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RL31_PELPD
ID   RL31_PELPD              Reviewed;          66 AA.
AC   A1ASD4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=50S ribosomal protein L31 {ECO:0000255|HAMAP-Rule:MF_00501};
GN   Name=rpmE {ECO:0000255|HAMAP-Rule:MF_00501}; OrderedLocusNames=Ppro_2650;
OS   Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Desulfuromonadaceae; Pelobacter.
OX   NCBI_TaxID=338966;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL   Submitted (OCT-2006) 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; CP000482; ABL00255.1; -; Genomic_DNA.
DR   RefSeq; WP_011736507.1; NC_008609.1.
DR   AlphaFoldDB; A1ASD4; -.
DR   SMR; A1ASD4; -.
DR   STRING; 338966.Ppro_2650; -.
DR   EnsemblBacteria; ABL00255; ABL00255; Ppro_2650.
DR   KEGG; ppd:Ppro_2650; -.
DR   eggNOG; COG0254; Bacteria.
DR   HOGENOM; CLU_114306_4_0_7; -.
DR   OMA; WYPDAKV; -.
DR   OrthoDB; 2014569at2; -.
DR   Proteomes; UP000006732; 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; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding; Zinc.
FT   CHAIN           1..66
FT                   /note="50S ribosomal protein L31"
FT                   /id="PRO_1000126682"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00501"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00501"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00501"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00501"
SQ   SEQUENCE   66 AA;  7586 MW;  A9AC7E1854F600C8 CRC64;
     MKEGIHPMYS DATVKCLCGN TFQTRSTRKE INTEICSACH PFFTGKQKLI DTAGRVERFK
     RRYGQV
 
 
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