GenomeNet

Database: UniProt
Entry: Q8DJZ6
LinkDB: Q8DJZ6
Original site: Q8DJZ6 
ID   PSBI_THEEB              Reviewed;          38 AA.
AC   Q8DJZ6; Q9F1L2;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   02-DEC-2020, entry version 109.
DE   RecName: Full=Photosystem II reaction center protein I {ECO:0000255|HAMAP-Rule:MF_01316};
DE            Short=PSII-I {ECO:0000255|HAMAP-Rule:MF_01316};
DE   AltName: Full=PSII 4.4 kDa protein {ECO:0000255|HAMAP-Rule:MF_01316};
GN   Name=psbI {ECO:0000255|HAMAP-Rule:MF_01316}; OrderedLocusNames=tsr1074;
OS   Thermosynechococcus elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Katoh H., Ikeuchi M.;
RT   "Cloning and disruption of the psbI gene from thermophilic
RT   Thermosynechococcus (formerly Synechococcus) elongatus BP-1.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=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).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-15, COFACTOR, AND SUBCELLULAR LOCATION.
RX   PubMed=17935689; DOI=10.1016/j.bbabio.2007.08.008;
RA   Kashino Y., Takahashi T., Inoue-Kashino N., Ban A., Ikeda Y., Satoh K.,
RA   Sugiura M.;
RT   "Ycf12 is a core subunit in the photosystem II complex.";
RL   Biochim. Biophys. Acta 1767:1269-1275(2007).
RN   [4]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21195048; DOI=10.1016/j.bbabio.2010.12.013;
RA   Kawakami K., Umena Y., Iwai M., Kawabata Y., Ikeuchi M., Kamiya N.,
RA   Shen J.R.;
RT   "Roles of PsbI and PsbM in photosystem II dimer formation and stability
RT   studied by deletion mutagenesis and X-ray crystallography.";
RL   Biochim. Biophys. Acta 1807:319-325(2011).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=14764885; DOI=10.1126/science.1093087;
RA   Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S.;
RT   "Architecture of the photosynthetic oxygen-evolving center.";
RL   Science 303:1831-1838(2004).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=16355230; DOI=10.1038/nature04224;
RA   Loll B., Kern J., Saenger W., Zouni A., Biesiadka J.;
RT   "Towards complete cofactor arrangement in the 3.0 A resolution structure of
RT   photosystem II.";
RL   Nature 438:1040-1044(2005).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, SUBCELLULAR LOCATION, FORMYLATION AT MET-1, MASS SPECTROMETRY, AND
RP   TOPOLOGY.
RC   STRAIN=BP-1;
RX   PubMed=19219048; DOI=10.1038/nsmb.1559;
RA   Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.;
RT   "Cyanobacterial photosystem II at 2.9-A resolution and the role of
RT   quinones, lipids, channels and chloride.";
RL   Nat. Struct. Mol. Biol. 16:334-342(2009).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP   COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, FORMYLATION AT MET-1, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=BP-1;
RX   PubMed=20558739; DOI=10.1074/jbc.m110.127589;
RA   Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W.,
RA   Zouni A.;
RT   "Crystal structure of monomeric photosystem II from Thermosynechococcus
RT   elongatus at 3.6 A resolution.";
RL   J. Biol. Chem. 285:26255-26262(2010).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=21367867; DOI=10.1074/jbc.m110.215970;
RA   Broser M., Glockner C., Gabdulkhakov A., Guskov A., Buchta J., Kern J.,
RA   Muh F., Dau H., Saenger W., Zouni A.;
RT   "Structural basis of cyanobacterial photosystem II inhibition by the
RT   herbicide terbutryn.";
RL   J. Biol. Chem. 286:15964-15972(2011).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=22665786; DOI=10.1073/pnas.1204598109;
RA   Kern J., Alonso-Mori R., Hellmich J., Tran R., Hattne J., Laksmono H.,
RA   Glockner C., Echols N., Sierra R.G., Sellberg J., Lassalle-Kaiser B.,
RA   Gildea R.J., Glatzel P., Grosse-Kunstleve R.W., Latimer M.J., McQueen T.A.,
RA   DiFiore D., Fry A.R., Messerschmidt M., Miahnahri A., Schafer D.W.,
RA   Seibert M.M., Sokaras D., Weng T.C., Zwart P.H., White W.E., Adams P.D.,
RA   Bogan M.J., Boutet S., Williams G.J., Messinger J., Sauter N.K., Zouni A.,
RA   Bergmann U., Yano J., Yachandra V.K.;
RT   "Room temperature femtosecond X-ray diffraction of photosystem II
RT   microcrystals.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:9721-9726(2012).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=23413188; DOI=10.1126/science.1234273;
RA   Kern J., Alonso-Mori R., Tran R., Hattne J., Gildea R.J., Echols N.,
RA   Glockner C., Hellmich J., Laksmono H., Sierra R.G., Lassalle-Kaiser B.,
RA   Koroidov S., Lampe A., Han G., Gul S., Difiore D., Milathianaki D.,
RA   Fry A.R., Miahnahri A., Schafer D.W., Messerschmidt M., Seibert M.M.,
RA   Koglin J.E., Sokaras D., Weng T.C., Sellberg J., Latimer M.J.,
RA   Grosse-Kunstleve R.W., Zwart P.H., White W.E., Glatzel P., Adams P.D.,
RA   Bogan M.J., Williams G.J., Boutet S., Messinger J., Zouni A., Sauter N.K.,
RA   Yachandra V.K., Bergmann U., Yano J.;
RT   "Simultaneous femtosecond X-ray spectroscopy and diffraction of photosystem
RT   II at room temperature.";
RL   Science 340:491-495(2013).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=25043005; DOI=10.1038/nature13453;
RA   Kupitz C., Basu S., Grotjohann I., Fromme R., Zatsepin N.A., Rendek K.N.,
RA   Hunter M.S., Shoeman R.L., White T.A., Wang D., James D., Yang J.H.,
RA   Cobb D.E., Reeder B., Sierra R.G., Liu H., Barty A., Aquila A.L.,
RA   Deponte D., Kirian R.A., Bari S., Bergkamp J.J., Beyerlein K.R.,
RA   Bogan M.J., Caleman C., Chao T.C., Conrad C.E., Davis K.M.,
RA   Fleckenstein H., Galli L., Hau-Riege S.P., Kassemeyer S., Laksmono H.,
RA   Liang M., Lomb L., Marchesini S., Martin A.V., Messerschmidt M.,
RA   Milathianaki D., Nass K., Ros A., Roy-Chowdhury S., Schmidt K., Seibert M.,
RA   Steinbrener J., Stellato F., Yan L., Yoon C., Moore T.A., Moore A.L.,
RA   Pushkar Y., Williams G.J., Boutet S., Doak R.B., Weierstall U., Frank M.,
RA   Chapman H.N., Spence J.C., Fromme P.;
RT   "Serial time-resolved crystallography of photosystem II using a femtosecond
RT   X-ray laser.";
RL   Nature 513:261-265(2014).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=25006873; DOI=10.1038/ncomms5371;
RA   Kern J., Tran R., Alonso-Mori R., Koroidov S., Echols N., Hattne J.,
RA   Ibrahim M., Gul S., Laksmono H., Sierra R.G., Gildea R.J., Han G.,
RA   Hellmich J., Lassalle-Kaiser B., Chatterjee R., Brewster A.S., Stan C.A.,
RA   Gloeckner C., Lampe A., DiFiore D., Milathianaki D., Fry A.R.,
RA   Seibert M.M., Koglin J.E., Gallo E., Uhlig J., Sokaras D., Weng T.C.,
RA   Zwart P.H., Skinner D.E., Bogan M.J., Messerschmidt M., Glatzel P.,
RA   Williams G.J., Boutet S., Adams P.D., Zouni A., Messinger J., Sauter N.K.,
RA   Bergmann U., Yano J., Yachandra V.K.;
RT   "Taking snapshots of photosynthetic water oxidation using femtosecond X-ray
RT   diffraction and spectroscopy.";
RL   Nat. Commun. 5:4371-4371(2014).
CC   -!- FUNCTION: One of the components of the core complex of photosystem II
CC       (PSII). May be required for formation of PSII dimers but not their
CC       subsequent stability (PubMed:21195048). PSII is a light-driven
CC       water:plastoquinone oxidoreductase that uses light energy to abstract
CC       electrons from H(2)O, generating O(2) and a proton gradient
CC       subsequently used for ATP formation. It consists of a core antenna
CC       complex that captures photons, and an electron transfer chain that
CC       converts photonic excitation into a charge separation.
CC       {ECO:0000255|HAMAP-Rule:MF_01316, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21195048, ECO:0000269|PubMed:21367867,
CC       ECO:0000269|PubMed:25006873}.
CC   -!- COFACTOR:
CC       Note=PSII binds multiple chlorophylls, carotenoids and specific lipids.
CC       {ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:19219048,
CC       ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC       ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
CC       ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005};
CC   -!- SUBUNIT: Cyanobacterial PSII is composed of 1 copy each of membrane
CC       proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK,
CC       PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral
CC       proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms
CC       dimeric complexes. {ECO:0000255|HAMAP-Rule:MF_01316,
CC       ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21195048, ECO:0000269|PubMed:21367867,
CC       ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
CC       ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01316, ECO:0000269|PubMed:14764885,
CC       ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689,
CC       ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21195048, ECO:0000269|PubMed:21367867,
CC       ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
CC       ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005}; Single-pass
CC       membrane protein {ECO:0000255|HAMAP-Rule:MF_01316,
CC       ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:19219048,
CC       ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC       ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
CC       ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005}.
CC   -!- MASS SPECTROMETRY: Mass=4437; Mass_error=4; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19219048};
CC   -!- MASS SPECTROMETRY: Mass=4435; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20558739};
CC   -!- DISRUPTION PHENOTYPE: Decreased yields of PSII dimers with increased
CC       PSII monomers, slightly slower photoautotrophic growth, about 20% less
CC       oxygen evolution. Formed PSII dimers are stable.
CC       {ECO:0000269|PubMed:21195048}.
CC   -!- SIMILARITY: Belongs to the PsbI family. {ECO:0000255|HAMAP-
CC       Rule:MF_01316}.
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; AB052849; BAB20622.1; -; Genomic_DNA.
DR   EMBL; BA000039; BAC08627.1; -; Genomic_DNA.
DR   RefSeq; NP_681865.1; NC_004113.1.
DR   RefSeq; WP_011056917.1; NC_004113.1.
DR   PDB; 1S5L; X-ray; 3.50 A; I/i=1-38.
DR   PDB; 2AXT; X-ray; 3.00 A; I/i=1-38.
DR   PDB; 3KZI; X-ray; 3.60 A; I=1-38.
DR   PDB; 4FBY; X-ray; 6.56 A; I/a=1-38.
DR   PDB; 4IXQ; X-ray; 5.70 A; I/i=1-38.
DR   PDB; 4IXR; X-ray; 5.90 A; I/i=1-38.
DR   PDB; 4PBU; X-ray; 5.00 A; I/i=1-38.
DR   PDB; 4PJ0; X-ray; 2.44 A; I/i=1-38.
DR   PDB; 4RVY; X-ray; 5.50 A; I/i=1-38.
DR   PDB; 4TNH; X-ray; 4.90 A; I/i=1-38.
DR   PDB; 4TNI; X-ray; 4.60 A; I/i=1-38.
DR   PDB; 4TNJ; X-ray; 4.50 A; I/i=1-38.
DR   PDB; 4TNK; X-ray; 5.20 A; I/i=1-38.
DR   PDB; 4V62; X-ray; 2.90 A; AI/BI=1-38.
DR   PDB; 4V82; X-ray; 3.20 A; AI/BI=1-38.
DR   PDB; 5E79; X-ray; 3.50 A; I/i=1-38.
DR   PDB; 5E7C; X-ray; 4.50 A; I/i=1-38.
DR   PDB; 5H2F; X-ray; 2.20 A; I/i=1-36.
DR   PDB; 5KAF; X-ray; 3.00 A; I/i=2-38.
DR   PDB; 5KAI; X-ray; 2.80 A; I/i=2-38.
DR   PDB; 5MX2; X-ray; 2.20 A; I/i=1-38.
DR   PDB; 5TIS; X-ray; 2.25 A; I/i=1-38.
DR   PDB; 5ZZN; X-ray; 2.10 A; I/i=1-37.
DR   PDB; 6DHE; X-ray; 2.05 A; I/i=1-36.
DR   PDB; 6DHF; X-ray; 2.08 A; I/i=1-36.
DR   PDB; 6DHG; X-ray; 2.50 A; I/i=1-36.
DR   PDB; 6DHH; X-ray; 2.20 A; I/i=1-36.
DR   PDB; 6DHO; X-ray; 2.07 A; I/i=1-36.
DR   PDB; 6DHP; X-ray; 2.04 A; I/i=1-36.
DR   PDB; 6W1O; X-ray; 2.08 A; I/i=1-38.
DR   PDB; 6W1P; X-ray; 2.26 A; I/i=1-38.
DR   PDB; 6W1Q; X-ray; 2.27 A; I/i=1-38.
DR   PDB; 6W1R; X-ray; 2.23 A; I/i=1-38.
DR   PDB; 6W1T; X-ray; 2.01 A; I/i=1-38.
DR   PDB; 6W1U; X-ray; 2.09 A; I/i=1-38.
DR   PDB; 6W1V; X-ray; 2.09 A; I/i=1-38.
DR   PDBsum; 1S5L; -.
DR   PDBsum; 2AXT; -.
DR   PDBsum; 3KZI; -.
DR   PDBsum; 4FBY; -.
DR   PDBsum; 4IXQ; -.
DR   PDBsum; 4IXR; -.
DR   PDBsum; 4PBU; -.
DR   PDBsum; 4PJ0; -.
DR   PDBsum; 4RVY; -.
DR   PDBsum; 4TNH; -.
DR   PDBsum; 4TNI; -.
DR   PDBsum; 4TNJ; -.
DR   PDBsum; 4TNK; -.
DR   PDBsum; 4V62; -.
DR   PDBsum; 4V82; -.
DR   PDBsum; 5E79; -.
DR   PDBsum; 5E7C; -.
DR   PDBsum; 5H2F; -.
DR   PDBsum; 5KAF; -.
DR   PDBsum; 5KAI; -.
DR   PDBsum; 5MX2; -.
DR   PDBsum; 5TIS; -.
DR   PDBsum; 5ZZN; -.
DR   PDBsum; 6DHE; -.
DR   PDBsum; 6DHF; -.
DR   PDBsum; 6DHG; -.
DR   PDBsum; 6DHH; -.
DR   PDBsum; 6DHO; -.
DR   PDBsum; 6DHP; -.
DR   PDBsum; 6W1O; -.
DR   PDBsum; 6W1P; -.
DR   PDBsum; 6W1Q; -.
DR   PDBsum; 6W1R; -.
DR   PDBsum; 6W1T; -.
DR   PDBsum; 6W1U; -.
DR   PDBsum; 6W1V; -.
DR   SMR; Q8DJZ6; -.
DR   DIP; DIP-48494N; -.
DR   IntAct; Q8DJZ6; 1.
DR   STRING; 197221.22294798; -.
DR   EnsemblBacteria; BAC08627; BAC08627; BAC08627.
DR   KEGG; tel:tsr1074; -.
DR   PATRIC; fig|197221.4.peg.1129; -.
DR   eggNOG; ENOG5033CII; Bacteria.
DR   EvolutionaryTrace; Q8DJZ6; -.
DR   Proteomes; UP000000440; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009539; C:photosystem II reaction center; IEA:InterPro.
DR   GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01316; PSII_PsbI; 1.
DR   InterPro; IPR003686; PSII_PsbI.
DR   InterPro; IPR037271; PSII_PsbI_sf.
DR   PANTHER; PTHR35772; PTHR35772; 1.
DR   Pfam; PF02532; PsbI; 1.
DR   SUPFAM; SSF161041; SSF161041; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Formylation; Membrane;
KW   Photosynthesis; Photosystem II; Reaction center; Reference proteome;
KW   Thylakoid; Transmembrane; Transmembrane helix.
FT   CHAIN           1..38
FT                   /note="Photosystem II reaction center protein I"
FT                   /id="PRO_0000219660"
FT   TOPO_DOM        1..5
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        6..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        22..38
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   MOD_RES         1
FT                   /note="N-formylmethionine"
FT                   /evidence="ECO:0000269|PubMed:19219048,
FT                   ECO:0000269|PubMed:20558739"
FT   HELIX           2..24
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           27..29
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          31..34
FT                   /evidence="ECO:0000244|PDB:5ZZN"
SQ   SEQUENCE   38 AA;  4405 MW;  02DDC30594997948 CRC64;
     METLKITVYI VVTFFVLLFV FGFLSGDPAR NPKRKDLE
//
DBGET integrated database retrieval system