RRP2_SPIOL
ID RRP2_SPIOL Reviewed; 260 AA.
AC P82277; A0A0K9R1W7;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2000, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=30S ribosomal protein 2, chloroplastic {ECO:0000303|PubMed:10874039};
DE AltName: Full=Chloroplastic small ribosomal subunit protein cS22 {ECO:0000303|PubMed:28007896};
DE AltName: Full=Plastid-specific 30S ribosomal protein 2;
DE Short=PSRP-2;
DE Flags: Precursor;
GN Name=PSRP2; ORFNames=SOVF_116380;
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], PROTEIN SEQUENCE OF 63-83, SUBUNIT, SUBCELLULAR
RP LOCATION, 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 63-83; 117-132; 157-187 AND
RP 202-220, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=cv. Alwaro;
RX PubMed=12605670; DOI=10.1046/j.1432-1033.2003.03359.x;
RA Yamaguchi K., Subramanian A.R.;
RT "Proteomic identification of all plastid-specific ribosomal proteins in
RT higher plant chloroplast 30S ribosomal subunit.";
RL Eur. J. Biochem. 270:190-205(2003).
RN [3]
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 [4]
RP MODELING ON THE 70S RIBOSOME, AND POSSIBLE RNA-BINDING.
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 [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBUNIT, AND SUBCELLULAR
RP 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: Component of the chloroplast ribosome (chloro-ribosome), a
CC dedicated translation machinery responsible for the synthesis of
CC chloroplast genome-encoded proteins, including proteins of the
CC transcription and translation machinery and components of the
CC photosynthetic apparatus (PubMed:10874039, PubMed:28007896). cS22 may
CC have a role in the recruitment of stored chloroplast mRNAs for active
CC protein synthesis (PubMed:12605670). {ECO:0000305|PubMed:10874039,
CC ECO:0000305|PubMed:12605670, ECO:0000305|PubMed:28007896}.
CC -!- SUBUNIT: Component of the chloroplast small ribosomal subunit (SSU).
CC Mature 70S chloroplast ribosomes of higher plants consist of a small
CC (30S) and a large (50S) subunit. The 30S small subunit contains 1
CC molecule of ribosomal RNA (16S rRNA) and 24 different proteins. The 50S
CC large subunit contains 3 rRNA molecules (23S, 5S and 4.5S rRNA) and 33
CC different proteins. {ECO:0000269|PubMed:10874039,
CC ECO:0000269|PubMed:28007896}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:10874039, ECO:0000269|PubMed:12605670,
CC ECO:0000269|PubMed:28007896}.
CC -!- MASS SPECTROMETRY: Mass=21666; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874039};
CC -!- MASS SPECTROMETRY: Mass=21665; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12605670};
CC -!- MASS SPECTROMETRY: Mass=21658; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10874039};
CC -!- SIMILARITY: Belongs to the chloroplast-specific ribosomal protein cS22
CC family. {ECO:0000305}.
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DR EMBL; AF240462; AAF64167.1; -; mRNA.
DR EMBL; KQ152842; KNA13500.1; -; Genomic_DNA.
DR PDB; 5MMJ; EM; 3.65 A; v=1-260.
DR PDB; 5MMM; EM; 3.40 A; v=1-260.
DR PDB; 5X8P; EM; 3.40 A; v=63-260.
DR PDB; 5X8R; EM; 3.70 A; v=63-260.
DR PDBsum; 5MMJ; -.
DR PDBsum; 5MMM; -.
DR PDBsum; 5X8P; -.
DR PDBsum; 5X8R; -.
DR AlphaFoldDB; P82277; -.
DR SMR; P82277; -.
DR STRING; 3562.P82277; -.
DR PRIDE; P82277; -.
DR Proteomes; UP000054095; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Plastid;
KW Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874039,
FT ECO:0000269|PubMed:12605670"
FT CHAIN 63..260
FT /note="30S ribosomal protein 2, chloroplastic"
FT /id="PRO_0000042177"
FT DOMAIN 84..162
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 184..260
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 63..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 260 AA; 28293 MW; 5D3CD265E46CB559 CRC64;
MATISSILPC HGLLQHCSSS SSSSKPKFSS QNLVQLQSFS NGFGLKLKTR VSTNPPLLKV
RAVVTEETSS SSTASSSSDG EGARRLYVGN IPRNLNNDEL RTIVEEHGAI EIAEVMYDKY
SGRSRRFGFV TMKTVEDANA VIEKLNDTEI GGRKIKVNIT EKPLEGMDIA TTQAEDSQFV
ESPYKVYIGN LAKTVTNELL KDFFSEKGKV LGAKVQRTPG TSKSNGFGFV SFSSEEEVEA
AIQALNNSVL EGQKIRVNKA
