ID   RL31_CLOBM              Reviewed;          72 AA.
AC   B1KSQ7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=50S ribosomal protein L31 {ECO:0000255|HAMAP-Rule:MF_00501};
GN   Name=rpmE {ECO:0000255|HAMAP-Rule:MF_00501}; OrderedLocusNames=CLK_3310;
OS   Clostridium botulinum (strain Loch Maree / Type A3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Loch Maree / Type A3;
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: Binds the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00501}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00501};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00501};
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00501}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family.
CC       Type A subfamily. {ECO:0000255|HAMAP-Rule:MF_00501}.
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DR   EMBL; CP000962; ACA54040.1; -; Genomic_DNA.
DR   RefSeq; WP_012342194.1; NC_010520.1.
DR   AlphaFoldDB; B1KSQ7; -.
DR   EnsemblBacteria; ACA54040; ACA54040; CLK_3310.
DR   KEGG; cbl:CLK_3310; -.
DR   HOGENOM; CLU_114306_4_3_9; -.
DR   OMA; WYPDAKV; -.
DR   Proteomes; UP000000722; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 4.10.830.30; -; 1.
DR   HAMAP; MF_00501; Ribosomal_L31_1; 1.
DR   InterPro; IPR034704; L28p-like.
DR   InterPro; IPR002150; Ribosomal_L31.
DR   InterPro; IPR027491; Ribosomal_L31_A.
DR   InterPro; IPR042105; Ribosomal_L31_sf.
DR   PANTHER; PTHR33280; PTHR33280; 1.
DR   Pfam; PF01197; Ribosomal_L31; 1.
DR   PRINTS; PR01249; RIBOSOMALL31.
DR   SUPFAM; SSF143800; SSF143800; 1.
DR   TIGRFAMs; TIGR00105; L31; 1.
DR   PROSITE; PS01143; RIBOSOMAL_L31; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; Zinc.
FT   CHAIN           1..72
FT                   /note="50S ribosomal protein L31"
FT                   /id="PRO_1000126595"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00501"
FT   BINDING         19
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00501"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00501"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00501"
SQ   SEQUENCE   72 AA;  8121 MW;  BA354AB596754D50 CRC64;
     MREGIHPEYN HDVLVKCACG NTFTTGSTNK ELKVEICSKC HPFFTGKQKI VDAGGRVDKF
     MKKFNLSNED VK