ID   PSBI_PHYPA              Reviewed;          36 AA.
AC   Q6YXN3;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   25-MAY-2022, entry version 71.
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   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004;
RX   PubMed=12954768; DOI=10.1093/nar/gkg726;
RA   Sugiura C., Kobayashi Y., Setsuyuki A., Sugita C., Sugita M.;
RT   "Complete chloroplast DNA sequence of the moss Physcomitrella patens:
RT   evidence for the loss and relocation of rpoA from the chloroplast to the
RT   nucleus.";
RL   Nucleic Acids Res. 31:5324-5331(2003).
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=BAC85063.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP005672; BAC85063.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_904213.2; NC_005087.1.
DR   AlphaFoldDB; Q6YXN3; -.
DR   SMR; Q6YXN3; -.
DR   GeneID; 2546798; -.
DR   KEGG; ppp:2546798; -.
DR   InParanoid; Q6YXN3; -.
DR   Proteomes; UP000006727; Chloroplast.
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; Reference proteome; Thylakoid; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..36
FT                   /note="Photosystem II reaction center protein I"
FT                   /id="PRO_0000219644"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01316"
SQ   SEQUENCE   36 AA;  4153 MW;  7D088FCB57BB6236 CRC64;
     MLTLKLFVYT VVIFFVSLFV FGFLSNDPGR NPGRKE