RL10_HAES1
ID RL10_HAES1 Reviewed; 163 AA.
AC Q0I0V0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-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=HS_0171;
OS Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=205914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129Pt;
RX PubMed=17172329; DOI=10.1128/jb.01422-06;
RA Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA Xie G., Inzana T.J.;
RT "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT influenzae Rd.";
RL J. Bacteriol. 189:1890-1898(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000436; ABI24449.1; -; Genomic_DNA.
DR RefSeq; WP_011608324.1; NC_008309.1.
DR AlphaFoldDB; Q0I0V0; -.
DR STRING; 205914.HS_0171; -.
DR EnsemblBacteria; ABI24449; ABI24449; HS_0171.
DR KEGG; hso:HS_0171; -.
DR eggNOG; COG0244; Bacteria.
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 Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..163
FT /note="50S ribosomal protein L10"
FT /id="PRO_1000005508"
SQ SEQUENCE 163 AA; 17548 MW; 564888A368DA643E CRC64;
MALNLQDKQA IVAEVNEAAK GALSAVIADS RGVTVDKMTE LRKAAREAGV SMRVVRNTLL
RRAVEGTAFE CLTDTFVGPT LIAFSNEHPG AAARLFKDFA KANDKFEIKG AAFEGKIQNV
EFLATLPTYE EAIARLMGTM KEAAAGKLAR TLAAYRDKLQ EAA