PSBT_THEVB
ID PSBT_THEVB Reviewed; 32 AA.
AC Q8DIQ0; Q9F1M2;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 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 [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=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).
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=NIES-2133 / IAM M-273 / 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=NIES-2133 / IAM M-273 / 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=NIES-2133 / IAM M-273 / 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=NIES-2133 / IAM M-273 / 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=NIES-2133 / IAM M-273 / 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=NIES-2133 / IAM M-273 / 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=NIES-2133 / IAM M-273 / 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 PDB; 7NHO; EM; 2.66 A; T=1-32.
DR PDB; 7NHP; EM; 2.72 A; T=1-32.
DR PDB; 7NHQ; EM; 2.68 A; T=1-32.
DR PDB; 7RF1; X-ray; 1.89 A; T/t=1-32.
DR PDB; 7RF2; X-ray; 2.08 A; T/t=1-32.
DR PDB; 7RF3; X-ray; 2.26 A; T/t=1-32.
DR PDB; 7RF4; X-ray; 2.27 A; T/t=1-32.
DR PDB; 7RF5; X-ray; 2.23 A; T/t=1-32.
DR PDB; 7RF6; X-ray; 2.01 A; T/t=1-32.
DR PDB; 7RF7; X-ray; 2.09 A; T/t=1-32.
DR PDB; 7RF8; 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 PDBsum; 7NHO; -.
DR PDBsum; 7NHP; -.
DR PDBsum; 7NHQ; -.
DR PDBsum; 7RF1; -.
DR PDBsum; 7RF2; -.
DR PDBsum; 7RF3; -.
DR PDBsum; 7RF4; -.
DR PDBsum; 7RF5; -.
DR PDBsum; 7RF6; -.
DR PDBsum; 7RF7; -.
DR PDBsum; 7RF8; -.
DR AlphaFoldDB; Q8DIQ0; -.
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:0007829|PDB:5ZZN"
SQ SEQUENCE 32 AA; 3875 MW; D8557803A0A3C7E4 CRC64;
METITYVFIF ACIIALFFFA IFFREPPRIT KK
