PSBB_ANTAG
ID PSBB_ANTAG Reviewed; 508 AA.
AC Q85AI7;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 69.
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 Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC Anthoceros.
OX NCBI_TaxID=48387;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX PubMed=12527781; DOI=10.1093/nar/gkg155;
RA Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT chloroplast genome: insight into the earliest land plants.";
RL Nucleic Acids Res. 31:716-721(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC TISSUE=Thallus;
RX PubMed=12711687; DOI=10.1093/nar/gkg327;
RA Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT "RNA editing in hornwort chloroplasts makes more than half the genes
RT functional.";
RL Nucleic Acids Res. 31:2417-2423(2003).
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 -!- RNA EDITING: Modified_positions=5 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 13 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 16 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 18 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 21 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 54 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 64 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 100 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 103 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 104 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 107 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 120 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 122 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 132 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 133 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 135 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 156 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 216 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 222 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 264 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 267 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 268 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 277 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 319 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 343 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 363 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 370 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 382 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 383 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 423 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 425 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 430 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 432 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 443 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 462 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 463 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}; Note=The nonsense codons at positions 277
CC and 425 are modified to sense codons.;
CC -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01495}.
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DR EMBL; AB086179; BAC55374.1; -; Genomic_DNA.
DR EMBL; AB087462; BAC55471.1; -; mRNA.
DR RefSeq; NP_777438.1; NC_004543.1.
DR AlphaFoldDB; Q85AI7; -.
DR SMR; Q85AI7; -.
DR GeneID; 2553397; -.
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 2: Evidence at transcript level;
KW Chlorophyll; Chloroplast; Chromophore; Membrane; Photosynthesis;
KW Photosystem II; Plastid; RNA editing; Thylakoid; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..508
FT /note="Photosystem II CP47 reaction center protein"
FT /id="PRO_0000077475"
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 508 AA; 56253 MW; C9DB91337929A558 CRC64;
MGLPWYRVHT VVLNDPGRLI AVHLMHTALV SGWAGSMALY ELAVFDPSDP VLDPMWRQGM
FVIPFMTRLG ITKSWGGWSI TGETVTNAGI WSYEGVAAVH IVLSGLLFLA AIWHWVYWDL
ELFRDERTGK PSLDLPKIFG IHLFLSGVLC FGFGAFHVTG LFGPGIWVSD PYGLTGKVEP
VAPAWGAEGF DPFVPGGIAS HHIAAGILGI LAGLFHLSVR PPQRLYKGLR MGNVETVLSS
SIAAVFFAAF VVAGTMWYGS AATPIELFGP TRYQWDQGFF QQEIDRRIRS SKAENLSLSE
AWSKIPEKLA FYDYIGNNPA KGGLFRAGAM DNGDGIAVGW LGHAVFKDKE GHELFVRRMP
TFFETFPVVL VDEEGIVRAD IPFRRAESKY SVEQVGVIVE FYGGELDGVS FSDPVTVKKY
ARRAQLGEIF EFDRATLKSD GVFRSSPRGW FTFGHATFAL LFFFGHIWHG ARTLFRDVFA
GIDSDLDAQV EFGAFEKLGD PTTKRQVV
