ID   RR4_PHYPA               Reviewed;         201 AA.
AC   Q6YXP3;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=30S ribosomal protein S4, chloroplastic;
GN   Name=rps4;
OS   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004;
RX   PubMed=12954768; DOI=10.1093/nar/gkg726;
RA   Sugiura C., Kobayashi Y., Setsuyuki A., Sugita C., Sugita M.;
RT   "Complete chloroplast DNA sequence of the moss Physcomitrella patens:
RT   evidence for the loss and relocation of rpoA from the chloroplast to the
RT   nucleus.";
RL   Nucleic Acids Res. 31:5324-5331(2003).
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; AP005672; BAC85050.1; -; Genomic_DNA.
DR   RefSeq; NP_904200.1; NC_005087.1.
DR   AlphaFoldDB; Q6YXP3; -.
DR   SMR; Q6YXP3; -.
DR   PRIDE; Q6YXP3; -.
DR   GeneID; 2546775; -.
DR   KEGG; ppp:2546775; -.
DR   InParanoid; Q6YXP3; -.
DR   OrthoDB; 1507367at2759; -.
DR   Proteomes; UP000006727; Chloroplast.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
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; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..201
FT                   /note="30S ribosomal protein S4, chloroplastic"
FT                   /id="PRO_0000132650"
FT   DOMAIN          89..150
FT                   /note="S4 RNA-binding"
SQ   SEQUENCE   201 AA;  23136 MW;  3AE34DD817381BBB CRC64;
     MSRYRGPRVR IIRRLGVLPG LTNKTPQLKS SSANQSTAKK ISQYRIRLEE KQKLRFHYGI
     TERQLLNYVR IARKAKGSTG QILLQLLEMR LDNIVFRLGM APTIPGARQL VNHRHVLVND
     CIVDIPSYRC KPEDSITVKN RQKSQAIITK NIDFSQKSKV PNHLTFDSTQ KKGLVNQILD
     RESIGLKINE LLVVEYYSRQ A