ID   RL3_ERYLH               Reviewed;         289 AA.
AC   Q2N9B1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=ELI_08190;
OS   Erythrobacter litoralis (strain HTCC2594).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=314225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2594;
RX   PubMed=19168610; DOI=10.1128/jb.00026-09;
RA   Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT   "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL   J. Bacteriol. 191:2419-2420(2009).
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; CP000157; ABC63730.1; -; Genomic_DNA.
DR   RefSeq; WP_011414562.1; NC_007722.1.
DR   AlphaFoldDB; Q2N9B1; -.
DR   SMR; Q2N9B1; -.
DR   STRING; 314225.ELI_08190; -.
DR   EnsemblBacteria; ABC63730; ABC63730; ELI_08190.
DR   KEGG; eli:ELI_08190; -.
DR   eggNOG; COG0087; Bacteria.
DR   HOGENOM; CLU_044142_2_0_5; -.
DR   OMA; KRMAGRY; -.
DR   OrthoDB; 1270636at2; -.
DR   Proteomes; UP000008808; Chromosome.
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; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..289
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_1000052047"
FT   REGION          230..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..261
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         152
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01325"
SQ   SEQUENCE   289 AA;  30935 MW;  43A2088641D75B5C CRC64;
     MRTGVIAKKV GMTRLFQEDG RHVPVTVLAL EDCQVVSQRT QERDGYFALQ VGSGVAKQKN
     VAKPQREAFA KAEVGLKMKV AEFRVEGEDG LLPVGAAISA EHFIAGQKVD ITGYTQGKGF
     AGAMKRWGFG GLRATHGVSI SHRSHGSTGN RQDPGRVFKG KKMAGHMGDR QRTQQNLEVV
     RTDPERGLIF VKGSVPGTKN SWMLIRDAVK LPLPEGVPFP GAVVEKNAPA KEADAPAADE
     QKLDDVANEE AVVEEKAADK QTNDTAAPAE ETPAEEAPKA DDSDAGKEG