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Entry: Q8DHA7
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ID   PSBM_THEEB              Reviewed;          36 AA.
AC   Q8DHA7;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   10-FEB-2021, entry version 108.
DE   RecName: Full=Photosystem II reaction center protein M {ECO:0000255|HAMAP-Rule:MF_00438};
DE            Short=PSII-M {ECO:0000255|HAMAP-Rule:MF_00438};
GN   Name=psbM {ECO:0000255|HAMAP-Rule:MF_00438}; OrderedLocusNames=tsl2052;
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 1-15, 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   [3]
RP   PROTEIN SEQUENCE OF 1-6, COFACTOR, AND SUBCELLULAR LOCATION.
RX   PubMed=17967798; DOI=10.1093/pcp/pcm148;
RA   Iwai M., Suzuki T., Dohmae N., Inoue Y., Ikeuchi M.;
RT   "Absence of the PsbZ subunit prevents association of PsbK and Ycf12 with
RT   the PSII complex in the thermophilic cyanobacterium Thermosynechococcus
RT   elongatus BP-1.";
RL   Plant Cell Physiol. 48:1758-1763(2007).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21195048; DOI=10.1016/j.bbabio.2010.12.013;
RA   Kawakami K., Umena Y., Iwai M., Kawabata Y., Ikeuchi M., Kamiya N.,
RA   Shen J.R.;
RT   "Roles of PsbI and PsbM in photosystem II dimer formation and stability
RT   studied by deletion mutagenesis and X-ray crystallography.";
RL   Biochim. Biophys. Acta 1807:319-325(2011).
RN   [5]
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   [6]
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   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP   COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, FORMYLATION AT MET-1, MASS
RP   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   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP   COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, FORMYLATION AT MET-1, AND MASS
RP   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   [9]
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   [10]
RP   X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) 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   [11]
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   [12]
RP   X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 1-34 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   [13]
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). 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. This
CC       subunit is found at the monomer-monomer interface. Probably involved in
CC       dimerization of PSII; at the monomer-monomer interface the only
CC       protein-protein contacts observed are between the 2 PsbM subunits.
CC       Lipids, chlorophylls and carotenoids contribute strongly to PSII
CC       dimerization. {ECO:0000255|HAMAP-Rule:MF_00438,
CC       ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21195048, 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:17967798, 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_00438,
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_00438, ECO:0000269|PubMed:14764885,
CC       ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689,
CC       ECO:0000269|PubMed:17967798, 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_00438,
CC       ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:17967798,
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=4011; Mass_error=2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19219048};
CC   -!- MASS SPECTROMETRY: Mass=4009; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20558739};
CC   -!- DISRUPTION PHENOTYPE: Decreased yields of PSII dimers with increased
CC       PSII monomers, slightly slower photoautotrophic growth, about 20% less
CC       oxygen evolution. Formed PSII dimers are less stable than wild-type.
CC       {ECO:0000269|PubMed:21195048}.
CC   -!- SIMILARITY: Belongs to the PsbM family. {ECO:0000255|HAMAP-
CC       Rule:MF_00438}.
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DR   EMBL; BA000039; BAC09604.1; -; Genomic_DNA.
DR   RefSeq; NP_682842.1; NC_004113.1.
DR   RefSeq; WP_011057887.1; NC_004113.1.
DR   PDB; 1S5L; X-ray; 3.50 A; M/m=1-36.
DR   PDB; 2AXT; X-ray; 3.00 A; M/m=1-36.
DR   PDB; 3KZI; X-ray; 3.60 A; M=1-36.
DR   PDB; 4FBY; X-ray; 6.56 A; M/e=1-36.
DR   PDB; 4IXQ; X-ray; 5.70 A; M/m=1-36.
DR   PDB; 4IXR; X-ray; 5.90 A; M/m=1-36.
DR   PDB; 4PBU; X-ray; 5.00 A; M/m=1-34.
DR   PDB; 4PJ0; X-ray; 2.44 A; M/m=1-36.
DR   PDB; 4RVY; X-ray; 5.50 A; M/m=1-34.
DR   PDB; 4TNH; X-ray; 4.90 A; M/m=1-36.
DR   PDB; 4TNI; X-ray; 4.60 A; M/m=1-36.
DR   PDB; 4TNJ; X-ray; 4.50 A; M/m=1-36.
DR   PDB; 4TNK; X-ray; 5.20 A; M/m=1-36.
DR   PDB; 4V62; X-ray; 2.90 A; AM/BM=1-36.
DR   PDB; 4V82; X-ray; 3.20 A; AM/BM=1-36.
DR   PDB; 5E79; X-ray; 3.50 A; M/m=1-34.
DR   PDB; 5E7C; X-ray; 4.50 A; M/m=1-34.
DR   PDB; 5KAF; X-ray; 3.00 A; M/m=2-36.
DR   PDB; 5KAI; X-ray; 2.80 A; M/m=2-36.
DR   PDB; 5MX2; X-ray; 2.20 A; M/m=1-36.
DR   PDB; 5TIS; X-ray; 2.25 A; M/m=1-36.
DR   PDB; 5ZZN; X-ray; 2.10 A; M/m=1-34.
DR   PDB; 6DHE; X-ray; 2.05 A; M/m=1-33.
DR   PDB; 6DHF; X-ray; 2.08 A; M/m=1-33.
DR   PDB; 6DHG; X-ray; 2.50 A; M/m=1-33.
DR   PDB; 6DHH; X-ray; 2.20 A; M/m=1-33.
DR   PDB; 6DHO; X-ray; 2.07 A; M/m=1-33.
DR   PDB; 6DHP; X-ray; 2.04 A; M/m=1-33.
DR   PDB; 6W1O; X-ray; 2.08 A; M/m=1-36.
DR   PDB; 6W1P; X-ray; 2.26 A; M/m=1-36.
DR   PDB; 6W1Q; X-ray; 2.27 A; M/m=1-36.
DR   PDB; 6W1R; X-ray; 2.23 A; M/m=1-36.
DR   PDB; 6W1T; X-ray; 2.01 A; M/m=1-36.
DR   PDB; 6W1U; X-ray; 2.09 A; M/m=1-36.
DR   PDB; 6W1V; X-ray; 2.09 A; M/m=1-36.
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; 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; Q8DHA7; -.
DR   DIP; DIP-48498N; -.
DR   IntAct; Q8DHA7; 1.
DR   STRING; 197221.22295779; -.
DR   EnsemblBacteria; BAC09604; BAC09604; BAC09604.
DR   KEGG; tel:tsl2052; -.
DR   OrthoDB; 2087962at2; -.
DR   EvolutionaryTrace; Q8DHA7; -.
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:0019684; P:photosynthesis, light reaction; IEA:InterPro.
DR   HAMAP; MF_00438; PSII_PsbM; 1.
DR   InterPro; IPR007826; PSII_PsbM.
DR   InterPro; IPR037269; PSII_PsbM_sf.
DR   Pfam; PF05151; PsbM; 1.
DR   SUPFAM; SSF161033; SSF161033; 1.
DR   TIGRFAMs; TIGR03038; PS_II_psbM; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Formylation; Membrane;
KW   Photosynthesis; Photosystem II; Reaction center; Reference proteome;
KW   Thylakoid; Transmembrane; Transmembrane helix.
FT   CHAIN           1..36
FT                   /note="Photosystem II reaction center protein M"
FT                   /id="PRO_0000217585"
FT   TOPO_DOM        1..8
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        9..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        23..36
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   MOD_RES         1
FT                   /note="N-formylmethionine"
FT                   /evidence="ECO:0000269|PubMed:19219048,
FT                   ECO:0000269|PubMed:20558739"
FT   HELIX           7..30
FT                   /evidence="ECO:0000244|PDB:5ZZN"
FT   HELIX           31..33
FT                   /evidence="ECO:0000244|PDB:2AXT"
SQ   SEQUENCE   36 AA;  3981 MW;  C7CE190547B00AD4 CRC64;
     MEVNQLGLIA TALFVLVPSV FLIILYVQTE SQQKSS
//
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