RL31_ECOLI
ID RL31_ECOLI Reviewed; 70 AA.
AC P0A7M9; P02432; Q2M8N2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=50S ribosomal protein L31;
DE AltName: Full=Large ribosomal subunit protein bL31-A {ECO:0000303|PubMed:24524803};
GN Name=rpmE; OrderedLocusNames=b3936, JW3907;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 1-62, AND SUBUNIT.
RC STRAIN=B;
RX PubMed=339950; DOI=10.1021/bi00596a020;
RA Brosius J.;
RT "Primary structure of Escherichia coli ribosomal protein L31.";
RL Biochemistry 17:501-508(1978).
RN [5]
RP PROTEIN SEQUENCE OF 1-10.
RC STRAIN=K12;
RX PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
RA Wasinger V.C., Humphery-Smith I.;
RT "Small genes/gene-products in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 169:375-382(1998).
RN [6]
RP PROTEIN SEQUENCE OF 64-70 (STRAIN MRE-600), AND EXAMINATION OF MOLECULAR
RP WEIGHT IN SEVERAL STRAINS.
RC STRAIN=B, K12 / D10, K12 / Q13, and MRE-600;
RX PubMed=10556732; DOI=10.1111/j.1574-6968.1999.tb08816.x;
RA Eistetter A.J., Butler P.D., Traut R.R., Fanning T.G.;
RT "Characterization of Escherichia coli 50S ribosomal protein L31.";
RL FEMS Microbiol. Lett. 180:345-349(1999).
RN [7]
RP MASS SPECTROMETRY, AND SUBUNIT.
RC STRAIN=K12 / ATCC 25404 / DSM 5698 / NCIMB 11290;
RX PubMed=10094780; DOI=10.1006/abio.1998.3077;
RA Arnold R.J., Reilly J.P.;
RT "Observation of Escherichia coli ribosomal proteins and their
RT posttranslational modifications by mass spectrometry.";
RL Anal. Biochem. 269:105-112(1999).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [9]
RP ZINC-BINDING, COFACTOR, AND MUTAGENESIS OF CYS-16; CYS-18 AND
RP 37-CYS--CYS-40.
RC STRAIN=BW21135;
RX PubMed=22196016; DOI=10.1016/j.jinorgbio.2011.11.022;
RA Hensley M.P., Gunasekera T.S., Easton J.A., Sigdel T.K., Sugarbaker S.A.,
RA Klingbeil L., Breece R.M., Tierney D.L., Crowder M.W.;
RT "Characterization of Zn(II)-responsive ribosomal proteins YkgM and L31 in
RT E. coli.";
RL J. Inorg. Biochem. 111:164-172(2012).
RN [10]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES,
RP AND SUBUNIT.
RC STRAIN=MRE-600;
RX PubMed=16272117; DOI=10.1126/science.1117230;
RA Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A.,
RA Holton J.M., Cate J.H.D.;
RT "Structures of the bacterial ribosome at 3.5 A resolution.";
RL Science 310:827-834(2005).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX
RP WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=27906160; DOI=10.1038/nature20822;
RA Ma C., Kurita D., Li N., Chen Y., Himeno H., Gao N.;
RT "Mechanistic insights into the alternative translation termination by ArfA
RT and RF2.";
RL Nature 541:550-553(2017).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX
RP WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=27906161; DOI=10.1038/nature20821;
RA Huter P., Mueller C., Beckert B., Arenz S., Berninghausen O., Beckmann R.,
RA Wilson D.N.;
RT "Structural basis for ArfA-RF2-mediated translation termination on mRNAs
RT lacking stop codons.";
RL Nature 541:546-549(2017).
RN [14]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.97 ANGSTROMS) OF 70S RIBOSOME IN
RP COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=27934701; DOI=10.1126/science.aai9127;
RA James N.R., Brown A., Gordiyenko Y., Ramakrishnan V.;
RT "Translational termination without a stop codon.";
RL Science 354:1437-1440(2016).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.52 ANGSTROMS) OF 70S RIBOSOME IN
RP COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=28077875; DOI=10.1038/nature21053;
RA Zeng F., Chen Y., Remis J., Shekhar M., Phillips J.C., Tajkhorshid E.,
RA Jin H.;
RT "Structural basis of co-translational quality control by ArfA and RF2 bound
RT to ribosome.";
RL Nature 541:554-557(2017).
CC -!- FUNCTION: Binds the 23S rRNA. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:22196016};
CC Note=Binds 1 zinc ion per subunit. Only 1 ligand appears to be Cys, the
CC other are thought to be His and either backbone amides or solvent
CC (PubMed:22196016). {ECO:0000269|PubMed:22196016};
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC {ECO:0000269|PubMed:10094780, ECO:0000269|PubMed:16272117,
CC ECO:0000269|PubMed:27906160, ECO:0000269|PubMed:27906161,
CC ECO:0000269|PubMed:27934701, ECO:0000269|PubMed:339950}.
CC -!- PTM: Proteolytically cleaved by protease VII to yield a peptide lacking
CC residues 63-70. It is not clear if this is due to protein degradation
CC or is a bona fide processing event in the strain used in PubMed:339950
CC and PubMed:10556732. In strains B, D10, MRE-600 and Q13 the only
CC protein seen in PubMed:10556732 was full-length; the last 7 amino acids
CC were sequenced only for strain MRE-600. {ECO:0000269|PubMed:10556732,
CC ECO:0000269|PubMed:339950}.
CC -!- MASS SPECTROMETRY: Mass=7871.0; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10094780};
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family.
CC Type A subfamily. {ECO:0000305}.
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DR EMBL; X78541; CAA55286.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03068.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76918.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77374.1; -; Genomic_DNA.
DR PIR; S40879; R5EC31.
DR RefSeq; NP_418371.1; NC_000913.3.
DR RefSeq; WP_000710769.1; NZ_STEB01000017.1.
DR PDB; 2J28; EM; 8.00 A; Z=1-70.
DR PDB; 2RDO; EM; 9.10 A; Z=1-70.
DR PDB; 3BBX; EM; 10.00 A; Z=1-70.
DR PDB; 3J9Y; EM; 3.90 A; 6=1-70.
DR PDB; 3J9Z; EM; 3.60 A; LZ=1-70.
DR PDB; 3JA1; EM; 3.60 A; L2=1-70.
DR PDB; 4V4H; X-ray; 3.46 A; BZ/DZ=1-70.
DR PDB; 4V4Q; X-ray; 3.46 A; BZ/DZ=1-70.
DR PDB; 4V5B; X-ray; 3.74 A; AZ/CZ=1-70.
DR PDB; 4V65; EM; 9.00 A; BS=1-70.
DR PDB; 4V66; EM; 9.00 A; BS=1-70.
DR PDB; 4V6K; EM; 8.25 A; Ab=1-70.
DR PDB; 4V6L; EM; 13.20 A; Bb=1-70.
DR PDB; 4V6N; EM; 12.10 A; A2=1-70.
DR PDB; 4V6O; EM; 14.70 A; B2=1-70.
DR PDB; 4V6P; EM; 13.50 A; B2=1-70.
DR PDB; 4V6Q; EM; 11.50 A; B2=1-70.
DR PDB; 4V6R; EM; 11.50 A; B2=1-70.
DR PDB; 4V6S; EM; 13.10 A; A2=1-70.
DR PDB; 4V6V; EM; 9.80 A; B4=1-70.
DR PDB; 5AFI; EM; 2.90 A; 6=1-70.
DR PDB; 5AKA; EM; 5.70 A; Z=1-70.
DR PDB; 5IQR; EM; 3.00 A; a=1-70.
DR PDB; 5KCS; EM; 3.90 A; 14=1-70.
DR PDB; 5KPS; EM; 3.90 A; 1=1-70.
DR PDB; 5KPV; EM; 4.10 A; Z=1-70.
DR PDB; 5KPW; EM; 3.90 A; Z=1-70.
DR PDB; 5KPX; EM; 3.90 A; Z=1-70.
DR PDB; 5L3P; EM; 3.70 A; 4=1-70.
DR PDB; 5LZA; EM; 3.60 A; 6=1-66.
DR PDB; 5LZB; EM; 5.30 A; 6=1-66.
DR PDB; 5LZC; EM; 4.80 A; 6=1-66.
DR PDB; 5LZD; EM; 3.40 A; 6=1-66.
DR PDB; 5LZE; EM; 3.50 A; 6=1-66.
DR PDB; 5LZF; EM; 4.60 A; 6=1-66.
DR PDB; 5MDV; EM; 2.97 A; a=1-70.
DR PDB; 5MDW; EM; 3.06 A; a=1-70.
DR PDB; 5MDY; EM; 3.35 A; a=1-70.
DR PDB; 5MDZ; EM; 3.10 A; a=1-70.
DR PDB; 5MGP; EM; 3.10 A; 6=1-66.
DR PDB; 5NP6; EM; 3.60 A; 4=1-66.
DR PDB; 5NWY; EM; 2.93 A; L=1-70.
DR PDB; 5O2R; EM; 3.40 A; 6=1-66.
DR PDB; 5U9F; EM; 3.20 A; 29=1-70.
DR PDB; 5U9G; EM; 3.20 A; 29=1-70.
DR PDB; 5UYK; EM; 3.90 A; 29=1-66.
DR PDB; 5UYL; EM; 3.60 A; 29=1-66.
DR PDB; 5UYM; EM; 3.20 A; 29=1-66.
DR PDB; 5UYN; EM; 4.00 A; 29=1-66.
DR PDB; 5UYP; EM; 3.90 A; 29=1-66.
DR PDB; 5UYQ; EM; 3.80 A; 29=1-66.
DR PDB; 5WDT; EM; 3.00 A; 6=1-66.
DR PDB; 5WE4; EM; 3.10 A; 6=1-66.
DR PDB; 5WE6; EM; 3.40 A; 6=1-66.
DR PDB; 5WFK; EM; 3.40 A; 6=1-66.
DR PDB; 6BU8; EM; 3.50 A; 29=1-66.
DR PDB; 6BY1; X-ray; 3.94 A; C0/D0=10-48.
DR PDB; 6C4I; EM; 3.24 A; 1=1-70.
DR PDB; 6ENF; EM; 3.20 A; 6=1-66.
DR PDB; 6ENJ; EM; 3.70 A; 6=1-66.
DR PDB; 6ENU; EM; 3.10 A; 6=1-66.
DR PDB; 6H4N; EM; 3.00 A; 6=1-66.
DR PDB; 6H58; EM; 7.90 A; 6/66=1-66.
DR PDB; 6HRM; EM; 2.96 A; a=1-66.
DR PDB; 6O9J; EM; 3.90 A; Z=1-70.
DR PDB; 6ORE; EM; 2.90 A; a=1-66.
DR PDB; 6OT3; EM; 3.90 A; a=1-66.
DR PDB; 6OUO; EM; 3.70 A; a=1-66.
DR PDB; 6Q97; EM; 3.90 A; a=1-66.
DR PDB; 6Q98; EM; 4.30 A; a=1-70.
DR PDB; 6Q9A; EM; 3.70 A; a=1-66.
DR PDB; 6SZS; EM; 3.06 A; 5=1-70.
DR PDB; 6TBV; EM; 2.70 A; L311=1-70.
DR PDB; 6TC3; EM; 2.70 A; L311=1-70.
DR PDB; 6WNT; EM; 3.10 A; A=1-70.
DR PDB; 6WNV; EM; 3.50 A; A=1-70.
DR PDB; 6WNW; EM; 3.20 A; A=1-70.
DR PDB; 6Y69; EM; 2.86 A; 6=1-66.
DR PDB; 7AC7; EM; 3.08 A; a=1-66.
DR PDB; 7ACJ; EM; 3.20 A; a=1-65.
DR PDB; 7ACR; EM; 3.44 A; a=1-65.
DR PDB; 7B5K; EM; 2.90 A; 5=1-66.
DR PDB; 7BL2; EM; 3.70 A; b=1-70.
DR PDB; 7BL3; EM; 3.50 A; b=1-70.
DR PDB; 7BL4; EM; 2.40 A; d=1-70.
DR PDB; 7BL5; EM; 3.30 A; b=1-70.
DR PDB; 7BL6; EM; 4.00 A; d=1-70.
DR PDB; 7D6Z; EM; 3.40 A; 6=1-70.
DR PDB; 7K50; EM; 3.40 A; A=1-66.
DR PDB; 7K51; EM; 3.50 A; A=1-66.
DR PDB; 7K52; EM; 3.40 A; A=1-66.
DR PDB; 7K53; EM; 3.20 A; A=1-66.
DR PDB; 7K54; EM; 3.20 A; A=1-66.
DR PDB; 7K55; EM; 3.30 A; A=1-66.
DR PDB; 7LV0; EM; 3.20 A; A=1-66.
DR PDB; 7N1P; EM; 2.33 A; Le=1-70.
DR PDB; 7N2C; EM; 2.72 A; Le=1-70.
DR PDB; 7N2U; EM; 2.53 A; Le=1-70.
DR PDB; 7N2V; EM; 2.54 A; Le=1-70.
DR PDB; 7N30; EM; 2.66 A; Le=1-70.
DR PDB; 7N31; EM; 2.69 A; Le=1-70.
DR PDB; 7NBU; EM; 3.11 A; 4=1-66.
DR PDB; 7O19; EM; 2.90 A; BI=1-70.
DR PDB; 7O1A; EM; 2.40 A; BI=1-70.
DR PDB; 7O1C; EM; 2.60 A; BI=1-70.
DR PDB; 7P3K; EM; 2.90 A; 4=1-70.
DR PDB; 7PJV; EM; 3.10 A; 6=1-70.
DR PDB; 7PJY; EM; 3.10 A; 6=1-70.
DR PDB; 7QG8; EM; 3.97 A; L=1-70.
DR PDB; 7QGH; EM; 4.48 A; L=1-70.
DR PDB; 7SSD; EM; 3.30 A; A=1-66.
DR PDB; 7SSL; EM; 3.80 A; A=1-66.
DR PDB; 7SSO; EM; 3.20 A; A=1-66.
DR PDB; 7ST2; EM; 2.90 A; A=1-66.
DR PDB; 7ST6; EM; 3.00 A; A=1-66.
DR PDB; 7ST7; EM; 3.20 A; A=1-66.
DR PDBsum; 2J28; -.
DR PDBsum; 2RDO; -.
DR PDBsum; 3BBX; -.
DR PDBsum; 3J9Y; -.
DR PDBsum; 3J9Z; -.
DR PDBsum; 3JA1; -.
DR PDBsum; 4V4H; -.
DR PDBsum; 4V4Q; -.
DR PDBsum; 4V5B; -.
DR PDBsum; 4V65; -.
DR PDBsum; 4V66; -.
DR PDBsum; 4V6K; -.
DR PDBsum; 4V6L; -.
DR PDBsum; 4V6N; -.
DR PDBsum; 4V6O; -.
DR PDBsum; 4V6P; -.
DR PDBsum; 4V6Q; -.
DR PDBsum; 4V6R; -.
DR PDBsum; 4V6S; -.
DR PDBsum; 4V6V; -.
DR PDBsum; 5AFI; -.
DR PDBsum; 5AKA; -.
DR PDBsum; 5IQR; -.
DR PDBsum; 5KCS; -.
DR PDBsum; 5KPS; -.
DR PDBsum; 5KPV; -.
DR PDBsum; 5KPW; -.
DR PDBsum; 5KPX; -.
DR PDBsum; 5L3P; -.
DR PDBsum; 5LZA; -.
DR PDBsum; 5LZB; -.
DR PDBsum; 5LZC; -.
DR PDBsum; 5LZD; -.
DR PDBsum; 5LZE; -.
DR PDBsum; 5LZF; -.
DR PDBsum; 5MDV; -.
DR PDBsum; 5MDW; -.
DR PDBsum; 5MDY; -.
DR PDBsum; 5MDZ; -.
DR PDBsum; 5MGP; -.
DR PDBsum; 5NP6; -.
DR PDBsum; 5NWY; -.
DR PDBsum; 5O2R; -.
DR PDBsum; 5U9F; -.
DR PDBsum; 5U9G; -.
DR PDBsum; 5UYK; -.
DR PDBsum; 5UYL; -.
DR PDBsum; 5UYM; -.
DR PDBsum; 5UYN; -.
DR PDBsum; 5UYP; -.
DR PDBsum; 5UYQ; -.
DR PDBsum; 5WDT; -.
DR PDBsum; 5WE4; -.
DR PDBsum; 5WE6; -.
DR PDBsum; 5WFK; -.
DR PDBsum; 6BU8; -.
DR PDBsum; 6BY1; -.
DR PDBsum; 6C4I; -.
DR PDBsum; 6ENF; -.
DR PDBsum; 6ENJ; -.
DR PDBsum; 6ENU; -.
DR PDBsum; 6H4N; -.
DR PDBsum; 6H58; -.
DR PDBsum; 6HRM; -.
DR PDBsum; 6O9J; -.
DR PDBsum; 6ORE; -.
DR PDBsum; 6OT3; -.
DR PDBsum; 6OUO; -.
DR PDBsum; 6Q97; -.
DR PDBsum; 6Q98; -.
DR PDBsum; 6Q9A; -.
DR PDBsum; 6SZS; -.
DR PDBsum; 6TBV; -.
DR PDBsum; 6TC3; -.
DR PDBsum; 6WNT; -.
DR PDBsum; 6WNV; -.
DR PDBsum; 6WNW; -.
DR PDBsum; 6Y69; -.
DR PDBsum; 7AC7; -.
DR PDBsum; 7ACJ; -.
DR PDBsum; 7ACR; -.
DR PDBsum; 7B5K; -.
DR PDBsum; 7BL2; -.
DR PDBsum; 7BL3; -.
DR PDBsum; 7BL4; -.
DR PDBsum; 7BL5; -.
DR PDBsum; 7BL6; -.
DR PDBsum; 7D6Z; -.
DR PDBsum; 7K50; -.
DR PDBsum; 7K51; -.
DR PDBsum; 7K52; -.
DR PDBsum; 7K53; -.
DR PDBsum; 7K54; -.
DR PDBsum; 7K55; -.
DR PDBsum; 7LV0; -.
DR PDBsum; 7N1P; -.
DR PDBsum; 7N2C; -.
DR PDBsum; 7N2U; -.
DR PDBsum; 7N2V; -.
DR PDBsum; 7N30; -.
DR PDBsum; 7N31; -.
DR PDBsum; 7NBU; -.
DR PDBsum; 7O19; -.
DR PDBsum; 7O1A; -.
DR PDBsum; 7O1C; -.
DR PDBsum; 7P3K; -.
DR PDBsum; 7PJV; -.
DR PDBsum; 7PJY; -.
DR PDBsum; 7QG8; -.
DR PDBsum; 7QGH; -.
DR PDBsum; 7SSD; -.
DR PDBsum; 7SSL; -.
DR PDBsum; 7SSO; -.
DR PDBsum; 7ST2; -.
DR PDBsum; 7ST6; -.
DR PDBsum; 7ST7; -.
DR AlphaFoldDB; P0A7M9; -.
DR SMR; P0A7M9; -.
DR BioGRID; 4261184; 44.
DR BioGRID; 852722; 7.
DR ComplexPortal; CPX-3807; 50S large ribosomal subunit.
DR IntAct; P0A7M9; 25.
DR STRING; 511145.b3936; -.
DR iPTMnet; P0A7M9; -.
DR jPOST; P0A7M9; -.
DR PaxDb; P0A7M9; -.
DR PRIDE; P0A7M9; -.
DR EnsemblBacteria; AAC76918; AAC76918; b3936.
DR EnsemblBacteria; BAE77374; BAE77374; BAE77374.
DR GeneID; 66672156; -.
DR GeneID; 948425; -.
DR KEGG; ecj:JW3907; -.
DR KEGG; eco:b3936; -.
DR PATRIC; fig|1411691.4.peg.2769; -.
DR EchoBASE; EB0882; -.
DR eggNOG; COG0254; Bacteria.
DR HOGENOM; CLU_114306_4_3_6; -.
DR InParanoid; P0A7M9; -.
DR OMA; WYPDAKV; -.
DR PhylomeDB; P0A7M9; -.
DR BioCyc; EcoCyc:EG10889-MON; -.
DR BioCyc; MetaCyc:EG10889-MON; -.
DR EvolutionaryTrace; P0A7M9; -.
DR PRO; PR:P0A7M9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:EcoCyc.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:1904689; P:negative regulation of cytoplasmic translational initiation; IEP:EcoCyc.
DR GO; GO:0006412; P:translation; IMP:EcoCyc.
DR GO; GO:0006413; P:translational initiation; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Metal-binding;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; Zinc.
FT CHAIN 1..70
FT /note="50S ribosomal protein L31"
FT /id="PRO_0000173102"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 16
FT /note="C->S: No Zn(2+) binding."
FT /evidence="ECO:0000269|PubMed:22196016"
FT MUTAGEN 18
FT /note="C->S: Binds Zn(2+) normally."
FT /evidence="ECO:0000269|PubMed:22196016"
FT MUTAGEN 37..40
FT /note="CSKC->SSKS: Binds Zn(2+) normally."
FT /evidence="ECO:0000269|PubMed:22196016"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:7BL4"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:7BL4"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:7BL4"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:7BL5"
FT TURN 42..46
FT /evidence="ECO:0007829|PDB:7BL5"
SQ SEQUENCE 70 AA; 7871 MW; D657A681A0B858CF CRC64;
MKKDIHPKYE EITASCSCGN VMKIRSTVGH DLNLDVCSKC HPFFTGKQRD VATGGRVDRF
NKRFNIPGSK
