ID A0A0S2W5F2_9FIRM Unreviewed; 175 AA.
AC A0A0S2W5F2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Large ribosomal subunit protein uL10 {ECO:0000256|HAMAP-Rule:MF_00362};
GN Name=rplJ {ECO:0000256|HAMAP-Rule:MF_00362};
GN ORFNames=IB211_02107 {ECO:0000313|EMBL:ALP94498.1};
OS Intestinimonas butyriciproducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Intestinimonas.
OX NCBI_TaxID=1297617 {ECO:0000313|EMBL:ALP94498.1, ECO:0000313|Proteomes:UP000064844};
RN [1] {ECO:0000313|EMBL:ALP94498.1, ECO:0000313|Proteomes:UP000064844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF211 {ECO:0000313|EMBL:ALP94498.1,
RC ECO:0000313|Proteomes:UP000064844};
RX PubMed=26620920; DOI=10.1038/ncomms10062;
RA Bui T.P., Ritari J., Boeren S., de Waard P., Plugge C.M., de Vos W.M.;
RT "Production of butyrate from lysine and the Amadori product fructoselysine
RT by a human gut commensal.";
RL Nat. Commun. 6:10062-10062(2015).
RN [2] {ECO:0000313|Proteomes:UP000064844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF211 {ECO:0000313|Proteomes:UP000064844};
RA de Vos W.M., Bui N.T.P., Plugge C.M., Ritari J.;
RT "A butyrogenic pathway from the amino acid lysine in a human gut
RT commensal.";
RL Submitted (APR-2015) 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:0000256|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:0000256|HAMAP-Rule:MF_00362}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000256|ARBA:ARBA00008889, ECO:0000256|HAMAP-Rule:MF_00362}.
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DR EMBL; CP011307; ALP94498.1; -; Genomic_DNA.
DR RefSeq; WP_058117987.1; NZ_CP011307.1.
DR AlphaFoldDB; A0A0S2W5F2; -.
DR STRING; 1297617.IB211_02107; -.
DR KEGG; ibu:IB211_02107; -.
DR PATRIC; fig|1297617.4.peg.2173; -.
DR eggNOG; COG0244; Bacteria.
DR Proteomes; UP000064844; 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 Gene3D; 6.10.250.290; -; 1.
DR HAMAP; MF_00362; Ribosomal_L10; 1.
DR InterPro; IPR001790; Ribosomal_uL10.
DR InterPro; IPR043141; Ribosomal_uL10-like_sf.
DR InterPro; IPR022973; Ribosomal_uL10_bac.
DR InterPro; IPR047865; Ribosomal_uL10_bac_type.
DR InterPro; IPR002363; Ribosomal_uL10_CS_bac.
DR PANTHER; PTHR11560; 39S RIBOSOMAL PROTEIN L10, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11560:SF8; 39S RIBOSOMAL PROTEIN L10, MITOCHONDRIAL; 1.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR SUPFAM; SSF160369; Ribosomal protein L10-like; 1.
DR PROSITE; PS01109; RIBOSOMAL_L10; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000064844};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_00362};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_00362}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_00362};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00362}.
SQ SEQUENCE 175 AA; 18537 MW; 3BDAD1D614E67F96 CRC64;
MPNAKILSEK QAVVAELTEK LKSAASGVLV DYKGITVAED TALRTECRKN EVDYAVVKNT
LVRFAINSVG MEEMDSALNG TTSLAVSHGD PIAPMRVINK FAKQFNGSKF AIKAGFMDGK
VLSLEEINAL AELPSKEVLQ AQVLGTMLAP ITSLAIVVKA ICEQKGGSVE APAAE
//