ID   RL19_BRASO              Reviewed;         128 AA.
AC   A4YK97;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=50S ribosomal protein L19 {ECO:0000255|HAMAP-Rule:MF_00402};
GN   Name=rplS {ECO:0000255|HAMAP-Rule:MF_00402}; OrderedLocusNames=BRADO0375;
OS   Bradyrhizobium sp. (strain ORS 278).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=114615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ORS 278;
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
CC   -!- FUNCTION: This protein is located at the 30S-50S ribosomal subunit
CC       interface and may play a role in the structure and function of the
CC       aminoacyl-tRNA binding site. {ECO:0000255|HAMAP-Rule:MF_00402}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL19 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00402}.
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DR   EMBL; CU234118; CAL74323.1; -; Genomic_DNA.
DR   RefSeq; WP_011923604.1; NC_009445.1.
DR   AlphaFoldDB; A4YK97; -.
DR   SMR; A4YK97; -.
DR   STRING; 114615.BRADO0375; -.
DR   EnsemblBacteria; CAL74323; CAL74323; BRADO0375.
DR   KEGG; bra:BRADO0375; -.
DR   eggNOG; COG0335; Bacteria.
DR   HOGENOM; CLU_103507_2_1_5; -.
DR   OMA; TITVYYE; -.
DR   OrthoDB; 1698718at2; -.
DR   BioCyc; BSP114615:BRADO_RS01775-MON; -.
DR   Proteomes; UP000001994; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.30.790; -; 1.
DR   HAMAP; MF_00402; Ribosomal_L19; 1.
DR   InterPro; IPR038657; L19_sf.
DR   InterPro; IPR001857; Ribosomal_L19.
DR   InterPro; IPR018257; Ribosomal_L19_CS.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR15680; PTHR15680; 1.
DR   Pfam; PF01245; Ribosomal_L19; 1.
DR   PIRSF; PIRSF002191; Ribosomal_L19; 1.
DR   PRINTS; PR00061; RIBOSOMALL19.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   TIGRFAMs; TIGR01024; rplS_bact; 1.
DR   PROSITE; PS01015; RIBOSOMAL_L19; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..128
FT                   /note="50S ribosomal protein L19"
FT                   /id="PRO_1000049640"
SQ   SEQUENCE   128 AA;  14409 MW;  81E5A6A7C152B32A CRC64;
     MNLIQQLEKE QFDKLSANKT IPEFGPGDTV IVNVKVVEGE RTRVQAYEGV CIGRSGGGIN
     ESFTVRKISY GEGVERVFPI LSPMIDSIKV VRRGKVRRAK LYYLRQLRGK SARIVEKQDR
     QQAAAVNE