochrome c549;
DE AltName: Full=Cytochrome c550 {ECO:0000255|HAMAP-Rule:MF_01378};
DE AltName: Full=Low-potential cytochrome c {ECO:0000255|HAMAP-Rule:MF_01378};
GN Name=psbV {ECO:0000255|HAMAP-Rule:MF_01378};
OS Limnospira maxima (Arthrospira maxima).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Sirenicapillariaceae; Limnospira.
OX NCBI_TaxID=129910;
RN [1]
RP PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH
RP HEME, COFACTOR, AND SUBUNIT.
RX PubMed=11478889; DOI=10.1021/bi002679p;
RA Sawaya M.R., Krogmann D.W., Serag A., Ho K.K., Yeates T.O., Kerfeld C.A.;
RT "Structures of cytochrome c-549 and cytochrome c6 from the cyanobacterium
RT Arthrospira maxima.";
RL Biochemistry 40:9215-9225(2001).
CC -!- FUNCTION: Low-potential cytochrome c that plays a role in the oxygen-
CC evolving complex of photosystem II. {ECO:0000305}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:11478889};
CC Note=Binds 1 heme c group covalently per subunit (PubMed:11478889).;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -260 mV.;
CC -!- SUBUNIT: The cyanobacterial oxygen-evolving complex is composed of
CC PsbO, PsbP, PsbQ, PsbV and PsbU (Potential). Homodimer in crystal
CC structure (PubMed:11478889). {ECO:0000255|HAMAP-Rule:MF_01378,
CC ECO:0000269|PubMed:11478889}.
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}.
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DR PDB; 1F1C; X-ray; 2.30 A; A/B=1-129.
DR PDBsum; 1F1C; -.
DR AlphaFoldDB; P82603; -.
DR SMR; P82603; -.
DR EvolutionaryTrace; P82603; -.
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 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Photosynthesis; Photosystem II; Thylakoid;
KW Transport.
FT CHAIN 1..129
FT /note="Cytochrome c-550"
FT /id="PRO_0000108381"
FT BINDING 35
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:11478889"
FT BINDING 38
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:11478889"
FT BINDING 39
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:0000269|PubMed:11478889"
FT BINDING 90
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:0000269|PubMed:11478889"
FT TURN 3..6
FT /evidence="ECO:0007829|PDB:1F1C"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:1F1C"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1F1C"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:1F1C"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:1F1C"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1F1C"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1F1C"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:1F1C"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1F1C"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:1F1C"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1F1C"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1F1C"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1F1C"
FT HELIX 107..124
FT /evidence="ECO:0007829|PDB:1F1C"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:1F1C"
SQ SEQUENCE 129 AA; 14198 MW; 84DEA1D5796AE876 CRC64;
LTEELRTFPI NAQGDTAVLS LKEIKKGQQV FNAACAQCHA LGVTRTNPDV NLSPEALALA
TPPRDNIAAL VDYIKNPTTY DGFVEISELH PSLKSSDIFP KMRNISEDDL YNVAGYILLQ
PKVRGEQWG
