RL10_ECOBW
ID RL10_ECOBW Reviewed; 165 AA.
AC C5A0S5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=50S ribosomal protein L10 {ECO:0000255|HAMAP-Rule:MF_00362};
GN Name=rplJ {ECO:0000255|HAMAP-Rule:MF_00362}; OrderedLocusNames=BWG_3644;
OS Escherichia coli (strain K12 / MC4100 / BW2952).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=595496;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MC4100 / BW2952;
RX PubMed=19376874; DOI=10.1128/jb.00118-09;
RA Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA Wang L.;
RT "Genomic sequencing reveals regulatory mutations and recombinational events
RT in the widely used MC4100 lineage of Escherichia coli K-12.";
RL J. Bacteriol. 191:4025-4029(2009).
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; CP001396; ACR61847.1; -; Genomic_DNA.
DR RefSeq; WP_001207201.1; NC_012759.1.
DR AlphaFoldDB; C5A0S5; -.
DR SMR; C5A0S5; -.
DR PRIDE; C5A0S5; -.
DR GeneID; 67415314; -.
DR KEGG; ebw:BWG_3644; -.
DR HOGENOM; CLU_092227_0_2_6; -.
DR OMA; VRDQKQA; -.
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_1000205440"
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