PSBC_SYNY3
ID PSBC_SYNY3 Reviewed; 460 AA.
AC P09193; P73749;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 143.
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};
GN Name=psbC {ECO:0000255|HAMAP-Rule:MF_01496}; OrderedLocusNames=sll0851;
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 [GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=24277560; DOI=10.1007/bf00029879;
RA Chisholm D., Williams J.G.K.;
RT "Nucleotide sequence of psbC, the gene encoding the CP-43 chlorophyll a-
RT binding protein of photosystem II, in the cyanobacterium Synechocystis
RT 6803.";
RL Plant Mol. Biol. 10:293-301(1988).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-288.
RX PubMed=3130247; DOI=10.1002/j.1460-2075.1988.tb02817.x;
RA Dzelzkalns V.A., Bogorad L.;
RT "Molecular analysis of a mutant defective in photosynthetic oxygen
RT evolution and isolation of a complementing clone by a novel screening
RT procedure.";
RL EMBO J. 7:333-338(1988).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=1903653; DOI=10.1021/bi00236a009;
RA Roegner M., Chisholm D.A., Diner B.A.;
RT "Site-directed mutagenesis of the psbC gene of photosystem II: isolation
RT and functional characterization of CP43-less photosystem II core
RT complexes.";
RL Biochemistry 30:5387-5395(1991).
RN [5]
RP SUBCELLULAR LOCATION, AND LACK OF PHOSPHORYLATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=9512353; DOI=10.1016/s0014-5793(98)00088-x;
RA Pursiheimo S., Rintamaeki E., Baena-Gonzalez E., Aro E.-M.;
RT "Thylakoid protein phosphorylation in evolutionally divergent species with
RT oxygenic photosynthesis.";
RL FEBS Lett. 423:178-182(1998).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, 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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=23148271; DOI=10.1098/rstb.2012.0066;
RA Boehm M., Yu J., Reisinger V., Beckova M., Eichacker L.A., Schlodder E.,
RA Komenda J., Nixon P.J.;
RT "Subunit composition of CP43-less photosystem II complexes of Synechocystis
RT sp. PCC 6803: implications for the assembly and repair of photosystem II.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 367:3444-3454(2012).
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 (By similarity). Required for
CC correct assembly of PSII (PubMed:1903653, PubMed:23148271).
CC {ECO:0000255|HAMAP-Rule:MF_01496, ECO:0000269|PubMed:1903653,
CC ECO:0000269|PubMed:23148271}.
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};
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:12069591}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01496, ECO:0000269|PubMed:12069591,
CC ECO:0000269|PubMed:9512353}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01496, ECO:0000269|PubMed:9512353}.
CC -!- DISRUPTION PHENOTYPE: Unable to grow photoautotrophically or evolve
CC O(2). About 10% mostly monomeric PSII accumulates, which corresponds to
CC RC47, an intermediate in the normal path of PSII assembly. The
CC intermediate is able to bind the primary and secondary electron donors
CC and acceptors and can transfer electrons. {ECO:0000269|PubMed:1903653,
CC ECO:0000269|PubMed:23148271}.
CC -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01496}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA85378.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA30071.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M21538; AAA85378.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000022; BAA17799.2; -; Genomic_DNA.
DR EMBL; X07018; CAA30071.1; ALT_INIT; Genomic_DNA.
DR PIR; S06469; S06469.
DR PDB; 6WJ6; EM; 2.58 A; C=1-460.
DR PDB; 7N8O; EM; 1.93 A; C/c=1-460.
DR PDB; 7RCV; EM; 2.01 A; C/c=1-460.
DR PDBsum; 6WJ6; -.
DR PDBsum; 7N8O; -.
DR PDBsum; 7RCV; -.
DR AlphaFoldDB; P09193; -.
DR SMR; P09193; -.
DR IntAct; P09193; 4.
DR STRING; 1148.163937832; -.
DR TCDB; 3.E.2.2.2; the photosynthetic reaction center (prc) family.
DR PaxDb; P09193; -.
DR EnsemblBacteria; BAA17799; BAA17799; BAA17799.
DR KEGG; syn:sll0851; -.
DR eggNOG; ENOG502Z7VA; Bacteria.
DR InParanoid; P09193; -.
DR OMA; WKDKNKM; -.
DR PhylomeDB; P09193; -.
DR BioCyc; MetaCyc:PSBC-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:0016168; F:chlorophyll binding; IEA:UniProtKB-UniRule.
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; Manganese; Membrane; Metal-binding;
KW Photosynthesis; Photosystem II; Reference proteome; Thylakoid;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..460
FT /note="Photosystem II CP43 reaction center protein"
FT /id="PRO_0000077532"
FT TRANSMEM 60..75
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT TRANSMEM 126..140
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT TRANSMEM 167..183
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT TRANSMEM 249..263
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT TRANSMEM 279..294
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT TRANSMEM 439..455
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT BINDING 354
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT CONFLICT 42
FT /note="A -> R (in Ref. 1; AAA85378 and 3; CAA30071)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="T -> N (in Ref. 3; CAA30071)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="Y -> I (in Ref. 3; CAA30071)"
FT /evidence="ECO:0000305"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 33..60
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:7N8O"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 96..121
FT /evidence="ECO:0007829|PDB:7N8O"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:7N8O"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 141..168
FT /evidence="ECO:0007829|PDB:7N8O"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:7N8O"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:7N8O"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:7N8O"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 217..240
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 255..279
FT /evidence="ECO:0007829|PDB:7N8O"
FT TURN 282..285
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 293..311
FT /evidence="ECO:0007829|PDB:7N8O"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:7N8O"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:7N8O"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 341..345
FT /evidence="ECO:0007829|PDB:7N8O"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 373..384
FT /evidence="ECO:0007829|PDB:7N8O"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 409..439
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 452..455
FT /evidence="ECO:0007829|PDB:7N8O"
SQ SEQUENCE 460 AA; 50303 MW; 06D59598F4B487DF CRC64;
MVTLSNTSMV GGRDLPSTGF AWWSGNARLI NLSGKLLGAH VAHAGLIVFW AGAMTLFEVA
HFIPEKPMYE QGLILLPHIA TLGWGVGPAG EVTDIFPFFV VGVLHLISSA VLGLGGIYHA
LRGPEVLEEY SSFFGYDWKD KNQMTNIIGY HLILLGCGAL LLVFKAMFFG GVYDTWAPGG
GDVRVITNPT LNPAIIFGYL LKAPFGGEGW IISVNNMEDI IGGHIWIGLI CISGGIWHIL
TKPFGWARRA LIWSGEAYLS YSLGALSLMG FIASVFVWFN NTAYPSEFYG PTGMEASQSQ
AFTFLVRDQR LGANIASAQG PTGLGKYLMR SPSGEIIFGG ETMRFWDFRG PWLEPLRGPN
GLDLDKLRND IQPWQVRRAA EYMTHAPLGS LNSVGGVITD VNSFNYVSPR AWLATSHFVL
GFFFLVGHLW HAGRARAAAA GFEKGIDRET EPTLFMPDLD
