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RR5_SPIOL
ID   RR5_SPIOL               Reviewed;         308 AA.
AC   Q9ST69; A0A0K9QCC0; P82131;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=30S ribosomal protein S5, chloroplastic {ECO:0000303|PubMed:10874039};
DE   AltName: Full=Chloroplastic small ribosomal subunit protein uS5c {ECO:0000303|PubMed:28007896};
DE   Flags: Precursor;
GN   Name=rps5; ORFNames=SOVF_195380;
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].
RC   STRAIN=cv. Melody; TISSUE=Leaf;
RA   Trifa Y., Diederich L., Lerbs-Mache S.;
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   PROTEIN SEQUENCE OF 56-87; 115-126; 148-160; 168-173; 184-190; 196-209;
RP   211-218; 220-222; 227-253; 255-268 AND 300-306.
RA   Yamaguchi K., von Knoblauch K., Subramanian A.R.;
RL   Submitted (OCT-1999) to UniProtKB.
RN   [4]
RP   PROTEIN SEQUENCE OF 56-87, 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 (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   [6]
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). uS5c binds
CC       directly to 16S ribosomal RNA (Ref.3). {ECO:0000269|PubMed:10874039,
CC       ECO:0000269|PubMed:28007896, ECO:0000269|Ref.3}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:10874039, ECO:0000269|PubMed:28007896}.
CC   -!- MASS SPECTROMETRY: Mass=27730; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10874039};
CC   -!- MASS SPECTROMETRY: Mass=27784; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10874039};
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC       {ECO:0000305}.
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DR   EMBL; X93159; CAA63650.1; -; mRNA.
DR   EMBL; KQ197116; KNA04905.1; -; Genomic_DNA.
DR   PDB; 4V61; EM; 9.40 A; AE=1-308.
DR   PDB; 5MMJ; EM; 3.65 A; e=1-308.
DR   PDB; 5MMM; EM; 3.40 A; e=1-308.
DR   PDB; 5X8P; EM; 3.40 A; e=56-308.
DR   PDB; 5X8R; EM; 3.70 A; e=56-308.
DR   PDB; 6ERI; EM; 3.00 A; BE=151-308.
DR   PDBsum; 4V61; -.
DR   PDBsum; 5MMJ; -.
DR   PDBsum; 5MMM; -.
DR   PDBsum; 5X8P; -.
DR   PDBsum; 5X8R; -.
DR   PDBsum; 6ERI; -.
DR   AlphaFoldDB; Q9ST69; -.
DR   SMR; Q9ST69; -.
DR   STRING; 3562.Q9ST69; -.
DR   PRIDE; Q9ST69; -.
DR   OrthoDB; 1504411at2759; -.
DR   EvolutionaryTrace; Q9ST69; -.
DR   Proteomes; UP000054095; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005763; C:mitochondrial small ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IEA:UniProt.
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:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_01307_B; Ribosomal_S5_B; 1.
DR   InterPro; IPR000851; Ribosomal_S5.
DR   InterPro; IPR005712; Ribosomal_S5_bac-type.
DR   InterPro; IPR005324; Ribosomal_S5_C.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR013810; Ribosomal_S5_N.
DR   InterPro; IPR018192; Ribosomal_S5_N_CS.
DR   PANTHER; PTHR13718; PTHR13718; 1.
DR   Pfam; PF00333; Ribosomal_S5; 1.
DR   Pfam; PF03719; Ribosomal_S5_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR01021; rpsE_bact; 1.
DR   PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR   PROSITE; PS50881; S5_DSRBD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic resistance; Chloroplast;
KW   Direct protein sequencing; Plastid; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding; Transit peptide.
FT   TRANSIT         1..55
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:10874039, ECO:0000269|Ref.3"
FT   CHAIN           56..308
FT                   /note="30S ribosomal protein S5, chloroplastic"
FT                   /id="PRO_0000248272"
FT   DOMAIN          152..215
FT                   /note="S5 DRBM"
FT   CONFLICT        59
FT                   /note="K -> T (in Ref. 2; KNA04905)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   308 AA;  33581 MW;  EE8E29B8D43E1CB1 CRC64;
     MATTATTTPS ATSLTTLHRR IPLFPTTTTL LSLSSSSKPL FLSLSSTRSF PTHLYCIKKD
     DIDITFFEQD NPDEEITFDP PEKPEGYIPP RAVDEPPFES EEEIALAYEE LYGAAYSGES
     LLGNDVYAMD SKIKKATGFG SKSKKEKIRD GFEENVVQVR RVTKVVKGGK HMRFRAIVVV
     GDKKGQVGVG VGKAKEVVSA VQKAAVDARR NIITVPMTKY LTFPHRNEAD YGAARVMLRP
     AAPGTGVIAG GAVRTVLEMA GVENALGKQL GSNNALNNAR ATIVAVQTMR QFSDVARDRG
     IPMEELWK
 
 
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