ID   RL3_CLOPE               Reviewed;         209 AA.
AC   Q8XHS3;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 2.
DT   25-MAY-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=CPE2405;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(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=BAB82111.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000016; BAB82111.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_003476250.1; NC_003366.1.
DR   AlphaFoldDB; Q8XHS3; -.
DR   SMR; Q8XHS3; -.
DR   STRING; 195102.gene:10491722; -.
DR   EnsemblBacteria; BAB82111; BAB82111; BAB82111.
DR   GeneID; 29570177; -.
DR   KEGG; cpe:CPE2405; -.
DR   HOGENOM; CLU_044142_4_1_9; -.
DR   OMA; KRMAGRY; -.
DR   Proteomes; UP000000818; 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..209
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_0000077091"
FT   REGION          129..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   209 AA;  22700 MW;  51FF9233D20BF040 CRC64;
     MKKAIIGKKV GMTQIFDENG RVIPVTVVEA GPCVVVQKKT VETDGYDAIQ VGFGELREKL
     VNKPRKGHFA KAGVSLRRTL KEFRMEDVAN YNVGDEIKVD TFEIGDKVDV SGVSKGKGFQ
     GTIKRWNASR GPMSHGSKFH RAPGSMGAAS DPSRTFKNKR MPGHMGAKNT TVLNLEVVKI
     MPEKNIILIK GGIPGPNKGT VVIRNSVKA