ID   PSBI_CUSOB              Reviewed;          37 AA.
AC   A8W3H4;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 45.
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   Cuscuta obtusiflora (Peruvian dodder).
OG   Plastid.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC   Cuscuta subgen. Grammica; Cuscuta sect. Cleistogrammica.
OX   NCBI_TaxID=437280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17956636; DOI=10.1186/1471-2229-7-57;
RA   McNeal J.R., Kuehl J.V., Boore J.L., dePamphilis C.W.;
RT   "Complete plastid genome sequences suggest strong selection for retention
RT   of photosynthetic genes in the parasitic plant genus Cuscuta.";
RL   BMC Plant Biol. 7:57-57(2007).
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 membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000255|HAMAP-Rule:MF_01316}.
CC   -!- SIMILARITY: Belongs to the PsbI family. {ECO:0000255|HAMAP-
CC       Rule:MF_01316}.
CC   -!- CAUTION: Only inflorescences, fruits, starved seedlings and stressed
CC       stem tips are green in this organism. {ECO:0000305}.
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DR   EMBL; EU189133; ABW20549.1; -; Genomic_DNA.
DR   RefSeq; YP_001531204.1; NC_009949.1.
DR   AlphaFoldDB; A8W3H4; -.
DR   SMR; A8W3H4; -.
DR   GeneID; 5714832; -.
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:0042170; C:plastid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-UniRule.
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   Membrane; Photosynthesis; Photosystem II; Plastid; Reaction center;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..37
FT                   /note="Photosystem II reaction center protein I"
FT                   /id="PRO_0000353226"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01316"
SQ   SEQUENCE   37 AA;  4441 MW;  520A7C9CA8275B62 CRC64;
     MFILKLFVYT VVIFFVSLFI FGFLSNDPRR NPEPEED