PSBB_CYACA
ID PSBB_CYACA Reviewed; 509 AA.
AC O19928;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 87.
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};
GN Name=psbB {ECO:0000255|HAMAP-Rule:MF_01495};
OS Cyanidium caldarium (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX NCBI_TaxID=2771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RK-1;
RX PubMed=11040290; DOI=10.1007/s002390010101;
RA Gloeckner G., Rosenthal A., Valentin K.-U.;
RT "The structure and gene repertoire of an ancient red algal plastid
RT genome.";
RL J. Mol. Evol. 51:382-390(2000).
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 -!- COFACTOR:
CC Note=Binds multiple chlorophylls. PSII binds additional chlorophylls,
CC carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_01495};
CC -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT,
CC PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-
CC evolving complex and a large number of cofactors. It forms dimeric
CC complexes. {ECO:0000255|HAMAP-Rule:MF_01495}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01495}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01495}.
CC -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01495}.
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DR EMBL; AF022186; AAB82661.1; -; Genomic_DNA.
DR PIR; T11996; T11996.
DR RefSeq; NP_045100.1; NC_001840.1.
DR PDB; 4YUU; X-ray; 2.77 A; B1/B2/b1/b2=1-509.
DR PDBsum; 4YUU; -.
DR AlphaFoldDB; O19928; -.
DR SMR; O19928; -.
DR GeneID; 800168; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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: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: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; Chloroplast; Chromophore; Membrane;
KW Photosynthesis; Photosystem II; Plastid; Thylakoid; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..509
FT /note="Photosystem II CP47 reaction center protein"
FT /id="PRO_0000077479"
FT TRANSMEM 21..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT TRANSMEM 101..115
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT TRANSMEM 140..156
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT TRANSMEM 203..218
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT TRANSMEM 237..252
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT TRANSMEM 457..472
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
SQ SEQUENCE 509 AA; 56562 MW; D786C058AD3217D6 CRC64;
MALPWYRVHT VVLNDPGRLI SVHLMHTALV SGWAGSMALY ELAVFDPSDP VLNPMWRQGM
FVMPFMARLG VTDSWGGWSI TGESVSNPGL WSFEGVALTH IVLSGLLFLA SIWHWVYWDL
DLFRDPRTLE PALDLPKVFG IHLVLSSLLC FGFGAFHVTG LFGPGIWISD AYGLTGRIQS
VAPAWGPEGF NPFNPGGIAS HHIAAGTVGI LAGVFHLNVR PPQRLYRALR MGNIETVLSS
SIAAVFFASF VVSGTMWYGA ASTPIELFGP TRYQWDSGYF QQEIEKRVEE SLSNGLSLPE
AWSNIPDKLA FYDYIGNNPA KGGLFRAGPM NKGDGIAEAW LGHPVFQDKE GHELIVRRMP
AFFENFPIIL VDKDGIIRAD IPFRRAESKY SIEQVGVTCS FYGGKLNNQS FKDASTVKKY
ARKAQFGEVF EFDRTILDSD GVFRSSPRGW FTFGHANFAL LFFFGHLWHG SRTLFRDVFA
GIGAEVTEQV EFGVFQKVGD KTTKKQGYV