ID   RL31_ACIAD              Reviewed;          74 AA.
AC   Q6FAA5;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=50S ribosomal protein L31 {ECO:0000255|HAMAP-Rule:MF_00501};
GN   Name=rpmE {ECO:0000255|HAMAP-Rule:MF_00501}; OrderedLocusNames=ACIAD2210;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG69008.1; -; Genomic_DNA.
DR   RefSeq; WP_004927788.1; NC_005966.1.
DR   AlphaFoldDB; Q6FAA5; -.
DR   SMR; Q6FAA5; -.
DR   STRING; 62977.ACIAD2210; -.
DR   EnsemblBacteria; CAG69008; CAG69008; ACIAD2210.
DR   GeneID; 45234544; -.
DR   KEGG; aci:ACIAD2210; -.
DR   eggNOG; COG0254; Bacteria.
DR   HOGENOM; CLU_114306_4_3_6; -.
DR   OMA; WYPDAKV; -.
DR   OrthoDB; 2014569at2; -.
DR   BioCyc; ASP62977:ACIAD_RS10130-MON; -.
DR   Proteomes; UP000000430; 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..74
FT                   /note="50S ribosomal protein L31"
FT                   /id="PRO_0000173072"
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         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00501"
FT   BINDING         41
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00501"
SQ   SEQUENCE   74 AA;  8316 MW;  13959A16883B5655 CRC64;
     MRADIHPKYQ TLVATCSCGN VIETRSALGK ETLYLDVCSA CHPFYTGKQK NVDTGGRIDK
     FKQRFSGMSR SIKR