ID   RL3_MALP2               Reviewed;         310 AA.
AC   Q8EUB3;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 2.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=MYPE10180;
OS   Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC   Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX   NCBI_TaxID=272633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HF-2;
RX   PubMed=12466555; DOI=10.1093/nar/gkf667;
RA   Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA   Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT   "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT   bacterial pathogen in humans.";
RL   Nucleic Acids Res. 30:5293-5300(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC44803.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000026; BAC44803.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011077831.1; NC_004432.1.
DR   AlphaFoldDB; Q8EUB3; -.
DR   SMR; Q8EUB3; -.
DR   STRING; 272633.26454475; -.
DR   EnsemblBacteria; BAC44803; BAC44803; BAC44803.
DR   KEGG; mpe:MYPE10180; -.
DR   eggNOG; COG0087; Bacteria.
DR   HOGENOM; CLU_044142_4_0_14; -.
DR   OMA; KRMAGRY; -.
DR   OrthoDB; 1270636at2; -.
DR   Proteomes; UP000002522; 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..310
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_0000077122"
FT   REGION          240..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   310 AA;  34172 MW;  F049163EB0878C1E CRC64;
     MKMILGRKIG MIQSFLEDGR RIPVTIIQAE PNVVLENKTQ EKNGYVATKV GFQQIEEKKL
     NKPQKGYFKK IKTDAFKHTK EFRNVSGYNV GDKILVDIFN SGDKVDAQAI TKGKGFTGAI
     KRWNFKVGPL GHGAGYPHRY QGSISFGRGG SQGQRVPKGQ KMSGHYGHEL VTISNLTVVS
     IELEKNLILV KGSVPGPVNS LVLLKTTVKS KKQVDPIKLS DPEAIARAIK EKEEQARLAL
     EAKKAEAHQK AEAEKEAKKQ EMLAKQKAAE EKQKAEAEKN EQPTATAEEA PAKTDDNATE
     KKEENNGGNQ