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RCEM_RHORU
ID   RCEM_RHORU              Reviewed;         306 AA.
AC   P10718;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Reaction center protein M chain;
DE   AltName: Full=Photosynthetic reaction center M subunit;
GN   Name=pufM;
OS   Rhodospirillum rubrum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=1085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2836391; DOI=10.1016/s0021-9258(18)68545-x;
RA   Belanger G., Berard J., Corriveau P., Gingras G.;
RT   "The structural genes coding for the L and M subunits of Rhodospirillum
RT   rubrum photoreaction center.";
RL   J. Biol. Chem. 263:7632-7638(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-51.
RX   PubMed=6199280; DOI=10.1515/bchm2.1983.364.2.1765;
RA   Theiler R., Suter F., Zuber H.;
RT   "N-terminal sequences of subunits L and M of the photosynthetic reaction
RT   centre from Rhodospirillum rubrum G-9+. Separation of the subunits by gel
RT   filtration on hydroxypropylated Sephadex G 100 in organic solvents.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 364:1765-1776(1983).
CC   -!- FUNCTION: The reaction center is a membrane-bound complex that mediates
CC       the initial photochemical event in the electron transfer process of
CC       photosynthesis.
CC   -!- SUBUNIT: Reaction center is composed of four bacteriochlorophylls, two
CC       bacteriopheophytins, two ubiquinones, one iron, and three highly
CC       hydrophobic polypeptide chains (designated L, M, and H).
CC   -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC       {ECO:0000305}.
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DR   EMBL; J03731; AAA26465.1; -; Genomic_DNA.
DR   PIR; B28170; B28170.
DR   AlphaFoldDB; P10718; -.
DR   SMR; P10718; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030077; C:plasma membrane light-harvesting complex; IEA:InterPro.
DR   GO; GO:0042717; C:plasma membrane-derived chromatophore membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042314; F:bacteriochlorophyll binding; IEA:UniProtKB-KW.
DR   GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR   CDD; cd09291; Photo-RC_M; 1.
DR   Gene3D; 1.20.85.10; -; 2.
DR   InterPro; IPR036854; Photo_II_D1/D2_sf.
DR   InterPro; IPR000484; Photo_RC_L/M.
DR   InterPro; IPR005781; Photo_RC_M.
DR   Pfam; PF00124; Photo_RC; 1.
DR   PRINTS; PR00256; REACTNCENTRE.
DR   SUPFAM; SSF81483; SSF81483; 1.
DR   TIGRFAMs; TIGR01115; pufM; 1.
DR   PROSITE; PS00244; REACTION_CENTER; 1.
PE   1: Evidence at protein level;
KW   Bacteriochlorophyll; Chlorophyll; Chromophore; Direct protein sequencing;
KW   Electron transport; Iron; Magnesium; Membrane; Metal-binding;
KW   Photosynthesis; Reaction center; Transmembrane; Transmembrane helix;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6199280"
FT   CHAIN           2..306
FT                   /note="Reaction center protein M chain"
FT                   /id="PRO_0000090419"
FT   TRANSMEM        53..79
FT                   /note="Helical"
FT   TRANSMEM        111..140
FT                   /note="Helical"
FT   TRANSMEM        143..168
FT                   /note="Helical"
FT   TRANSMEM        198..226
FT                   /note="Helical"
FT   TRANSMEM        260..286
FT                   /note="Helical"
FT   BINDING         181
FT                   /ligand="(7R,8Z)-bacteriochlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:30034"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT   BINDING         201
FT                   /ligand="(7R,8Z)-bacteriochlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:30034"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT   BINDING         218
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         233
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         251
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT   BINDING         265
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
SQ   SEQUENCE   306 AA;  34149 MW;  FE769E65AB9C3BCF CRC64;
     MSEYQNILTG VQVRTAPHSA PIAKGIFPRL GKPGFSYWLG KIGDAQIGPI YLGTTGVLSL
     VFGFFAIEII GFNLLASVNW SPMEFGRQFF WLGLEPPAAE YGLGFAPLAE GGWWQIAGFF
     LTTSILLWWV RMYRRARALK MGTHTAWAFA SAIFLFLSLG FIRPLLMGNF SESVPFGIFP
     HLEWTNSFSL NYGNFFYNPF HMLSIAFLYG SALLSAMHGA TILAVSRLGG DREVEQITDR
     GTAAERAALF WRWTMGFNAT MESIHRWAWW FAVLCTFTGA IGILLTGTVV DNWFEWGVKH
     GLAPAP
 
 
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