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Database: UniProt
Entry: Q8DJ43
LinkDB: Q8DJ43
Original site: Q8DJ43 
ID   PSBH_THEEB              Reviewed;          66 AA.
AC   Q8DJ43;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   02-DEC-2020, entry version 115.
DE   RecName: Full=Photosystem II reaction center protein H {ECO:0000255|HAMAP-Rule:MF_00752};
DE            Short=PSII-H {ECO:0000255|HAMAP-Rule:MF_00752};
GN   Name=psbH {ECO:0000255|HAMAP-Rule:MF_00752}; OrderedLocusNames=tsl1386;
OS   Thermosynechococcus elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
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   [2]
RP   PROTEIN SEQUENCE OF 2-8, CLEAVAGE OF INITIATOR METHIONINE, COFACTOR, AND
RP   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   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=BP-1;
RX   PubMed=16699922; DOI=10.1007/s11120-005-9013-0;
RA   Iwai M., Katayama M., Ikeuchi M.;
RT   "Absence of the psbH gene product destabilizes the Photosystem II complex
RT   and prevents association of the Photosystem II-X protein in the
RT   thermophilic cyanobacterium Thermosynechococcus elongatus BP-1.";
RL   Photosyn. Res. 87:313-322(2006).
RN   [4]
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   [5]
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   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND 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   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 2-66 IN PHOTOSYSTEM II, FUNCTION,
RP   COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND MASS 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   [8]
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   [9]
RP   X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) OF 2-66 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   [10]
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   [11]
RP   X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 2-66 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   [12]
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), required for its stability and/or assembly. PSII is a light-
CC       driven water:plastoquinone oxidoreductase that uses light energy to
CC       abstract 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_00752, ECO:0000269|PubMed:16699922,
CC       ECO:0000269|PubMed:20558739, 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_00752,
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_00752, 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:21367867, ECO:0000269|PubMed:22665786,
CC       ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC       ECO:0000269|PubMed:25043005}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00752, 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:21367867, ECO:0000269|PubMed:22665786,
CC       ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC       ECO:0000269|PubMed:25043005}.
CC   -!- MASS SPECTROMETRY: Mass=7227; Mass_error=5; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19219048};
CC   -!- MASS SPECTROMETRY: Mass=7223; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20558739};
CC   -!- MASS SPECTROMETRY: Mass=7178; Method=MALDI; Note=Missing initiator Met
CC       and CO(2).; Evidence={ECO:0000269|PubMed:20558739};
CC   -!- DISRUPTION PHENOTYPE: Not essential for photoautotrophic growth,
CC       however PSII is less stable, a considerable amount is missing the
CC       oxygen evolving complex, and it is missing PsbX.
CC       {ECO:0000269|PubMed:16699922}.
CC   -!- SIMILARITY: Belongs to the PsbH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00752}.
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DR   EMBL; BA000039; BAC08938.1; -; Genomic_DNA.
DR   RefSeq; NP_682176.1; NC_004113.1.
DR   RefSeq; WP_011057226.1; NC_004113.1.
DR   PDB; 1S5L; X-ray; 3.50 A; H/h=1-66.
DR   PDB; 2AXT; X-ray; 3.00 A; H/h=1-66.
DR   PDB; 3KZI; X-ray; 3.60 A; H=2-66.
DR   PDB; 4FBY; X-ray; 6.56 A; H/W=2-66.
DR   PDB; 4IXQ; X-ray; 5.70 A; H/h=1-66.
DR   PDB; 4IXR; X-ray; 5.90 A; H/h=1-66.
DR   PDB; 4PBU; X-ray; 5.00 A; H/h=2-66.
DR   PDB; 4PJ0; X-ray; 2.44 A; H/h=1-66.
DR   PDB; 4RVY; X-ray; 5.50 A; H/h=2-66.
DR   PDB; 4TNH; X-ray; 4.90 A; H/h=1-66.
DR   PDB; 4TNI; X-ray; 4.60 A; H/h=1-66.
DR   PDB; 4TNJ; X-ray; 4.50 A; H/h=1-66.
DR   PDB; 4TNK; X-ray; 5.20 A; H/h=1-66.
DR   PDB; 4V62; X-ray; 2.90 A; AH/BH=1-66.
DR   PDB; 4V82; X-ray; 3.20 A; AH/BH=1-66.
DR   PDB; 5E79; X-ray; 3.50 A; H/h=2-66.
DR   PDB; 5E7C; X-ray; 4.50 A; H/h=2-66.
DR   PDB; 5H2F; X-ray; 2.20 A; H/h=2-64.
DR   PDB; 5KAF; X-ray; 3.00 A; H/h=1-66.
DR   PDB; 5KAI; X-ray; 2.80 A; H/h=2-64.
DR   PDB; 5MX2; X-ray; 2.20 A; H/h=1-66.
DR   PDB; 5TIS; X-ray; 2.25 A; H/h=1-66.
DR   PDB; 5ZZN; X-ray; 2.10 A; H/h=2-64.
DR   PDB; 6DHE; X-ray; 2.05 A; H/h=2-66.
DR   PDB; 6DHF; X-ray; 2.08 A; H/h=2-66.
DR   PDB; 6DHG; X-ray; 2.50 A; H/h=2-66.
DR   PDB; 6DHH; X-ray; 2.20 A; H/h=2-66.
DR   PDB; 6DHO; X-ray; 2.07 A; H/h=2-66.
DR   PDB; 6DHP; X-ray; 2.04 A; H/h=2-66.
DR   PDB; 6W1O; X-ray; 2.08 A; H/h=1-66.
DR   PDB; 6W1P; X-ray; 2.26 A; H/h=1-66.
DR   PDB; 6W1Q; X-ray; 2.27 A; H/h=1-66.
DR   PDB; 6W1R; X-ray; 2.23 A; H/h=1-66.
DR   PDB; 6W1T; X-ray; 2.01 A; H/h=1-66.
DR   PDB; 6W1U; X-ray; 2.09 A; H/h=1-66.
DR   PDB; 6W1V; X-ray; 2.09 A; H/h=1-66.
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; Q8DJ43; -.
DR   DIP; DIP-48493N; -.
DR   IntAct; Q8DJ43; 1.
DR   STRING; 197221.22295110; -.
DR   EnsemblBacteria; BAC08938; BAC08938; BAC08938.
DR   KEGG; tel:tsl1386; -.
DR   PATRIC; fig|197221.4.peg.1458; -.
DR   eggNOG; ENOG50332MV; Bacteria.
DR   OMA; PLMAVFM; -.
DR   EvolutionaryTrace; Q8DJ43; -.
DR   Proteomes; UP000000440; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042301; F:phosphate ion binding; IEA:InterPro.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0050821; P:protein stabilization; IEA:InterPro.
DR   Gene3D; 1.20.5.880; -; 1.
DR   HAMAP; MF_00752; PSII_PsbH; 1.
DR   InterPro; IPR001056; PSII_PsbH.
DR   InterPro; IPR036863; PSII_PsbH_sf.
DR   PANTHER; PTHR34469; PTHR34469; 1.
DR   Pfam; PF00737; PsbH; 1.
DR   SUPFAM; SSF161025; SSF161025; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Membrane; Photosynthesis;
KW   Photosystem II; Reference proteome; Thylakoid; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:17935689,
FT                   ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739"
FT   CHAIN           2..66
FT                   /note="Photosystem II reaction center protein H"
FT                   /id="PRO_0000070546"
FT   TOPO_DOM        2..30
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        31..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        45..66
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   HELIX           6..11
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           12..15
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            24..27
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           28..49
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            56..58
FT                   /evidence="ECO:0000244|PDB:2AXT"
FT   HELIX           62..64
FT                   /evidence="ECO:0000244|PDB:5E79"
SQ   SEQUENCE   66 AA;  7354 MW;  A7558EDCD943741D CRC64;
     MARRTWLGDI LRPLNSEYGK VAPGWGTTPL MAVFMGLFLV FLLIILEIYN STLILDGVNV
     SWKALG
//
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