ID   RR4_ATRBE               Reviewed;         201 AA.
AC   Q8S8X2;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=30S ribosomal protein S4, chloroplastic;
GN   Name=rps4;
OS   Atropa belladonna (Belladonna) (Deadly nightshade).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Hyoscyameae; Atropa.
OX   NCBI_TaxID=33113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Ab5p(kan);
RX   PubMed=12200487; DOI=10.1093/oxfordjournals.molbev.a004222;
RA   Schmitz-Linneweber C., Regel R., Du T.G., Hupfer H., Herrmann R.G.,
RA   Maier R.M.;
RT   "The plastid chromosome of Atropa belladonna and its comparison with that
RT   of Nicotiana tabacum: the role of RNA editing in generating divergence in
RT   the process of plant speciation.";
RL   Mol. Biol. Evol. 19:1602-1612(2002).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
CC       {ECO:0000250}.
CC   -!- FUNCTION: With S5 and S12 plays an important role in translational
CC       accuracy. {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. The
CC       interaction surface between S4 and S5 is involved in control of
CC       translational fidelity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ316582; CAC88046.1; -; Genomic_DNA.
DR   RefSeq; NP_783234.1; NC_004561.1.
DR   AlphaFoldDB; Q8S8X2; -.
DR   SMR; Q8S8X2; -.
DR   GeneID; 806499; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00165; S4; 1.
DR   Gene3D; 3.10.290.10; -; 1.
DR   HAMAP; MF_01306_B; Ribosomal_S4_B; 1.
DR   InterPro; IPR022801; Ribosomal_S4/S9.
DR   InterPro; IPR001912; Ribosomal_S4/S9_N.
DR   InterPro; IPR005709; Ribosomal_S4_bac-type.
DR   InterPro; IPR018079; Ribosomal_S4_CS.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   PANTHER; PTHR11831; PTHR11831; 1.
DR   Pfam; PF00163; Ribosomal_S4; 1.
DR   Pfam; PF01479; S4; 1.
DR   SMART; SM01390; Ribosomal_S4; 1.
DR   SMART; SM00363; S4; 1.
DR   TIGRFAMs; TIGR01017; rpsD_bact; 1.
DR   PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Plastid; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..201
FT                   /note="30S ribosomal protein S4, chloroplastic"
FT                   /id="PRO_0000132541"
FT   DOMAIN          89..149
FT                   /note="S4 RNA-binding"
FT   REGION          17..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   201 AA;  23407 MW;  A6FAB64817B1875B CRC64;
     MSRYRGPRFK KIRRLGALPG LTNKKPRTGS DLRNQSRSGK KSQYRIRLEE KQKLRFHYGL
     TERQLLKYVR IARKAKGSTG QVLLQLLEMR LDNILFRLGM ASTIPAARQL VNHRHILVNG
     RIVDIPSYRC KPRDIITAKD EQKSRALIQI SLDSSPHEEL PNHLTLHPFQ YKGLVNQIID
     SKWVGLKINE LLVVEYYSRQ T