RL31_ECODH
ID RL31_ECODH Reviewed; 70 AA.
AC B1XBA2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=50S ribosomal protein L31 {ECO:0000255|HAMAP-Rule:MF_00501};
GN Name=rpmE {ECO:0000255|HAMAP-Rule:MF_00501};
GN OrderedLocusNames=ECDH10B_4125;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(2008).
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; CP000948; ACB04948.1; -; Genomic_DNA.
DR RefSeq; WP_000710769.1; NC_010473.1.
DR AlphaFoldDB; B1XBA2; -.
DR SMR; B1XBA2; -.
DR GeneID; 66672156; -.
DR KEGG; ecd:ECDH10B_4125; -.
DR HOGENOM; CLU_114306_4_3_6; -.
DR OMA; WYPDAKV; -.
DR BioCyc; ECOL316385:ECDH10B_RS21005-MON; -.
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_1000126617"
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
