ID   RL10_SHIDS              Reviewed;         165 AA.
AC   Q32AF7;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=50S ribosomal protein L10 {ECO:0000255|HAMAP-Rule:MF_00362};
GN   Name=rplJ {ECO:0000255|HAMAP-Rule:MF_00362}; OrderedLocusNames=SDY_3743;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Forms part of the ribosomal stalk, playing a central role in
CC       the interaction of the ribosome with GTP-bound translation factors.
CC       {ECO:0000255|HAMAP-Rule:MF_00362}.
CC   -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit. The
CC       N-terminus interacts with L11 and the large rRNA to form the base of
CC       the stalk. The C-terminus forms an elongated spine to which L12 dimers
CC       bind in a sequential fashion forming a multimeric L10(L12)X complex.
CC       {ECO:0000255|HAMAP-Rule:MF_00362}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00362}.
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DR   EMBL; CP000034; ABB63698.1; -; Genomic_DNA.
DR   RefSeq; WP_001207201.1; NC_007606.1.
DR   RefSeq; YP_405189.1; NC_007606.1.
DR   AlphaFoldDB; Q32AF7; -.
DR   SMR; Q32AF7; -.
DR   STRING; 300267.SDY_3743; -.
DR   EnsemblBacteria; ABB63698; ABB63698; SDY_3743.
DR   GeneID; 67415314; -.
DR   KEGG; sdy:SDY_3743; -.
DR   PATRIC; fig|300267.13.peg.4438; -.
DR   HOGENOM; CLU_092227_0_2_6; -.
DR   OMA; VRDQKQA; -.
DR   Proteomes; UP000002716; Chromosome.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0070180; F:large ribosomal subunit 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; cd05797; Ribosomal_L10; 1.
DR   Gene3D; 3.30.70.1730; -; 1.
DR   HAMAP; MF_00362; Ribosomal_L10; 1.
DR   InterPro; IPR022973; Ribosomal_L10.
DR   InterPro; IPR043141; Ribosomal_L10-like_sf.
DR   InterPro; IPR002363; Ribosomal_L10_eubac_CS.
DR   InterPro; IPR001790; Ribosomal_L10P.
DR   PANTHER; PTHR11560; PTHR11560; 1.
DR   Pfam; PF00466; Ribosomal_L10; 1.
DR   SUPFAM; SSF160369; SSF160369; 1.
DR   PROSITE; PS01109; RIBOSOMAL_L10; 1.
PE   3: Inferred from homology;
KW   Acetylation; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..165
FT                   /note="50S ribosomal protein L10"
FT                   /id="PRO_0000234886"
FT   MOD_RES         37
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00362"
FT   MOD_RES         105
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00362"
SQ   SEQUENCE   165 AA;  17712 MW;  F15822B0EDB6AC02 CRC64;
     MALNLQDKQA IVAEVSEVAK GALSAVVADS RGVTVDKMTE LRKAGREAGV YMRVVRNTLL
     RRAVEGTPFE CLKDAFVGPT LIAYSMEHPG AAARLFKEFA KANAKFEVKA AAFEGELIPA
     SQIDRLATLP TYEEAIARLM ATMKEASAGK LVRTLAAVRD AKEAA