PSAE_SYNP2
ID PSAE_SYNP2 Reviewed; 70 AA.
AC P31969; B1XMA3;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Photosystem I reaction center subunit IV;
GN Name=psaE; OrderedLocusNames=SYNPCC7002_A1393;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8412664; DOI=10.1111/j.1365-2958.1993.tb01680.x;
RA Zhao J., Snyder W., Muhlenhoff U., Rhiel E., Bryant D.A.;
RT "Cloning and characterization of the psaE gene of the cyanobacterium
RT Synechococcus sp. PCC 7002: characterization of a psaE mutant and
RT overproduction of the protein in Escherichia coli.";
RL Mol. Microbiol. 9:183-194(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=8193119; DOI=10.1021/bi00186a004;
RA Falzone C.J., Kao Y.-H., Zhao J., Bryant D.A., Lecomte J.T.J.;
RT "Three-dimensional solution structure of PsaE from the cyanobacterium
RT Synechococcus sp. strain PCC 7002, a photosystem I protein that shows
RT structural homology with SH3 domains.";
RL Biochemistry 33:6052-6062(1994).
CC -!- FUNCTION: Stabilizes the interaction between PsaC and the PSI core,
CC assists the docking of the ferredoxin to PSI and interacts with
CC ferredoxin-NADP oxidoreductase.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane
CC protein.
CC -!- SIMILARITY: Belongs to the PsaE family. {ECO:0000305}.
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DR EMBL; M99379; AAA27355.1; -; Genomic_DNA.
DR EMBL; CP000951; ACA99389.1; -; Genomic_DNA.
DR RefSeq; WP_012307012.1; NC_010475.1.
DR PDB; 1PSE; NMR; -; A=2-70.
DR PDB; 1PSF; NMR; -; A=2-70.
DR PDBsum; 1PSE; -.
DR PDBsum; 1PSF; -.
DR AlphaFoldDB; P31969; -.
DR SMR; P31969; -.
DR STRING; 32049.SYNPCC7002_A1393; -.
DR EnsemblBacteria; ACA99389; ACA99389; SYNPCC7002_A1393.
DR KEGG; syp:SYNPCC7002_A1393; -.
DR eggNOG; ENOG503313D; Bacteria.
DR HOGENOM; CLU_136462_2_1_3; -.
DR OMA; NYSGINT; -.
DR EvolutionaryTrace; P31969; -.
DR Proteomes; UP000001688; Chromosome.
DR GO; GO:0009538; C:photosystem I 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_00613; PSI_PsaE; 1.
DR InterPro; IPR008990; Elect_transpt_acc-like_dom_sf.
DR InterPro; IPR003375; PSI_PsaE.
DR PANTHER; PTHR34549; PTHR34549; 1.
DR Pfam; PF02427; PSI_PsaE; 1.
DR SUPFAM; SSF50090; SSF50090; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Photosynthesis; Photosystem I; Reference proteome;
KW Thylakoid.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..70
FT /note="Photosystem I reaction center subunit IV"
FT /id="PRO_0000204410"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1PSE"
FT TURN 17..20
FT /evidence="ECO:0007829|PDB:1PSE"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:1PSE"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:1PSE"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:1PSE"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1PSE"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1PSE"
SQ SEQUENCE 70 AA; 7668 MW; BEADE690494B8928 CRC64;
MAIERGSKVK ILRKESYWYG DVGTVASIDK SGIIYPVIVR FNKVNYNGFS GSAGGLNTNN
FAEHELEVVG
