ID   RL10_ACIF5              Reviewed;         173 AA.
AC   B5ELX0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=50S ribosomal protein L10 {ECO:0000255|HAMAP-Rule:MF_00362};
GN   Name=rplJ {ECO:0000255|HAMAP-Rule:MF_00362}; OrderedLocusNames=Lferr_0488;
OS   Acidithiobacillus ferrooxidans (strain ATCC 53993 / BNL-5-31)
OS   (Leptospirillum ferrooxidans (ATCC 53993)).
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=380394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53993 / BNL-5-31;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Borole A.P.;
RT   "Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001132; ACH82742.1; -; Genomic_DNA.
DR   RefSeq; WP_009568780.1; NC_011206.1.
DR   AlphaFoldDB; B5ELX0; -.
DR   SMR; B5ELX0; -.
DR   GeneID; 66431374; -.
DR   KEGG; afe:Lferr_0488; -.
DR   eggNOG; COG0244; Bacteria.
DR   HOGENOM; CLU_092227_0_0_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   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..173
FT                   /note="50S ribosomal protein L10"
FT                   /id="PRO_1000120906"
SQ   SEQUENCE   173 AA;  18722 MW;  079DA0CDC0209D83 CRC64;
     MSLKLAEKEQ VVATLQTRLT RAQATVVAEY RGLTVAQMTV FRAEAQKQSV HVQVVKNTLL
     KRALAGTPFA VMDHLLKGPL VFAAAEDPVA LAKLFTDHAK RLEKLVIIGG VLSGKQIDAA
     AIAQLSKMPS REELLAKLLG TMQAPVAGFV RTLNEVPSRF VRTLAAVRDQ RAA