ID   RL10_MOOTA              Reviewed;         176 AA.
AC   Q2RFN7;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=50S ribosomal protein L10 {ECO:0000255|HAMAP-Rule:MF_00362};
GN   Name=rplJ {ECO:0000255|HAMAP-Rule:MF_00362}; OrderedLocusNames=Moth_2470;
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39073 / JCM 9320;
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT   thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(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; CP000232; ABC20752.1; -; Genomic_DNA.
DR   RefSeq; WP_011393947.1; NC_007644.1.
DR   RefSeq; YP_431295.1; NC_007644.1.
DR   AlphaFoldDB; Q2RFN7; -.
DR   SMR; Q2RFN7; -.
DR   STRING; 264732.Moth_2470; -.
DR   EnsemblBacteria; ABC20752; ABC20752; Moth_2470.
DR   GeneID; 61291195; -.
DR   KEGG; mta:Moth_2470; -.
DR   PATRIC; fig|264732.11.peg.2688; -.
DR   eggNOG; COG0244; Bacteria.
DR   HOGENOM; CLU_092227_2_1_9; -.
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..176
FT                   /note="50S ribosomal protein L10"
FT                   /id="PRO_0000234857"
SQ   SEQUENCE   176 AA;  19069 MW;  95E3C861200F8DB1 CRC64;
     MNKQREAKVA ATQEIKDKLG TSILSILADY RGLNVAEMTK LRRQLREAGV EFKVVKNTLT
     ARAARELGLD GLEPHLQGPT AIAFSATDPV APAKILNEVV RNSKTFQIKV GVLQGKIIGI
     NEIKALSDLP SREELLAKMV GGFQAPLSGL VNVLAGNMRN LVYALEAIRK QKEAVA