RCEM_CERSP
ID RCEM_CERSP Reviewed; 308 AA.
AC P0C0Y9; P02953; Q9RFB8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Reaction center protein M chain;
DE AltName: Full=Photosynthetic reaction center M subunit;
GN Name=pufM;
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16593385; DOI=10.1073/pnas.80.21.6505;
RA Williams J.C., Steiner L.A., Ogden R.C., Simon M.I., Feher G.;
RT "Primary structure of the M subunit of the reaction center from
RT Rhodopseudomonas sphaeroides.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:6505-6509(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Y;
RX PubMed=2126457; DOI=10.1016/0300-9084(90)90116-x;
RA Arnoux B., Ducruix A., Astier C., Picaud M., Roth M., Reiss-Husson F.;
RT "Towards the understanding of the function of Rb sphaeroides Y wild type
RT reaction center: gene cloning, protein and detergent structures in the
RT three-dimensional crystals.";
RL Biochimie 72:525-530(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RX PubMed=6095283; DOI=10.1073/pnas.81.23.7303;
RA Williams J.C., Steiner L.A., Feher G., Simon M.I.;
RT "Primary structure of the L subunit of the reaction center from
RT Rhodopseudomonas sphaeroides.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:7303-7307(1984).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
RX PubMed=2036404; DOI=10.1021/bi00236a005;
RA Chang C.-H., El-Kabbani O., Tiede D., Norris J., Schiffer M.;
RT "Structure of the membrane-bound protein photosynthetic reaction center
RT from Rhodobacter sphaeroides.";
RL Biochemistry 30:5352-5360(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RC STRAIN=R-26;
RX PubMed=3054889; DOI=10.1073/pnas.85.22.8487;
RA Allen J.P., Feher G., Yeates T.O., Komiya H., Rees D.C.;
RT "Structure of the reaction center from Rhodobacter sphaeroides R-26:
RT protein-cofactor (quinones and Fe2+) interactions.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:8487-8491(1988).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RC STRAIN=R-26;
RX PubMed=2819866; DOI=10.1073/pnas.84.17.6162;
RA Allen J.P., Feher G., Yeates T.O., Komiya H., Rees D.C.;
RT "Structure of the reaction center from Rhodobacter sphaeroides R-26: the
RT protein subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6162-6166(1987).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS).
RX PubMed=9537989; DOI=10.1021/bi971717a;
RA McAuley-Hecht K.E., Fyfe P.K., Ridge J.P., Prince S.M., Hunter C.N.,
RA Isaacs N.W., Cogdell R.J., Jones M.R.;
RT "Structural studies of wild-type and mutant reaction centers from an
RT antenna-deficient strain of Rhodobacter sphaeroides: monitoring the optical
RT properties of the complex from bacterial cell to crystal.";
RL Biochemistry 37:4740-4750(1998).
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; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC {ECO:0000305}.
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DR EMBL; K00827; AAA26179.1; -; Genomic_DNA.
DR EMBL; X63405; CAA45001.1; -; Genomic_DNA.
DR EMBL; X63404; CAA45000.1; -; Genomic_DNA.
DR EMBL; M10206; AAA26178.1; -; Genomic_DNA.
DR PIR; A03456; WNRFMS.
DR PIR; S24213; S24213.
DR RefSeq; WP_002720420.1; NZ_WTFI01000042.1.
DR PDB; 1AIG; X-ray; 2.60 A; M/O=2-308.
DR PDB; 1AIJ; X-ray; 2.20 A; M/S=2-308.
DR PDB; 1DS8; X-ray; 2.50 A; M/S=2-307.
DR PDB; 1DV3; X-ray; 2.50 A; M/S=2-307.
DR PDB; 1DV6; X-ray; 2.50 A; M/S=2-307.
DR PDB; 1E14; X-ray; 2.70 A; M=2-308.
DR PDB; 1E6D; X-ray; 2.30 A; M=2-308.
DR PDB; 1F6N; X-ray; 2.80 A; M=2-308.
DR PDB; 1FNP; X-ray; 2.60 A; M=2-308.
DR PDB; 1FNQ; X-ray; 2.60 A; M=2-308.
DR PDB; 1JGW; X-ray; 2.80 A; M=2-308.
DR PDB; 1JGX; X-ray; 3.01 A; M=2-308.
DR PDB; 1JGY; X-ray; 2.70 A; M=2-308.
DR PDB; 1JGZ; X-ray; 2.70 A; M=2-308.
DR PDB; 1JH0; X-ray; 3.50 A; M=2-308.
DR PDB; 1K6L; X-ray; 3.10 A; M=2-308.
DR PDB; 1K6N; X-ray; 3.10 A; M=2-308.
DR PDB; 1KBY; X-ray; 2.50 A; M=2-308.
DR PDB; 1L9B; X-ray; 2.40 A; M=2-308.
DR PDB; 1L9J; X-ray; 3.25 A; M/S=2-308.
DR PDB; 1M3X; X-ray; 2.55 A; M=2-308.
DR PDB; 1MPS; X-ray; 2.55 A; M=2-308.
DR PDB; 1OGV; X-ray; 2.35 A; M=2-308.
DR PDB; 1PCR; X-ray; 2.65 A; M=2-308.
DR PDB; 1PSS; X-ray; 3.00 A; M=7-302.
DR PDB; 1PST; X-ray; 3.00 A; M=7-302.
DR PDB; 1QOV; X-ray; 2.10 A; M=2-308.
DR PDB; 1RG5; X-ray; 2.50 A; M=2-308.
DR PDB; 1RGN; X-ray; 2.80 A; M=2-308.
DR PDB; 1RQK; X-ray; 2.70 A; M=2-308.
DR PDB; 1RVJ; X-ray; 2.75 A; M=2-307.
DR PDB; 1RY5; X-ray; 2.10 A; M=2-308.
DR PDB; 1RZH; X-ray; 1.80 A; M=2-308.
DR PDB; 1RZZ; X-ray; 2.40 A; M/S=2-308.
DR PDB; 1S00; X-ray; 2.60 A; M/S=2-308.
DR PDB; 1UMX; X-ray; 2.80 A; M=2-308.
DR PDB; 1YF6; X-ray; 2.25 A; M=2-308.
DR PDB; 1YST; X-ray; 3.00 A; M=2-306.
DR PDB; 1Z9J; X-ray; 4.50 A; B=2-308.
DR PDB; 1Z9K; X-ray; 4.60 A; B=2-308.
DR PDB; 2BNP; X-ray; 2.70 A; B=2-308.
DR PDB; 2BNS; X-ray; 2.50 A; B=2-308.
DR PDB; 2BOZ; X-ray; 2.40 A; M=2-308.
DR PDB; 2GMR; X-ray; 2.50 A; M=2-308.
DR PDB; 2GNU; X-ray; 2.20 A; M=3-302.
DR PDB; 2HG3; X-ray; 2.70 A; M=2-308.
DR PDB; 2HG9; X-ray; 2.45 A; M=2-308.
DR PDB; 2HH1; X-ray; 2.55 A; M=2-308.
DR PDB; 2HHK; X-ray; 2.50 A; M=2-308.
DR PDB; 2HIT; X-ray; 2.75 A; M=2-308.
DR PDB; 2HJ6; X-ray; 3.00 A; M=2-308.
DR PDB; 2J8C; X-ray; 1.87 A; M=2-308.
DR PDB; 2J8D; X-ray; 2.07 A; M=2-308.
DR PDB; 2JIY; X-ray; 2.20 A; M=1-308.
DR PDB; 2JJ0; X-ray; 2.80 A; M=2-308.
DR PDB; 2RCR; X-ray; 3.10 A; M=2-308.
DR PDB; 2UWS; X-ray; 2.90 A; M=2-308.
DR PDB; 2UWT; X-ray; 2.50 A; M=2-308.
DR PDB; 2UWU; X-ray; 2.04 A; M=2-308.
DR PDB; 2UWV; X-ray; 2.13 A; M=2-308.
DR PDB; 2UWW; X-ray; 2.05 A; M=2-308.
DR PDB; 2UX3; X-ray; 2.50 A; M=2-308.
DR PDB; 2UX4; X-ray; 2.51 A; M=2-308.
DR PDB; 2UX5; X-ray; 2.21 A; M=2-308.
DR PDB; 2UXJ; X-ray; 2.25 A; M=2-308.
DR PDB; 2UXK; X-ray; 2.31 A; M=2-308.
DR PDB; 2UXL; X-ray; 2.88 A; M=2-308.
DR PDB; 2UXM; X-ray; 2.70 A; M=2-308.
DR PDB; 3DSY; X-ray; 3.00 A; M=2-308.
DR PDB; 3DTA; X-ray; 3.20 A; M=2-308.
DR PDB; 3DTR; X-ray; 3.10 A; M=2-308.
DR PDB; 3DTS; X-ray; 3.10 A; M=2-308.
DR PDB; 3DU2; X-ray; 3.10 A; M=2-308.
DR PDB; 3DU3; X-ray; 2.80 A; M=2-308.
DR PDB; 3DUQ; X-ray; 2.70 A; M=2-308.
DR PDB; 3I4D; X-ray; 2.01 A; M=2-308.
DR PDB; 3V3Y; X-ray; 2.80 A; M=2-303.
DR PDB; 3V3Z; X-ray; 2.90 A; M=2-303.
DR PDB; 3ZUM; X-ray; 2.50 A; M=2-308.
DR PDB; 3ZUW; X-ray; 2.31 A; M=2-308.
DR PDB; 4H99; X-ray; 2.97 A; M=2-303.
DR PDB; 4H9L; X-ray; 2.77 A; M=2-303.
DR PDB; 4HBH; X-ray; 2.93 A; M=2-303.
DR PDB; 4HBJ; X-ray; 2.74 A; M=2-303.
DR PDB; 4IN7; X-ray; 2.85 A; M=2-303.
DR PDB; 4LWY; X-ray; 2.90 A; M=1-303.
DR PDB; 4N7K; X-ray; 2.85 A; M=2-304.
DR PDB; 4RCR; X-ray; 2.80 A; M=2-308.
DR PDB; 4TQQ; X-ray; 2.50 A; M=2-303.
DR PDB; 4V9G; X-ray; 7.78 A; AM/BM=1-308.
DR PDB; 5LSE; X-ray; 2.50 A; M=2-308.
DR PDB; 5V33; X-ray; 3.49 A; M=2-303.
DR PDB; 6Z02; X-ray; 2.10 A; M=2-303.
DR PDB; 6Z1J; X-ray; 2.10 A; M=2-303.
DR PDB; 6Z27; X-ray; 2.10 A; M=2-303.
DR PDB; 7MH3; X-ray; 2.30 A; M=1-308.
DR PDB; 7MH4; X-ray; 2.48 A; M=1-308.
DR PDB; 7MH5; X-ray; 2.85 A; M=1-308.
DR PDB; 7MH8; X-ray; 2.75 A; M=1-308.
DR PDB; 7MH9; X-ray; 3.10 A; M=1-308.
DR PDBsum; 1AIG; -.
DR PDBsum; 1AIJ; -.
DR PDBsum; 1DS8; -.
DR PDBsum; 1DV3; -.
DR PDBsum; 1DV6; -.
DR PDBsum; 1E14; -.
DR PDBsum; 1E6D; -.
DR PDBsum; 1F6N; -.
DR PDBsum; 1FNP; -.
DR PDBsum; 1FNQ; -.
DR PDBsum; 1JGW; -.
DR PDBsum; 1JGX; -.
DR PDBsum; 1JGY; -.
DR PDBsum; 1JGZ; -.
DR PDBsum; 1JH0; -.
DR PDBsum; 1K6L; -.
DR PDBsum; 1K6N; -.
DR PDBsum; 1KBY; -.
DR PDBsum; 1L9B; -.
DR PDBsum; 1L9J; -.
DR PDBsum; 1M3X; -.
DR PDBsum; 1MPS; -.
DR PDBsum; 1OGV; -.
DR PDBsum; 1PCR; -.
DR PDBsum; 1PSS; -.
DR PDBsum; 1PST; -.
DR PDBsum; 1QOV; -.
DR PDBsum; 1RG5; -.
DR PDBsum; 1RGN; -.
DR PDBsum; 1RQK; -.
DR PDBsum; 1RVJ; -.
DR PDBsum; 1RY5; -.
DR PDBsum; 1RZH; -.
DR PDBsum; 1RZZ; -.
DR PDBsum; 1S00; -.
DR PDBsum; 1UMX; -.
DR PDBsum; 1YF6; -.
DR PDBsum; 1YST; -.
DR PDBsum; 1Z9J; -.
DR PDBsum; 1Z9K; -.
DR PDBsum; 2BNP; -.
DR PDBsum; 2BNS; -.
DR PDBsum; 2BOZ; -.
DR PDBsum; 2GMR; -.
DR PDBsum; 2GNU; -.
DR PDBsum; 2HG3; -.
DR PDBsum; 2HG9; -.
DR PDBsum; 2HH1; -.
DR PDBsum; 2HHK; -.
DR PDBsum; 2HIT; -.
DR PDBsum; 2HJ6; -.
DR PDBsum; 2J8C; -.
DR PDBsum; 2J8D; -.
DR PDBsum; 2JIY; -.
DR PDBsum; 2JJ0; -.
DR PDBsum; 2RCR; -.
DR PDBsum; 2UWS; -.
DR PDBsum; 2UWT; -.
DR PDBsum; 2UWU; -.
DR PDBsum; 2UWV; -.
DR PDBsum; 2UWW; -.
DR PDBsum; 2UX3; -.
DR PDBsum; 2UX4; -.
DR PDBsum; 2UX5; -.
DR PDBsum; 2UXJ; -.
DR PDBsum; 2UXK; -.
DR PDBsum; 2UXL; -.
DR PDBsum; 2UXM; -.
DR PDBsum; 3DSY; -.
DR PDBsum; 3DTA; -.
DR PDBsum; 3DTR; -.
DR PDBsum; 3DTS; -.
DR PDBsum; 3DU2; -.
DR PDBsum; 3DU3; -.
DR PDBsum; 3DUQ; -.
DR PDBsum; 3I4D; -.
DR PDBsum; 3V3Y; -.
DR PDBsum; 3V3Z; -.
DR PDBsum; 3ZUM; -.
DR PDBsum; 3ZUW; -.
DR PDBsum; 4H99; -.
DR PDBsum; 4H9L; -.
DR PDBsum; 4HBH; -.
DR PDBsum; 4HBJ; -.
DR PDBsum; 4IN7; -.
DR PDBsum; 4LWY; -.
DR PDBsum; 4N7K; -.
DR PDBsum; 4RCR; -.
DR PDBsum; 4TQQ; -.
DR PDBsum; 4V9G; -.
DR PDBsum; 5LSE; -.
DR PDBsum; 5V33; -.
DR PDBsum; 6Z02; -.
DR PDBsum; 6Z1J; -.
DR PDBsum; 6Z27; -.
DR PDBsum; 7MH3; -.
DR PDBsum; 7MH4; -.
DR PDBsum; 7MH5; -.
DR PDBsum; 7MH8; -.
DR PDBsum; 7MH9; -.
DR AlphaFoldDB; P0C0Y9; -.
DR SMR; P0C0Y9; -.
DR DIP; DIP-60490N; -.
DR IntAct; P0C0Y9; 1.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR DrugBank; DB08215; Terbutryn.
DR DrugBank; DB08690; Ubiquinone Q2.
DR TCDB; 3.E.2.1.1; the photosynthetic reaction center (prc) family.
DR GeneID; 57470574; -.
DR GeneID; 67446989; -.
DR OMA; IFPHLDW; -.
DR OrthoDB; 634532at2; -.
DR EvolutionaryTrace; P0C0Y9; -.
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 3D-structure; Bacteriochlorophyll; Chlorophyll; Chromophore;
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 CHAIN 2..308
FT /note="Reaction center protein M chain"
FT /id="PRO_0000090417"
FT TRANSMEM 54..80
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 183
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 203
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 220
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 235
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 253
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT BINDING 267
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT CONFLICT 141
FT /note="L -> M (in Ref. 2; CAA45001)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:2J8C"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:1RZH"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1PSS"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:1RZH"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3V3Y"
FT HELIX 55..78
FT /evidence="ECO:0007829|PDB:1RZH"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:1RZH"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1RZH"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2RCR"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 114..140
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 146..162
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 180..193
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 201..226
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:1RZH"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 235..240
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 244..257
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 265..286
FT /evidence="ECO:0007829|PDB:1RZH"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:1RZH"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:1YST"
FT HELIX 295..301
FT /evidence="ECO:0007829|PDB:1RZH"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:2J8D"
SQ SEQUENCE 308 AA; 34509 MW; 30B3737DF8658250 CRC64;
MAEYQNIFSQ VQVRGPADLG MTEDVNLANR SGVGPFSTLL GWFGNAQLGP IYLGSLGVLS
LFSGLMWFFT IGIWFWYQAG WNPAVFLRDL FFFSLEPPAP EYGLSFAAPL KEGGLWLIAS
FFMFVAVWSW WGRTYLRAQA LGMGKHTAWA FLSAIWLWMV LGFIRPILMG SWSEAVPYGI
FSHLDWTNNF SLVHGNLFYN PFHGLSIAFL YGSALLFAMH GATILAVSRF GGERELEQIA
DRGTAAERAA LFWRWTMGFN ATMEGIHRWA IWMAVLVTLT GGIGILLSGT VVDNWYVWGQ
NHGMAPLN
