RR9_SPIOL
ID RR9_SPIOL Reviewed; 208 AA.
AC P82278; A0A0K9RY17;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=30S ribosomal protein S9, chloroplastic {ECO:0000303|PubMed:24352233};
DE AltName: Full=Chloroplastic small ribosomal subunit protein uS9c {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=PRPS9; ORFNames=SOVF_016530;
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 {ECO:0000305};
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 NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 52-61; 103-114 AND 117-128,
RP SUBUNIT, SUBCELLULAR LOCATION, ACETYLATION AT THR-52, 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), AND INTERACTION WITH
RP PSRP1.
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). uS9c binds
CC directly to 16S ribosomal RNA (PubMed:10874039). uS9c interacts with
CC translation factor pY (PSRP1) (PubMed:18042701).
CC {ECO:0000269|PubMed:10874039, ECO:0000269|PubMed:18042701,
CC ECO:0000269|PubMed:28007896}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:10874039, ECO:0000269|PubMed:28007896}.
CC -!- MASS SPECTROMETRY: Mass=17106; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874039};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS9 family.
CC {ECO:0000305}.
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DR EMBL; KQ133176; KNA24353.1; -; Genomic_DNA.
DR EMBL; AF242547; AAF64170.1; -; mRNA.
DR PDB; 4V61; EM; 9.40 A; AI=12-208.
DR PDB; 5MMJ; EM; 3.65 A; i=1-208.
DR PDB; 5MMM; EM; 3.40 A; i=1-208.
DR PDB; 5X8P; EM; 3.40 A; i=52-208.
DR PDB; 5X8R; EM; 3.70 A; i=52-208.
DR PDB; 6ERI; EM; 3.00 A; BI=67-207.
DR PDBsum; 4V61; -.
DR PDBsum; 5MMJ; -.
DR PDBsum; 5MMM; -.
DR PDBsum; 5X8P; -.
DR PDBsum; 5X8R; -.
DR PDBsum; 6ERI; -.
DR AlphaFoldDB; P82278; -.
DR SMR; P82278; -.
DR STRING; 3562.P82278; -.
DR iPTMnet; P82278; -.
DR OrthoDB; 1430790at2759; -.
DR EvolutionaryTrace; P82278; -.
DR Proteomes; UP000054095; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000312; C:plastid small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_00532_B; Ribosomal_S9_B; 1.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR000754; Ribosomal_S9.
DR InterPro; IPR023035; Ribosomal_S9_bac/plastid.
DR InterPro; IPR020574; Ribosomal_S9_CS.
DR PANTHER; PTHR21569; PTHR21569; 1.
DR Pfam; PF00380; Ribosomal_S9; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR PROSITE; PS00360; RIBOSOMAL_S9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chloroplast; Direct protein sequencing; Plastid;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874039"
FT CHAIN 52..208
FT /note="30S ribosomal protein S9, chloroplastic"
FT /id="PRO_0000030643"
FT REGION 185..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..208
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:10874039"
SQ SEQUENCE 208 AA; 22382 MW; E5CACAFE18FD34D5 CRC64;
MAVSISSLTS SFASLSFTSN LTPKPQTLPM ARTKPFSLSN PAVVKPLVIT ATSATAPVEV
AETADLEKFV KSRLPGGFAA QTVIGTGRRK CAIARVVLQE GTGKFIINYR DAKEYLQGNP
LWLQYVKTPL ATLGYETNYD VFVKAHGGGL SGQAQAISLG VARALLKVSA SHRAPLKQEG
LLTRDSRIVE RKKPGLKKAR KAPQFSKR
