RL10_BRUAB
ID RL10_BRUAB Reviewed; 172 AA.
AC P41107; Q57CP6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=50S ribosomal protein L10;
GN Name=rplJ; OrderedLocusNames=BruAb1_1250;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-143.
RC STRAIN=19;
RX PubMed=8125331; DOI=10.1016/0378-1119(94)90744-7;
RA Oliveira S.C., Zhu Y., Splitter G.A.;
RT "Sequences of the rplJL operon containing the L10 and L7/L12 genes from
RT Brucella abortus.";
RL Gene 140:137-138(1994).
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:0000250}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23000.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE017223; AAX74588.1; -; Genomic_DNA.
DR EMBL; L23505; AAA23000.1; ALT_FRAME; Genomic_DNA.
DR PIR; I40349; I40349.
DR RefSeq; WP_011265350.1; NC_006932.1.
DR AlphaFoldDB; P41107; -.
DR SMR; P41107; -.
DR EnsemblBacteria; AAX74588; AAX74588; BruAb1_1250.
DR KEGG; bmb:BruAb1_1250; -.
DR HOGENOM; CLU_092227_0_0_5; -.
DR OMA; VRDQKQA; -.
DR Proteomes; UP000000540; Chromosome I.
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..172
FT /note="50S ribosomal protein L10"
FT /id="PRO_0000154599"
FT CONFLICT 71
FT /note="V -> A (in Ref. 2; AAA23000)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="A -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 172 AA; 17973 MW; 5DC5A40297E6E065 CRC64;
MDRAEKREFV AWLNGAFKES GSVVVAHYTG LTVAQMSDLR SKMRDAGGSV KVAKNRLAKI
ALQGTESEGI VDLFTGQTVV AYANDPITAP KVAVEFAKAN DKLVILGGAM GATTLNADGV
KSLASLPSLD ELRAKLVGMI QTPAQRLAVL TSAPAGQIAR VIGAHARKNE AA
