RL10_ECOLI
ID RL10_ECOLI Reviewed; 165 AA.
AC P0A7J3; P02408; Q2M8S1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=50S ribosomal protein L10;
DE AltName: Full=50S ribosomal protein L8;
DE AltName: Full=Large ribosomal subunit protein uL10 {ECO:0000303|PubMed:24524803};
GN Name=rplJ; OrderedLocusNames=b3985, JW3948;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=377281; DOI=10.1073/pnas.76.4.1697;
RA Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P.;
RT "Nucleotide sequence of the ribosomal protein gene cluster adjacent to the
RT gene for RNA polymerase subunit beta in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 2-165, AND SUBUNIT.
RC STRAIN=MRE-600;
RX PubMed=773698; DOI=10.1016/0014-5793(76)80267-0;
RA Pettersson I., Hardy S.J.S., Liljas A.;
RT "The ribosomal protein L8 is a complex L7/L12 and L10.";
RL FEBS Lett. 64:135-138(1976).
RN [6]
RP PROTEIN SEQUENCE OF 2-165, SEQUENCE REVISION, AND SUBUNIT.
RC STRAIN=MRE-600;
RX PubMed=782920; DOI=10.1016/0014-5793(76)80870-8;
RA Dovgas N.V., Vinokurov L.M., Velmoga I.S., Alakhov Y.B., Ovchinnikov Y.A.;
RT "The primary structure of protein L10 from Escherichia coli ribosomes.";
RL FEBS Lett. 67:58-61(1976).
RN [7]
RP PROTEIN SEQUENCE OF 2-165, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=797648; DOI=10.1515/bchm2.1976.357.2.1751;
RA Heiland I., Brauer D., Wittmann-Liebold B.;
RT "Primary structure of protein L10 from the large subunit of Escherichia
RT coli ribosomes.";
RL Hoppe-Seyler's Z. Physiol. Chem. 357:1751-1770(1976).
RN [8]
RP MECHANISM OF TRANSLATION REGULATION.
RX PubMed=2448482; DOI=10.1016/0022-2836(87)90287-7;
RA Climie S.C., Friesen J.D.;
RT "Feedback regulation of the rplJL-rpoBC ribosomal protein operon of
RT Escherichia coli requires a region of mRNA secondary structure.";
RL J. Mol. Biol. 198:371-381(1987).
RN [9]
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 [10]
RP SUBUNIT, STOICHIOMETRY, AND MASS SPECTROMETRY.
RX PubMed=15923259; DOI=10.1073/pnas.0502193102;
RA Ilag L.L., Videler H., McKay A.R., Sobott F., Fucini P., Nierhaus K.H.,
RA Robinson C.V.;
RT "Heptameric (L12)6/L10 rather than canonical pentameric complexes are found
RT by tandem MS of intact ribosomes from thermophilic bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8192-8197(2005).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-37 AND LYS-105, AND
RP IDENTIFICATION BY MASS 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 [12]
RP MUTAGENESIS OF 156-ALA--ALA-165.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22102582; DOI=10.1093/nar/gkr1031;
RA Mandava C.S., Peisker K., Ederth J., Kumar R., Ge X., Szaflarski W.,
RA Sanyal S.;
RT "Bacterial ribosome requires multiple L12 dimers for efficient initiation
RT and elongation of protein synthesis involving IF2 and EF-G.";
RL Nucleic Acids Res. 40:2054-2064(2012).
RN [13]
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 [14]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 1-148 IN TNAC-STALLED
RP 50S RIBOSOMAL SUBUNIT, AND SUBUNIT.
RC STRAIN=K12 / A19 / KC6;
RX PubMed=25310980; DOI=10.1016/j.celrep.2014.09.011;
RA Bischoff L., Berninghausen O., Beckmann R.;
RT "Molecular basis for the ribosome functioning as an L-tryptophan sensor.";
RL Cell Rep. 9:469-475(2014).
RN [15]
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 [16]
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 [17]
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 [18]
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: Forms part of the ribosomal stalk, playing a central role in
CC the interaction of the ribosome with GTP-bound translation factors.
CC {ECO:0000269|PubMed:15923259}.
CC -!- FUNCTION: Protein L10 is also a translational repressor protein. It
CC controls the translation of the rplJL-rpoBC operon by binding to its
CC mRNA. {ECO:0000269|PubMed:2448482}.
CC -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit
CC (PubMed:15923259). The N-terminus interacts with L11 and the large rRNA
CC to form the base of the stalk. The C-terminus forms an elongated spine
CC to which 2 L12 dimers bind in a sequential fashion forming a pentameric
CC L10(L12)(L12)2 complex. Two L12 dimers associate with a copy of L10 to
CC form a very strong complex (called L8). {ECO:0000269|PubMed:10094780,
CC ECO:0000269|PubMed:15923259, ECO:0000269|PubMed:25310980,
CC ECO:0000269|PubMed:27906160, ECO:0000269|PubMed:27906161,
CC ECO:0000269|PubMed:27934701, ECO:0000269|PubMed:773698,
CC ECO:0000269|PubMed:782920, ECO:0000269|PubMed:797648}.
CC -!- INTERACTION:
CC P0A7J3; P37351: rpiB; NbExp=2; IntAct=EBI-546827, EBI-557460;
CC -!- MASS SPECTROMETRY: Mass=17581.1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10094780};
CC -!- MASS SPECTROMETRY: Mass=66643; Mass_error=13; Method=Electrospray;
CC Note=Isolated L10(L12)4.; Evidence={ECO:0000269|PubMed:15923259};
CC -!- MASS SPECTROMETRY: Mass=17580; Mass_error=2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15923259};
CC -!- MISCELLANEOUS: Ribosomal protein L8 appears to be an aggregate of
CC ribosomal proteins L7/L12 and L10. {ECO:0000269|PubMed:773698}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000305}.
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DR EMBL; V00339; CAA23623.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43083.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76959.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77335.1; -; Genomic_DNA.
DR PIR; S12574; R5EC10.
DR RefSeq; NP_418412.1; NC_000913.3.
DR RefSeq; WP_001207201.1; NZ_STEB01000045.1.
DR PDB; 3J7Z; EM; 3.90 A; 5=1-165.
DR PDB; 3J9Y; EM; 3.90 A; 5=1-165.
DR PDB; 3J9Z; EM; 3.60 A; LD=2-165.
DR PDB; 3JA1; EM; 3.60 A; LJ=2-165.
DR PDB; 3JCJ; EM; 3.70 A; e=1-165.
DR PDB; 4UY8; EM; 3.80 A; 5=1-148.
DR PDB; 4V6N; EM; 12.10 A; AJ=2-165.
DR PDB; 4V6O; EM; 14.70 A; BJ=2-165.
DR PDB; 4V6P; EM; 13.50 A; BJ=2-165.
DR PDB; 4V6Q; EM; 11.50 A; BJ=2-165.
DR PDB; 4V6R; EM; 11.50 A; BJ=2-165.
DR PDB; 4V6S; EM; 13.10 A; AJ=2-165.
DR PDB; 4V6V; EM; 9.80 A; BJ=2-165.
DR PDB; 4V7B; EM; 6.80 A; B5=1-165.
DR PDB; 4V7C; EM; 7.60 A; BJ=1-165.
DR PDB; 4V7D; EM; 7.60 A; AJ=1-165.
DR PDB; 4V85; X-ray; 3.20 A; BH=1-165.
DR PDB; 4V89; X-ray; 3.70 A; BH=1-165.
DR PDB; 4V9O; X-ray; 2.90 A; A5/C5/E5=1-165.
DR PDB; 4V9P; X-ray; 2.90 A; A5/E5=1-165.
DR PDB; 4YBB; X-ray; 2.10 A; DI=2-136.
DR PDB; 5ADY; EM; 4.50 A; 7=1-165.
DR PDB; 5AFI; EM; 2.90 A; 5=1-165.
DR PDB; 5GAD; EM; 3.70 A; I=1-165.
DR PDB; 5GAE; EM; 3.33 A; I=1-165.
DR PDB; 5GAF; EM; 4.30 A; I=2-126.
DR PDB; 5GAG; EM; 3.80 A; I=1-165.
DR PDB; 5GAH; EM; 3.80 A; I=1-165.
DR PDB; 5H5U; EM; 3.00 A; I=2-165.
DR PDB; 5IQR; EM; 3.00 A; H=1-165.
DR PDB; 5IT8; X-ray; 3.12 A; DI=2-136.
DR PDB; 5J5B; X-ray; 2.80 A; DI=2-136.
DR PDB; 5J7L; X-ray; 3.00 A; DI=2-136.
DR PDB; 5J88; X-ray; 3.32 A; DI=2-136.
DR PDB; 5J8A; X-ray; 3.10 A; DI=2-136.
DR PDB; 5J91; X-ray; 2.96 A; DI=2-136.
DR PDB; 5JC9; X-ray; 3.03 A; DI=2-136.
DR PDB; 5KCR; EM; 3.60 A; 1J=1-165.
DR PDB; 5KCS; EM; 3.90 A; 1J=1-165.
DR PDB; 5KPS; EM; 3.90 A; H=1-165.
DR PDB; 5KPV; EM; 4.10 A; G=1-165.
DR PDB; 5KPW; EM; 3.90 A; G=1-165.
DR PDB; 5KPX; EM; 3.90 A; G=1-165.
DR PDB; 5L3P; EM; 3.70 A; J=1-165.
DR PDB; 5MDV; EM; 2.97 A; H=1-165.
DR PDB; 5MDW; EM; 3.06 A; H=1-165.
DR PDB; 5MDY; EM; 3.35 A; H=1-165.
DR PDB; 5MDZ; EM; 3.10 A; H=1-165.
DR PDB; 5NCO; EM; 4.80 A; I=2-126.
DR PDB; 5NP6; EM; 3.60 A; 3=1-131.
DR PDB; 5O2R; EM; 3.40 A; 5=1-131.
DR PDB; 5U9F; EM; 3.20 A; 10=1-165.
DR PDB; 5U9G; EM; 3.20 A; 10=1-165.
DR PDB; 5UYK; EM; 3.90 A; 10=1-131.
DR PDB; 5UYL; EM; 3.60 A; 10=1-131.
DR PDB; 5UYM; EM; 3.20 A; 10=1-131.
DR PDB; 5UYN; EM; 4.00 A; 10=1-131.
DR PDB; 5UYP; EM; 3.90 A; 10=1-131.
DR PDB; 5UYQ; EM; 3.80 A; 10=1-131.
DR PDB; 5WDT; EM; 3.00 A; 5=1-131.
DR PDB; 5WE4; EM; 3.10 A; 5=1-131.
DR PDB; 5WE6; EM; 3.40 A; 5=1-131.
DR PDB; 5WFK; EM; 3.40 A; 5=1-131.
DR PDB; 6BU8; EM; 3.50 A; 10=1-131.
DR PDB; 6BY1; X-ray; 3.94 A; C5=2-110.
DR PDB; 6C4I; EM; 3.24 A; I=1-165.
DR PDB; 6GWT; EM; 3.80 A; 5=1-131.
DR PDB; 6GXM; EM; 3.80 A; 5=1-131.
DR PDB; 6GXN; EM; 3.90 A; 5=1-131.
DR PDB; 6GXO; EM; 3.90 A; 5=1-131.
DR PDB; 6GXP; EM; 4.40 A; 5=1-131.
DR PDB; 6HRM; EM; 2.96 A; H=2-131.
DR PDB; 6I0Y; EM; 3.20 A; 5=1-165.
DR PDB; 6O9K; EM; 4.00 A; G=1-117.
DR PDB; 6Q97; EM; 3.90 A; H=2-131.
DR PDB; 6Q98; EM; 4.30 A; H=1-165.
DR PDB; 6Q9A; EM; 3.70 A; H=2-131.
DR PDB; 6WD6; EM; 3.70 A; h=1-131.
DR PDB; 6WDB; EM; 4.00 A; h=1-131.
DR PDB; 6WDC; EM; 4.20 A; h=1-131.
DR PDB; 6WDD; EM; 3.20 A; h=1-131.
DR PDB; 6WDE; EM; 3.00 A; h=1-131.
DR PDB; 6WDF; EM; 3.30 A; h=1-131.
DR PDB; 6WDG; EM; 3.30 A; h=1-131.
DR PDB; 6WDH; EM; 4.30 A; h=1-131.
DR PDB; 6WDI; EM; 4.00 A; h=1-131.
DR PDB; 6WDJ; EM; 3.70 A; h=1-131.
DR PDB; 6WDK; EM; 3.60 A; h=1-131.
DR PDB; 6WDL; EM; 3.70 A; h=1-131.
DR PDB; 6WDM; EM; 3.60 A; h=1-131.
DR PDB; 6WNT; EM; 3.10 A; h=1-131.
DR PDB; 6WNV; EM; 3.50 A; h=1-131.
DR PDB; 6WNW; EM; 3.20 A; h=1-131.
DR PDB; 6XZ7; EM; 2.10 A; H=2-136.
DR PDB; 6XZA; EM; 2.66 A; H2=2-136.
DR PDB; 6XZB; EM; 2.54 A; H2=2-136.
DR PDB; 7ABZ; EM; 3.21 A; H=2-131.
DR PDB; 7AC7; EM; 3.08 A; H=2-131.
DR PDB; 7BL5; EM; 3.30 A; e=1-165.
DR PDB; 7BV8; EM; 3.14 A; I=1-165.
DR PDB; 7JSZ; EM; 3.70 A; h=1-165.
DR PDB; 7JT2; EM; 3.50 A; h=1-165.
DR PDB; 7JT3; EM; 3.70 A; h=1-165.
DR PDB; 7K50; EM; 3.40 A; h=1-131.
DR PDB; 7K51; EM; 3.50 A; h=1-131.
DR PDB; 7K52; EM; 3.40 A; h=1-131.
DR PDB; 7K53; EM; 3.20 A; h=1-131.
DR PDB; 7K54; EM; 3.20 A; h=1-131.
DR PDB; 7K55; EM; 3.30 A; h=1-131.
DR PDB; 7LV0; EM; 3.20 A; h=1-131.
DR PDB; 7N1P; EM; 2.33 A; LJ=1-165.
DR PDB; 7N2C; EM; 2.72 A; LJ=1-165.
DR PDB; 7N2V; EM; 2.54 A; LJ=1-165.
DR PDB; 7OJ0; EM; 3.50 A; 5=2-131.
DR PDB; 7PJV; EM; 3.10 A; 5=1-165.
DR PDB; 7PJY; EM; 3.10 A; 5=1-165.
DR PDB; 7SSO; EM; 3.20 A; h=1-131.
DR PDB; 7ST2; EM; 2.90 A; h=1-131.
DR PDBsum; 3J7Z; -.
DR PDBsum; 3J9Y; -.
DR PDBsum; 3J9Z; -.
DR PDBsum; 3JA1; -.
DR PDBsum; 3JCJ; -.
DR PDBsum; 4UY8; -.
DR PDBsum; 4V6N; -.
DR PDBsum; 4V6O; -.
DR PDBsum; 4V6P; -.
DR PDBsum; 4V6Q; -.
DR PDBsum; 4V6R; -.
DR PDBsum; 4V6S; -.
DR PDBsum; 4V6V; -.
DR PDBsum; 4V7B; -.
DR PDBsum; 4V7C; -.
DR PDBsum; 4V7D; -.
DR PDBsum; 4V85; -.
DR PDBsum; 4V89; -.
DR PDBsum; 4V9O; -.
DR PDBsum; 4V9P; -.
DR PDBsum; 4YBB; -.
DR PDBsum; 5ADY; -.
DR PDBsum; 5AFI; -.
DR PDBsum; 5GAD; -.
DR PDBsum; 5GAE; -.
DR PDBsum; 5GAF; -.
DR PDBsum; 5GAG; -.
DR PDBsum; 5GAH; -.
DR PDBsum; 5H5U; -.
DR PDBsum; 5IQR; -.
DR PDBsum; 5IT8; -.
DR PDBsum; 5J5B; -.
DR PDBsum; 5J7L; -.
DR PDBsum; 5J88; -.
DR PDBsum; 5J8A; -.
DR PDBsum; 5J91; -.
DR PDBsum; 5JC9; -.
DR PDBsum; 5KCR; -.
DR PDBsum; 5KCS; -.
DR PDBsum; 5KPS; -.
DR PDBsum; 5KPV; -.
DR PDBsum; 5KPW; -.
DR PDBsum; 5KPX; -.
DR PDBsum; 5L3P; -.
DR PDBsum; 5MDV; -.
DR PDBsum; 5MDW; -.
DR PDBsum; 5MDY; -.
DR PDBsum; 5MDZ; -.
DR PDBsum; 5NCO; -.
DR PDBsum; 5NP6; -.
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; 6GWT; -.
DR PDBsum; 6GXM; -.
DR PDBsum; 6GXN; -.
DR PDBsum; 6GXO; -.
DR PDBsum; 6GXP; -.
DR PDBsum; 6HRM; -.
DR PDBsum; 6I0Y; -.
DR PDBsum; 6O9K; -.
DR PDBsum; 6Q97; -.
DR PDBsum; 6Q98; -.
DR PDBsum; 6Q9A; -.
DR PDBsum; 6WD6; -.
DR PDBsum; 6WDB; -.
DR PDBsum; 6WDC; -.
DR PDBsum; 6WDD; -.
DR PDBsum; 6WDE; -.
DR PDBsum; 6WDF; -.
DR PDBsum; 6WDG; -.
DR PDBsum; 6WDH; -.
DR PDBsum; 6WDI; -.
DR PDBsum; 6WDJ; -.
DR PDBsum; 6WDK; -.
DR PDBsum; 6WDL; -.
DR PDBsum; 6WDM; -.
DR PDBsum; 6WNT; -.
DR PDBsum; 6WNV; -.
DR PDBsum; 6WNW; -.
DR PDBsum; 6XZ7; -.
DR PDBsum; 6XZA; -.
DR PDBsum; 6XZB; -.
DR PDBsum; 7ABZ; -.
DR PDBsum; 7AC7; -.
DR PDBsum; 7BL5; -.
DR PDBsum; 7BV8; -.
DR PDBsum; 7JSZ; -.
DR PDBsum; 7JT2; -.
DR PDBsum; 7JT3; -.
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; 7N2V; -.
DR PDBsum; 7OJ0; -.
DR PDBsum; 7PJV; -.
DR PDBsum; 7PJY; -.
DR PDBsum; 7SSO; -.
DR PDBsum; 7ST2; -.
DR AlphaFoldDB; P0A7J3; -.
DR SMR; P0A7J3; -.
DR BioGRID; 852784; 1.
DR ComplexPortal; CPX-3807; 50S large ribosomal subunit.
DR DIP; DIP-35816N; -.
DR IntAct; P0A7J3; 111.
DR STRING; 511145.b3985; -.
DR MoonProt; P0A7J3; -.
DR iPTMnet; P0A7J3; -.
DR jPOST; P0A7J3; -.
DR PaxDb; P0A7J3; -.
DR PRIDE; P0A7J3; -.
DR EnsemblBacteria; AAC76959; AAC76959; b3985.
DR EnsemblBacteria; BAE77335; BAE77335; BAE77335.
DR GeneID; 67415314; -.
DR GeneID; 948490; -.
DR KEGG; ecj:JW3948; -.
DR KEGG; eco:b3985; -.
DR PATRIC; fig|1411691.4.peg.2727; -.
DR EchoBASE; EB0864; -.
DR eggNOG; COG0244; Bacteria.
DR HOGENOM; CLU_092227_0_2_6; -.
DR InParanoid; P0A7J3; -.
DR OMA; VRDQKQA; -.
DR PhylomeDB; P0A7J3; -.
DR BioCyc; EcoCyc:EG10871-MON; -.
DR BioCyc; MetaCyc:EG10871-MON; -.
DR PRO; PR:P0A7J3; -.
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:0015934; C:large ribosomal subunit; IDA:CAFA.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; IMP:CAFA.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0017148; P:negative regulation of translation; IDA:CAFA.
DR GO; GO:0006412; P:translation; IDA:CAFA.
DR CDD; cd05797; Ribosomal_L10; 1.
DR Gene3D; 3.30.70.1730; -; 1.
DR HAMAP; MF_00362; Ribosomal_L10; 1.
DR InterPro; IPR022973; Ribosomal_L10.
DR InterPro; IPR043141; Ribosomal_L10-like_sf.
DR InterPro; IPR002363; Ribosomal_L10_eubac_CS.
DR InterPro; IPR001790; Ribosomal_L10P.
DR PANTHER; PTHR11560; PTHR11560; 1.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR SUPFAM; SSF160369; SSF160369; 1.
DR PROSITE; PS01109; RIBOSOMAL_L10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Reference proteome;
KW Repressor; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:773698,
FT ECO:0000269|PubMed:782920, ECO:0000269|PubMed:797648"
FT CHAIN 2..165
FT /note="50S ribosomal protein L10"
FT /id="PRO_0000154627"
FT MOD_RES 37
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 156..165
FT /note="Missing: Generation time doubles, only 1 L12 dimer
FT binds to the ribosome. Decreased association of IF-2 with
FT L7/L12 and decreased stimulation of GTPase activity of EF-G
FT by L7/L12."
FT /evidence="ECO:0000269|PubMed:22102582"
FT CONFLICT 84
FT /note="Y -> YR (in Ref. 5; AA sequence, 6; AA sequence and
FT 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="E -> Q (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..21
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:6XZ7"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 92..103
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:6I0Y"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:6I0Y"
SQ SEQUENCE 165 AA; 17712 MW; F15822B0EDB6AC02 CRC64;
MALNLQDKQA IVAEVSEVAK GALSAVVADS RGVTVDKMTE LRKAGREAGV YMRVVRNTLL
RRAVEGTPFE CLKDAFVGPT LIAYSMEHPG AAARLFKEFA KANAKFEVKA AAFEGELIPA
SQIDRLATLP TYEEAIARLM ATMKEASAGK LVRTLAAVRD AKEAA
