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Database: UniProt
Entry: P0A431
LinkDB: P0A431
Original site: P0A431 
ID   PSBO_THEEB              Reviewed;         272 AA.
AC   P0A431; P55221; Q54074;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   02-DEC-2020, entry version 104.
DE   RecName: Full=Photosystem II manganese-stabilizing polypeptide;
DE            Short=MSP;
DE   Flags: Precursor;
GN   Name=psbO; OrderedLocusNames=tll0444;
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   X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 27-272 IN PHOTOSYSTEM II,
RP   COFACTOR, 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   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 26-272 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   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 26-272 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   [5]
RP   X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 27-272 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   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 26-272 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   [7]
RP   X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) OF 27-272 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   [8]
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   [9]
RP   X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 30-272 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   [10]
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: Part of the oxygen-evolving complex associated with
CC       photosystem II (PSII). PSII is a light-driven water plastoquinone
CC       oxidoreductase, using light energy to abstract electrons from H(2)O,
CC       generating a proton gradient subsequently used for ATP formation.
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: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_01378, 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}; Peripheral
CC       membrane protein {ECO:0000255|HAMAP-Rule:MF_01378,
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}; Lumenal side {ECO:0000255|HAMAP-
CC       Rule:MF_01378, 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       Note=Associated with PSII on the lumenal side of the thylakoid
CC       membrane.
CC   -!- MASS SPECTROMETRY: Mass=26830; Mass_error=30; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19219048};
CC   -!- MASS SPECTROMETRY: Mass=26820; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20558739};
CC   -!- SIMILARITY: Belongs to the PsbO family. {ECO:0000305}.
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DR   EMBL; BA000039; BAC07996.1; -; Genomic_DNA.
DR   RefSeq; NP_681234.1; NC_004113.1.
DR   RefSeq; WP_011056297.1; NC_004113.1.
DR   PDB; 1S5L; X-ray; 3.50 A; O/o=27-272.
DR   PDB; 2AXT; X-ray; 3.00 A; O/o=26-272.
DR   PDB; 3KZI; X-ray; 3.60 A; O=27-272.
DR   PDB; 4FBY; X-ray; 6.56 A; O/f=27-272.
DR   PDB; 4IXQ; X-ray; 5.70 A; O/o=1-272.
DR   PDB; 4IXR; X-ray; 5.90 A; O/o=1-272.
DR   PDB; 4PBU; X-ray; 5.00 A; O/o=30-272.
DR   PDB; 4PJ0; X-ray; 2.44 A; O/o=1-272.
DR   PDB; 4RVY; X-ray; 5.50 A; O/o=30-272.
DR   PDB; 4TNH; X-ray; 4.90 A; O/o=1-272.
DR   PDB; 4TNI; X-ray; 4.60 A; O/o=1-272.
DR   PDB; 4TNJ; X-ray; 4.50 A; O/o=1-272.
DR   PDB; 4TNK; X-ray; 5.20 A; O/o=1-272.
DR   PDB; 4V62; X-ray; 2.90 A; AO/BO=26-272.
DR   PDB; 4V82; X-ray; 3.20 A; AO/BO=26-272.
DR   PDB; 5E79; X-ray; 3.50 A; O/o=30-272.
DR   PDB; 5E7C; X-ray; 4.50 A; O/o=30-272.
DR   PDB; 5H2F; X-ray; 2.20 A; O/o=30-272.
DR   PDB; 5KAF; X-ray; 3.00 A; O/o=1-272.
DR   PDB; 5KAI; X-ray; 2.80 A; O/o=1-272.
DR   PDB; 5MX2; X-ray; 2.20 A; O/o=1-272.
DR   PDB; 5TIS; X-ray; 2.25 A; O/o=1-272.
DR   PDB; 5ZZN; X-ray; 2.10 A; O/o=30-272.
DR   PDB; 6DHE; X-ray; 2.05 A; O/o=29-272.
DR   PDB; 6DHF; X-ray; 2.08 A; O/o=29-272.
DR   PDB; 6DHG; X-ray; 2.50 A; O/o=29-272.
DR   PDB; 6DHH; X-ray; 2.20 A; O/o=29-272.
DR   PDB; 6DHO; X-ray; 2.07 A; O/o=29-272.
DR   PDB; 6DHP; X-ray; 2.04 A; O/o=29-272.
DR   PDB; 6W1O; X-ray; 2.08 A; O/o=1-272.
DR   PDB; 6W1P; X-ray; 2.26 A; O/o=1-272.
DR   PDB; 6W1Q; X-ray; 2.27 A; O/o=1-272.
DR   PDB; 6W1R; X-ray; 2.23 A; O/o=1-272.
DR   PDB; 6W1T; X-ray; 2.01 A; O/o=1-272.
DR   PDB; 6W1U; X-ray; 2.09 A; O/o=1-272.
DR   PDB; 6W1V; X-ray; 2.09 A; O/o=1-272.
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; P0A431; -.
DR   DIP; DIP-48499N; -.
DR   IntAct; P0A431; 1.
DR   STRING; 197221.22294165; -.
DR   EnsemblBacteria; BAC07996; BAC07996; BAC07996.
DR   KEGG; tel:tll0444; -.
DR   PATRIC; fig|197221.4.peg.468; -.
DR   eggNOG; ENOG502Z7ZP; Bacteria.
DR   OMA; GKANDCP; -.
DR   OrthoDB; 1569080at2; -.
DR   EvolutionaryTrace; P0A431; -.
DR   Proteomes; UP000000440; Chromosome.
DR   GO; GO:0009654; C:photosystem II oxygen evolving complex; IEA:InterPro.
DR   GO; GO:0010242; F:oxygen evolving activity; IEA:InterPro.
DR   GO; GO:0010207; P:photosystem II assembly; IEA:InterPro.
DR   GO; GO:0042549; P:photosystem II stabilization; IEA:InterPro.
DR   InterPro; IPR011250; OMP/PagP_b-brl.
DR   InterPro; IPR002628; PSII_MSP.
DR   PANTHER; PTHR34058; PTHR34058; 1.
DR   Pfam; PF01716; MSP; 1.
DR   SUPFAM; SSF56925; SSF56925; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Membrane; Photosynthesis; Photosystem II; Reference proteome;
KW   Signal; Thylakoid.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:19219048,
FT                   ECO:0000269|PubMed:20558739"
FT   CHAIN           27..272
FT                   /note="Photosystem II manganese-stabilizing polypeptide"
FT                   /id="PRO_0000029567"
FT   HELIX           33..36
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            37..40
FT                   /evidence="ECO:0000244|PDB:5MX2"
FT   HELIX           41..43
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          55..57
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          60..62
FT                   /evidence="ECO:0000244|PDB:5TIS"
FT   STRAND          64..79
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          84..86
FT                   /evidence="ECO:0000244|PDB:4PJ0"
FT   STRAND          91..93
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          95..98
FT                   /evidence="ECO:0000244|PDB:1S5L"
FT   STRAND          104..113
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          119..127
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          129..135
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            136..138
FT                   /evidence="ECO:0000244|PDB:1S5L"
FT   STRAND          141..147
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          152..154
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          160..163
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          167..175
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          190..196
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           206..208
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           209..212
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          218..231
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            232..235
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          236..246
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   TURN            250..253
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   STRAND          258..271
FT                   /evidence="ECO:0000244|PDB:5ZZN"
SQ   SEQUENCE   272 AA;  29608 MW;  1F053A3453990141 CRC64;
     MKYRILMATL LAVCLGIFSL SAPAFAAKQT LTYDDIVGTG LANKCPTLDD TARGAYPIDS
     SQTYRIARLC LQPTTFLVKE EPKNKRQEAE FVPTKLVTRE TTSLDQIQGE LKVNSDGSLT
     FVEEDGIDFQ PVTVQMAGGE RIPLLFTVKN LVASTQPNVT SITTSTDFKG EFNVPSYRTA
     NFLDPKGRGL ASGYDSAIAL PQAKEEELAR ANVKRFSLTK GQISLNVAKV DGRTGEIAGT
     FESEQLSDDD MGAHEPHEVK IQGVFYASIE PA
//
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