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 01-MAY-2013, entry version 95.
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 277:1453-1474(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 BETA-METHYLTHIOLATION AT ASP-89.
RX PubMed=8844851;
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 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).
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).
CC -!- MASS SPECTROMETRY: Mass=13651.3; Method=MALDI; Range=2-124;
CC Source=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.
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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_000913.2.
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=28-123.
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=23-122.
DR PDB; 2GYB; EM; 15.00 A; L=23-122.
DR PDB; 2I2P; X-ray; 3.22 A; L=2-123.
DR PDB; 2I2U; X-ray; 3.22 A; L=2-123.
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; 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 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; 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 ProteinModelPortal; P0A7S3; -.
DR SMR; P0A7S3; 2-124.
DR DIP; DIP-35806N; -.
DR IntAct; P0A7S3; 26.
DR STRING; 511145.b3342; -.
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 KO; K02950; -.
DR OMA; SCPERRG; -.
DR ProtClustDB; PRK05163; -.
DR BioCyc; EcoCyc:EG10911-MONOMER; -.
DR BioCyc; ECOL316407:JW3304-MONOMER; -.
DR DrugBank; DB00479; Amikacin.
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; DB00684; Tobramycin.
DR EvolutionaryTrace; 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: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; Ribosomal_S12; 1.
DR PIRSF; PIRSF002133; Ribosomal_S12/S23; 1.
DR PRINTS; PR01034; RIBOSOMALS12.
DR SUPFAM; SSF50249; Nucleic_acid_OB; 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; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 124 30S ribosomal protein S12.
FT /FTId=PRO_0000146219.
FT MOD_RES 89 89 3-methylthioaspartic acid.
FT MOD_RES 108 108 N6-acetyllysine.
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.
FT MUTAGEN 88 88 K->Q: Confers low-level resistance to
FT streptomycin and a 15% decrease in the
FT translational elongation rate.
FT HELIX 4 9
FT TURN 24 26
FT STRAND 28 36
FT STRAND 37 40
FT STRAND 43 45
FT STRAND 50 57
FT TURN 58 60
FT STRAND 64 66
FT STRAND 69 71
FT STRAND 79 84
FT STRAND 88 90
FT STRAND 95 97
FT STRAND 99 101
FT TURN 115 118
SQ SEQUENCE 124 AA; 13737 MW; 94A57F4C4FF0FC5E CRC64;
MATVNQLVRK PRARKVAKSN VPALEACPQK RGVCTRVYTT TPKKPNSALR KVCRVRLTNG
FEVTSYIGGE GHNLQEHSVI LIRGGRVKDL PGVRYHTVRG ALDCSGVKDR KQARSKYGVK
RPKA
//
