PSBJ_THEVB
ID PSBJ_THEVB Reviewed; 40 AA.
AC P59087;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Photosystem II reaction center protein J {ECO:0000255|HAMAP-Rule:MF_01305};
DE Short=PSII-J {ECO:0000255|HAMAP-Rule:MF_01305};
GN Name=psbJ {ECO:0000255|HAMAP-Rule:MF_01305}; OrderedLocusNames=tsr1544;
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).
RN [2]
RP FUNCTION, SUBUNIT, MASS SPECTROMETRY, AND DISRUPTION PHENOTYPE.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=22387395; DOI=10.1016/j.bbabio.2012.02.017;
RA Nowaczyk M.M., Krause K., Mieseler M., Sczibilanski A., Ikeuchi M.,
RA Roegner M.;
RT "Deletion of psbJ leads to accumulation of Psb27-Psb28 photosystem II
RT complexes in Thermosynechococcus elongatus.";
RL Biochim. Biophys. Acta 1817:1339-1345(2012).
RN [3]
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 [4]
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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP SUBUNIT, SUBCELLULAR LOCATION, ACETYLATION AT MET-2, 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 [6]
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, ACETYLATION AT MET-2, 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 [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) OF 2-40 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 [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) 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 [11]
RP X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP 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: One of the components of the core complex of photosystem II
CC (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that
CC uses light energy to abstract electrons from H(2)O, generating O(2) and
CC a proton gradient subsequently used for ATP formation. It consists of a
CC core antenna complex that captures photons, and an electron transfer
CC chain that converts photonic excitation into a charge separation.
CC {ECO:0000255|HAMAP-Rule:MF_01305, ECO:0000269|PubMed:20558739,
CC ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22387395,
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: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, 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_01305,
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:22387395,
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_01305, ECO:0000269|PubMed:14764885,
CC ECO:0000269|PubMed:16355230, 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_01305,
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 -!- MASS SPECTROMETRY: Mass=4002; Method=MALDI; Note=Suggests the protein
CC is 1 residue shorter at the N-terminus and N-formylated.;
CC Evidence={ECO:0000269|PubMed:22387395};
CC -!- DISRUPTION PHENOTYPE: No change in growth rate or oxygen evolution
CC under standard growth conditions (50 umol photons/m(2)/s and 45 degrees
CC Celsius). Dimeric PSII less stable upon isolation, soluble protein
CC Psb28 associates substoichiometrically with PSII. Only the D1 protein
CC translated from the psbA2 or psbA3 gene is found in PSII.
CC {ECO:0000269|PubMed:22387395}.
CC -!- SIMILARITY: Belongs to the PsbJ family. {ECO:0000255|HAMAP-
CC Rule:MF_01305}.
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DR EMBL; BA000039; BAC09096.1; -; Genomic_DNA.
DR RefSeq; NP_682334.1; NC_004113.1.
DR PDB; 1S5L; X-ray; 3.50 A; J/j=1-40.
DR PDB; 2AXT; X-ray; 3.00 A; J/j=1-40.
DR PDB; 3KZI; X-ray; 3.60 A; J=1-40.
DR PDB; 4FBY; X-ray; 6.56 A; J/b=2-40.
DR PDB; 4IXQ; X-ray; 5.70 A; J/j=1-40.
DR PDB; 4IXR; X-ray; 5.90 A; J/j=1-40.
DR PDB; 4PBU; X-ray; 5.00 A; J/j=1-40.
DR PDB; 4PJ0; X-ray; 2.44 A; J/j=1-40.
DR PDB; 4RVY; X-ray; 5.50 A; J/j=1-40.
DR PDB; 4TNH; X-ray; 4.90 A; J/j=1-40.
DR PDB; 4TNI; X-ray; 4.60 A; J/j=1-40.
DR PDB; 4TNJ; X-ray; 4.50 A; J/j=1-40.
DR PDB; 4TNK; X-ray; 5.20 A; J/j=1-40.
DR PDB; 4V62; X-ray; 2.90 A; AJ/BJ=1-40.
DR PDB; 4V82; X-ray; 3.20 A; AJ/BJ=1-40.
DR PDB; 5E79; X-ray; 3.50 A; J/j=3-40.
DR PDB; 5E7C; X-ray; 4.50 A; J/j=3-40.
DR PDB; 5H2F; X-ray; 2.20 A; J/j=1-40.
DR PDB; 5KAF; X-ray; 3.00 A; J/j=1-40.
DR PDB; 5KAI; X-ray; 2.80 A; J/j=1-40.
DR PDB; 5MX2; X-ray; 2.20 A; J/j=1-40.
DR PDB; 5TIS; X-ray; 2.25 A; J/j=1-40.
DR PDB; 5ZZN; X-ray; 2.10 A; J/j=1-40.
DR PDB; 6DHE; X-ray; 2.05 A; J/j=5-40.
DR PDB; 6DHF; X-ray; 2.08 A; J/j=5-40.
DR PDB; 6DHG; X-ray; 2.50 A; J/j=5-40.
DR PDB; 6DHH; X-ray; 2.20 A; J/j=5-40.
DR PDB; 6DHO; X-ray; 2.07 A; J/j=5-40.
DR PDB; 6DHP; X-ray; 2.04 A; J/j=5-40.
DR PDB; 6W1O; X-ray; 2.08 A; J/j=1-40.
DR PDB; 6W1P; X-ray; 2.26 A; J/j=1-40.
DR PDB; 6W1Q; X-ray; 2.27 A; J/j=1-40.
DR PDB; 6W1R; X-ray; 2.23 A; J/j=1-40.
DR PDB; 6W1T; X-ray; 2.01 A; J/j=1-40.
DR PDB; 6W1U; X-ray; 2.09 A; J/j=1-40.
DR PDB; 6W1V; X-ray; 2.09 A; J/j=1-40.
DR PDB; 7RF1; X-ray; 1.89 A; J/j=1-40.
DR PDB; 7RF2; X-ray; 2.08 A; J/j=1-40.
DR PDB; 7RF3; X-ray; 2.26 A; J/j=1-40.
DR PDB; 7RF4; X-ray; 2.27 A; J/j=1-40.
DR PDB; 7RF5; X-ray; 2.23 A; J/j=1-40.
DR PDB; 7RF6; X-ray; 2.01 A; J/j=1-40.
DR PDB; 7RF7; X-ray; 2.09 A; J/j=1-40.
DR PDB; 7RF8; X-ray; 2.09 A; J/j=1-40.
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; 7RF1; -.
DR PDBsum; 7RF2; -.
DR PDBsum; 7RF3; -.
DR PDBsum; 7RF4; -.
DR PDBsum; 7RF5; -.
DR PDBsum; 7RF6; -.
DR PDBsum; 7RF7; -.
DR PDBsum; 7RF8; -.
DR AlphaFoldDB; P59087; -.
DR SMR; P59087; -.
DR DIP; DIP-48495N; -.
DR IntAct; P59087; 1.
DR STRING; 197221.22295269; -.
DR iPTMnet; P59087; -.
DR EnsemblBacteria; BAC09096; BAC09096; BAC09096.
DR KEGG; tel:tsr1544; -.
DR PATRIC; fig|197221.4.peg.1620; -.
DR eggNOG; ENOG5033ABP; Bacteria.
DR OrthoDB; 2085237at2; -.
DR EvolutionaryTrace; P59087; -.
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_01305; PSII_PsbJ; 1.
DR InterPro; IPR002682; PSII_PsbJ.
DR InterPro; IPR037267; PSII_PsbJ_sf.
DR Pfam; PF01788; PsbJ; 1.
DR SUPFAM; SSF161021; SSF161021; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Membrane; Photosynthesis; Photosystem II;
KW Reaction center; Reference proteome; Thylakoid; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:19219048,
FT ECO:0000269|PubMed:20558739"
FT CHAIN 2..40
FT /note="Photosystem II reaction center protein J"
FT /id="PRO_0000216623"
FT TOPO_DOM 2..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TRANSMEM 12..26
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:19219048"
FT TOPO_DOM 27..40
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:19219048"
FT MOD_RES 2
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:19219048,
FT ECO:0000269|PubMed:20558739"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:5ZZN"
FT HELIX 10..32
FT /evidence="ECO:0007829|PDB:5ZZN"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:5H2F"
SQ SEQUENCE 40 AA; 4105 MW; 4D05FAA8C690069E CRC64;
MMSEGGRIPL WIVATVAGMG VIVIVGLFFY GAYAGLGSSL
