ID   RL3_PASMU               Reviewed;         209 AA.
AC   Q9CL32;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Synonyms=rpl3 {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=PM1415;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03499.1; -; Genomic_DNA.
DR   RefSeq; WP_005724032.1; NC_002663.1.
DR   AlphaFoldDB; Q9CL32; -.
DR   SMR; Q9CL32; -.
DR   STRING; 747.DR93_268; -.
DR   PRIDE; Q9CL32; -.
DR   EnsemblBacteria; AAK03499; AAK03499; PM1415.
DR   GeneID; 62225668; -.
DR   KEGG; pmu:PM1415; -.
DR   HOGENOM; CLU_044142_4_1_6; -.
DR   OMA; KRMAGRY; -.
DR   Proteomes; UP000000809; 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..209
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_0000077131"
FT   MOD_RES         150
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01325"
SQ   SEQUENCE   209 AA;  22383 MW;  393D9E0FC016E3DD CRC64;
     MIGLVGRKVG MTRIFNEDGV SIPVTVIEIE ANRVTQVKTV ETDGYSAIQV TTGSKKASRV
     TKPEAGHFVK AGVEAGRGLW EFRTTEGEEF TLGQEINVDI FADVKKVDVT GTSKGKGFAG
     GVKRWNFRTQ DATHGNSLSH RVLGSIGQNQ TPGRVFKGKK MAGHLGNERV TVQSLEVVRV
     DAERKLLLVK GAVPGATNGD VIVKPAVKA