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Database: UniProt
Entry: Q9F1L5
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ID   PSBU_THEEB              Reviewed;         134 AA.
AC   Q9F1L5;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   02-DEC-2020, entry version 119.
DE   RecName: Full=Photosystem II 12 kDa extrinsic protein {ECO:0000255|HAMAP-Rule:MF_00589};
DE   AltName: Full=PS II complex 12 kDa extrinsic protein {ECO:0000255|HAMAP-Rule:MF_00589};
DE   AltName: Full=PSII-U {ECO:0000255|HAMAP-Rule:MF_00589};
DE   Flags: Precursor;
GN   Name=psbU {ECO:0000255|HAMAP-Rule:MF_00589}; OrderedLocusNames=tll2409;
OS   Thermosynechococcus elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Katoh H., Ikeuchi M.;
RT   "Cloning and disruption of the psbU gene from thermophilic
RT   Thermosynechococcus (formerly Synechococcus) elongatus BP-1.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
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 31-39, 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   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   [5]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 31-134 IN PHOTOSYSTEM II,
RP   COFACTOR, 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) OF 31-134 IN PHOTOSYSTEM II,
RP   COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
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 31-134 IN PHOTOSYSTEM II,
RP   FUNCTION, 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) OF 31-134 IN PHOTOSYSTEM II,
RP   FUNCTION, 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 31-134 IN PHOTOSYSTEM II,
RP   COFACTOR, 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 38-134 IN PHOTOSYSTEM II,
RP   COFACTOR, 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: Stabilizes the structure of photosystem II oxygen-evolving
CC       complex (OEC), the ion environment of oxygen evolution and protects the
CC       OEC against heat-induced inactivation. PSII is a light-driven water
CC       plastoquinone oxidoreductase, using light energy to abstract electrons
CC       from H(2)O, generating a proton gradient subsequently used for ATP
CC       formation. {ECO:0000255|HAMAP-Rule:MF_00589,
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:0000255|HAMAP-Rule:MF_00589, 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   -!- SUBUNIT: The cyanobacterial oxygen-evolving complex is composed of
CC       PsbO, PsbP, PsbQ, PsbV and PsbU. PsbP and PsbQ are not seen in the
CC       crystal structures; however there is biochemical evidence that they are
CC       part of the OEC (By similarity). Cyanobacterial PSII is composed of 1
CC       copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF,
CC       PsbH, 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:0000250, 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}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00589, ECO:0000269|PubMed:14764885,
CC       ECO:0000269|PubMed:17935689, 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}; Peripheral membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00589, 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}; Lumenal side {ECO:0000255|HAMAP-
CC       Rule:MF_00589, 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}. Note=Associated with photosystem II at
CC       the lumenal side of the thylakoid membrane.
CC   -!- MASS SPECTROMETRY: Mass=11649; Mass_error=8; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19219048};
CC   -!- MASS SPECTROMETRY: Mass=11641; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20558739};
CC   -!- SIMILARITY: Belongs to the PsbU family. {ECO:0000255|HAMAP-
CC       Rule:MF_00589}.
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DR   EMBL; AB052848; BAB20625.1; -; Genomic_DNA.
DR   EMBL; BA000039; BAC09961.1; -; Genomic_DNA.
DR   RefSeq; NP_683199.1; NC_004113.1.
DR   RefSeq; WP_011058241.1; NC_004113.1.
DR   PDB; 1S5L; X-ray; 3.50 A; U/u=1-134.
DR   PDB; 2AXT; X-ray; 3.00 A; U/u=31-134.
DR   PDB; 3KZI; X-ray; 3.60 A; U=31-134.
DR   PDB; 4FBY; X-ray; 6.56 A; U/h=31-134.
DR   PDB; 4IXQ; X-ray; 5.70 A; U/u=1-134.
DR   PDB; 4IXR; X-ray; 5.90 A; U/u=1-134.
DR   PDB; 4PBU; X-ray; 5.00 A; U/u=38-134.
DR   PDB; 4PJ0; X-ray; 2.44 A; U/u=1-134.
DR   PDB; 4RVY; X-ray; 5.50 A; U/u=38-134.
DR   PDB; 4TNH; X-ray; 4.90 A; U/u=1-134.
DR   PDB; 4TNI; X-ray; 4.60 A; U/u=1-134.
DR   PDB; 4TNJ; X-ray; 4.50 A; U/u=1-134.
DR   PDB; 4TNK; X-ray; 5.20 A; U/u=1-134.
DR   PDB; 4V62; X-ray; 2.90 A; AU/BU=31-134.
DR   PDB; 4V82; X-ray; 3.20 A; AU/BU=31-134.
DR   PDB; 5E79; X-ray; 3.50 A; U/u=38-134.
DR   PDB; 5E7C; X-ray; 4.50 A; U/u=38-134.
DR   PDB; 5H2F; X-ray; 2.20 A; U/u=38-134.
DR   PDB; 5KAF; X-ray; 3.00 A; U/u=1-134.
DR   PDB; 5KAI; X-ray; 2.80 A; U/u=1-134.
DR   PDB; 5MX2; X-ray; 2.20 A; U/u=1-134.
DR   PDB; 5TIS; X-ray; 2.25 A; U/u=1-134.
DR   PDB; 5ZZN; X-ray; 2.10 A; U/u=38-134.
DR   PDB; 6DHE; X-ray; 2.05 A; U/u=38-134.
DR   PDB; 6DHF; X-ray; 2.08 A; U/u=38-134.
DR   PDB; 6DHG; X-ray; 2.50 A; U/u=38-134.
DR   PDB; 6DHH; X-ray; 2.20 A; U/u=38-134.
DR   PDB; 6DHO; X-ray; 2.07 A; U/u=38-134.
DR   PDB; 6DHP; X-ray; 2.04 A; U/u=38-134.
DR   PDB; 6W1O; X-ray; 2.08 A; U/u=1-134.
DR   PDB; 6W1P; X-ray; 2.26 A; U/u=1-134.
DR   PDB; 6W1Q; X-ray; 2.27 A; U/u=1-134.
DR   PDB; 6W1R; X-ray; 2.23 A; U/u=1-134.
DR   PDB; 6W1T; X-ray; 2.01 A; U/u=1-134.
DR   PDB; 6W1U; X-ray; 2.09 A; U/u=1-134.
DR   PDB; 6W1V; X-ray; 2.09 A; U/u=1-134.
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; Q9F1L5; -.
DR   DIP; DIP-48501N; -.
DR   IntAct; Q9F1L5; 1.
DR   STRING; 197221.22296137; -.
DR   EnsemblBacteria; BAC09961; BAC09961; BAC09961.
DR   KEGG; tel:tll2409; -.
DR   PATRIC; fig|197221.4.peg.2532; -.
DR   eggNOG; COG1555; Bacteria.
DR   OMA; PTMAGKI; -.
DR   OrthoDB; 1626529at2; -.
DR   EvolutionaryTrace; Q9F1L5; -.
DR   Proteomes; UP000000440; Chromosome.
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:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0042549; P:photosystem II stabilization; IEA:InterPro.
DR   HAMAP; MF_00589; PSII_PsbU; 1.
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; Reference proteome; Signal; Thylakoid;
KW   Transport.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00589,
FT                   ECO:0000269|PubMed:17935689"
FT   CHAIN           31..134
FT                   /note="Photosystem II 12 kDa extrinsic protein"
FT                   /id="PRO_0000029602"
FT   HELIX           33..39
FT                   /evidence="ECO:0000244|PDB:1S5L"
FT   HELIX           42..46
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           50..52
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          54..56
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            57..59
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           62..67
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           74..82
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           88..93
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           99..108
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           109..111
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           119..122
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           123..125
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            126..128
FT                   /evidence="ECO:0000244|PDB:5ZZN"
SQ   SEQUENCE   134 AA;  15018 MW;  C75346D2DA75447F CRC64;
     MQRLGRWLAL AYFVGVSLLG WINWSAPTLA ATASTEEELV NVVDEKLGTA YGEKIDLNNT
     NIAAFIQYRG LYPTLAKLIV KNAPYESVED VLNIPGLTER QKQILRENLE HFTVTEVETA
     LVEGGDRYNN GLYK
//
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