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30S ribosomal protein S12 (Small ribosomal subunit protein uS12)

 RS12_ECOLI              Reviewed;         124 AA.
P0A7S3; P02367; Q2M707; Q9F5N3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 142.
RecName: Full=30S ribosomal protein S12;
AltName: Full=Small ribosomal subunit protein uS12 {ECO:0000303|PubMed:24524803};
Name=rpsL; Synonyms=strA; OrderedLocusNames=b3342, JW3304;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
PRELIMINARY PROTEIN SEQUENCE OF 2-124, AND SUBUNIT.
STRAIN=K;
PubMed=320034; DOI=10.1016/0014-5793(77)80004-5;
Funatsu G., Yaguchi M., Wittmann-Liebold B.;
"Primary structure of protein S12 from the small Escherichia coli
ribosomal subunit.";
FEBS Lett. 73:12-17(1977).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=6989816;
Post L.E., Nomura M.;
"DNA sequences from the str operon of Escherichia coli.";
J. Biol. Chem. 255:4660-4666(1980).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS STREPTOMYCIN
RESISTANT.
STRAIN=B/R WP2;
PubMed=1552908; DOI=10.1007/BF00299141;
Timms A.R., Steingrimsdottir H., Lehmann A.R., Bridges B.A.;
"Mutant sequences in the rpsL gene of Escherichia coli B/r:
mechanistic implications for spontaneous and ultraviolet light
mutagenesis.";
Mol. Gen. Genet. 232:89-96(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT STREPTOMYCIN RESISTANT.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574, and K12 / W3110 / ZK126;
Kharat A.S., Blot M.;
"Nucleotide information of the rpsL150 allele of MC4100, strain of
Escherichia coli.";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
STRAIN=K12;
PubMed=151587; DOI=10.1016/0092-8674(78)90096-X;
Post L.E., Arfsten A.E., Reusser F., Nomura M.;
"DNA sequences of promoter regions for the str and spc ribosomal
protein operons in E. coli.";
Cell 15:215-229(1978).
[8]
PROTEIN SEQUENCE OF 2-11, CROSS-LINKING TO RRNA, AND SUBUNIT.
STRAIN=MRE-600;
PubMed=7556101;
Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.;
"Protein-rRNA binding features and their structural and functional
implications in ribosomes as determined by cross-linking studies.";
EMBO J. 14:4578-4588(1995).
[9]
EFFECT OF MUTATIONS ON RRNA FOLDING.
STRAIN=UD1A1;
PubMed=2477554; DOI=10.1016/0022-2836(89)90509-3;
Allen P.N., Noller H.F.;
"Mutations in ribosomal proteins S4 and S12 influence the higher order
structure of 16 S ribosomal RNA.";
J. Mol. Biol. 208:457-468(1989).
[10]
MUTAGENESIS OF LEU-57 AND LYS-88.
STRAIN=K12;
PubMed=10209746; DOI=10.1046/j.1365-2958.1999.01307.x;
Toivonen J.M., Boocock M.R., Jacobs H.T.;
"Modelling in Escherichia coli of mutations in mitoribosomal protein
S12: novel mutant phenotypes of rpsL.";
Mol. Microbiol. 31:1735-1746(1999).
[11]
METHYLTHIOLATION AT ASP-89.
PubMed=8844851; DOI=10.1002/pro.5560050816;
Kowalak J.A., Walsh K.A.;
"Beta-methylthio-aspartic acid: identification of a novel
posttranslational modification in ribosomal protein S12 from
Escherichia coli.";
Protein Sci. 5:1625-1632(1996).
[12]
MASS SPECTROMETRY, AND SUBUNIT.
STRAIN=K12 / ATCC 25404 / DSM 5698 / NCIMB 11290;
PubMed=10094780; DOI=10.1006/abio.1998.3077;
Arnold R.J., Reilly J.P.;
"Observation of Escherichia coli ribosomal proteins and their
posttranslational modifications by mass spectrometry.";
Anal. Biochem. 269:105-112(1999).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[14]
REVIEW ON TRANSLATIONAL ACCURACY.
Kurland C.G., Hughes D., Ehrenberg M.;
"Limitations of translational accuracy.";
(In) Neidhardt F.C., Curtiss R. III, Ingraham J.L., Lin E.C.C.,
Low K.B. Magasanik B., Reznikoff W.S., Riley M., Schaechter M.,
Umbarger H.E. (eds.);
Escherichia coli and Salmonella: Cellular and molecular biology (2nd
ed.), pp.979-1004, American Society for Microbiology Press, Washington
D.C. (1996).
[15]
NOMENCLATURE.
PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
Williamson J.R., Wilson D., Yonath A., Yusupov M.;
"A new system for naming ribosomal proteins.";
Curr. Opin. Struct. Biol. 24:165-169(2014).
[16]
STRUCTURE BY ELECTRON MICROSCOPY (11 ANGSTROMS) OF KIRROMYCIN-STALLED
RIBOSOMES COMPLEXED WITH EF-TU/AMINOACYL-TRNA/GTP, AND SUBUNIT.
PubMed=12093756; DOI=10.1093/emboj/cdf326;
Valle M., Sengupta J., Swami N.K., Grassucci R.A., Burkhardt N.,
Nierhaus K.H., Agrawal R.K., Frank J.;
"Cryo-EM reveals an active role for aminoacyl-tRNA in the
accommodation process.";
EMBO J. 21:3557-3567(2002).
[17]
STRUCTURE BY ELECTRON MICROSCOPY (13 ANGSTROMS) OF KIRROMYCIN-STALLED
RIBOSOMES COMPLEXED WITH EF-TU/AMINOACYL-TRNA/GTP, AND SUBUNIT.
STRAIN=MRE-600;
PubMed=12379845; DOI=10.1038/nsb859;
Stark H., Rodnina M.V., Wieden H.-J., Zemlin F., Wintermeyer W.,
Van Heel M.;
"Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in
the codon-recognition complex.";
Nat. Struct. Biol. 9:849-854(2002).
[18]
3D-STRUCTURE MODELING, AND SUBUNIT.
PubMed=12244297; DOI=10.1038/nsb841;
Tung C.-S., Joseph S., Sanbonmatsu K.Y.;
"All-atom homology model of the Escherichia coli 30S ribosomal
subunit.";
Nat. Struct. Biol. 9:750-755(2002).
[19]
STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS), AND SUBUNIT.
STRAIN=MRE-600;
PubMed=12809609; DOI=10.1016/S0092-8674(03)00427-6;
Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M.,
Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S.,
Frank J.;
"Study of the structural dynamics of the E. coli 70S ribosome using
real-space refinement.";
Cell 113:789-801(2003).
[20]
X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME
STRUCTURES, AND SUBUNIT.
STRAIN=MRE-600;
PubMed=16272117; DOI=10.1126/science.1117230;
Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W.,
Vila-Sanjurjo A., Holton J.M., Cate J.H.D.;
"Structures of the bacterial ribosome at 3.5 A resolution.";
Science 310:827-834(2005).
[21]
STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 70S RIBOSOME IN
COMPLEX WITH ARFA AND RF2, INTERACTION WITH ARFA, AND SUBUNIT.
PubMed=27906160; DOI=10.1038/nature20822;
Ma C., Kurita D., Li N., Chen Y., Himeno H., Gao N.;
"Mechanistic insights into the alternative translation termination by
ArfA and RF2.";
Nature 541:550-553(2017).
[22] {ECO:0000244|PDB:5MGP}
STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 2-124 OF 70S
RIBOSOME IN COMPLEX WITH ARFA AND RF2, INTERACTION WITH RF2, AND
SUBUNIT.
PubMed=27906161; DOI=10.1038/nature20821;
Huter P., Mueller C., Beckert B., Arenz S., Berninghausen O.,
Beckmann R., Wilson D.N.;
"Structural basis for ArfA-RF2-mediated translation termination on
mRNAs lacking stop codons.";
Nature 541:546-549(2017).
[23]
STRUCTURE BY ELECTRON MICROSCOPY (2.97 ANGSTROMS) OF 70S RIBOSOME IN
COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
PubMed=27934701; DOI=10.1126/science.aai9127;
James N.R., Brown A., Gordiyenko Y., Ramakrishnan V.;
"Translational termination without a stop codon.";
Science 354:1437-1440(2016).
[24]
STRUCTURE BY ELECTRON MICROSCOPY (3.52 ANGSTROMS) OF 70S RIBOSOME IN
COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
PubMed=28077875; DOI=10.1038/nature21053;
Zeng F., Chen Y., Remis J., Shekhar M., Phillips J.C., Tajkhorshid E.,
Jin H.;
"Structural basis of co-translational quality control by ArfA and RF2
bound to ribosome.";
Nature 541:554-557(2017).
-!- FUNCTION: With S4 and S5 plays an important role in translational
accuracy.
-!- FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that
are involved in tRNA selection in the A site and with the mRNA
backbone. Located at the interface of the 30S and 50S subunits, it
traverses the body of the 30S subunit contacting proteins on the
other side and probably holding the rRNA structure together. The
combined cluster of proteins S8, S12 and S17 appears to hold
together the shoulder and platform of the 30S subunit (By
similarity). {ECO:0000250|UniProtKB:Q5SHN3,
ECO:0000269|PubMed:7556101}.
-!- FUNCTION: Cryo-EM studies suggest that S12 contacts the EF-Tu
bound tRNA in the A-site during codon-recognition. This contact is
most likely broken as the aminoacyl-tRNA moves into the peptidyl
transferase center in the 50S subunit.
{ECO:0000305|PubMed:12093756}.
-!- SUBUNIT: Part of the 30S ribosomal subunit (PubMed:320034,
PubMed:7556101, PubMed:12809609, PubMed:16272117, PubMed:27934701,
PubMed:10094780, PubMed:12093756, PubMed:12379845,
PubMed:12244297, PubMed:27906160, PubMed:27906161). Contacts
proteins S8 and S17. Interacts with ArfA (PubMed:27906160,
PubMed:27906161). May interact with IF1 in the 30S initiation
complex (By similarity). {ECO:0000250|UniProtKB:Q5SHN3,
ECO:0000269|PubMed:10094780, ECO:0000269|PubMed:12093756,
ECO:0000269|PubMed:12244297, ECO:0000269|PubMed:12379845,
ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:16272117,
ECO:0000269|PubMed:27906160, ECO:0000269|PubMed:27906161,
ECO:0000269|PubMed:27934701, ECO:0000269|PubMed:320034,
ECO:0000269|PubMed:7556101}.
-!- INTERACTION:
P0A8A8:rimP; NbExp=3; IntAct=EBI-543960, EBI-561065;
-!- MASS SPECTROMETRY: Mass=13651.3; Method=MALDI; Range=2-124;
Evidence={ECO:0000269|PubMed:10094780};
-!- MISCELLANEOUS: At least 19 substitutions or deletions in 11 codons
can promote streptomycin resistance, dependence or
pseudodependence; all but one of the streptomycin resistant
mutations (K42R) are associated with hyperaccurate translation and
thus reduced translational efficiency.
{ECO:0000269|PubMed:1552908, ECO:0000269|Ref.5}.
-!- MISCELLANEOUS: The streptomycin sensitive allele is dominant to
resistant alleles.
-!- SIMILARITY: Belongs to the universal ribosomal protein uS12
family. {ECO:0000305}.
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EMBL; V00355; CAA23648.1; -; Genomic_DNA.
EMBL; U18997; AAA58139.1; -; Genomic_DNA.
EMBL; U00096; AAC76367.1; -; Genomic_DNA.
EMBL; AP009048; BAE77949.1; -; Genomic_DNA.
EMBL; AF312716; AAG30936.1; -; Genomic_DNA.
EMBL; AF312717; AAG30937.1; -; Genomic_DNA.
EMBL; V00354; CAA23647.1; -; Genomic_DNA.
EMBL; J01688; AAA50988.1; -; Genomic_DNA.
PIR; S13738; R3EC12.
RefSeq; NP_417801.1; NC_000913.3.
RefSeq; WP_000246815.1; NZ_CP011343.2.
PDB; 1M5G; Model; -; L=2-124.
PDB; 1MJ1; EM; 13.00 A; O=5-123.
PDB; 1ZN1; EM; 14.10 A; L=28-124.
PDB; 2YKR; EM; 9.80 A; L=2-124.
PDB; 3DEG; EM; -; D=2-124.
PDB; 3EP2; EM; -; L=2-124.
PDB; 3EQ3; EM; -; L=2-124.
PDB; 3EQ4; EM; -; L=2-124.
PDB; 3J0D; EM; 11.10 A; I=2-124.
PDB; 3J0E; EM; 9.90 A; F=2-124.
PDB; 3J9Y; EM; 3.90 A; l=1-124.
PDB; 3J9Z; EM; 3.60 A; SL=2-124.
PDB; 3JA1; EM; 3.60 A; SL=2-124.
PDB; 3JBU; EM; 3.64 A; L=1-124.
PDB; 3JBV; EM; 3.32 A; L=1-124.
PDB; 3JCD; EM; 3.70 A; l=1-124.
PDB; 3JCE; EM; 3.20 A; l=1-124.
PDB; 3JCJ; EM; 3.70 A; t=1-124.
PDB; 3JCN; EM; 4.60 A; o=1-124.
PDB; 4A2I; EM; 16.50 A; L=2-124.
PDB; 4ADV; EM; 13.50 A; L=2-124.
PDB; 4U1U; X-ray; 2.95 A; AL/CL=2-124.
PDB; 4U1V; X-ray; 3.00 A; AL/CL=2-124.
PDB; 4U20; X-ray; 2.90 A; AL/CL=2-124.
PDB; 4U24; X-ray; 2.90 A; AL/CL=2-124.
PDB; 4U25; X-ray; 2.90 A; AL/CL=2-124.
PDB; 4U26; X-ray; 2.80 A; AL/CL=2-124.
PDB; 4U27; X-ray; 2.80 A; AL/CL=2-124.
PDB; 4V47; EM; 12.30 A; BL=2-124.
PDB; 4V48; EM; 11.50 A; BL=2-124.
PDB; 4V4H; X-ray; 3.46 A; AL/CL=1-124.
PDB; 4V4Q; X-ray; 3.46 A; AL/CL=2-124.
PDB; 4V4V; EM; 15.00 A; AL=23-123.
PDB; 4V4W; EM; 15.00 A; AL=23-123.
PDB; 4V50; X-ray; 3.22 A; AL/CL=2-124.
PDB; 4V52; X-ray; 3.21 A; AL/CL=2-124.
PDB; 4V53; X-ray; 3.54 A; AL/CL=2-124.
PDB; 4V54; X-ray; 3.30 A; AL/CL=2-124.
PDB; 4V55; X-ray; 4.00 A; AL/CL=2-124.
PDB; 4V56; X-ray; 3.93 A; AL/CL=2-124.
PDB; 4V57; X-ray; 3.50 A; AL/CL=2-124.
PDB; 4V5B; X-ray; 3.74 A; BL/DL=2-124.
PDB; 4V5H; EM; 5.80 A; AL=2-124.
PDB; 4V5Y; X-ray; 4.45 A; AL/CL=2-124.
PDB; 4V64; X-ray; 3.50 A; AL/CL=2-124.
PDB; 4V65; EM; 9.00 A; AD=1-124.
PDB; 4V66; EM; 9.00 A; AD=1-124.
PDB; 4V69; EM; 6.70 A; AL=2-124.
PDB; 4V6C; X-ray; 3.19 A; AL/CL=1-124.
PDB; 4V6D; X-ray; 3.81 A; AL/CL=1-124.
PDB; 4V6E; X-ray; 3.71 A; AL/CL=1-124.
PDB; 4V6K; EM; 8.25 A; BP=1-124.
PDB; 4V6L; EM; 13.20 A; AP=1-124.
PDB; 4V6M; EM; 7.10 A; AL=2-124, AO=2-89.
PDB; 4V6N; EM; 12.10 A; BO=2-124.
PDB; 4V6O; EM; 14.70 A; AO=2-124.
PDB; 4V6P; EM; 13.50 A; AO=2-124.
PDB; 4V6Q; EM; 11.50 A; AO=2-124.
PDB; 4V6R; EM; 11.50 A; AO=2-124.
PDB; 4V6S; EM; 13.10 A; BN=2-124.
PDB; 4V6T; EM; 8.30 A; AL=2-124.
PDB; 4V6V; EM; 9.80 A; AL=2-124.
PDB; 4V6Y; EM; 12.00 A; AL=1-124.
PDB; 4V6Z; EM; 12.00 A; AL=1-124.
PDB; 4V70; EM; 17.00 A; AL=1-124.
PDB; 4V71; EM; 20.00 A; AL=1-124.
PDB; 4V72; EM; 13.00 A; AL=1-124.
PDB; 4V73; EM; 15.00 A; AL=1-124.
PDB; 4V74; EM; 17.00 A; AL=1-124.
PDB; 4V75; EM; 12.00 A; AL=1-124.
PDB; 4V76; EM; 17.00 A; AL=1-124.
PDB; 4V77; EM; 17.00 A; AL=1-124.
PDB; 4V78; EM; 20.00 A; AL=1-124.
PDB; 4V79; EM; 15.00 A; AL=1-124.
PDB; 4V7A; EM; 9.00 A; AL=1-124.
PDB; 4V7B; EM; 6.80 A; AL=1-124.
PDB; 4V7C; EM; 7.60 A; AL=2-124.
PDB; 4V7D; EM; 7.60 A; BL=2-124.
PDB; 4V7I; EM; 9.60 A; BL=1-124.
PDB; 4V7S; X-ray; 3.25 A; AL/CL=2-124.
PDB; 4V7T; X-ray; 3.19 A; AL/CL=2-124.
PDB; 4V7U; X-ray; 3.10 A; AL/CL=2-124.
PDB; 4V7V; X-ray; 3.29 A; AL/CL=2-124.
PDB; 4V85; X-ray; 3.20 A; L=1-124.
PDB; 4V89; X-ray; 3.70 A; AL=1-124.
PDB; 4V9C; X-ray; 3.30 A; AL/CL=1-124.
PDB; 4V9D; X-ray; 3.00 A; AL/BL=2-124.
PDB; 4V9O; X-ray; 2.90 A; BL/DL/FL/HL=1-124.
PDB; 4V9P; X-ray; 2.90 A; BL/DL/FL/HL=1-124.
PDB; 4WF1; X-ray; 3.09 A; AL/CL=2-124.
PDB; 4WOI; X-ray; 3.00 A; AL/DL=1-124.
PDB; 4WWW; X-ray; 3.10 A; QL/XL=2-124.
PDB; 4YBB; X-ray; 2.10 A; AL/BL=2-124.
PDB; 5AFI; EM; 2.90 A; l=1-124.
PDB; 5H5U; EM; 3.00 A; s=2-124.
PDB; 5IQR; EM; 3.00 A; q=1-124.
PDB; 5IT8; X-ray; 3.12 A; AL/BL=2-124.
PDB; 5J5B; X-ray; 2.80 A; AL/BL=2-124.
PDB; 5J7L; X-ray; 3.00 A; AL/BL=2-124.
PDB; 5J88; X-ray; 3.32 A; AL/BL=2-124.
PDB; 5J8A; X-ray; 3.10 A; AL/BL=2-124.
PDB; 5J91; X-ray; 2.96 A; AL/BL=2-124.
PDB; 5JC9; X-ray; 3.03 A; AL/BL=2-124.
PDB; 5JTE; EM; 3.60 A; AL=1-124.
PDB; 5JU8; EM; 3.60 A; AL=1-124.
PDB; 5KCR; EM; 3.60 A; 1l=1-124.
PDB; 5KCS; EM; 3.90 A; 1l=1-124.
PDB; 5KPS; EM; 3.90 A; 17=1-124.
PDB; 5KPV; EM; 4.10 A; 16=1-124.
PDB; 5KPW; EM; 3.90 A; 16=1-124.
PDB; 5KPX; EM; 3.90 A; 16=1-124.
PDB; 5L3P; EM; 3.70 A; l=1-124.
PDB; 5LZA; EM; 3.60 A; l=2-124.
PDB; 5LZB; EM; 5.30 A; l=2-124.
PDB; 5LZC; EM; 4.80 A; l=2-124.
PDB; 5LZD; EM; 3.40 A; l=2-124.
PDB; 5LZE; EM; 3.50 A; l=2-124.
PDB; 5LZF; EM; 4.60 A; l=2-124.
PDB; 5MDV; EM; 2.97 A; q=1-124.
PDB; 5MDW; EM; 3.06 A; q=1-124.
PDB; 5MDY; EM; 3.35 A; q=1-124.
PDB; 5MDZ; EM; 3.10 A; q=1-124.
PDB; 5ME0; EM; 13.50 A; L=2-124.
PDB; 5ME1; EM; 13.50 A; L=2-124.
PDB; 5MGP; EM; 3.10 A; l=2-124.
PDB; 5MY1; EM; 7.60 A; L=2-124.
PDB; 5NO2; EM; 5.16 A; L=2-15.
PDB; 5NO3; EM; 5.16 A; L=2-15.
PDB; 5NO4; EM; 5.16 A; L=2-15.
PDB; 5NP6; EM; 3.60 A; O=2-124.
PDB; 5NWY; EM; 2.93 A; B=1-124.
PDB; 5O2R; EM; 3.40 A; l=2-124.
PDB; 5U4I; EM; 3.50 A; l=2-124.
PDB; 5U4J; EM; 3.70 A; l=1-124.
PDB; 5U9F; EM; 3.20 A; L=1-124.
PDB; 5U9G; EM; 3.20 A; L=1-124.
PDB; 5UYK; EM; 3.90 A; L=2-124.
PDB; 5UYL; EM; 3.60 A; L=2-124.
PDB; 5UYM; EM; 3.20 A; L=2-124.
PDB; 5UYN; EM; 4.00 A; L=2-124.
PDB; 5UYP; EM; 3.90 A; L=2-124.
PDB; 5UYQ; EM; 3.80 A; L=2-124.
PDBsum; 1M5G; -.
PDBsum; 1MJ1; -.
PDBsum; 1ZN1; -.
PDBsum; 2YKR; -.
PDBsum; 3DEG; -.
PDBsum; 3EP2; -.
PDBsum; 3EQ3; -.
PDBsum; 3EQ4; -.
PDBsum; 3J0D; -.
PDBsum; 3J0E; -.
PDBsum; 3J9Y; -.
PDBsum; 3J9Z; -.
PDBsum; 3JA1; -.
PDBsum; 3JBU; -.
PDBsum; 3JBV; -.
PDBsum; 3JCD; -.
PDBsum; 3JCE; -.
PDBsum; 3JCJ; -.
PDBsum; 3JCN; -.
PDBsum; 4A2I; -.
PDBsum; 4ADV; -.
PDBsum; 4U1U; -.
PDBsum; 4U1V; -.
PDBsum; 4U20; -.
PDBsum; 4U24; -.
PDBsum; 4U25; -.
PDBsum; 4U26; -.
PDBsum; 4U27; -.
PDBsum; 4V47; -.
PDBsum; 4V48; -.
PDBsum; 4V4H; -.
PDBsum; 4V4Q; -.
PDBsum; 4V4V; -.
PDBsum; 4V4W; -.
PDBsum; 4V50; -.
PDBsum; 4V52; -.
PDBsum; 4V53; -.
PDBsum; 4V54; -.
PDBsum; 4V55; -.
PDBsum; 4V56; -.
PDBsum; 4V57; -.
PDBsum; 4V5B; -.
PDBsum; 4V5H; -.
PDBsum; 4V5Y; -.
PDBsum; 4V64; -.
PDBsum; 4V65; -.
PDBsum; 4V66; -.
PDBsum; 4V69; -.
PDBsum; 4V6C; -.
PDBsum; 4V6D; -.
PDBsum; 4V6E; -.
PDBsum; 4V6K; -.
PDBsum; 4V6L; -.
PDBsum; 4V6M; -.
PDBsum; 4V6N; -.
PDBsum; 4V6O; -.
PDBsum; 4V6P; -.
PDBsum; 4V6Q; -.
PDBsum; 4V6R; -.
PDBsum; 4V6S; -.
PDBsum; 4V6T; -.
PDBsum; 4V6V; -.
PDBsum; 4V6Y; -.
PDBsum; 4V6Z; -.
PDBsum; 4V70; -.
PDBsum; 4V71; -.
PDBsum; 4V72; -.
PDBsum; 4V73; -.
PDBsum; 4V74; -.
PDBsum; 4V75; -.
PDBsum; 4V76; -.
PDBsum; 4V77; -.
PDBsum; 4V78; -.
PDBsum; 4V79; -.
PDBsum; 4V7A; -.
PDBsum; 4V7B; -.
PDBsum; 4V7C; -.
PDBsum; 4V7D; -.
PDBsum; 4V7I; -.
PDBsum; 4V7S; -.
PDBsum; 4V7T; -.
PDBsum; 4V7U; -.
PDBsum; 4V7V; -.
PDBsum; 4V85; -.
PDBsum; 4V89; -.
PDBsum; 4V9C; -.
PDBsum; 4V9D; -.
PDBsum; 4V9O; -.
PDBsum; 4V9P; -.
PDBsum; 4WF1; -.
PDBsum; 4WOI; -.
PDBsum; 4WWW; -.
PDBsum; 4YBB; -.
PDBsum; 5AFI; -.
PDBsum; 5H5U; -.
PDBsum; 5IQR; -.
PDBsum; 5IT8; -.
PDBsum; 5J5B; -.
PDBsum; 5J7L; -.
PDBsum; 5J88; -.
PDBsum; 5J8A; -.
PDBsum; 5J91; -.
PDBsum; 5JC9; -.
PDBsum; 5JTE; -.
PDBsum; 5JU8; -.
PDBsum; 5KCR; -.
PDBsum; 5KCS; -.
PDBsum; 5KPS; -.
PDBsum; 5KPV; -.
PDBsum; 5KPW; -.
PDBsum; 5KPX; -.
PDBsum; 5L3P; -.
PDBsum; 5LZA; -.
PDBsum; 5LZB; -.
PDBsum; 5LZC; -.
PDBsum; 5LZD; -.
PDBsum; 5LZE; -.
PDBsum; 5LZF; -.
PDBsum; 5MDV; -.
PDBsum; 5MDW; -.
PDBsum; 5MDY; -.
PDBsum; 5MDZ; -.
PDBsum; 5ME0; -.
PDBsum; 5ME1; -.
PDBsum; 5MGP; -.
PDBsum; 5MY1; -.
PDBsum; 5NO2; -.
PDBsum; 5NO3; -.
PDBsum; 5NO4; -.
PDBsum; 5NP6; -.
PDBsum; 5NWY; -.
PDBsum; 5O2R; -.
PDBsum; 5U4I; -.
PDBsum; 5U4J; -.
PDBsum; 5U9F; -.
PDBsum; 5U9G; -.
PDBsum; 5UYK; -.
PDBsum; 5UYL; -.
PDBsum; 5UYM; -.
PDBsum; 5UYN; -.
PDBsum; 5UYP; -.
PDBsum; 5UYQ; -.
DisProt; DP00145; -.
ProteinModelPortal; P0A7S3; -.
SMR; P0A7S3; -.
BioGrid; 852156; 1.
DIP; DIP-35806N; -.
IntAct; P0A7S3; 30.
STRING; 316385.ECDH10B_p2; -.
DrugBank; DB00479; Amikacin.
DrugBank; DB06696; Arbekacin.
DrugBank; DB00452; Framycetin.
DrugBank; DB00798; Gentamicin.
DrugBank; DB04729; GENTAMICIN C1A.
DrugBank; DB01172; Kanamycin.
DrugBank; DB00994; Neomycin.
DrugBank; DB00955; Netilmicin.
DrugBank; DB03615; Ribostamycin.
DrugBank; DB00919; Spectinomycin.
DrugBank; DB01082; Streptomycin.
DrugBank; DB00560; Tigecycline.
DrugBank; DB00684; Tobramycin.
iPTMnet; P0A7S3; -.
PaxDb; P0A7S3; -.
PRIDE; P0A7S3; -.
EnsemblBacteria; AAC76367; AAC76367; b3342.
EnsemblBacteria; BAE77949; BAE77949; BAE77949.
GeneID; 34154647; -.
GeneID; 947845; -.
KEGG; ecj:JW3304; -.
KEGG; eco:b3342; -.
PATRIC; fig|1411691.4.peg.3389; -.
EchoBASE; EB0904; -.
EcoGene; EG10911; rpsL.
eggNOG; COG0048; LUCA.
HOGENOM; HOG000040063; -.
InParanoid; P0A7S3; -.
KO; K02950; -.
PhylomeDB; P0A7S3; -.
BioCyc; EcoCyc:EG10911-MONOMER; -.
BioCyc; MetaCyc:EG10911-MONOMER; -.
EvolutionaryTrace; P0A7S3; -.
PRO; PR:P0A7S3; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:EcoliWiki.
GO; GO:0034336; F:misfolded RNA binding; IDA:EcoCyc.
GO; GO:0019843; F:rRNA binding; IDA:EcoCyc.
GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
GO; GO:0000372; P:Group I intron splicing; IDA:EcoCyc.
GO; GO:1990145; P:maintenance of translational fidelity; IMP:EcoCyc.
GO; GO:0033120; P:positive regulation of RNA splicing; IDA:EcoCyc.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
GO; GO:0034337; P:RNA folding; IDA:EcoCyc.
GO; GO:0006412; P:translation; IMP:EcoCyc.
CDD; cd03368; Ribosomal_S12; 1.
HAMAP; MF_00403_B; Ribosomal_S12_B; 1.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR006032; Ribosomal_S12/S23.
InterPro; IPR005679; Ribosomal_S12_bac.
PANTHER; PTHR11652; PTHR11652; 1.
Pfam; PF00164; Ribosom_S12_S23; 1.
PIRSF; PIRSF002133; Ribosomal_S12/S23; 1.
PRINTS; PR01034; RIBOSOMALS12.
SUPFAM; SSF50249; SSF50249; 1.
TIGRFAMs; TIGR00981; rpsL_bact; 1.
PROSITE; PS00055; RIBOSOMAL_S12; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Antibiotic resistance; Complete proteome;
Direct protein sequencing; Methylation; Reference proteome;
Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
tRNA-binding.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7556101}.
CHAIN 2 124 30S ribosomal protein S12.
/FTId=PRO_0000146219.
MOD_RES 89 89 3-methylthioaspartic acid.
{ECO:0000269|PubMed:8844851}.
MOD_RES 108 108 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
VARIANT 43 43 K -> R (confers streptomycin resistance
but not hyperaccurate translation).
MUTAGEN 57 57 L->H: Protein is not incorporated into
ribosomes. {ECO:0000269|PubMed:10209746}.
MUTAGEN 88 88 K->Q: Confers low-level resistance to
streptomycin and a 15% decrease in the
translational elongation rate.
{ECO:0000269|PubMed:10209746}.
HELIX 4 9 {ECO:0000244|PDB:4U26}.
TURN 24 26 {ECO:0000244|PDB:4U27}.
STRAND 30 36 {ECO:0000244|PDB:4U26}.
STRAND 37 40 {ECO:0000244|PDB:4V50}.
STRAND 43 45 {ECO:0000244|PDB:4V6C}.
STRAND 52 57 {ECO:0000244|PDB:4U26}.
TURN 58 60 {ECO:0000244|PDB:4V54}.
STRAND 62 66 {ECO:0000244|PDB:4U26}.
STRAND 69 71 {ECO:0000244|PDB:4WF1}.
STRAND 79 84 {ECO:0000244|PDB:4U26}.
STRAND 90 92 {ECO:0000244|PDB:4U27}.
STRAND 95 97 {ECO:0000244|PDB:4U26}.
STRAND 99 101 {ECO:0000244|PDB:4U1V}.
TURN 114 118 {ECO:0000244|PDB:4U26}.
SEQUENCE 124 AA; 13737 MW; 94A57F4C4FF0FC5E CRC64;
MATVNQLVRK PRARKVAKSN VPALEACPQK RGVCTRVYTT TPKKPNSALR KVCRVRLTNG
FEVTSYIGGE GHNLQEHSVI LIRGGRVKDL PGVRYHTVRG ALDCSGVKDR KQARSKYGVK
RPKA


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