ID   RL1_CLOBB               Reviewed;         229 AA.
AC   B2TIG5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
GN   Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318}; OrderedLocusNames=CLL_A0228;
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile in
CC       the ribosome, and is involved in E site tRNA release.
CC       {ECO:0000255|HAMAP-Rule:MF_01318}.
CC   -!- FUNCTION: Protein L1 is also a translational repressor protein, it
CC       controls the translation of the L11 operon by binding to its mRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01318}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01318}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01318}.
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DR   EMBL; CP001056; ACD22701.1; -; Genomic_DNA.
DR   RefSeq; WP_012423549.1; NC_018648.1.
DR   AlphaFoldDB; B2TIG5; -.
DR   SMR; B2TIG5; -.
DR   EnsemblBacteria; ACD22701; ACD22701; CLL_A0228.
DR   KEGG; cbk:CLL_A0228; -.
DR   PATRIC; fig|935198.13.peg.202; -.
DR   HOGENOM; CLU_062853_0_0_9; -.
DR   OMA; GWTDVDV; -.
DR   OrthoDB; 1671455at2; -.
DR   Proteomes; UP000001195; Chromosome.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00403; Ribosomal_L1; 1.
DR   Gene3D; 3.40.50.790; -; 1.
DR   HAMAP; MF_01318_B; Ribosomal_L1_B; 1.
DR   InterPro; IPR005878; Ribosom_L1_bac-type.
DR   InterPro; IPR002143; Ribosomal_L1.
DR   InterPro; IPR023674; Ribosomal_L1-like.
DR   InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR   InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR   InterPro; IPR023673; Ribosomal_L1_CS.
DR   Pfam; PF00687; Ribosomal_L1; 1.
DR   PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR   SUPFAM; SSF56808; SSF56808; 1.
DR   TIGRFAMs; TIGR01169; rplA_bact; 1.
DR   PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE   3: Inferred from homology;
KW   Repressor; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW   Translation regulation; tRNA-binding.
FT   CHAIN           1..229
FT                   /note="50S ribosomal protein L1"
FT                   /id="PRO_1000141380"
SQ   SEQUENCE   229 AA;  24564 MW;  2310C578E26D1A4D CRC64;
     MGKKYIESSK LIDKSALYNS TEALDLTVKT AKANFDETIE LHVRLGVDPR HADQQVRGAV
     VLPNGTGKTV RVLVFAKGDK ATEAQEAGAD FVGAEDLVQK IQSENWFDYD VVVATPDMMG
     VVGRIGRVLG PKGLMPNPKS GTVTFDVAKA IAEIKAGKVE YRVDKTSIVH CPIGKKSFGT
     EKLKENFTTL MEALVKAKPA AAKGQYLKSI TVSSTMGPGA KINPTKALD