ID   RL3_RHOPA               Reviewed;         241 AA.
AC   P60456;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
DE   AltName: Full=RRP-L3;
GN   Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=RPA3250;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 143-170, POST-TRANSLATIONAL MODIFICATIONS, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=15473684; DOI=10.1021/pr049940z;
RA   Strader M.B., VerBerkmoes N.C., Tabb D.L., Connelly H.M., Barton J.W.,
RA   Bruce B.D., Pelletier D.A., Davison B.H., Hettich R.L., Larimer F.W.,
RA   Hurst G.B.;
RT   "Characterization of the 70S ribosome from Rhodopseudomonas palustris using
RT   an integrated 'top-down' and 'bottom-up' mass spectrometric approach.";
RL   J. Proteome Res. 3:965-978(2004).
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, on either Lys-155 or Lys-158.
CC   -!- PTM: Methylated by PrmB. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC   -!- MASS SPECTROMETRY: Mass=25622.2; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15473684};
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01325}.
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DR   EMBL; BX572603; CAE28691.1; -; Genomic_DNA.
DR   RefSeq; WP_011158795.1; NC_005296.1.
DR   AlphaFoldDB; P60456; -.
DR   SMR; P60456; -.
DR   IntAct; P60456; 1.
DR   STRING; 258594.RPA3250; -.
DR   PRIDE; P60456; -.
DR   EnsemblBacteria; CAE28691; CAE28691; RPA3250.
DR   GeneID; 66894336; -.
DR   KEGG; rpa:RPA3250; -.
DR   eggNOG; COG0087; Bacteria.
DR   HOGENOM; CLU_044142_2_0_5; -.
DR   OMA; KRMAGRY; -.
DR   PhylomeDB; P60456; -.
DR   BioCyc; RPAL258594:TX73_RS16580-MON; -.
DR   Proteomes; UP000001426; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Methylation; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..241
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_0000077145"
FT   REGION          139..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..153
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   241 AA;  25608 MW;  2EFED16235668352 CRC64;
     MRSGVIAQKV GMTRVFTEAG EHIPVTVLKL GNCQVLGHRT KEKNGYVALQ VGSGSRKTVY
     MPKAERGQFA AAKVEPKRKV EEFRVSEDAL LPVGAEIQAD HFVVGQFVDV TGTSTGKGFA
     GGMKRWNFGG LRATHGVSVS HRSIGSTGGR QDPGKTFKNK KMPGHMGVDR VTTLNLRVVQ
     TDVERGLILV EGAVPGTKGG WIRVRDAVKK ALPADAPKPG KFRLANGDAA AEAPAAEQEG
     A