UCRIB_SYNY3
ID UCRIB_SYNY3 Reviewed; 180 AA.
AC P26290;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Cytochrome b6-f complex iron-sulfur subunit 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01335};
DE Short=ISP 2 {ECO:0000255|HAMAP-Rule:MF_01335};
DE Short=RISP 2 {ECO:0000255|HAMAP-Rule:MF_01335};
DE AltName: Full=Rieske iron-sulfur protein 2 {ECO:0000255|HAMAP-Rule:MF_01335};
GN Name=petC2 {ECO:0000255|HAMAP-Rule:MF_01335}; OrderedLocusNames=sll1316;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1907512; DOI=10.1007/bf00039508;
RA Mayes S.R., Barber J.;
RT "Primary structure of the psbN-psbH-petC-petA gene cluster of the
RT cyanobacterium Synechocystis PCC 6803.";
RL Plant Mol. Biol. 17:289-293(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP PROTEIN SEQUENCE OF 2-17.
RX PubMed=9298645; DOI=10.1002/elps.1150180806;
RA Sazuka T., Ohara O.;
RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT PCC6803: linking 130 protein spots with their respective genes.";
RL Electrophoresis 18:1252-1258(1997).
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 -!- SEQUENCE CAUTION:
CC Sequence=BAA17628.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA41421.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; X58532; CAA41422.1; -; Genomic_DNA.
DR EMBL; X58532; CAA41421.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000022; BAA17628.1; ALT_INIT; Genomic_DNA.
DR PIR; S16572; S16572.
DR AlphaFoldDB; P26290; -.
DR SMR; P26290; -.
DR STRING; 1148.1652708; -.
DR TCDB; 3.D.3.5.1; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR PaxDb; P26290; -.
DR EnsemblBacteria; BAA17628; BAA17628; BAA17628.
DR KEGG; syn:sll1316; -.
DR eggNOG; COG0723; Bacteria.
DR InParanoid; P26290; -.
DR OMA; KGDPTYI; -.
DR PhylomeDB; P26290; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0016491; F:oxidoreductase activity; IBA:GO_Central.
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; IPR000595; cNMP-bd_dom.
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 1: Evidence at protein level;
KW 2Fe-2S; Direct protein sequencing; Disulfide bond; Electron transport;
KW Iron; Iron-sulfur; Membrane; Metal-binding; Reference proteome; Thylakoid;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298645"
FT CHAIN 2..180
FT /note="Cytochrome b6-f complex iron-sulfur subunit 2"
FT /id="PRO_0000127785"
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT DOMAIN 66..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 180 AA; 18996 MW; 351CB0C7DF892B5C CRC64;
MTQISGSPDV PDLGRRQFMN LLTFGTITGV AAGALYPAVK YLIPPSSGGS GGGVTAKDAL
GNDVKVTEFL ASHNAGDRVL AQGLKGDPTY IVVQGDDTIA NYGINAVCTH LGCVVPWNAS
ENKFMCPCHG SQYNAEGKVV RGPAPLSLAL AHATVTDDDK LVLSTWTETD FRTDEDPWWA
