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PSBB_MARPO
ID   PSBB_MARPO              Reviewed;         508 AA.
AC   P06412;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 96.
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   Marchantia polymorpha (Liverwort) (Marchantia aquatica).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=3197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3199436; DOI=10.1016/0022-2836(88)90003-4;
RA   Fukuzawa H., Kohchi T., Sano T., Shirai H., Umesono K., Inokuchi H.,
RA   Ozeki H., Ohyama K.;
RT   "Structure and organization of Marchantia polymorpha chloroplast genome.
RT   III. Gene organization of the large single copy region from rbcL to
RT   trnI(CAU).";
RL   J. Mol. Biol. 203:333-351(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   DOI=10.1038/322572a0;
RA   Ohyama K., Fukuzawa H., Kohchi T., Shirai H., Sano T., Sano S., Umesono K.,
RA   Shiki Y., Takeuchi M., Chang Z., Aota S., Inokuchi H., Ozeki H.;
RT   "Chloroplast gene organization deduced from complete sequence of liverwort
RT   Marchantia polymorpha chloroplast DNA.";
RL   Nature 322:572-574(1986).
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; X04465; CAA28110.1; -; Genomic_DNA.
DR   PIR; A03472; QJLV6A.
DR   RefSeq; NP_039324.1; NC_001319.1.
DR   AlphaFoldDB; P06412; -.
DR   SMR; P06412; -.
DR   GeneID; 2702561; -.
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   3: Inferred from homology;
KW   Chlorophyll; Chloroplast; Chromophore; Membrane; Photosynthesis;
KW   Photosystem II; Plastid; Thylakoid; Transmembrane; Transmembrane helix.
FT   CHAIN           1..508
FT                   /note="Photosystem II CP47 reaction center protein"
FT                   /id="PRO_0000077486"
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;  56225 MW;  C89E7D6A54614F09 CRC64;
     MGLPWYRVHT VVLNDPGRLI AVHLMHTALV SGWAGSMALY ELAVFDPSDP VLDPMWRQGM
     FVIPFMTRLG ITKSWGGWSI TGETVTNAGI WSYEGVAAVH IVLSGLLFLA AIWHWVYWDL
     ELFRDERTGK PSLDLPKIFG IHLFLSGVLC FAFGAFHVTG LFGPGIWISD PYGLTGKVQP
     VAPAWGAEGF DPFVPGGIAS HHIAAGILGI LAGLFHLSVR PPQRLYKGLR MGNVETVLSS
     SIAAVFFAAF VVAGTMWYGS AATPIELFGP TRYQWDQGFF QQEIDRRIRS SKAENLSLSE
     AWSKIPEKLA FYDYIGNNPA KGGLFRAGAM DNGDGIAVGW LGHAVFKDKE GNELFVRRMP
     TFFETFPVVL VDEQGIVRAD VPFRRAESKY SVEQVGVTVE FYGGELDGVS FSDPATVKKY
     ARRAQLGEIF EFDRATLKSD GVFRSSPRGW FTFGHATFAL LFFFGHIWHG ARTLFRDVFA
     GIDPDLDAQV EFGAFQKLGD PTTKRQVI
 
 
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