PSBM_THEVB
ID PSBM_THEVB Reviewed; 36 AA.
AC Q8DHA7;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
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 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 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=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 [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=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 [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=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 [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=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 [11]
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 [12]
RP X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 1-34 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 [13]
RP X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP COFACTOR, 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. 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 PDB; 7NHO; EM; 2.66 A; M=1-36.
DR PDB; 7NHP; EM; 2.72 A; M=1-36.
DR PDB; 7NHQ; EM; 2.68 A; M=1-36.
DR PDB; 7RF1; X-ray; 1.89 A; M/m=1-36.
DR PDB; 7RF2; X-ray; 2.08 A; M/m=1-36.
DR PDB; 7RF3; X-ray; 2.26 A; M/m=1-36.
DR PDB; 7RF4; X-ray; 2.27 A; M/m=1-36.
DR PDB; 7RF5; X-ray; 2.23 A; M/m=1-36.
DR PDB; 7RF6; X-ray; 2.01 A; M/m=1-36.
DR PDB; 7RF7; X-ray; 2.09 A; M/m=1-36.
DR PDB; 7RF8; 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 PDBsum; 7NHO; -.
DR PDBsum; 7NHP; -.
DR PDBsum; 7NHQ; -.
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; Q8DHA7; -.
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:0031676; C:plasma membrane-derived 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:0007829|PDB:5ZZN"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:7NHP"
SQ SEQUENCE 36 AA; 3981 MW; C7CE190547B00AD4 CRC64;
MEVNQLGLIA TALFVLVPSV FLIILYVQTE SQQKSS
