PSBU_THEVL
ID PSBU_THEVL Reviewed; 104 AA.
AC P56152;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Photosystem II 12 kDa extrinsic protein;
DE AltName: Full=PS II complex 12 kDa extrinsic protein;
DE AltName: Full=PSII-U;
GN Name=psbU;
OS Thermostichus vulcanus (Synechococcus vulcanus).
OC Bacteria; Cyanobacteria; Thermostichales; Thermostichaceae; Thermostichus.
OX NCBI_TaxID=32053;
RN [1]
RP PROTEIN SEQUENCE OF 1-65, SUGGESTION OF FUNCTION IN OXYGEN-EVOLUTION,
RP ASSOCIATION WITH PHOTOSYSTEM II, AND SUBUNIT.
RX PubMed=1314738; DOI=10.1016/0014-5793(92)81235-e;
RA Shen J.-R., Ikeuchi M., Inoue Y.;
RT "Stoichiometric association of extrinsic cytochrome c550 and 12 kDa protein
RT with a highly purified oxygen-evolving photosystem II core complex from
RT Synechococcus vulcanus.";
RL FEBS Lett. 301:145-149(1992).
RN [2]
RP PROTEIN SEQUENCE OF 25-34, COMPOSITION OF PHOTOSYSTEM II, AND SUBUNIT.
RX PubMed=12461137; DOI=10.1093/pcp/pcf168;
RA Kashino Y., Koike H., Yoshio M., Egashira H., Ikeuchi M., Pakrasi H.B.,
RA Satoh K.;
RT "Low-molecular-mass polypeptide components of a photosystem II preparation
RT from the thermophilic cyanobacterium Thermosynechococcus vulcanus.";
RL Plant Cell Physiol. 43:1366-1373(2002).
RN [3]
RP TIGHT ASSOCIATION WITH PHOTOSYSTEM II, AND SUBUNIT.
RX PubMed=8397205; DOI=10.1016/s0021-9258(20)80743-1;
RA Shen J.-R., Inoue Y.;
RT "Cellular localization of cytochrome c550. Its specific association with
RT cyanobacterial photosystem II.";
RL J. Biol. Chem. 268:20408-20413(1993).
RN [4]
RP RECONSTITUTION EXPERIMENTS.
RX PubMed=12941874; DOI=10.1093/pcp/pcg106;
RA Enami I., Iwai M., Akiyama A., Suzuki T., Okumura A., Katoh T., Tada O.,
RA Ohta H., Shen J.-R.;
RT "Comparison of binding and functional properties of two extrinsic
RT components, cyt c550 and a 12 kDa protein, in cyanobacterial PSII with
RT those in red algal PSII.";
RL Plant Cell Physiol. 44:820-827(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12518057; DOI=10.1073/pnas.0135651100;
RA Kamiya N., Shen J.-R.;
RT "Crystal structure of oxygen-evolving photosystem II from
RT Thermosynechococcus vulcanus at 3.7-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:98-103(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 7-104 IN PHOTOSYSTEM II, FUNCTION,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19433803; DOI=10.1073/pnas.0812797106;
RA Kawakami K., Umena Y., Kamiya N., Shen J.R.;
RT "Location of chloride and its possible functions in oxygen-evolving
RT photosystem II revealed by X-ray crystallography.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8567-8572(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 8-104 IN PHOTOSYSTEM II, COFACTOR,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=21499260; DOI=10.1038/nature09913;
RA Umena Y., Kawakami K., Shen J.R., Kamiya N.;
RT "Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9
RT A.";
RL Nature 473:55-60(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 8-104 IN PHOTOSYSTEM II, FUNCTION,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23426624; DOI=10.1073/pnas.1219922110;
RA Koua F.H., Umena Y., Kawakami K., Shen J.R.;
RT "Structure of Sr-substituted photosystem II at 2.1 A resolution and its
RT implications in the mechanism of water oxidation.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:3889-3894(2013).
CC -!- FUNCTION: Stabilizes the structure of photosystem II (PSII) oxygen-
CC evolving complex (OEC), the ion environment of oxygen evolution and
CC protects the OEC against heat-induced inactivation. Requires cytochrome
CC c-550 (PsbV) or OEC3 (PsbO) to bind to photosystem II (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:0000269|PubMed:1314738,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:23426624}.
CC -!- COFACTOR:
CC Note=PSII binds multiple chlorophylls, carotenoids and specific lipids.
CC {ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803,
CC ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624};
CC -!- SUBUNIT: With PsbO,P,Q and V forms the oxygen-evolving complex of
CC photosystem II (Probable). Cyanobacterial PSII is composed of 1 copy
CC each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH,
CC PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, 3
CC peripheral proteins PsbO, PsbU, PsbV and a large number of cofactors.
CC It forms dimeric complexes. {ECO:0000269|PubMed:12461137,
CC ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:1314738,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC ECO:0000269|PubMed:23426624, ECO:0000269|PubMed:8397205}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803,
CC ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624}; Peripheral
CC membrane protein {ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC ECO:0000269|PubMed:23426624}; Lumenal side
CC {ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803,
CC ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624}.
CC Note=Associated with photosystem II at the lumenal side of the
CC thylakoid membrane.
CC -!- SIMILARITY: Belongs to the PsbU family. {ECO:0000305}.
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DR PDB; 3A0B; X-ray; 3.70 A; U/u=7-104.
DR PDB; 3A0H; X-ray; 4.00 A; U/u=7-104.
DR PDB; 3WU2; X-ray; 1.90 A; U/u=1-104.
DR PDB; 4IL6; X-ray; 2.10 A; U/u=8-104.
DR PDB; 4UB6; X-ray; 1.95 A; U/u=1-104.
DR PDB; 4UB8; X-ray; 1.95 A; U/u=1-104.
DR PDB; 5B5E; X-ray; 1.87 A; U/u=1-104.
DR PDB; 5B66; X-ray; 1.85 A; U/u=1-104.
DR PDB; 5GTH; X-ray; 2.50 A; U/u=1-104.
DR PDB; 5GTI; X-ray; 2.50 A; U/u=1-104.
DR PDB; 5V2C; X-ray; 1.90 A; U/u=1-104.
DR PDB; 5WS5; X-ray; 2.35 A; U/u=1-104.
DR PDB; 5WS6; X-ray; 2.35 A; U/u=1-104.
DR PDB; 6JLJ; X-ray; 2.15 A; U/u=1-104.
DR PDB; 6JLK; X-ray; 2.15 A; U/u=1-104.
DR PDB; 6JLL; X-ray; 2.15 A; U/u=1-104.
DR PDB; 6JLM; X-ray; 2.35 A; U/u=1-104.
DR PDB; 6JLN; X-ray; 2.40 A; U/u=1-104.
DR PDB; 6JLO; X-ray; 2.40 A; U/u=1-104.
DR PDB; 6JLP; X-ray; 2.50 A; U/u=1-104.
DR PDB; 7CJI; X-ray; 2.35 A; U/u=1-104.
DR PDB; 7CJJ; X-ray; 2.40 A; U/u=1-104.
DR PDB; 7COU; X-ray; 2.25 A; U/u=1-104.
DR PDB; 7D1T; EM; 1.95 A; U/u=8-104.
DR PDB; 7D1U; EM; 2.08 A; U/u=8-104.
DR PDB; 7EDA; EM; 2.78 A; U=1-104.
DR PDBsum; 3A0B; -.
DR PDBsum; 3A0H; -.
DR PDBsum; 3WU2; -.
DR PDBsum; 4IL6; -.
DR PDBsum; 4UB6; -.
DR PDBsum; 4UB8; -.
DR PDBsum; 5B5E; -.
DR PDBsum; 5B66; -.
DR PDBsum; 5GTH; -.
DR PDBsum; 5GTI; -.
DR PDBsum; 5V2C; -.
DR PDBsum; 5WS5; -.
DR PDBsum; 5WS6; -.
DR PDBsum; 6JLJ; -.
DR PDBsum; 6JLK; -.
DR PDBsum; 6JLL; -.
DR PDBsum; 6JLM; -.
DR PDBsum; 6JLN; -.
DR PDBsum; 6JLO; -.
DR PDBsum; 6JLP; -.
DR PDBsum; 7CJI; -.
DR PDBsum; 7CJJ; -.
DR PDBsum; 7COU; -.
DR PDBsum; 7D1T; -.
DR PDBsum; 7D1U; -.
DR PDBsum; 7EDA; -.
DR AlphaFoldDB; P56152; -.
DR SMR; P56152; -.
DR DIP; DIP-48860N; -.
DR IntAct; P56152; 1.
DR EvolutionaryTrace; P56152; -.
DR GO; GO:0019898; C:extrinsic component of membrane; IEA:InterPro.
DR GO; GO:0009654; C:photosystem II oxygen evolving complex; IEA:InterPro.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0042549; P:photosystem II stabilization; IEA:InterPro.
DR InterPro; IPR010527; PSII_PsbU.
DR Pfam; PF06514; PsbU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Membrane;
KW Photosynthesis; Photosystem II; Thylakoid; Transport.
FT CHAIN 1..104
FT /note="Photosystem II 12 kDa extrinsic protein"
FT /id="PRO_0000219669"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:7EDA"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:7EDA"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:5B66"
SQ SEQUENCE 104 AA; 11645 MW; 41047DED6BB7946A CRC64;
ATASTEEELV NVVDEKLGTA YGEKIDLNNT NIAAFIQYRG LYPTLAKLIV KNAPYESVED
VLNIPGLTER QKQILRENLE HFTVTEVETA LVEGGDRYNN GLYK
