PRSP1_SPIOL
ID PRSP1_SPIOL Reviewed; 302 AA.
AC P19954; A0A0K9QHQ6;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 2.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Ribosome-binding factor PSRP1, chloroplastic {ECO:0000303|PubMed:10874039};
DE AltName: Full=30S ribosomal protein 1;
DE AltName: Full=CS-S5 {ECO:0000303|PubMed:2693942};
DE Short=CS5;
DE AltName: Full=Plastid-specific 30S ribosomal protein 1 {ECO:0000303|PubMed:2376575};
DE Short=PSrp-1 {ECO:0000303|PubMed:2376575};
DE AltName: Full=Ribosomal protein 1;
DE AltName: Full=S22 {ECO:0000303|PubMed:1731992};
DE AltName: Full=Translation factor pY {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=PSRP1; Synonyms=RPS22, RPS30; ORFNames=SOVF_177810;
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], AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Geant d'hiver; TISSUE=Leaf;
RX PubMed=2693942; DOI=10.1007/bf00261178;
RA Zhou D.-X., Mache R.;
RT "Presence in the stroma of chloroplasts of a large pool of a ribosomal
RT protein not structurally related to any Escherichia coli ribosomal
RT protein.";
RL Mol. Gen. Genet. 219:204-208(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION.
RX PubMed=2259340; DOI=10.1007/bf00315812;
RA Zhou D.X., Mache R.;
RT "Presence in the stroma of chloroplasts of a large pool of a ribosomal
RT protein not structurally related to any Escherichia coli ribosomal
RT protein.";
RL Mol. Gen. Genet. 223:167-167(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 67-96; 105-125; 140-165;
RP 190-217 AND 230-259, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Alwaro; TISSUE=Leaf;
RX PubMed=2376575; DOI=10.1016/s0021-9258(19)38228-6;
RA Johnson C.H., Kruft V., Subramanian A.R.;
RT "Identification of a plastid-specific ribosomal protein in the 30 S subunit
RT of chloroplast ribosomes and isolation of the cDNA clone encoding its
RT cytoplasmic precursor.";
RL J. Biol. Chem. 265:12790-12795(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver; TISSUE=Leaf;
RX PubMed=1731992; DOI=10.1007/bf00034960;
RA Bisanz-Seyer C., Mache R.;
RT "Organization and expression of the nuclear gene coding for the plastid-
RT specific S22 ribosomal protein from spinach.";
RL Plant Mol. Biol. 18:337-341(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Viroflay; TISSUE=Leaf;
RX PubMed=24352233; DOI=10.1038/nature12817;
RA Dohm J.C., Minoche A.E., Holtgraewe D., Capella-Gutierrez S.,
RA Zakrzewski F., Tafer H., Rupp O., Soerensen T.R., Stracke R., Reinhardt R.,
RA Goesmann A., Kraft T., Schulz B., Stadler P.F., Schmidt T., Gabaldon T.,
RA Lehrach H., Weisshaar B., Himmelbauer H.;
RT "The genome of the recently domesticated crop plant sugar beet (Beta
RT vulgaris).";
RL Nature 505:546-549(2014).
RN [6]
RP PROTEIN SEQUENCE OF 67-72, AND MASS SPECTROMETRY.
RC STRAIN=cv. Alwaro; TISSUE=Leaf;
RX PubMed=10874039; DOI=10.1074/jbc.m004350200;
RA Yamaguchi K., von Knoblauch K., Subramanian A.R.;
RT "The plastid ribosomal proteins. Identification of all the proteins in the
RT 30S subunit of an organelle ribosome (chloroplast).";
RL J. Biol. Chem. 275:28455-28465(2000).
RN [7]
RP MODELING ON THE 70S RIBOSOME, RNA-BINDING, AND INTERACTION WITH PROTEINS
RP S9; S13 AND RRF.
RX PubMed=18042701; DOI=10.1073/pnas.0709856104;
RA Sharma M.R., Wilson D.N., Datta P.P., Barat C., Schluenzen F., Fucini P.,
RA Agrawal R.K.;
RT "Cryo-EM study of the spinach chloroplast ribosome reveals the structural
RT and functional roles of plastid-specific ribosomal proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19315-19320(2007).
RN [8]
RP FUNCTION IN STABILIZATION OF THE RIBOSOME, CRYOELECTRON MICROSCOPY,
RP RIBOSOME-BINDING, AND NOT A RIBOSOMAL PROTEIN.
RX PubMed=19965869; DOI=10.1074/jbc.m109.062299;
RA Sharma M.R., Donhofer A., Barat C., Marquez V., Datta P.P., Fucini P.,
RA Wilson D.N., Agrawal R.K.;
RT "PSRP1 is not a ribosomal protein, but a ribosome-binding factor that is
RT recycled by the ribosome-recycling factor (RRF) and elongation factor G
RT (EF-G).";
RL J. Biol. Chem. 285:4006-4014(2010).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=28007896; DOI=10.15252/embj.201695959;
RA Bieri P., Leibundgut M., Saurer M., Boehringer D., Ban N.;
RT "The complete structure of the chloroplast 70S ribosome in complex with
RT translation factor pY.";
RL EMBO J. 36:475-486(2017).
CC -!- FUNCTION: Ribosome-binding factor involved in light- and temperature-
CC dependent control of protein synthesis. Interacts with 16S sRNA
CC nucleotides at the A-site and P-site, where it protects the decoding
CC center and inhibits translation by preventing tRNA binding. Stabilizes
CC 70S ribosomes against dissociation. May be recycled by the combined
CC action of ribosome-recycling factor (RRF) and EF-G.
CC {ECO:0000269|PubMed:19965869, ECO:0000269|PubMed:28007896}.
CC -!- SUBUNIT: Binds to the mRNA channel of the chloroplast small ribosomal
CC subunit and interacts with 16S sRNA nucleotides at the A-site and P-
CC site. {ECO:0000269|PubMed:28007896}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:2376575, ECO:0000269|PubMed:2693942,
CC ECO:0000269|PubMed:28007896}.
CC -!- MASS SPECTROMETRY: Mass=26805.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874039};
CC -!- MASS SPECTROMETRY: Mass=26943; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10874039};
CC -!- SIMILARITY: Belongs to the HPF/YfiA ribosome-associated protein family.
CC Long plastid HPF subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:2693942, PubMed:2259340,
CC PubMed:2376575, PubMed:1731992, PubMed:10874039, PubMed:18042701)
CC thought to be a ribosomal protein. {ECO:0000305|PubMed:10874039,
CC ECO:0000305|PubMed:1731992, ECO:0000305|PubMed:18042701,
CC ECO:0000305|PubMed:2259340, ECO:0000305|PubMed:2376575,
CC ECO:0000305|PubMed:2693942}.
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DR EMBL; X15344; CAA33403.1; -; mRNA.
DR EMBL; M55322; AAA34039.1; -; mRNA.
DR EMBL; X59270; CAA41960.1; -; Genomic_DNA.
DR EMBL; KQ180281; KNA06792.1; -; Genomic_DNA.
DR PIR; S19131; R3SPS5.
DR PDB; 5MMJ; EM; 3.65 A; y=1-302.
DR PDB; 5MMM; EM; 3.40 A; y=1-302.
DR PDB; 5X8P; EM; 3.40 A; y=67-302.
DR PDB; 5X8R; EM; 3.70 A; y=67-302.
DR PDB; 6ERI; EM; 3.00 A; BV=73-178.
DR PDBsum; 5MMJ; -.
DR PDBsum; 5MMM; -.
DR PDBsum; 5X8P; -.
DR PDBsum; 5X8R; -.
DR PDBsum; 6ERI; -.
DR AlphaFoldDB; P19954; -.
DR SMR; P19954; -.
DR STRING; 3562.P19954; -.
DR Proteomes; UP000054095; Unassembled WGS sequence.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045900; P:negative regulation of translational elongation; IBA:GO_Central.
DR GO; GO:0044238; P:primary metabolic process; IEA:InterPro.
DR CDD; cd00552; RaiA; 1.
DR Gene3D; 3.30.160.100; -; 1.
DR Gene3D; 3.30.505.50; -; 1.
DR HAMAP; MF_00839; HPF; 1.
DR InterPro; IPR034694; HPF_long/plastid.
DR InterPro; IPR036567; RHF-like.
DR InterPro; IPR003489; RHF/RaiA.
DR InterPro; IPR032528; Ribosom_S30AE_C.
DR InterPro; IPR038416; Ribosom_S30AE_C_sf.
DR Pfam; PF16321; Ribosom_S30AE_C; 1.
DR Pfam; PF02482; Ribosomal_S30AE; 1.
DR SUPFAM; SSF69754; SSF69754; 1.
DR TIGRFAMs; TIGR00741; yfiA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Plastid;
KW Reference proteome; RNA-binding; rRNA-binding; Transit peptide;
KW Translation regulation.
FT TRANSIT 1..66
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874039,
FT ECO:0000269|PubMed:2376575"
FT CHAIN 67..302
FT /note="Ribosome-binding factor PSRP1, chloroplastic"
FT /id="PRO_0000030635"
FT CONFLICT 29
FT /note="P -> L (in Ref. 4; AAA34039)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 302 AA; 33749 MW; 0AA7AED70B52A02F CRC64;
MATLCTSAIN MNPNLTNSLS NSINLSSTPT NLSSLRSTFT NSCSLGLNVA VKSVQISRNK
PNVVCMSWDG PLSSVKLILQ GRNLEVSDNV RSHVEDKVGK SVAKHSHLVR EVDVRLSARG
GDLSKGPKLR RCEVTLFTKR HGVIRAEEDA ESLYSSIDLV SSIIQRKLRK IKDKVSDHGR
HMKGFNRSKV RDPEPVRITR EEVLEEVESA PAPVSVEDDD FIEEVVRTKY FDMPPLTITE
AVEQLENVDH DFYAFRNEET GDINILYKRK EGGYGLIIPK DGKTEKLESL PVQTDKQPSF
AE
