ID   RL3_BRUAB               Reviewed;         237 AA.
AC   Q57CQ8;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=BruAb1_1238;
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).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC       subunit. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC       proteins L14 and L19. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC   -!- PTM: Methylated by PrmB. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01325}.
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DR   EMBL; AE017223; AAX74576.1; -; Genomic_DNA.
DR   RefSeq; WP_002964362.1; NC_006932.1.
DR   AlphaFoldDB; Q57CQ8; -.
DR   SMR; Q57CQ8; -.
DR   EnsemblBacteria; AAX74576; AAX74576; BruAb1_1238.
DR   GeneID; 3787853; -.
DR   KEGG; bmb:BruAb1_1238; -.
DR   HOGENOM; CLU_044142_2_0_5; -.
DR   OMA; KRMAGRY; -.
DR   Proteomes; UP000000540; Chromosome I.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F: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   HAMAP; MF_01325_B; Ribosomal_L3_B; 1.
DR   InterPro; IPR000597; Ribosomal_L3.
DR   InterPro; IPR019927; Ribosomal_L3_bac/org-type.
DR   InterPro; IPR019926; Ribosomal_L3_CS.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR11229; PTHR11229; 1.
DR   Pfam; PF00297; Ribosomal_L3; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   TIGRFAMs; TIGR03625; L3_bact; 1.
DR   PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE   3: Inferred from homology;
KW   Methylation; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..237
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_0000241323"
FT   REGION          133..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         151
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01325"
SQ   SEQUENCE   237 AA;  25064 MW;  C89617EBC6E50AE5 CRC64;
     MRSGVIAQKL GMTRVYNDAG EHVPVTVLRM ENCHVVAQRT VEKNGYTAVQ LGVGMAKVKN
     TSKAMRGHFA KAEVEPKAKL AEFRVSPDNL LEVGVEITAE HFVAGQKVDV TGTSIGKGFA
     GVMKRHNFGG HRASHGNSIT HRSHGSTGQR QDPGKVFKGK KMAGHMGQTR VTTQNIEVVS
     TDSDRGLILV RGAVPGSKGA WILVRDAVKA SLPENAPKPA GLRAGAKAEA AATEGGE