ID   PSAL_SPIOL              Reviewed;         216 AA.
AC   Q41385;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Photosystem I reaction center subunit XI, chloroplastic;
DE            Short=PSI-L;
DE   AltName: Full=PSI subunit V;
DE   Flags: Precursor;
GN   Name=PSAL;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Monatol;
RX   PubMed=8343606; DOI=10.1007/bf00047411;
RA   Flieger K., Oelmueller R., Herrmann R.G.;
RT   "Isolation and characterization of cDNA clones encoding a 18.8 kDa
RT   polypeptide, the product of the gene psaL, associated with photosystem I
RT   reaction center from spinach.";
RL   Plant Mol. Biol. 22:703-709(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 158-178.
RX   PubMed=2013332; DOI=10.1016/0014-5793(91)80324-v;
RA   Ikeuchi M., Inoue Y.;
RT   "Two new components of 9 and 14 kDa from spinach photosystem I complex.";
RL   FEBS Lett. 280:332-334(1991).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the PsaL family. {ECO:0000305}.
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DR   EMBL; X64445; CAA45775.1; -; mRNA.
DR   PIR; S35151; S35151.
DR   PDB; 2O01; X-ray; 3.40 A; L=53-216.
DR   PDB; 2WSC; X-ray; 3.30 A; L=1-216.
DR   PDB; 2WSE; X-ray; 3.49 A; L=1-216.
DR   PDB; 2WSF; X-ray; 3.48 A; L=1-216.
DR   PDBsum; 2O01; -.
DR   PDBsum; 2WSC; -.
DR   PDBsum; 2WSE; -.
DR   PDBsum; 2WSF; -.
DR   AlphaFoldDB; Q41385; -.
DR   SMR; Q41385; -.
DR   EvolutionaryTrace; Q41385; -.
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:0009538; C:photosystem I reaction center; IEA:InterPro.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1240.10; -; 1.
DR   InterPro; IPR003757; PSI_PsaL.
DR   InterPro; IPR036592; PSI_PsaL_sf.
DR   InterPro; IPR022980; PSI_suXI.
DR   PANTHER; PTHR34803; PTHR34803; 1.
DR   Pfam; PF02605; PsaL; 1.
DR   SUPFAM; SSF81568; SSF81568; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Direct protein sequencing; Membrane;
KW   Photosynthesis; Photosystem I; Plastid; Thylakoid; Transit peptide;
KW   Transmembrane; Transmembrane helix.
FT   TRANSIT         1..47
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..216
FT                   /note="Photosystem I reaction center subunit XI,
FT                   chloroplastic"
FT                   /id="PRO_0000029427"
FT   TOPO_DOM        48..134
FT                   /note="Stromal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        156..188
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..216
FT                   /note="Stromal"
FT                   /evidence="ECO:0000255"
FT   STRAND          55..58
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   TURN            74..76
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   TURN            79..85
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   STRAND          87..92
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   HELIX           97..107
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   STRAND          110..113
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   HELIX           114..118
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   STRAND          127..129
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   TURN            134..138
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   HELIX           139..143
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   TURN            144..152
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   TURN            171..173
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   HELIX           181..195
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   TURN            197..199
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   HELIX           200..204
FT                   /evidence="ECO:0007829|PDB:2WSC"
SQ   SEQUENCE   216 AA;  22937 MW;  603DCA983C7C383B CRC64;
     MAATTSPMAS QLKSGFTTKA LVVPKGISGP ALRGFPSPRR HTSFTVRAIK TEKPTYQVIQ
     PLNGDPFIGG LETPVTSSPL IAWYLSNLPA YRTAVNPLLR GVEVGLAHGF LLVGPFVKAG
     PLRNTEYAGA AGSLAAAGLV VILSMCLTMY GIASFKEGEP SIAPALTLTG RKKQPDQLQS
     ADGWAKFTGG FFFGGVSGVT WACFLMYVLD LPYYFK