ID   RL3_LEPBP               Reviewed;         207 AA.
AC   B0SSH7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=LEPBI_I1964;
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=456481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris;
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
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; CP000786; ABZ98067.1; -; Genomic_DNA.
DR   RefSeq; WP_012388940.1; NC_010602.1.
DR   AlphaFoldDB; B0SSH7; -.
DR   SMR; B0SSH7; -.
DR   STRING; 456481.LEPBI_I1964; -.
DR   KEGG; lbi:LEPBI_I1964; -.
DR   HOGENOM; CLU_044142_4_1_12; -.
DR   OMA; KRMAGRY; -.
DR   OrthoDB; 1270636at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS09705-MON; -.
DR   Proteomes; UP000001847; Chromosome I.
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; 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.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..207
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_1000141882"
FT   REGION          129..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   207 AA;  21809 MW;  7374469FFF15FFDA CRC64;
     MAKGLIGEKL GMAHIFNNDG KMVTVTVLRV GPCFVSQVKT EANDGYEAVQ LAFGDAKEKH
     LTKAELGHIK KANIATPKKT LVEFKGFEGV AVGSEVKLAD IFALDDTVKV TGTSKGKGTQ
     GVVKRHGFAG GPAGHGSRFQ RHPGSIGSNT TPGRVFKGLK MGGRMGSEQT TVRNLKVVKI
     DADANLVFVS GPVPGRERGI VTIEKIG