PSBC_THEVL
ID PSBC_THEVL Reviewed; 451 AA.
AC D0VWR7;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Photosystem II CP43 reaction center protein {ECO:0000255|HAMAP-Rule:MF_01496};
DE AltName: Full=PSII 43 kDa protein {ECO:0000255|HAMAP-Rule:MF_01496};
DE AltName: Full=Protein CP-43 {ECO:0000255|HAMAP-Rule:MF_01496};
DE Flags: Fragment;
GN Name=psbC {ECO:0000255|HAMAP-Rule:MF_01496};
OS Thermostichus vulcanus (Synechococcus vulcanus).
OC Bacteria; Cyanobacteria; Thermostichales; Thermostichaceae; Thermostichus.
OX NCBI_TaxID=32053;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 11-451 IN PHOTOSYSTEM II,
RP COFACTOR, 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 5-451 IN COMPLEX WITH CA-MN4-O5
RP CLUSTER AND CHLOROPHYLL A IN PHOTOSYSTEM II, FUNCTION, COFACTOR, SUBUNIT,
RP SUBCELLULAR LOCATION, AND POSSIBLE CL(-) LIGAND.
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 5-451 IN COMPLEX WITH CA-MN4-O5
RP CLUSTER AND CHLOROPHYLL A IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR
RP 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_01496,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:23426624}.
CC -!- COFACTOR:
CC Note=Binds multiple chlorophylls and provides some of the ligands for
CC the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also
CC provide a ligand for a Cl- that is required for oxygen evolution. PSII
CC binds additional chlorophylls, carotenoids and specific lipids.
CC {ECO:0000255|HAMAP-Rule:MF_01496, ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC 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_01496,
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_01496, 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_01496, 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. PsbC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01496}.
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DR PDB; 1IZL; X-ray; 3.70 A; C/M=11-451.
DR PDB; 3A0B; X-ray; 3.70 A; C/c=5-451.
DR PDB; 3A0H; X-ray; 4.00 A; C/c=5-451.
DR PDB; 3WU2; X-ray; 1.90 A; C/c=1-451.
DR PDB; 4IL6; X-ray; 2.10 A; C/c=1-451.
DR PDB; 4UB6; X-ray; 1.95 A; C/c=1-451.
DR PDB; 4UB8; X-ray; 1.95 A; C/c=1-451.
DR PDB; 5B5E; X-ray; 1.87 A; C/c=1-451.
DR PDB; 5B66; X-ray; 1.85 A; C/c=1-451.
DR PDB; 5GTH; X-ray; 2.50 A; C/c=1-451.
DR PDB; 5GTI; X-ray; 2.50 A; C/c=1-451.
DR PDB; 5V2C; X-ray; 1.90 A; C/c=1-451.
DR PDB; 5WS5; X-ray; 2.35 A; C/c=1-451.
DR PDB; 5WS6; X-ray; 2.35 A; C/c=1-451.
DR PDB; 6JLJ; X-ray; 2.15 A; C/c=1-451.
DR PDB; 6JLK; X-ray; 2.15 A; C/c=1-451.
DR PDB; 6JLL; X-ray; 2.15 A; C/c=1-451.
DR PDB; 6JLM; X-ray; 2.35 A; C/c=1-451.
DR PDB; 6JLN; X-ray; 2.40 A; C/c=1-451.
DR PDB; 6JLO; X-ray; 2.40 A; C/c=1-451.
DR PDB; 6JLP; X-ray; 2.50 A; C/c=1-451.
DR PDB; 7CJI; X-ray; 2.35 A; C/c=1-451.
DR PDB; 7CJJ; X-ray; 2.40 A; C/c=1-451.
DR PDB; 7COU; X-ray; 2.25 A; C/c=1-451.
DR PDB; 7CZL; EM; 3.78 A; C/c=5-450.
DR PDB; 7D1T; EM; 1.95 A; C/c=1-451.
DR PDB; 7D1U; EM; 2.08 A; C/c=1-451.
DR PDB; 7DXH; EM; 3.14 A; c=1-451.
DR PDB; 7EDA; EM; 2.78 A; C=1-451.
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; 7DXH; -.
DR PDBsum; 7EDA; -.
DR AlphaFoldDB; D0VWR7; -.
DR SMR; D0VWR7; -.
DR DIP; DIP-61465N; -.
DR IntAct; D0VWR7; 1.
DR EvolutionaryTrace; D0VWR7; -.
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 Gene3D; 1.10.10.670; -; 1.
DR HAMAP; MF_01496; PSII_PsbC_CP43; 1.
DR InterPro; IPR000932; PS_antenna-like.
DR InterPro; IPR036001; PS_II_antenna-like_sf.
DR InterPro; IPR005869; PSII_PsbC.
DR InterPro; IPR044900; PSII_PsbC_sf.
DR PANTHER; PTHR33180; PTHR33180; 1.
DR Pfam; PF00421; PSII; 1.
DR SUPFAM; SSF161077; SSF161077; 1.
DR TIGRFAMs; TIGR01153; psbC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chlorophyll; Chromophore; Magnesium; Manganese; Membrane;
KW Metal-binding; Photosynthesis; Photosystem II; Thylakoid; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..451
FT /note="Photosystem II CP43 reaction center protein"
FT /id="PRO_0000422601"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 51..66
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 67..116
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 117..131
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 132..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 158..174
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 175..239
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 240..254
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 255..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 270..285
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 286..429
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 430..446
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 447..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21499260"
FT BINDING 13
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 27
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 30
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 92
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 106
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 138
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 211
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 225
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="12"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21499260"
FT BINDING 345
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496,
FT ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624,
FT ECO:0000303|PubMed:19433803"
FT BINDING 404
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 415
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 418
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 451
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 24..52
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:7EDA"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 87..112
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 132..159
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:7COU"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 208..231
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 236..241
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 246..270
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 284..301
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 331..336
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 355..360
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 364..374
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 400..430
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:5V2C"
FT HELIX 443..446
FT /evidence="ECO:0007829|PDB:5B66"
SQ SEQUENCE 451 AA; 49165 MW; 1BF60FF132C5D382 CRC64;
ATNRDQESSG FAWWAGNARL INLSGKLLGA HVAHAGLIVF WAGAMTLFEL AHFIPEKPMY
EQGLILIPHI ATLGWGVGPG GEVVDTFPFF VVGVVHLISS AVLGFGGVYH AIRGPETLEE
YSSFFGYDWK DKNKMTTILG FHLIVLGIGA LLLVAKAMFF GGLYDTWAPG GGDVRVITNP
TLDPRVIFGY LLKSPFGGEG WIVSVNNLED VVGGHIWIGL ICIAGGIWHI LTTPFGWARR
AFIWSGEAYL SYSLGALSMM GFIATCFVWF NNTVYPSEFY GPTGPEASQA QAMTFLIRDQ
KLGANVGSAQ GPTGLGKYLM RSPTGEIIFG GETMRFWDFR GPWLEPLRGP NGLDLNKIKN
DIQPWQERRA AEYMTHAPLG SLNSVGGVAT EINSVNFVSP RSWLATSHFV LAFFFLVGHL
WHAGRARAAA AGFEKGIDRE SEPVLSMPSL D
