RR21_SPIOL
ID RR21_SPIOL Reviewed; 180 AA.
AC P82024; A0A0K9RHF9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=30S ribosomal protein S21, chloroplastic {ECO:0000303|PubMed:10874039};
DE AltName: Full=Chloroplastic small ribosomal subunit protein bS21c {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=rps21; ORFNames=SOVF_070750;
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 [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 [2]
RP PROTEIN SEQUENCE OF 80-114, SUBUNIT, SUBCELLULAR LOCATION, AND MASS
RP 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 [3]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.4 ANGSTROMS).
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 [4]
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. {ECO:0000305|PubMed:10874039,
CC 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 (PubMed:10874039, PubMed:28007896). bS21c binds
CC directly to 16S ribosomal RNA (PubMed:10874039).
CC {ECO:0000269|PubMed:10874039, ECO:0000269|PubMed:28007896}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:10874039}.
CC -!- MASS SPECTROMETRY: Mass=13631; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874039};
CC -!- MASS SPECTROMETRY: Mass=13631; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10874039};
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS21 family.
CC {ECO:0000255}.
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DR EMBL; KQ142159; KNA18384.1; -; Genomic_DNA.
DR PDB; 4V61; EM; 9.40 A; U=80-114.
DR PDB; 5MMJ; EM; 3.65 A; u=1-180.
DR PDB; 5MMM; EM; 3.40 A; u=1-180.
DR PDB; 5X8P; EM; 3.40 A; u=44-180.
DR PDB; 5X8R; EM; 3.70 A; u=44-180.
DR PDB; 6ERI; EM; 3.00 A; BU=83-141.
DR PDBsum; 4V61; -.
DR PDBsum; 5MMJ; -.
DR PDBsum; 5MMM; -.
DR PDBsum; 5X8P; -.
DR PDBsum; 5X8R; -.
DR PDBsum; 6ERI; -.
DR AlphaFoldDB; P82024; -.
DR SMR; P82024; -.
DR STRING; 3562.P82024; -.
DR OrthoDB; 1513992at2759; -.
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 GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 1.20.5.1150; -; 1.
DR HAMAP; MF_00358; Ribosomal_S21; 1.
DR InterPro; IPR001911; Ribosomal_S21.
DR InterPro; IPR038380; S21_sf.
DR PANTHER; PTHR21109; PTHR21109; 1.
DR Pfam; PF01165; Ribosomal_S21; 1.
DR PRINTS; PR00976; RIBOSOMALS21.
DR TIGRFAMs; TIGR00030; S21p; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Plastid;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; Transit peptide.
FT TRANSIT 1..79
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874039"
FT CHAIN 80..180
FT /note="30S ribosomal protein S21, chloroplastic"
FT /id="PRO_0000249185"
FT REGION 14..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 180 AA; 20582 MW; D01E38EA61D12404 CRC64;
MASTSSLLNF LSPLFPSNTS LPPSSNPKFP NPNSLSSQQN SISISSKKHE NAAIAKKEEY
PGDLMAVVCP SLAFSNTLYF RSAYNVQVLV DDNENEERLL NRFRREVMRA GVIQECKRRR
YFENKQEEKK RKHREAAKRN SRRRRGPFRG PFPGKEEATK VDKKEDDGDN WDMPEGGAPF
