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Database: UniProt
Entry: Q8DIQ0
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Original site: Q8DIQ0 
ID   PSBT_THEEB              Reviewed;          32 AA.
AC   Q8DIQ0; Q9F1M2;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   07-APR-2021, entry version 104.
DE   RecName: Full=Photosystem II reaction center protein T {ECO:0000255|HAMAP-Rule:MF_00808};
DE            Short=PSII-T {ECO:0000255|HAMAP-Rule:MF_00808};
DE            Short=PSII-Tc {ECO:0000303|PubMed:15653799};
GN   Name=psbT {ECO:0000255|HAMAP-Rule:MF_00808}; OrderedLocusNames=tsr1531;
OS   Thermosynechococcus elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15653799; DOI=10.1093/pcp/pch207;
RA   Iwai M., Katoh H., Katayama M., Ikeuchi M.;
RT   "PSII-Tc protein plays an important role in dimerization of photosystem
RT   II.";
RL   Plant Cell Physiol. 45:1809-1816(2004).
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   PROTEIN SEQUENCE OF 1-9, COFACTOR, AND SUBCELLULAR LOCATION.
RX   PubMed=17967798; DOI=10.1093/pcp/pcm148;
RA   Iwai M., Suzuki T., Dohmae N., Inoue Y., Ikeuchi M.;
RT   "Absence of the PsbZ subunit prevents association of PsbK and Ycf12 with
RT   the PSII complex in the thermophilic cyanobacterium Thermosynechococcus
RT   elongatus BP-1.";
RL   Plant Cell Physiol. 48:1758-1763(2007).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR, SUBUNIT,
RP   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) OF 1-30 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: Seems to play a role in the dimerization of PSII. PSII is a
CC       light-driven water plastoquinone oxidoreductase, using light energy to
CC       abstract electrons from H(2)O, generating a proton gradient
CC       subsequently used for ATP formation. {ECO:0000255|HAMAP-Rule:MF_00808,
CC       ECO:0000269|PubMed:15653799, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21367867, 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:17967798,
CC       ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC       ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC       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, 3 peripheral proteins PsbO,
CC       PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
CC       {ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC       ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC       ECO:0000269|PubMed:25043005}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00808, ECO:0000269|PubMed:14764885,
CC       ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689,
CC       ECO:0000269|PubMed:17967798, 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}; Single-pass
CC       membrane protein {ECO:0000255|HAMAP-Rule:MF_00808,
CC       ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:17967798,
CC       ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC       ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC       ECO:0000269|PubMed:25043005}.
CC   -!- MASS SPECTROMETRY: Mass=3906; Mass_error=4; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19219048};
CC   -!- MASS SPECTROMETRY: Mass=3904; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20558739};
CC   -!- DISRUPTION PHENOTYPE: No detectable dimeric PSII, loss of another
CC       protein that may be PsbM. {ECO:0000269|PubMed:15653799}.
CC   -!- SIMILARITY: Belongs to the PsbT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00808}.
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DR   EMBL; AB052566; BAB19262.1; -; Genomic_DNA.
DR   EMBL; BA000039; BAC09083.1; -; Genomic_DNA.
DR   RefSeq; NP_682321.1; NC_004113.1.
DR   RefSeq; WP_011057371.1; NC_004113.1.
DR   PDB; 1S5L; X-ray; 3.50 A; T/t=1-32.
DR   PDB; 2AXT; X-ray; 3.00 A; T/t=1-32.
DR   PDB; 3KZI; X-ray; 3.60 A; T=1-32.
DR   PDB; 4FBY; X-ray; 6.56 A; T/g=1-32.
DR   PDB; 4IXQ; X-ray; 5.70 A; T/t=1-32.
DR   PDB; 4IXR; X-ray; 5.90 A; T/t=1-32.
DR   PDB; 4PBU; X-ray; 5.00 A; T/t=1-30.
DR   PDB; 4PJ0; X-ray; 2.44 A; T/t=1-32.
DR   PDB; 4RVY; X-ray; 5.50 A; T/t=1-30.
DR   PDB; 4TNH; X-ray; 4.90 A; T/t=1-32.
DR   PDB; 4TNI; X-ray; 4.60 A; T/t=1-32.
DR   PDB; 4TNJ; X-ray; 4.50 A; T/t=1-32.
DR   PDB; 4TNK; X-ray; 5.20 A; T/t=1-32.
DR   PDB; 4V62; X-ray; 2.90 A; AT/BT=1-32.
DR   PDB; 4V82; X-ray; 3.20 A; AT/BT=1-32.
DR   PDB; 5E79; X-ray; 3.50 A; T/t=1-30.
DR   PDB; 5E7C; X-ray; 4.50 A; T/t=1-30.
DR   PDB; 5H2F; X-ray; 2.20 A; T/t=1-30.
DR   PDB; 5KAF; X-ray; 3.00 A; T/t=2-32.
DR   PDB; 5KAI; X-ray; 2.80 A; T/t=2-32.
DR   PDB; 5MX2; X-ray; 2.20 A; T/t=1-32.
DR   PDB; 5TIS; X-ray; 2.25 A; T/t=1-32.
DR   PDB; 5ZZN; X-ray; 2.10 A; T/t=1-30.
DR   PDB; 6DHE; X-ray; 2.05 A; T/t=1-30.
DR   PDB; 6DHF; X-ray; 2.08 A; T/t=1-30.
DR   PDB; 6DHG; X-ray; 2.50 A; T/t=1-30.
DR   PDB; 6DHH; X-ray; 2.20 A; T/t=1-30.
DR   PDB; 6DHO; X-ray; 2.07 A; T/t=1-30.
DR   PDB; 6DHP; X-ray; 2.04 A; T/t=1-30.
DR   PDB; 6W1O; X-ray; 2.08 A; T/t=1-30.
DR   PDB; 6W1P; X-ray; 2.26 A; T/t=1-30.
DR   PDB; 6W1Q; X-ray; 2.27 A; T/t=1-30.
DR   PDB; 6W1R; X-ray; 2.23 A; T/t=1-32.
DR   PDB; 6W1T; X-ray; 2.01 A; T/t=1-30.
DR   PDB; 6W1U; X-ray; 2.09 A; T/t=1-32.
DR   PDB; 6W1V; X-ray; 2.09 A; T/t=1-32.
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; Q8DIQ0; -.
DR   DIP; DIP-48500N; -.
DR   IntAct; Q8DIQ0; 1.
DR   STRING; 197221.22295256; -.
DR   EnsemblBacteria; BAC09083; BAC09083; BAC09083.
DR   KEGG; tel:tsr1531; -.
DR   eggNOG; ENOG502ZXRT; Bacteria.
DR   EvolutionaryTrace; Q8DIQ0; -.
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:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00808; PSII_PsbT; 1.
DR   InterPro; IPR001743; PSII_PsbT.
DR   InterPro; IPR037268; PSII_PsbT_sf.
DR   Pfam; PF01405; PsbT; 1.
DR   SUPFAM; SSF161029; SSF161029; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Formylation; Membrane;
KW   Photosynthesis; Photosystem II; Reference proteome; Thylakoid;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..32
FT                   /note="Photosystem II reaction center protein T"
FT                   /id="PRO_0000218004"
FT   TOPO_DOM        1..3
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        4..18
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00808,
FT                   ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        19..32
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..22
FT                   /evidence="ECO:0007744|PDB:5ZZN"
SQ   SEQUENCE   32 AA;  3875 MW;  D8557803A0A3C7E4 CRC64;
     METITYVFIF ACIIALFFFA IFFREPPRIT KK
//
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