ID   RL3_MYCPN               Reviewed;         287 AA.
AC   P75580;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=MPN_165;
GN   ORFNames=MP666;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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   -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01325}.
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DR   EMBL; U00089; AAB96314.1; -; Genomic_DNA.
DR   PIR; S73992; S73992.
DR   RefSeq; NP_109853.1; NC_000912.1.
DR   RefSeq; WP_010874522.1; NC_000912.1.
DR   AlphaFoldDB; P75580; -.
DR   SMR; P75580; -.
DR   IntAct; P75580; 12.
DR   STRING; 272634.MPN_165; -.
DR   PRIDE; P75580; -.
DR   EnsemblBacteria; AAB96314; AAB96314; MPN_165.
DR   KEGG; mpn:MPN_165; -.
DR   PATRIC; fig|272634.6.peg.183; -.
DR   HOGENOM; CLU_044142_4_0_14; -.
DR   OMA; KRMAGRY; -.
DR   BioCyc; MPNE272634:G1GJ3-274-MON; -.
DR   Proteomes; UP000000808; 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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..287
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_0000077123"
FT   REGION          228..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..246
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   287 AA;  31247 MW;  2B6EC905363AF259 CRC64;
     MEIRGIFGVK VGMSQVFTTN NERLPITVIY CEPNQVAGVK TEAKDKYSAT LLSFDTVENK
     KLNKPQQGFF EKNNLKPTKH LQEIRNMTGF EMGQQITPQN LFQVGEYVDV SAISKGRGFT
     GAIKRWNFKI GPLGHGAGYP HRFQGSVQAG RGGASAQRVF KGKKMSGHYG HEKVTVQNLR
     IVGFDEANML VLVSGAIAGP EGGVVLIRTA KKKPGVVKPI ELAVQTEKAP EAKPAKLSKK
     KQAKELAKAQ AANQQTVEAK VDTPVVEPKP TEVKKAAPVV EKKGEDK