RL31_ECO81
ID RL31_ECO81 Reviewed; 70 AA.
AC B7N2S7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=50S ribosomal protein L31 {ECO:0000255|HAMAP-Rule:MF_00501};
GN Name=rpmE {ECO:0000255|HAMAP-Rule:MF_00501}; OrderedLocusNames=ECED1_4638;
OS Escherichia coli O81 (strain ED1a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585397;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED1a;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928162; CAR10746.2; -; Genomic_DNA.
DR RefSeq; WP_000710769.1; NC_011745.1.
DR AlphaFoldDB; B7N2S7; -.
DR SMR; B7N2S7; -.
DR EnsemblBacteria; CAR10746; CAR10746; ECED1_4638.
DR GeneID; 66672156; -.
DR KEGG; ecq:ECED1_4638; -.
DR HOGENOM; CLU_114306_4_3_6; -.
DR OMA; WYPDAKV; -.
DR Proteomes; UP000000748; 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 Acetylation; Metal-binding; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; Zinc.
FT CHAIN 1..70
FT /note="50S ribosomal protein L31"
FT /id="PRO_1000176962"
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 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"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00501"
SQ SEQUENCE 70 AA; 7871 MW; D657A681A0B858CF CRC64;
MKKDIHPKYE EITASCSCGN VMKIRSTVGH DLNLDVCSKC HPFFTGKQRD VATGGRVDRF
NKRFNIPGSK
