ID   RL10_ECOSE              Reviewed;         165 AA.
AC   B6I5J5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=50S ribosomal protein L10 {ECO:0000255|HAMAP-Rule:MF_00362};
GN   Name=rplJ {ECO:0000255|HAMAP-Rule:MF_00362}; OrderedLocusNames=ECSE_4272;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA   Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL   DNA Res. 15:375-386(2008).
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; AP009240; BAG79796.1; -; Genomic_DNA.
DR   RefSeq; WP_001207201.1; NC_011415.1.
DR   AlphaFoldDB; B6I5J5; -.
DR   SMR; B6I5J5; -.
DR   EnsemblBacteria; BAG79796; BAG79796; ECSE_4272.
DR   GeneID; 67415314; -.
DR   KEGG; ecy:ECSE_4272; -.
DR   HOGENOM; CLU_092227_0_2_6; -.
DR   OMA; VRDQKQA; -.
DR   Proteomes; UP000008199; 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; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..165
FT                   /note="50S ribosomal protein L10"
FT                   /id="PRO_1000120958"
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