ID   RL7_CLOBK               Reviewed;         123 AA.
AC   B1IGG3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368};
GN   Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368}; OrderedLocusNames=CLD_1015;
OS   Clostridium botulinum (strain Okra / Type B1).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okra / Type B1;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
CC   -!- FUNCTION: Forms part of the ribosomal stalk which helps the ribosome
CC       interact with GTP-bound translation factors. Is thus essential for
CC       accurate translation. {ECO:0000255|HAMAP-Rule:MF_00368}.
CC   -!- SUBUNIT: Homodimer. Part of the ribosomal stalk of the 50S ribosomal
CC       subunit. Forms a multimeric L10(L12)X complex, where L10 forms an
CC       elongated spine to which 2 to 4 L12 dimers bind in a sequential
CC       fashion. Binds GTP-bound translation factors. {ECO:0000255|HAMAP-
CC       Rule:MF_00368}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00368}.
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DR   EMBL; CP000939; ACA45954.1; -; Genomic_DNA.
DR   RefSeq; WP_003357259.1; NC_010516.1.
DR   AlphaFoldDB; B1IGG3; -.
DR   SMR; B1IGG3; -.
DR   EnsemblBacteria; ACA45954; ACA45954; CLD_1015.
DR   GeneID; 45609665; -.
DR   GeneID; 5186877; -.
DR   KEGG; cbb:CLD_1015; -.
DR   HOGENOM; CLU_086499_3_2_9; -.
DR   OMA; LEDKWGV; -.
DR   Proteomes; UP000008541; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00387; Ribosomal_L7_L12; 1.
DR   Gene3D; 1.20.5.710; -; 1.
DR   Gene3D; 3.30.1390.10; -; 1.
DR   HAMAP; MF_00368; Ribosomal_L7_L12; 1.
DR   InterPro; IPR000206; Ribosomal_L7/12.
DR   InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR   InterPro; IPR013823; Ribosomal_L7/L12_C.
DR   InterPro; IPR008932; Ribosomal_L7/L12_oligo.
DR   InterPro; IPR036235; Ribosomal_L7/L12_oligo_N_sf.
DR   PANTHER; PTHR45987; PTHR45987; 1.
DR   Pfam; PF00542; Ribosomal_L12; 1.
DR   Pfam; PF16320; Ribosomal_L12_N; 1.
DR   SUPFAM; SSF48300; SSF48300; 1.
DR   SUPFAM; SSF54736; SSF54736; 1.
DR   TIGRFAMs; TIGR00855; L12; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..123
FT                   /note="50S ribosomal protein L7/L12"
FT                   /id="PRO_1000121416"
SQ   SEQUENCE   123 AA;  12663 MW;  C04A6D52013ACF83 CRC64;
     MKKEEIIQAI KEMTVLELNE LVEACEEEFG VSAAAPVAVA GAGAAAGAGA AEEKTEFDVV
     LADAGSEKIK VIKAVREVTG LGLKEAKALV DGAPKTLKEA ASKEDGEAIK AKLEEVGAKV
     ELK