PSBB_THEVL
ID PSBB_THEVL Reviewed; 505 AA.
AC D0VWR1;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Photosystem II CP47 reaction center protein {ECO:0000255|HAMAP-Rule:MF_01495};
DE AltName: Full=PSII 47 kDa protein {ECO:0000255|HAMAP-Rule:MF_01495};
DE AltName: Full=Protein CP-47 {ECO:0000255|HAMAP-Rule:MF_01495};
DE Flags: Fragment;
GN Name=psbB {ECO:0000255|HAMAP-Rule:MF_01495};
OS Thermostichus vulcanus (Synechococcus vulcanus).
OC Bacteria; Cyanobacteria; Thermostichales; Thermostichaceae; Thermostichus.
OX NCBI_TaxID=32053;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12518057; DOI=10.1073/pnas.0135651100;
RA Kamiya N., Shen J.-R.;
RT "Crystal structure of oxygen-evolving photosystem II from
RT Thermosynechococcus vulcanus at 3.7-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:98-103(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 1-488 IN COMPLEX WITH CHLOROPHYLL
RP A IN PHOTOSYSTEM II, FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19433803; DOI=10.1073/pnas.0812797106;
RA Kawakami K., Umena Y., Kamiya N., Shen J.R.;
RT "Location of chloride and its possible functions in oxygen-evolving
RT photosystem II revealed by X-ray crystallography.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8567-8572(2009).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-488 IN COMPLEX WITH CHLOROPHYLL
RP A IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=21499260; DOI=10.1038/nature09913;
RA Umena Y., Kawakami K., Shen J.R., Kamiya N.;
RT "Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9
RT A.";
RL Nature 473:55-60(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23426624; DOI=10.1073/pnas.1219922110;
RA Koua F.H., Umena Y., Kawakami K., Shen J.R.;
RT "Structure of Sr-substituted photosystem II at 2.1 A resolution and its
RT implications in the mechanism of water oxidation.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:3889-3894(2013).
CC -!- FUNCTION: One of the components of the core complex of photosystem II
CC (PSII). It binds chlorophyll and helps catalyze the primary light-
CC induced photochemical processes of PSII. PSII is a light-driven
CC water:plastoquinone oxidoreductase, using light energy to abstract
CC electrons from H(2)O, generating O(2) and a proton gradient
CC subsequently used for ATP formation. {ECO:0000255|HAMAP-Rule:MF_01495,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:23426624}.
CC -!- COFACTOR:
CC Note=Binds multiple chlorophylls. PSII binds additional chlorophylls,
CC carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_01495,
CC ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803,
CC ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624};
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_01495,
CC ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803,
CC ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01495, ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC ECO:0000269|PubMed:23426624}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01495, ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC ECO:0000269|PubMed:23426624}.
CC -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01495, ECO:0000305}.
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DR PDB; 1IZL; X-ray; 3.70 A; B/L=1-505.
DR PDB; 3A0B; X-ray; 3.70 A; B/b=1-488.
DR PDB; 3A0H; X-ray; 4.00 A; B/b=1-488.
DR PDB; 3WU2; X-ray; 1.90 A; B/b=1-504.
DR PDB; 4IL6; X-ray; 2.10 A; B/b=1-505.
DR PDB; 4UB6; X-ray; 1.95 A; B/b=1-505.
DR PDB; 4UB8; X-ray; 1.95 A; B/b=1-505.
DR PDB; 5B5E; X-ray; 1.87 A; B/b=1-505.
DR PDB; 5B66; X-ray; 1.85 A; B/b=1-505.
DR PDB; 5GTH; X-ray; 2.50 A; B/b=1-505.
DR PDB; 5GTI; X-ray; 2.50 A; B/b=1-505.
DR PDB; 5V2C; X-ray; 1.90 A; B/b=1-504.
DR PDB; 5WS5; X-ray; 2.35 A; B/b=1-505.
DR PDB; 5WS6; X-ray; 2.35 A; B/b=1-505.
DR PDB; 6JLJ; X-ray; 2.15 A; B/b=1-505.
DR PDB; 6JLK; X-ray; 2.15 A; B/b=1-505.
DR PDB; 6JLL; X-ray; 2.15 A; B/b=1-505.
DR PDB; 6JLM; X-ray; 2.35 A; B/b=1-505.
DR PDB; 6JLN; X-ray; 2.40 A; B/b=1-505.
DR PDB; 6JLO; X-ray; 2.40 A; B/b=1-505.
DR PDB; 6JLP; X-ray; 2.50 A; B/b=1-505.
DR PDB; 7CJI; X-ray; 2.35 A; B/b=1-505.
DR PDB; 7CJJ; X-ray; 2.40 A; B/b=1-505.
DR PDB; 7COU; X-ray; 2.25 A; B/b=1-505.
DR PDB; 7CZL; EM; 3.78 A; B/b=1-505.
DR PDB; 7D1T; EM; 1.95 A; B/b=1-505.
DR PDB; 7D1U; EM; 2.08 A; B/b=1-505.
DR PDB; 7DXA; EM; 3.14 A; b=1-505.
DR PDB; 7DXH; EM; 3.14 A; b=1-505.
DR PDB; 7EDA; EM; 2.78 A; B=1-504.
DR PDBsum; 1IZL; -.
DR PDBsum; 3A0B; -.
DR PDBsum; 3A0H; -.
DR PDBsum; 3WU2; -.
DR PDBsum; 4IL6; -.
DR PDBsum; 4UB6; -.
DR PDBsum; 4UB8; -.
DR PDBsum; 5B5E; -.
DR PDBsum; 5B66; -.
DR PDBsum; 5GTH; -.
DR PDBsum; 5GTI; -.
DR PDBsum; 5V2C; -.
DR PDBsum; 5WS5; -.
DR PDBsum; 5WS6; -.
DR PDBsum; 6JLJ; -.
DR PDBsum; 6JLK; -.
DR PDBsum; 6JLL; -.
DR PDBsum; 6JLM; -.
DR PDBsum; 6JLN; -.
DR PDBsum; 6JLO; -.
DR PDBsum; 6JLP; -.
DR PDBsum; 7CJI; -.
DR PDBsum; 7CJJ; -.
DR PDBsum; 7COU; -.
DR PDBsum; 7CZL; -.
DR PDBsum; 7D1T; -.
DR PDBsum; 7D1U; -.
DR PDBsum; 7DXA; -.
DR PDBsum; 7DXH; -.
DR PDBsum; 7EDA; -.
DR AlphaFoldDB; D0VWR1; -.
DR SMR; D0VWR1; -.
DR DIP; DIP-61464N; -.
DR IntAct; D0VWR1; 1.
DR EvolutionaryTrace; D0VWR1; -.
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:0016168; F:chlorophyll 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 HAMAP; MF_01495; PSII_PsbB_CP47; 1.
DR InterPro; IPR000932; PS_antenna-like.
DR InterPro; IPR036001; PS_II_antenna-like_sf.
DR InterPro; IPR017486; PSII_PsbB.
DR PANTHER; PTHR33180; PTHR33180; 1.
DR Pfam; PF00421; PSII; 1.
DR SUPFAM; SSF161077; SSF161077; 1.
DR TIGRFAMs; TIGR03039; PS_II_CP47; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chlorophyll; Chromophore; Magnesium; Membrane; Metal-binding;
KW Photosynthesis; Photosystem II; Thylakoid; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..505
FT /note="Photosystem II CP47 reaction center protein"
FT /id="PRO_0000422600"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 20..35
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01495,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 36..99
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 100..114
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01495,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 115..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 139..155
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01495,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 156..201
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 202..217
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01495,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 218..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 236..251
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01495,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 252..455
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 456..471
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01495,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 472..505
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21499260"
FT BINDING 8
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="2"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21499260"
FT BINDING 22
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21499260"
FT BINDING 25
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="4"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21499260"
FT BINDING 99
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="8"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21499260"
FT BINDING 113
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="11"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21499260"
FT BINDING 141
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21499260"
FT BINDING 156
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="10"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21499260"
FT BINDING 200
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="14"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21499260"
FT BINDING 201
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="9"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21499260"
FT BINDING 215
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="13"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21499260"
FT BINDING 454
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="7"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21499260"
FT BINDING 465
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="16"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21499260"
FT BINDING 468
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21499260"
FT NON_TER 1
FT NON_TER 505
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 15..43
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:7COU"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:7DXA"
FT HELIX 92..115
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 134..154
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:7DXA"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 194..217
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 228..231
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 233..257
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:7EDA"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 278..292
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 297..302
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 306..311
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:4UB6"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 335..346
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:7DXA"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:7DXA"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 397..403
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 404..407
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:7EDA"
FT HELIX 413..423
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 426..432
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 434..437
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 446..473
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 491..497
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:5B66"
SQ SEQUENCE 505 AA; 56017 MW; 26086E2C5B573647 CRC64;
GLPWYRVHTV LINDPGRLIA AHLMHTALVA GWAGSMALYE LATFDPSDPV LNPMWRQGMF
VLPFMARLGV TGSWSGWSIT GETGIDPGFW SFEGVALAHI VLSGLLFLAA CWHWVYWDLE
LFRDPRTGEP ALDLPKMFGI HLFLAGLLCF GFGAFHLTGL FGPGMWVSDP YGLTGSVQPV
APEWGPDGFN PYNPGGVVAH HIAAGIVGII AGLFHILVRP PQRLYKALRM GNIETVLSSS
IAAVFFAAFV VAGTMWYGSA TTPIELFGPT RYQWDSSYFQ QEINRRVQAS LASGATLEEA
WSAIPEKLAF YDYIGNNPAK GGLFRTGPMN KGDGIAQAWK GHAVFRNKEG EELFVRRMPA
FFESFPVILT DKNGVVKADI PFRRAESKYS FEQQGVTVSF YGGELNGQTF TDPPTVKSYA
RKAIFGEIFE FDTETLNSDG IFRTSPRGWF TFAHAVFALL FFFGHIWHGA RTLFRDVFSG
IDPELSPEQV EWGFYQKVGD VTTRK
