PSBM_SYNY3
ID PSBM_SYNY3 Reviewed; 35 AA.
AC P72701;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=sml0003;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP PROTEIN SEQUENCE OF 1-9, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=12069591; DOI=10.1021/bi026012+;
RA Kashino Y., Lauber W.M., Carroll J.A., Wang Q., Whitmarsh J., Satoh K.,
RA Pakrasi H.B.;
RT "Proteomic analysis of a highly active photosystem II preparation from the
RT cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel
RT polypeptides.";
RL Biochemistry 41:8004-8012(2002).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=18834146; DOI=10.1021/bi800804h;
RA Bentley F.K., Luo H., Dilbeck P., Burnap R.L., Eaton-Rye J.J.;
RT "Effects of inactivating psbM and psbT on photodamage and assembly of
RT photosystem II in Synechocystis sp. PCC 6803.";
RL Biochemistry 47:11637-11646(2008).
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 (By similarity).
CC Involved in assembly of monomeric PSII from the CP43-less intermediate.
CC {ECO:0000255|HAMAP-Rule:MF_00438, ECO:0000269|PubMed:18834146}.
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 -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00438, ECO:0000269|PubMed:12069591}; Single-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00438}.
CC -!- DISRUPTION PHENOTYPE: Decreased photoautotrophic growth. Decreased
CC assembly of PSII monomers and dimers, increased levels of the CP43-less
CC intermediate. A double psbM-psbT mutants only assembles PSII monomers,
CC not PSII dimers. A double psbM-psb27 mutant is incapable of
CC photoautotrophic growth, but does assemble the CP43-less assembly
CC intermediate. Cells are light sensitive and rapidly photoinactivated;
CC recovery requires protein synthesis and can occur in the dark.
CC {ECO:0000269|PubMed:18834146}.
CC -!- SIMILARITY: Belongs to the PsbM family. {ECO:0000255|HAMAP-
CC Rule:MF_00438}.
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DR EMBL; BA000022; BAA16708.1; -; Genomic_DNA.
DR PIR; S74556; S74556.
DR PDB; 6WJ6; EM; 2.58 A; M=1-35.
DR PDB; 7N8O; EM; 1.93 A; M/m=1-35.
DR PDB; 7RCV; EM; 2.01 A; M/m=1-35.
DR PDBsum; 6WJ6; -.
DR PDBsum; 7N8O; -.
DR PDBsum; 7RCV; -.
DR AlphaFoldDB; P72701; -.
DR SMR; P72701; -.
DR IntAct; P72701; 5.
DR STRING; 1148.1651781; -.
DR PaxDb; P72701; -.
DR EnsemblBacteria; BAA16708; BAA16708; BAA16708.
DR KEGG; syn:sml0003; -.
DR InParanoid; P72701; -.
DR BioCyc; MetaCyc:PSBM-MON; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030096; C:plasma membrane-derived thylakoid photosystem II; IDA:UniProtKB.
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; Membrane; Photosynthesis;
KW Photosystem II; Reaction center; Reference proteome; Thylakoid;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..35
FT /note="Photosystem II reaction center protein M"
FT /id="PRO_0000217589"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00438"
FT HELIX 7..28
FT /evidence="ECO:0007829|PDB:7N8O"
SQ SEQUENCE 35 AA; 3882 MW; EFDEBFECC272AA3B CRC64;
MQVNNLGFIA SILFVLVPTV FLLILFIQTG KQSES
