PSBI_PINTH
ID PSBI_PINTH Reviewed; 36 AA.
AC P41599;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Photosystem II reaction center protein I {ECO:0000255|HAMAP-Rule:MF_01316};
DE Short=PSII-I {ECO:0000255|HAMAP-Rule:MF_01316};
DE AltName: Full=PSII 4.8 kDa protein {ECO:0000255|HAMAP-Rule:MF_01316};
GN Name=psbI {ECO:0000255|HAMAP-Rule:MF_01316};
OS Pinus thunbergii (Japanese black pine) (Pinus thunbergiana).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=3350;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7937893; DOI=10.1073/pnas.91.21.9794;
RA Wakasugi T., Tsudzuki J., Ito S., Nakashima K., Tsudzuki T., Sugiura M.;
RT "Loss of all ndh genes as determined by sequencing the entire chloroplast
RT genome of the black pine Pinus thunbergii.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9794-9798(1994).
CC -!- FUNCTION: One of the components of the core complex of photosystem II
CC (PSII), required for its stability and/or assembly. PSII is a light-
CC driven water:plastoquinone oxidoreductase that uses light energy to
CC abstract electrons from H(2)O, generating O(2) and a proton gradient
CC subsequently used for ATP formation. It consists of a core antenna
CC complex that captures photons, and an electron transfer chain that
CC converts photonic excitation into a charge separation.
CC {ECO:0000255|HAMAP-Rule:MF_01316}.
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_01316}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01316}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01316}.
CC -!- SIMILARITY: Belongs to the PsbI family. {ECO:0000255|HAMAP-
CC Rule:MF_01316}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA04314.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D17510; BAA04314.1; ALT_INIT; Genomic_DNA.
DR PIR; T07434; T07434.
DR RefSeq; NP_042355.2; NC_001631.1.
DR AlphaFoldDB; P41599; -.
DR SMR; P41599; -.
DR GeneID; 809087; -.
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:0009539; C:photosystem II reaction center; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01316; PSII_PsbI; 1.
DR InterPro; IPR003686; PSII_PsbI.
DR InterPro; IPR037271; PSII_PsbI_sf.
DR PANTHER; PTHR35772; PTHR35772; 1.
DR Pfam; PF02532; PsbI; 1.
DR SUPFAM; SSF161041; SSF161041; 1.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; Photosynthesis; Photosystem II; Plastid;
KW Reaction center; Thylakoid; Transmembrane; Transmembrane helix.
FT CHAIN 1..36
FT /note="Photosystem II reaction center protein I"
FT /id="PRO_0000219646"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01316"
SQ SEQUENCE 36 AA; 4137 MW; 3A8B4B9A04D7B220 CRC64;
MLTLKLFVYA VVVFFISLFI FGFLSNDPGR NPGRKE