PSBH_PHYPA
ID PSBH_PHYPA Reviewed; 74 AA.
AC Q6YXN1; A9RTF8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Photosystem II reaction center protein H {ECO:0000255|HAMAP-Rule:MF_00752};
DE Short=PSII-H {ECO:0000255|HAMAP-Rule:MF_00752};
DE AltName: Full=Photosystem II 10 kDa phosphoprotein {ECO:0000255|HAMAP-Rule:MF_00752};
GN Name=psbH {ECO:0000255|HAMAP-Rule:MF_00752}; ORFNames=PHYPADRAFT_119144;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
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_00752}.
CC -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC PsbB, PsbC, PsbD, numerous small proteins, at least 3 peripheral
CC proteins of the oxygen-evolving complex and a large number of
CC cofactors. It forms dimeric complexes. {ECO:0000255|HAMAP-
CC Rule:MF_00752}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00752}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00752}.
CC -!- PTM: Phosphorylation is a light-dependent reaction catalyzed by a
CC membrane-bound kinase; phosphorylation occurs on Thr residue(s) in the
CC N-terminus of the protein. {ECO:0000255|HAMAP-Rule:MF_00752}.
CC -!- SIMILARITY: Belongs to the PsbH family. {ECO:0000255|HAMAP-
CC Rule:MF_00752}.
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DR EMBL; AP005672; BAC85021.1; -; Genomic_DNA.
DR EMBL; DS544916; EDQ77795.1; -; Genomic_DNA.
DR RefSeq; NP_904172.1; NC_005087.1.
DR RefSeq; XP_001757310.1; XM_001757258.1.
DR AlphaFoldDB; Q6YXN1; -.
DR SMR; Q6YXN1; -.
DR STRING; 3218.PP1S27_266V6.1; -.
DR EnsemblPlants; Pp3c21_5650V3.3; PAC:32916113.CDS.1; Pp3c21_5650.
DR GeneID; 2546702; -.
DR Gramene; Pp3c21_5650V3.3; PAC:32916113.CDS.1; Pp3c21_5650.
DR KEGG; ppp:2546702; -.
DR eggNOG; ENOG502S8Y7; Eukaryota.
DR HOGENOM; CLU_190203_1_0_1; -.
DR InParanoid; Q6YXN1; -.
DR OMA; PLMAVFM; -.
DR OrthoDB; 1583583at2759; -.
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:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0042301; F:phosphate ion binding; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR GO; GO:0050821; P:protein stabilization; IEA:InterPro.
DR Gene3D; 1.20.5.880; -; 1.
DR HAMAP; MF_00752; PSII_PsbH; 1.
DR InterPro; IPR001056; PSII_PsbH.
DR InterPro; IPR036863; PSII_PsbH_sf.
DR PANTHER; PTHR34469; PTHR34469; 1.
DR Pfam; PF00737; PsbH; 1.
DR SUPFAM; SSF161025; SSF161025; 1.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; Phosphoprotein; Photosynthesis; Photosystem II;
KW Plastid; Reference proteome; Thylakoid; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..74
FT /note="Photosystem II reaction center protein H"
FT /id="PRO_0000070527"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
SQ SEQUENCE 74 AA; 7892 MW; 4E5622AD8888C764 CRC64;
MATQIIDDTP KTKGKRSGLG DILKPLNSEY GKVAPGWGTT PLMGVAMGLF AVFLVIILEL
YNSSVLLDGV PVSW
