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UCRI_THEVB
ID   UCRI_THEVB              Reviewed;         180 AA.
AC   P0C8N8; Q79V50; Q9X9T2;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=tlr0959;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
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; BA000039; BAC08511.1; -; Genomic_DNA.
DR   RefSeq; NP_681749.1; NC_004113.1.
DR   RefSeq; WP_011056803.1; NC_004113.1.
DR   PDB; 3AZC; X-ray; 2.00 A; A=54-180.
DR   PDBsum; 3AZC; -.
DR   AlphaFoldDB; P0C8N8; -.
DR   SMR; P0C8N8; -.
DR   STRING; 197221.22294682; -.
DR   EnsemblBacteria; BAC08511; BAC08511; BAC08511.
DR   KEGG; tel:tlr0959; -.
DR   PATRIC; fig|197221.4.peg.1006; -.
DR   eggNOG; COG0723; Bacteria.
DR   OMA; KGDPTYI; -.
DR   OrthoDB; 1632945at2; -.
DR   Proteomes; UP000000440; 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   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; 3D-structure; Disulfide bond; Electron transport; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Reference proteome; Thylakoid;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..180
FT                   /note="Cytochrome b6-f complex iron-sulfur subunit"
FT                   /id="PRO_0000361773"
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"
FT   HELIX           66..70
FT                   /evidence="ECO:0007829|PDB:3AZC"
FT   STRAND          78..82
FT                   /evidence="ECO:0007829|PDB:3AZC"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:3AZC"
FT   STRAND          88..93
FT                   /evidence="ECO:0007829|PDB:3AZC"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:3AZC"
FT   STRAND          101..105
FT                   /evidence="ECO:0007829|PDB:3AZC"
FT   TURN            109..111
FT                   /evidence="ECO:0007829|PDB:3AZC"
FT   TURN            119..122
FT                   /evidence="ECO:0007829|PDB:3AZC"
FT   STRAND          123..125
FT                   /evidence="ECO:0007829|PDB:3AZC"
FT   TURN            127..129
FT                   /evidence="ECO:0007829|PDB:3AZC"
FT   STRAND          139..143
FT                   /evidence="ECO:0007829|PDB:3AZC"
FT   STRAND          150..155
FT                   /evidence="ECO:0007829|PDB:3AZC"
FT   STRAND          161..165
FT                   /evidence="ECO:0007829|PDB:3AZC"
FT   TURN            171..173
FT                   /evidence="ECO:0007829|PDB:3AZC"
SQ   SEQUENCE   180 AA;  19316 MW;  EBB4352DB5DAB6B7 CRC64;
     MAQVSGMSDV PDMGRRQFMN LLTFGTITGT ALGALYPVVK YFIPPASGGT GGGAVAKDAL
     GNDIKVSEYL AKHLPGDRSL AQGIKGDPTY VIVTEDHQIA NYGLNAVCTH LGCVVPWNVS
     ENKFICPCHG SQYDSTGKVV RGPAPLSLAL VKATVTEDDK LVFTPWTEID FRTGKEPWWT
 
 
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