ID   RL31_CLOBJ              Reviewed;          72 AA.
AC   C1FQ93;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=50S ribosomal protein L31 {ECO:0000255|HAMAP-Rule:MF_00501};
GN   Name=rpmE {ECO:0000255|HAMAP-Rule:MF_00501}; OrderedLocusNames=CLM_0178;
OS   Clostridium botulinum (strain Kyoto / Type A2).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyoto / Type A2;
RA   Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA   Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001581; ACO84599.1; -; Genomic_DNA.
DR   RefSeq; WP_003355803.1; NC_012563.1.
DR   AlphaFoldDB; C1FQ93; -.
DR   STRING; 536232.CLM_0178; -.
DR   EnsemblBacteria; ACO84599; ACO84599; CLM_0178.
DR   GeneID; 5184390; -.
DR   KEGG; cby:CLM_0178; -.
DR   eggNOG; COG0254; Bacteria.
DR   HOGENOM; CLU_114306_4_3_9; -.
DR   OMA; WYPDAKV; -.
DR   Proteomes; UP000001374; 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_1000176955"
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;  8107 MW;  BA3550AF966F5750 CRC64;
     MREGIHPEYN HDVVVKCACG NTFTTGSTNK ELKVEICSKC HPFFTGKQKI VDAGGRVDKF
     MKKFNLSNED VK