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UCRI_PARMW
ID   UCRI_PARMW              Reviewed;         178 AA.
AC   Q7U566;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 126.
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}; OrderedLocusNames=SYNW1841;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
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}.
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DR   EMBL; BX569694; CAE08356.1; -; Genomic_DNA.
DR   RefSeq; WP_011128699.1; NC_005070.1.
DR   AlphaFoldDB; Q7U566; -.
DR   SMR; Q7U566; -.
DR   STRING; 84588.SYNW1841; -.
DR   EnsemblBacteria; CAE08356; CAE08356; SYNW1841.
DR   KEGG; syw:SYNW1841; -.
DR   eggNOG; COG0723; Bacteria.
DR   HOGENOM; CLU_055690_8_0_3; -.
DR   OMA; KGDPTYI; -.
DR   OrthoDB; 1632945at2; -.
DR   BioCyc; MetaCyc:TX72_RS09270-MON; -.
DR   Proteomes; UP000001422; Chromosome.
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   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR10134; PTHR10134; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   PRINTS; PR00162; RIESKE.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
DR   PROSITE; PS51318; TAT; 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..178
FT                   /note="Cytochrome b6-f complex iron-sulfur subunit"
FT                   /id="PRO_0000127783"
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT   DOMAIN          65..161
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT   BINDING         107
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT   BINDING         109
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT   BINDING         125
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT   BINDING         128
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
FT   DISULFID        112..127
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01335"
SQ   SEQUENCE   178 AA;  18735 MW;  DE3A1443271528A4 CRC64;
     MTQLSSSDVP GMGRRQFMNL LTFGSVTGVA LGALYPVVNY FIPPRAAGAG GGTTAKDELG
     NAITATGWLS SHPEGDRSLV QGLKGDPTYL IVEGPDAIGS YGINAICTHL GCVVPWNSGA
     NKFMCPCHGS QYDATGKVVR GPAPLSLALA NVSVENDNVF VSQWTETDFR TGDKPWWA
 
 
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