RR1_SPIOL
ID RR1_SPIOL Reviewed; 411 AA.
AC P29344; A0A0K9R6V0; P82132; P82133;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=30S ribosomal protein S1, chloroplastic {ECO:0000303|PubMed:10874039};
DE AltName: Full=CS1;
DE AltName: Full=Chloroplastic small ribosomal subunit protein bS1c {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=RPS1; ORFNames=SOVF_099990;
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].
RX PubMed=1527032; DOI=10.1016/s0021-9258(18)41743-7;
RA Franzetti B., Carol P., Mache R.;
RT "Characterization and RNA-binding properties of a chloroplast S1-like
RT ribosomal protein.";
RL J. Biol. Chem. 267:19075-19081(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver; TISSUE=Leaf;
RX PubMed=1508710; DOI=10.1093/nar/20.16.4153;
RA Franzetti B., Zhou D.-X., Mache R.;
RT "Structure and expression of the nuclear gene coding for the plastid CS1
RT ribosomal protein from spinach.";
RL Nucleic Acids Res. 20:4153-4157(1992).
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 PROTEIN SEQUENCE OF 42-51, 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 [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). Actively
CC engaged in the initiation complex formation via a strong mRNA-binding
CC activity. Possesses a poly(A)-binding activity which might play a role
CC as a control element in chloroplast mRNA translation (PubMed:1527032).
CC {ECO:0000269|PubMed:1527032, 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. {ECO:0000269|PubMed:10874039,
CC ECO:0000269|PubMed:28007896}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:10874039, ECO:0000269|PubMed:28007896}.
CC -!- MASS SPECTROMETRY: Mass=40900; Method=MALDI; Note=S1 alpha form.;
CC Evidence={ECO:0000269|PubMed:10874039};
CC -!- MASS SPECTROMETRY: Mass=36890; Method=MALDI; Note=S1 beta form.;
CC Evidence={ECO:0000269|PubMed:10874039};
CC -!- MISCELLANEOUS: Two different forms exist, S1 alpha and S1 beta.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000305}.
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DR EMBL; M82923; AAA34045.1; -; mRNA.
DR EMBL; X66135; CAA46927.1; -; Genomic_DNA.
DR EMBL; KQ148526; KNA15241.1; -; Genomic_DNA.
DR PIR; A44121; A44121.
DR PDB; 5X8P; EM; 3.40 A; 8=42-411.
DR PDB; 5X8R; EM; 3.70 A; 8=42-411.
DR PDBsum; 5X8P; -.
DR PDBsum; 5X8R; -.
DR AlphaFoldDB; P29344; -.
DR SMR; P29344; -.
DR STRING; 3562.P29344; -.
DR PRIDE; P29344; -.
DR OrthoDB; 828313at2759; -.
DR Proteomes; UP000054095; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 3.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR035104; Ribosomal_protein_S1-like.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR Pfam; PF00575; S1; 2.
DR PRINTS; PR00681; RIBOSOMALS1.
DR SMART; SM00316; S1; 3.
DR SUPFAM; SSF50249; SSF50249; 3.
DR PROSITE; PS50126; S1; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Plastid;
KW Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; Transit peptide.
FT TRANSIT 1..41
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874039"
FT CHAIN 42..411
FT /note="30S ribosomal protein S1, chloroplastic"
FT /id="PRO_0000030632"
FT DOMAIN 96..166
FT /note="S1 motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 184..248
FT /note="S1 motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 261..329
FT /note="S1 motif 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
SQ SEQUENCE 411 AA; 44787 MW; 0813BF86217F75D6 CRC64;
MASLAQQLAG GLRCPPLSNS NLSKPFSPKH TLKPRFSPIV SAVAVSNAQT RERQKLKQLF
EDAYERCRNA PMEGVSFTID DFHTALDKYD FNSEMGSRVK GTVFCTDANG ALVDITAKSS
AYLPLAEACI YRIKNVEEAG IIPGVREEFV IIGENEADDS LILSLRQIQY ELAWERCRQL
QAEDVVVKGK IVGANKGGVV ALVEGLRGFV PFSQISSKSS AEELLEKEIP LKFVEVDEEQ
SRLVMSNRKA MADSQAQLGI GSVVTGTVQS LKPYGAFIDI GGINGLLHVS QISHDRVSDI
ATVLQPGDTL KVMILSHDRE RGRVSLSTKK LEPTPGDMIR NPKLVFEKAE EMAQTFRQRI
AQAEAMARAD MLRFQPESGL TLSSDGILGP LTSDLPAEGL DLSVVPPAVE S
