ID   RL3_ACIC1               Reviewed;         222 AA.
AC   A0LRM0;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=Acel_0306;
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
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; CP000481; ABK52080.1; -; Genomic_DNA.
DR   RefSeq; WP_011719143.1; NC_008578.1.
DR   AlphaFoldDB; A0LRM0; -.
DR   SMR; A0LRM0; -.
DR   STRING; 351607.Acel_0306; -.
DR   EnsemblBacteria; ABK52080; ABK52080; Acel_0306.
DR   KEGG; ace:Acel_0306; -.
DR   eggNOG; COG0087; Bacteria.
DR   HOGENOM; CLU_044142_4_1_11; -.
DR   OMA; KRMAGRY; -.
DR   OrthoDB; 1270636at2; -.
DR   Proteomes; UP000008221; 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..222
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_0000353590"
FT   REGION          129..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   222 AA;  23478 MW;  7B0CE646D1B50D31 CRC64;
     MPKQVKGLLG EKLGMTQVFD ESGRVIPVTV VRAGPCVVTQ VRTPDRDGYS AVQLGYGAVD
     PRRVNKPLAG HFRAAGVTPR RYLAEVRTGD AAEYTVGQEV TVEIFTPGQR VDVAGVSKGK
     GFAGLMKRHN FRGLPDSHGT ERKHRSPGSI GACATPGRVF KGLRMAGRMG GRRVTVQNLA
     VQAVKPEENL LLLQGAVPGP NGGLVYVRTA AKGKANRDGG AA