ID   PSBJ_PROMA              Reviewed;          65 AA.
AC   Q7VDN7;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Photosystem II reaction center protein J {ECO:0000255|HAMAP-Rule:MF_01305};
DE            Short=PSII-J {ECO:0000255|HAMAP-Rule:MF_01305};
GN   Name=psbJ {ECO:0000255|HAMAP-Rule:MF_01305}; OrderedLocusNames=Pro_0331;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
CC   -!- FUNCTION: One of the components of the core complex of photosystem II
CC       (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that
CC       uses light energy to abstract electrons from H(2)O, generating O(2) and
CC       a proton gradient subsequently used for ATP formation. It consists of a
CC       core antenna complex that captures photons, and an electron transfer
CC       chain that converts photonic excitation into a charge separation.
CC       {ECO:0000255|HAMAP-Rule:MF_01305}.
CC   -!- SUBUNIT: Cyanobacterial PSII is composed of 1 copy each of membrane
CC       proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK,
CC       PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral
CC       proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms
CC       dimeric complexes. {ECO:0000255|HAMAP-Rule:MF_01305}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01305}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01305}.
CC   -!- SIMILARITY: Belongs to the PsbJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01305}.
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DR   EMBL; AE017126; AAP99377.1; -; Genomic_DNA.
DR   RefSeq; NP_874725.1; NC_005042.1.
DR   RefSeq; WP_011124486.1; NC_005042.1.
DR   AlphaFoldDB; Q7VDN7; -.
DR   SMR; Q7VDN7; -.
DR   STRING; 167539.Pro_0331; -.
DR   EnsemblBacteria; AAP99377; AAP99377; Pro_0331.
DR   GeneID; 54199693; -.
DR   KEGG; pma:Pro_0331; -.
DR   PATRIC; fig|167539.5.peg.340; -.
DR   eggNOG; ENOG5030SSF; Bacteria.
DR   HOGENOM; CLU_2829784_0_0_3; -.
DR   OMA; SWERRWT; -.
DR   OrthoDB; 1939278at2; -.
DR   Proteomes; UP000001420; Chromosome.
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:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01305; PSII_PsbJ; 1.
DR   InterPro; IPR002682; PSII_PsbJ.
DR   InterPro; IPR037267; PSII_PsbJ_sf.
DR   Pfam; PF01788; PsbJ; 1.
DR   SUPFAM; SSF161021; SSF161021; 1.
PE   3: Inferred from homology;
KW   Membrane; Photosynthesis; Photosystem II; Reaction center;
KW   Reference proteome; Thylakoid; Transmembrane; Transmembrane helix.
FT   CHAIN           1..65
FT                   /note="Photosystem II reaction center protein J"
FT                   /id="PRO_0000292225"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01305"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   65 AA;  7022 MW;  7787DD52B5E37244 CRC64;
     MSSKLKGPDG RLPDRLPDGR PAVSWERRWT EGQLPLWLVA TAGGIAVIFV LGIFFYGSYT
     GVGSA