GenomeNet

Database: UniProt
Entry: P0A7S3
LinkDB: P0A7S3
Original site: P0A7S3 
ID   RS12_ECOLI              Reviewed;         124 AA.
AC   P0A7S3; P02367; Q2M707; Q9F5N3;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   29-OCT-2014, entry version 110.
DE   RecName: Full=30S ribosomal protein S12;
GN   Name=rpsL; Synonyms=strA; OrderedLocusNames=b3342, JW3304;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-124.
RC   STRAIN=K;
RX   PubMed=320034; DOI=10.1016/0014-5793(77)80004-5;
RA   Funatsu G., Yaguchi M., Wittmann-Liebold B.;
RT   "Primary structure of protein S12 from the small Escherichia coli
RT   ribosomal subunit.";
RL   FEBS Lett. 73:12-17(1977).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=6989816;
RA   Post L.E., Nomura M.;
RT   "DNA sequences from the str operon of Escherichia coli.";
RL   J. Biol. Chem. 255:4660-4666(1980).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS STREPTOMYCIN
RP   RESISTANT.
RC   STRAIN=B/R WP2;
RX   PubMed=1552908; DOI=10.1007/BF00299141;
RA   Timms A.R., Steingrimsdottir H., Lehmann A.R., Bridges B.A.;
RT   "Mutant sequences in the rpsL gene of Escherichia coli B/r:
RT   mechanistic implications for spontaneous and ultraviolet light
RT   mutagenesis.";
RL   Mol. Gen. Genet. 232:89-96(1992).
RN   [4]
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.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT STREPTOMYCIN RESISTANT.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574, and K12 / W3110 / ZK126;
RA   Kharat A.S., Blot M.;
RT   "Nucleotide information of the rpsL150 allele of MC4100, strain of
RT   Escherichia coli.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RC   STRAIN=K12;
RX   PubMed=151587; DOI=10.1016/0092-8674(78)90096-X;
RA   Post L.E., Arfsten A.E., Reusser F., Nomura M.;
RT   "DNA sequences of promoter regions for the str and spc ribosomal
RT   protein operons in E. coli.";
RL   Cell 15:215-229(1978).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-11, AND CROSS-LINKING TO RRNA.
RC   STRAIN=MRE-600;
RX   PubMed=7556101;
RA   Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.;
RT   "Protein-rRNA binding features and their structural and functional
RT   implications in ribosomes as determined by cross-linking studies.";
RL   EMBO J. 14:4578-4588(1995).
RN   [9]
RP   EFFECT OF MUTATIONS ON RRNA FOLDING.
RC   STRAIN=UD1A1;
RX   PubMed=2477554; DOI=10.1016/0022-2836(89)90509-3;
RA   Allen P.N., Noller H.F.;
RT   "Mutations in ribosomal proteins S4 and S12 influence the higher order
RT   structure of 16 S ribosomal RNA.";
RL   J. Mol. Biol. 208:457-468(1989).
RN   [10]
RP   MUTAGENESIS OF LEU-57 AND LYS-88.
RC   STRAIN=K12;
RX   PubMed=10209746; DOI=10.1046/j.1365-2958.1999.01307.x;
RA   Toivonen J.M., Boocock M.R., Jacobs H.T.;
RT   "Modelling in Escherichia coli of mutations in mitoribosomal protein
RT   S12: novel mutant phenotypes of rpsL.";
RL   Mol. Microbiol. 31:1735-1746(1999).
RN   [11]
RP   METHYLTHIOLATION AT ASP-89.
RX   PubMed=8844851; DOI=10.1002/pro.5560050816;
RA   Kowalak J.A., Walsh K.A.;
RT   "Beta-methylthio-aspartic acid: identification of a novel
RT   posttranslational modification in ribosomal protein S12 from
RT   Escherichia coli.";
RL   Protein Sci. 5:1625-1632(1996).
RN   [12]
RP   MASS SPECTROMETRY.
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   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108, AND IDENTIFICATION BY
RP   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   [14]
RP   STRUCTURE BY ELECTRON MICROSCOPY (11 ANGSTROMS) OF KIRROMYCIN-STALLED
RP   RIBOSOMES COMPLEXED WITH EF-TU/AMINOACYL-TRNA/GTP.
RX   PubMed=12093756; DOI=10.1093/emboj/cdf326;
RA   Valle M., Sengupta J., Swami N.K., Grassucci R.A., Burkhardt N.,
RA   Nierhaus K.H., Agrawal R.K., Frank J.;
RT   "Cryo-EM reveals an active role for aminoacyl-tRNA in the
RT   accommodation process.";
RL   EMBO J. 21:3557-3567(2002).
RN   [15]
RP   STRUCTURE BY ELECTRON MICROSCOPY (13 ANGSTROMS) OF KIRROMYCIN-STALLED
RP   RIBOSOMES COMPLEXED WITH EF-TU/AMINOACYL-TRNA/GTP.
RC   STRAIN=MRE-600;
RX   PubMed=12379845; DOI=10.1038/nsb859;
RA   Stark H., Rodnina M.V., Wieden H.-J., Zemlin F., Wintermeyer W.,
RA   Van Heel M.;
RT   "Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in
RT   the codon-recognition complex.";
RL   Nat. Struct. Biol. 9:849-854(2002).
RN   [16]
RP   3D-STRUCTURE MODELING.
RX   PubMed=12244297; DOI=10.1038/nsb841;
RA   Tung C.-S., Joseph S., Sanbonmatsu K.Y.;
RT   "All-atom homology model of the Escherichia coli 30S ribosomal
RT   subunit.";
RL   Nat. Struct. Biol. 9:750-755(2002).
RN   [17]
RP   STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
RC   STRAIN=MRE-600;
RX   PubMed=12809609; DOI=10.1016/S0092-8674(03)00427-6;
RA   Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M.,
RA   Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S.,
RA   Frank J.;
RT   "Study of the structural dynamics of the E. coli 70S ribosome using
RT   real-space refinement.";
RL   Cell 113:789-801(2003).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME
RP   STRUCTURES.
RC   STRAIN=MRE-600;
RX   PubMed=16272117; DOI=10.1126/science.1117230;
RA   Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W.,
RA   Vila-Sanjurjo A., 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   [19]
RP   REVIEW ON TRANSLATIONAL ACCURACY.
RA   Kurland C.G., Hughes D., Ehrenberg M.;
RT   "Limitations of translational accuracy.";
RL   (In) Neidhardt F.C., Curtiss R. III, Ingraham J.L., Lin E.C.C.,
RL   Low K.B. Magasanik B., Reznikoff W.S., Riley M., Schaechter M.,
RL   Umbarger H.E. (eds.);
RL   Escherichia coli and Salmonella: Cellular and molecular biology (2nd
RL   ed.), pp.979-1004, American Society for Microbiology Press, Washington
RL   D.C. (1996).
CC   -!- FUNCTION: With S4 and S5 plays an important role in translational
CC       accuracy.
CC   -!- FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that
CC       are involved in tRNA selection in the A site and with the mRNA
CC       backbone. Located at the interface of the 30S and 50S subunits, it
CC       traverses the body of the 30S subunit contacting proteins on the
CC       other side and probably holding the rRNA structure together. The
CC       combined cluster of proteins S8, S12 and S17 appears to hold
CC       together the shoulder and platform of the 30S subunit (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: Cryo-EM studies suggest that S12 contacts the EF-Tu
CC       bound tRNA in the A-site during codon-recognition. This contact is
CC       most likely broken as the aminoacyl-tRNA moves into the peptidyl
CC       transferase center in the 50S subunit.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S8
CC       and S17. May interact with IF1 in the 30S initiation complex (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P0A8A8:rimP; NbExp=3; IntAct=EBI-543960, EBI-561065;
CC   -!- MASS SPECTROMETRY: Mass=13651.3; Method=MALDI; Range=2-124;
CC       Evidence={ECO:0000269|PubMed:10094780};
CC   -!- MISCELLANEOUS: At least 19 substitutions or deletions in 11 codons
CC       can promote streptomycin resistance, dependence or
CC       pseudodependence; all but one of the streptomycin resistant
CC       mutations (K42R) are associated with hyperaccurate translation and
CC       thus reduced translational efficiency.
CC   -!- MISCELLANEOUS: The streptomycin sensitive allele is dominant to
CC       resistant alleles.
CC   -!- SIMILARITY: Belongs to the ribosomal protein S12P family.
CC       {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; V00355; CAA23648.1; -; Genomic_DNA.
DR   EMBL; U18997; AAA58139.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76367.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77949.1; -; Genomic_DNA.
DR   EMBL; AF312716; AAG30936.1; -; Genomic_DNA.
DR   EMBL; AF312717; AAG30937.1; -; Genomic_DNA.
DR   EMBL; V00354; CAA23647.1; -; Genomic_DNA.
DR   EMBL; J01688; AAA50988.1; -; Genomic_DNA.
DR   PIR; S13738; R3EC12.
DR   RefSeq; NP_417801.1; NC_000913.3.
DR   RefSeq; YP_492090.1; NC_007779.1.
DR   PDB; 1M5G; Model; -; L=2-124.
DR   PDB; 1MJ1; EM; 13.00 A; O=5-123.
DR   PDB; 1P6G; EM; 12.30 A; L=2-124.
DR   PDB; 1P87; EM; 11.50 A; L=2-124.
DR   PDB; 1VS5; X-ray; 3.46 A; L=1-124.
DR   PDB; 1VS7; X-ray; 3.46 A; L=1-124.
DR   PDB; 1ZN1; EM; 14.10 A; L=28-124.
DR   PDB; 2AVY; X-ray; 3.46 A; L=2-124.
DR   PDB; 2AW7; X-ray; 3.46 A; L=2-124.
DR   PDB; 2GY9; EM; 15.00 A; L=23-123.
DR   PDB; 2GYB; EM; 15.00 A; L=23-123.
DR   PDB; 2I2P; X-ray; 3.22 A; L=2-124.
DR   PDB; 2I2U; X-ray; 3.22 A; L=2-124.
DR   PDB; 2QAL; X-ray; 3.21 A; L=2-124.
DR   PDB; 2QAN; X-ray; 3.21 A; L=2-124.
DR   PDB; 2QB9; X-ray; 3.54 A; L=2-124.
DR   PDB; 2QBB; X-ray; 3.54 A; L=2-124.
DR   PDB; 2QBD; X-ray; 3.30 A; L=2-124.
DR   PDB; 2QBF; X-ray; 3.30 A; L=2-124.
DR   PDB; 2QBH; X-ray; 4.00 A; L=2-124.
DR   PDB; 2QBJ; X-ray; 4.00 A; L=2-124.
DR   PDB; 2QOU; X-ray; 3.93 A; L=2-124.
DR   PDB; 2QOW; X-ray; 3.93 A; L=2-124.
DR   PDB; 2QOY; X-ray; 3.50 A; L=2-124.
DR   PDB; 2QP0; X-ray; 3.50 A; L=2-124.
DR   PDB; 2VHO; X-ray; 3.74 A; L=2-124.
DR   PDB; 2VHP; X-ray; 3.74 A; L=2-124.
DR   PDB; 2WWL; EM; 5.80 A; L=2-124.
DR   PDB; 2YKR; EM; 9.80 A; L=2-124.
DR   PDB; 2Z4K; X-ray; 4.45 A; L=2-124.
DR   PDB; 2Z4M; X-ray; 4.45 A; L=2-124.
DR   PDB; 3DEG; EM; -; D=2-124.
DR   PDB; 3DF1; X-ray; 3.50 A; L=2-123.
DR   PDB; 3DF3; X-ray; 3.50 A; L=2-123.
DR   PDB; 3E1A; EM; -; D=1-124.
DR   PDB; 3E1C; EM; -; D=1-124.
DR   PDB; 3EP2; EM; -; L=2-124.
DR   PDB; 3EQ3; EM; -; L=2-124.
DR   PDB; 3EQ4; EM; -; L=2-124.
DR   PDB; 3FIH; EM; 6.70 A; L=2-124.
DR   PDB; 3I1M; X-ray; 3.19 A; L=1-124.
DR   PDB; 3I1O; X-ray; 3.19 A; L=1-124.
DR   PDB; 3I1Q; X-ray; 3.81 A; L=1-124.
DR   PDB; 3I1S; X-ray; 3.81 A; L=1-124.
DR   PDB; 3I1Z; X-ray; 3.71 A; L=1-124.
DR   PDB; 3I21; X-ray; 3.71 A; L=1-124.
DR   PDB; 3IZV; EM; -; P=1-124.
DR   PDB; 3IZW; EM; -; P=1-124.
DR   PDB; 3J00; EM; -; L=2-124.
DR   PDB; 3J0D; EM; 11.10 A; I=2-124.
DR   PDB; 3J0E; EM; 9.90 A; F=2-124.
DR   PDB; 3J0U; EM; 12.10 A; O=2-124.
DR   PDB; 3J0V; EM; 14.70 A; O=2-124.
DR   PDB; 3J0X; EM; 13.50 A; O=2-124.
DR   PDB; 3J0Z; EM; 11.50 A; O=2-124.
DR   PDB; 3J10; EM; 11.50 A; O=2-124.
DR   PDB; 3J13; EM; 13.10 A; N=2-124.
DR   PDB; 3J18; EM; 8.30 A; L=2-124.
DR   PDB; 3J36; EM; 9.80 A; L=2-124.
DR   PDB; 3J4V; EM; 12.00 A; L=1-124.
DR   PDB; 3J4W; EM; 12.00 A; L=1-124.
DR   PDB; 3J4Y; EM; 17.00 A; L=1-124.
DR   PDB; 3J4Z; EM; 20.00 A; L=1-124.
DR   PDB; 3J53; EM; 13.00 A; L=1-124.
DR   PDB; 3J55; EM; 15.00 A; L=1-124.
DR   PDB; 3J57; EM; 17.00 A; L=1-124.
DR   PDB; 3J59; EM; 12.00 A; L=1-124.
DR   PDB; 3J5B; EM; 17.00 A; L=1-124.
DR   PDB; 3J5D; EM; 17.00 A; L=1-124.
DR   PDB; 3J5F; EM; 20.00 A; L=1-124.
DR   PDB; 3J5H; EM; 15.00 A; L=1-124.
DR   PDB; 3J5J; EM; 9.00 A; L=1-124.
DR   PDB; 3J5N; EM; 6.80 A; L=1-124.
DR   PDB; 3J5T; EM; 7.60 A; L=2-124.
DR   PDB; 3J5X; EM; 7.60 A; L=2-124.
DR   PDB; 3KC4; EM; -; L=1-124.
DR   PDB; 3OAQ; X-ray; 3.25 A; L=2-124.
DR   PDB; 3OAR; X-ray; 3.25 A; L=2-124.
DR   PDB; 3OFA; X-ray; 3.19 A; L=2-124.
DR   PDB; 3OFB; X-ray; 3.19 A; L=2-124.
DR   PDB; 3OFO; X-ray; 3.10 A; L=2-124.
DR   PDB; 3OFP; X-ray; 3.10 A; L=2-124.
DR   PDB; 3OFX; X-ray; 3.29 A; L=2-124.
DR   PDB; 3OFY; X-ray; 3.29 A; L=2-124.
DR   PDB; 3OR9; X-ray; 3.30 A; L=1-124.
DR   PDB; 3ORA; X-ray; 3.30 A; L=1-124.
DR   PDB; 3SFS; X-ray; 3.20 A; L=1-124.
DR   PDB; 3UOQ; X-ray; 3.70 A; L=1-124.
DR   PDB; 4A2I; EM; 16.50 A; L=2-124.
DR   PDB; 4ADV; EM; 13.50 A; L=2-124.
DR   PDB; 4GAQ; X-ray; 3.30 A; L=1-124.
DR   PDB; 4GAS; X-ray; 3.30 A; L=1-124.
DR   PDB; 4GD1; X-ray; 3.00 A; L=2-124.
DR   PDB; 4GD2; X-ray; 3.00 A; L=2-124.
DR   PDB; 4KIY; X-ray; 2.90 A; L=1-124.
DR   PDB; 4KJ0; X-ray; 2.90 A; L=1-124.
DR   PDB; 4KJ2; X-ray; 2.90 A; L=1-124.
DR   PDB; 4KJ4; X-ray; 2.90 A; L=1-124.
DR   PDB; 4KJ6; X-ray; 2.90 A; L=1-124.
DR   PDB; 4KJ8; X-ray; 2.90 A; L=1-124.
DR   PDB; 4KJA; X-ray; 2.90 A; L=1-124.
DR   PDB; 4KJC; X-ray; 2.90 A; L=1-124.
DR   PDB; 4PE9; X-ray; 2.95 A; L=2-124.
DR   PDB; 4PEA; X-ray; 2.95 A; L=2-124.
DR   PDB; 4TOL; X-ray; 3.00 A; L=2-124.
DR   PDB; 4TON; X-ray; 3.00 A; L=2-124.
DR   PDB; 4TOU; X-ray; 2.90 A; L=2-124.
DR   PDB; 4TOW; X-ray; 2.90 A; L=2-124.
DR   PDB; 4TP0; X-ray; 2.90 A; L=2-124.
DR   PDB; 4TP2; X-ray; 2.90 A; L=2-124.
DR   PDB; 4TP4; X-ray; 2.90 A; L=2-124.
DR   PDB; 4TP6; X-ray; 2.90 A; L=2-124.
DR   PDB; 4TP8; X-ray; 2.80 A; L=2-124.
DR   PDB; 4TPA; X-ray; 2.80 A; L=2-124.
DR   PDB; 4TPC; X-ray; 2.80 A; L=2-124.
DR   PDB; 4TPE; X-ray; 2.80 A; L=2-124.
DR   PDBsum; 1M5G; -.
DR   PDBsum; 1MJ1; -.
DR   PDBsum; 1P6G; -.
DR   PDBsum; 1P87; -.
DR   PDBsum; 1VS5; -.
DR   PDBsum; 1VS7; -.
DR   PDBsum; 1ZN1; -.
DR   PDBsum; 2AVY; -.
DR   PDBsum; 2AW7; -.
DR   PDBsum; 2GY9; -.
DR   PDBsum; 2GYB; -.
DR   PDBsum; 2I2P; -.
DR   PDBsum; 2I2U; -.
DR   PDBsum; 2QAL; -.
DR   PDBsum; 2QAN; -.
DR   PDBsum; 2QB9; -.
DR   PDBsum; 2QBB; -.
DR   PDBsum; 2QBD; -.
DR   PDBsum; 2QBF; -.
DR   PDBsum; 2QBH; -.
DR   PDBsum; 2QBJ; -.
DR   PDBsum; 2QOU; -.
DR   PDBsum; 2QOW; -.
DR   PDBsum; 2QOY; -.
DR   PDBsum; 2QP0; -.
DR   PDBsum; 2VHO; -.
DR   PDBsum; 2VHP; -.
DR   PDBsum; 2WWL; -.
DR   PDBsum; 2YKR; -.
DR   PDBsum; 2Z4K; -.
DR   PDBsum; 2Z4M; -.
DR   PDBsum; 3DEG; -.
DR   PDBsum; 3DF1; -.
DR   PDBsum; 3DF3; -.
DR   PDBsum; 3E1A; -.
DR   PDBsum; 3E1C; -.
DR   PDBsum; 3EP2; -.
DR   PDBsum; 3EQ3; -.
DR   PDBsum; 3EQ4; -.
DR   PDBsum; 3FIH; -.
DR   PDBsum; 3I1M; -.
DR   PDBsum; 3I1O; -.
DR   PDBsum; 3I1Q; -.
DR   PDBsum; 3I1S; -.
DR   PDBsum; 3I1Z; -.
DR   PDBsum; 3I21; -.
DR   PDBsum; 3IZV; -.
DR   PDBsum; 3IZW; -.
DR   PDBsum; 3J00; -.
DR   PDBsum; 3J0D; -.
DR   PDBsum; 3J0E; -.
DR   PDBsum; 3J0U; -.
DR   PDBsum; 3J0V; -.
DR   PDBsum; 3J0X; -.
DR   PDBsum; 3J0Z; -.
DR   PDBsum; 3J10; -.
DR   PDBsum; 3J13; -.
DR   PDBsum; 3J18; -.
DR   PDBsum; 3J36; -.
DR   PDBsum; 3J4V; -.
DR   PDBsum; 3J4W; -.
DR   PDBsum; 3J4Y; -.
DR   PDBsum; 3J4Z; -.
DR   PDBsum; 3J53; -.
DR   PDBsum; 3J55; -.
DR   PDBsum; 3J57; -.
DR   PDBsum; 3J59; -.
DR   PDBsum; 3J5B; -.
DR   PDBsum; 3J5D; -.
DR   PDBsum; 3J5F; -.
DR   PDBsum; 3J5H; -.
DR   PDBsum; 3J5J; -.
DR   PDBsum; 3J5N; -.
DR   PDBsum; 3J5T; -.
DR   PDBsum; 3J5X; -.
DR   PDBsum; 3KC4; -.
DR   PDBsum; 3OAQ; -.
DR   PDBsum; 3OAR; -.
DR   PDBsum; 3OFA; -.
DR   PDBsum; 3OFB; -.
DR   PDBsum; 3OFO; -.
DR   PDBsum; 3OFP; -.
DR   PDBsum; 3OFX; -.
DR   PDBsum; 3OFY; -.
DR   PDBsum; 3OR9; -.
DR   PDBsum; 3ORA; -.
DR   PDBsum; 3SFS; -.
DR   PDBsum; 3UOQ; -.
DR   PDBsum; 4A2I; -.
DR   PDBsum; 4ADV; -.
DR   PDBsum; 4GAQ; -.
DR   PDBsum; 4GAS; -.
DR   PDBsum; 4GD1; -.
DR   PDBsum; 4GD2; -.
DR   PDBsum; 4KIY; -.
DR   PDBsum; 4KJ0; -.
DR   PDBsum; 4KJ2; -.
DR   PDBsum; 4KJ4; -.
DR   PDBsum; 4KJ6; -.
DR   PDBsum; 4KJ8; -.
DR   PDBsum; 4KJA; -.
DR   PDBsum; 4KJC; -.
DR   PDBsum; 4PE9; -.
DR   PDBsum; 4PEA; -.
DR   PDBsum; 4TOL; -.
DR   PDBsum; 4TON; -.
DR   PDBsum; 4TOU; -.
DR   PDBsum; 4TOW; -.
DR   PDBsum; 4TP0; -.
DR   PDBsum; 4TP2; -.
DR   PDBsum; 4TP4; -.
DR   PDBsum; 4TP6; -.
DR   PDBsum; 4TP8; -.
DR   PDBsum; 4TPA; -.
DR   PDBsum; 4TPC; -.
DR   PDBsum; 4TPE; -.
DR   DisProt; DP00145; -.
DR   ProteinModelPortal; P0A7S3; -.
DR   SMR; P0A7S3; 2-124.
DR   BioGrid; 852156; 1.
DR   DIP; DIP-35806N; -.
DR   IntAct; P0A7S3; 27.
DR   STRING; 511145.b3342; -.
DR   ChEMBL; CHEMBL2363135; -.
DR   DrugBank; DB00479; Amikacin.
DR   DrugBank; DB06696; Arbekacin.
DR   DrugBank; DB00452; Framycetin.
DR   DrugBank; DB00798; Gentamicin.
DR   DrugBank; DB01172; Kanamycin.
DR   DrugBank; DB00994; Neomycin.
DR   DrugBank; DB00955; Netilmicin.
DR   DrugBank; DB00919; Spectinomycin.
DR   DrugBank; DB01082; Streptomycin.
DR   DrugBank; DB00560; Tigecycline.
DR   DrugBank; DB00684; Tobramycin.
DR   PaxDb; P0A7S3; -.
DR   PRIDE; P0A7S3; -.
DR   EnsemblBacteria; AAC76367; AAC76367; b3342.
DR   EnsemblBacteria; BAE77949; BAE77949; BAE77949.
DR   GeneID; 12932620; -.
DR   GeneID; 947845; -.
DR   KEGG; ecj:Y75_p3834; -.
DR   KEGG; eco:b3342; -.
DR   PATRIC; 32122116; VBIEscCol129921_3435.
DR   EchoBASE; EB0904; -.
DR   EcoGene; EG10911; rpsL.
DR   eggNOG; COG0048; -.
DR   HOGENOM; HOG000040063; -.
DR   InParanoid; P0A7S3; -.
DR   KO; K02950; -.
DR   OMA; CYQRKGV; -.
DR   OrthoDB; EOG61ZTNF; -.
DR   PhylomeDB; P0A7S3; -.
DR   BioCyc; EcoCyc:EG10911-MONOMER; -.
DR   BioCyc; ECOL316407:JW3304-MONOMER; -.
DR   EvolutionaryTrace; P0A7S3; -.
DR   PRO; PR:P0A7S3; -.
DR   Genevestigator; P0A7S3; -.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:EcoCyc.
DR   GO; GO:0034336; F:misfolded RNA binding; IDA:EcoCyc.
DR   GO; GO:0019843; F:rRNA binding; IDA:EcoCyc.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000372; P:Group I intron splicing; IDA:EcoCyc.
DR   GO; GO:0033120; P:positive regulation of RNA splicing; IDA:EcoCyc.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:0034337; P:RNA folding; IDA:EcoCyc.
DR   GO; GO:0006412; P:translation; IMP:EcoCyc.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00403_B; Ribosomal_S12_B; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR006032; Ribosomal_S12/S23.
DR   InterPro; IPR005679; Ribosomal_S12_bac.
DR   PANTHER; PTHR11652; PTHR11652; 1.
DR   Pfam; PF00164; Ribosom_S12_S23; 1.
DR   PIRSF; PIRSF002133; Ribosomal_S12/S23; 1.
DR   PRINTS; PR01034; RIBOSOMALS12.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00981; rpsL_bact; 1.
DR   PROSITE; PS00055; RIBOSOMAL_S12; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Antibiotic resistance; Complete proteome;
KW   Direct protein sequencing; Methylation; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW   tRNA-binding.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:7556101}.
FT   CHAIN         2    124       30S ribosomal protein S12.
FT                                /FTId=PRO_0000146219.
FT   MOD_RES      89     89       3-methylthioaspartic acid.
FT                                {ECO:0000269|PubMed:8844851}.
FT   MOD_RES     108    108       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:18723842}.
FT   VARIANT      43     43       K -> R (confers streptomycin resistance
FT                                but not hyperaccurate translation).
FT   MUTAGEN      57     57       L->H: Protein is not incorporated into
FT                                ribosomes. {ECO:0000269|PubMed:10209746}.
FT   MUTAGEN      88     88       K->Q: Confers low-level resistance to
FT                                streptomycin and a 15% decrease in the
FT                                translational elongation rate.
FT                                {ECO:0000269|PubMed:10209746}.
FT   HELIX         4      9
FT   TURN         24     26
FT   STRAND       30     32
FT   STRAND       36     40
FT   STRAND       43     45
FT   STRAND       50     57
FT   TURN         58     60
FT   STRAND       62     66
FT   STRAND       69     71
FT   STRAND       80     82
FT   STRAND       88     90
FT   STRAND       95     97
FT   STRAND       99    101
FT   TURN        114    118
SQ   SEQUENCE   124 AA;  13737 MW;  94A57F4C4FF0FC5E CRC64;
     MATVNQLVRK PRARKVAKSN VPALEACPQK RGVCTRVYTT TPKKPNSALR KVCRVRLTNG
     FEVTSYIGGE GHNLQEHSVI LIRGGRVKDL PGVRYHTVRG ALDCSGVKDR KQARSKYGVK
     RPKA
//
DBGET integrated database retrieval system