UCRI_SYNE7
ID UCRI_SYNE7 Reviewed; 179 AA.
AC Q31NV7;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cytochrome b6-f complex iron-sulfur subunit {ECO:0000255|HAMAP-Rule:MF_01335};
DE EC=7.1.1.6 {ECO:0000255|HAMAP-Rule:MF_01335};
DE AltName: Full=Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein {ECO:0000255|HAMAP-Rule:MF_01335};
DE Short=ISP {ECO:0000255|HAMAP-Rule:MF_01335};
DE Short=RISP {ECO:0000255|HAMAP-Rule:MF_01335};
DE AltName: Full=Rieske iron-sulfur protein {ECO:0000255|HAMAP-Rule:MF_01335};
GN Name=petC {ECO:0000255|HAMAP-Rule:MF_01335};
GN OrderedLocusNames=Synpcc7942_1232;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the cytochrome b6-f complex, which mediates
CC electron transfer between photosystem II (PSII) and photosystem I
CC (PSI), cyclic electron flow around PSI, and state transitions.
CC {ECO:0000255|HAMAP-Rule:MF_01335}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinol + 2 H(+)(in) + 2 oxidized [plastocyanin] = a
CC plastoquinone + 4 H(+)(out) + 2 reduced [plastocyanin];
CC Xref=Rhea:RHEA:22148, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562,
CC Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17757, ChEBI:CHEBI:29036, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:62192; EC=7.1.1.6; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01335};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01335};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01335};
CC -!- SUBUNIT: The 4 large subunits of the cytochrome b6-f complex are
CC cytochrome b6, subunit IV (17 kDa polypeptide, PetD), cytochrome f and
CC the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and
CC PetN. The complex functions as a dimer. {ECO:0000255|HAMAP-
CC Rule:MF_01335}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01335}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01335}. Note=The transmembrane helix obliquely spans the
CC membrane in one monomer, and its extrinsic C-terminal domain is part of
CC the other monomer. {ECO:0000255|HAMAP-Rule:MF_01335}.
CC -!- MISCELLANEOUS: The Rieske iron-sulfur protein is a high potential 2Fe-
CC 2S protein.
CC -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC {ECO:0000255|HAMAP-Rule:MF_01335}.
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; CP000100; ABB57262.1; -; Genomic_DNA.
DR RefSeq; WP_011242632.1; NC_007604.1.
DR AlphaFoldDB; Q31NV7; -.
DR SMR; Q31NV7; -.
DR STRING; 1140.Synpcc7942_1232; -.
DR TCDB; 3.D.3.5.3; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR PRIDE; Q31NV7; -.
DR EnsemblBacteria; ABB57262; ABB57262; Synpcc7942_1232.
DR KEGG; syf:Synpcc7942_1232; -.
DR eggNOG; COG0723; Bacteria.
DR HOGENOM; CLU_055690_8_0_3; -.
DR OMA; KGDPTYI; -.
DR OrthoDB; 1632945at2; -.
DR BioCyc; MetaCyc:SYNPCC7942_1232-MON; -.
DR BioCyc; SYNEL:SYNPCC7942_1232-MON; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0045158; F:electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009496; F:plastoquinol--plastocyanin reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR Gene3D; 2.102.10.10; -; 1.
DR HAMAP; MF_01335; Cytb6_f_Rieske; 1.
DR InterPro; IPR023960; Cyt_b6_f_Rieske.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR014349; Rieske_Fe-S_prot.
DR InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR PANTHER; PTHR10134; PTHR10134; 1.
DR Pfam; PF00355; Rieske; 1.
DR PRINTS; PR00162; RIESKE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Disulfide bond; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Thylakoid; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..179
FT /note="Cytochrome b6-f complex iron-sulfur subunit"
FT /id="PRO_0000298467"
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT DOMAIN 61..162
FT /note="Rieske"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT BINDING 108
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT BINDING 110
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT BINDING 126
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT BINDING 129
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT DISULFID 113..128
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
SQ SEQUENCE 179 AA; 18834 MW; EC139A4D25CAA047 CRC64;
MTQVSGASDV PSMGRRQFMN LLTFGSVTGV ALGALYPVVN YFIPPSSGGS GGGVAAKDAL
GNDVVLSKFL ADHNVGDRTL VQGLKGDPTY LVVESSEAIG DYGINAVCTH LGCVVPWNAS
ENKFKCPCHG SQYDATGKVV RGPAPLSLAL AHVSVTDDKV FLSPWTETDF RTGDNPWWA
