RS12_ECOLI
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 03-AUG-2022, entry version 170.
DE RecName: Full=30S ribosomal protein S12;
DE AltName: Full=Small ribosomal subunit protein uS12 {ECO:0000303|PubMed:24524803};
GN Name=rpsL; Synonyms=strA; OrderedLocusNames=b3342, JW3304;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-124, AND SUBUNIT.
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 ribosomal
RT subunit.";
RL FEBS Lett. 73:12-17(1977).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6989816; DOI=10.1016/s0021-9258(19)85545-x;
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 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: mechanistic
RT implications for spontaneous and ultraviolet light 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., Mau B.,
RA 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 MG1655
RT 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 protein
RT operons in E. coli.";
RL Cell 15:215-229(1978).
RN [8]
RP PROTEIN SEQUENCE OF 2-11, CROSS-LINKING TO RRNA, AND SUBUNIT.
RC STRAIN=MRE-600;
RX PubMed=7556101; DOI=10.1002/j.1460-2075.1995.tb00137.x;
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 S12:
RT 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 posttranslational
RT modification in ribosomal protein S12 from Escherichia coli.";
RL Protein Sci. 5:1625-1632(1996).
RN [12]
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108, 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 [14]
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 ed.),
RL pp.979-1004, American Society for Microbiology Press, Washington D.C.
RL (1996).
RN [15]
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 [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (11 ANGSTROMS) OF KIRROMYCIN-STALLED
RP RIBOSOMES COMPLEXED WITH EF-TU/AMINOACYL-TRNA/GTP, AND SUBUNIT.
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 accommodation
RT process.";
RL EMBO J. 21:3557-3567(2002).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (13 ANGSTROMS) OF KIRROMYCIN-STALLED
RP RIBOSOMES COMPLEXED WITH EF-TU/AMINOACYL-TRNA/GTP, AND SUBUNIT.
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 the
RT codon-recognition complex.";
RL Nat. Struct. Biol. 9:849-854(2002).
RN [18]
RP 3D-STRUCTURE MODELING, AND SUBUNIT.
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 subunit.";
RL Nat. Struct. Biol. 9:750-755(2002).
RN [19]
RP STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS), AND SUBUNIT.
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., Frank J.;
RT "Study of the structural dynamics of the E. coli 70S ribosome using real-
RT space refinement.";
RL Cell 113:789-801(2003).
RN [20]
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 [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX
RP WITH ARFA AND RF2, INTERACTION WITH ARFA, 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 [22] {ECO:0007744|PDB:5MGP}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 2-124 OF 70S RIBOSOME
RP IN COMPLEX WITH ARFA AND RF2, INTERACTION WITH 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 [23]
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 [24]
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: With S4 and S5 plays an important role in translational
CC accuracy.
CC -!- FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that are
CC involved in tRNA selection in the A site and with the mRNA backbone.
CC Located at the interface of the 30S and 50S subunits, it traverses the
CC body of the 30S subunit contacting proteins on the other side and
CC probably holding the rRNA structure together. The combined cluster of
CC proteins S8, S12 and S17 appears to hold together the shoulder and
CC platform of the 30S subunit (By similarity).
CC {ECO:0000250|UniProtKB:Q5SHN3, ECO:0000269|PubMed:7556101}.
CC -!- FUNCTION: Cryo-EM studies suggest that S12 contacts the EF-Tu bound
CC tRNA in the A-site during codon-recognition. This contact is most
CC likely broken as the aminoacyl-tRNA moves into the peptidyl transferase
CC center in the 50S subunit. {ECO:0000305|PubMed:12093756}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit (PubMed:320034,
CC PubMed:7556101, PubMed:12809609, PubMed:16272117, PubMed:27934701,
CC PubMed:10094780, PubMed:12093756, PubMed:12379845, PubMed:12244297,
CC PubMed:27906160, PubMed:27906161). Contacts proteins S8 and S17.
CC Interacts with ArfA (PubMed:27906160, PubMed:27906161). May interact
CC with IF1 in the 30S initiation complex (By similarity).
CC {ECO:0000250|UniProtKB:Q5SHN3, ECO:0000269|PubMed:10094780,
CC ECO:0000269|PubMed:12093756, ECO:0000269|PubMed:12244297,
CC ECO:0000269|PubMed:12379845, ECO:0000269|PubMed:12809609,
CC ECO:0000269|PubMed:16272117, ECO:0000269|PubMed:27906160,
CC ECO:0000269|PubMed:27906161, ECO:0000269|PubMed:27934701,
CC ECO:0000269|PubMed:320034, ECO:0000269|PubMed:7556101}.
CC -!- INTERACTION:
CC P0A7S3; P0A8A8: rimP; NbExp=3; IntAct=EBI-543960, EBI-561065;
CC -!- MASS SPECTROMETRY: Mass=13651.3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10094780};
CC -!- MISCELLANEOUS: At least 19 substitutions or deletions in 11 codons can
CC promote streptomycin resistance, dependence or pseudodependence; all
CC but one of the streptomycin resistant mutations (K42R) are associated
CC with hyperaccurate translation and thus reduced translational
CC efficiency. {ECO:0000269|PubMed:1552908, ECO:0000269|Ref.5}.
CC -!- MISCELLANEOUS: The streptomycin sensitive allele is dominant to
CC resistant alleles.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS12 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) 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; WP_000246815.1; NZ_STEB01000004.1.
DR PDB; 1MJ1; EM; 13.00 A; O=5-123.
DR PDB; 1ZN1; EM; 14.10 A; L=28-124.
DR PDB; 2YKR; EM; 9.80 A; L=2-124.
DR PDB; 3DEG; EM; -; D=2-124.
DR PDB; 3EP2; EM; -; L=2-124.
DR PDB; 3EQ3; EM; -; L=2-124.
DR PDB; 3EQ4; EM; -; L=2-124.
DR PDB; 3IY8; EM; 14.10 A; 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; 3J9Y; EM; 3.90 A; l=1-124.
DR PDB; 3J9Z; EM; 3.60 A; SL=2-124.
DR PDB; 3JA1; EM; 3.60 A; SL=2-124.
DR PDB; 3JBU; EM; 3.64 A; L=1-124.
DR PDB; 3JBV; EM; 3.32 A; L=1-124.
DR PDB; 3JCD; EM; 3.70 A; l=1-124.
DR PDB; 3JCE; EM; 3.20 A; l=1-124.
DR PDB; 3JCJ; EM; 3.70 A; t=1-124.
DR PDB; 3JCN; EM; 4.60 A; o=1-124.
DR PDB; 4A2I; EM; 16.50 A; L=2-124.
DR PDB; 4ADV; EM; 13.50 A; L=2-124.
DR PDB; 4U1U; X-ray; 2.95 A; AL/CL=2-124.
DR PDB; 4U1V; X-ray; 3.00 A; AL/CL=2-124.
DR PDB; 4U20; X-ray; 2.90 A; AL/CL=2-124.
DR PDB; 4U24; X-ray; 2.90 A; AL/CL=2-124.
DR PDB; 4U25; X-ray; 2.90 A; AL/CL=2-124.
DR PDB; 4U26; X-ray; 2.80 A; AL/CL=2-124.
DR PDB; 4U27; X-ray; 2.80 A; AL/CL=2-124.
DR PDB; 4V47; EM; 12.30 A; BL=2-124.
DR PDB; 4V48; EM; 11.50 A; BL=2-124.
DR PDB; 4V4H; X-ray; 3.46 A; AL/CL=1-124.
DR PDB; 4V4Q; X-ray; 3.46 A; AL/CL=2-124.
DR PDB; 4V4V; EM; 15.00 A; AL=23-123.
DR PDB; 4V4W; EM; 15.00 A; AL=23-123.
DR PDB; 4V50; X-ray; 3.22 A; AL/CL=2-124.
DR PDB; 4V52; X-ray; 3.21 A; AL/CL=2-124.
DR PDB; 4V53; X-ray; 3.54 A; AL/CL=2-124.
DR PDB; 4V54; X-ray; 3.30 A; AL/CL=2-124.
DR PDB; 4V55; X-ray; 4.00 A; AL/CL=2-124.
DR PDB; 4V56; X-ray; 3.93 A; AL/CL=2-124.
DR PDB; 4V57; X-ray; 3.50 A; AL/CL=2-124.
DR PDB; 4V5B; X-ray; 3.74 A; BL/DL=2-124.
DR PDB; 4V5H; EM; 5.80 A; AL=2-124.
DR PDB; 4V5Y; X-ray; 4.45 A; AL/CL=2-124.
DR PDB; 4V64; X-ray; 3.50 A; AL/CL=2-124.
DR PDB; 4V65; EM; 9.00 A; AD=1-124.
DR PDB; 4V66; EM; 9.00 A; AD=1-124.
DR PDB; 4V69; EM; 6.70 A; AL=2-124.
DR PDB; 4V6C; X-ray; 3.19 A; AL/CL=1-124.
DR PDB; 4V6D; X-ray; 3.81 A; AL/CL=1-124.
DR PDB; 4V6E; X-ray; 3.71 A; AL/CL=1-124.
DR PDB; 4V6K; EM; 8.25 A; BP=1-124.
DR PDB; 4V6L; EM; 13.20 A; AP=1-124.
DR PDB; 4V6M; EM; 7.10 A; AL=2-124, AO=2-89.
DR PDB; 4V6N; EM; 12.10 A; BO=2-124.
DR PDB; 4V6O; EM; 14.70 A; AO=2-124.
DR PDB; 4V6P; EM; 13.50 A; AO=2-124.
DR PDB; 4V6Q; EM; 11.50 A; AO=2-124.
DR PDB; 4V6R; EM; 11.50 A; AO=2-124.
DR PDB; 4V6S; EM; 13.10 A; BN=2-124.
DR PDB; 4V6T; EM; 8.30 A; AL=2-124.
DR PDB; 4V6V; EM; 9.80 A; AL=2-124.
DR PDB; 4V6Y; EM; 12.00 A; AL=1-124.
DR PDB; 4V6Z; EM; 12.00 A; AL=1-124.
DR PDB; 4V70; EM; 17.00 A; AL=1-124.
DR PDB; 4V71; EM; 20.00 A; AL=1-124.
DR PDB; 4V72; EM; 13.00 A; AL=1-124.
DR PDB; 4V73; EM; 15.00 A; AL=1-124.
DR PDB; 4V74; EM; 17.00 A; AL=1-124.
DR PDB; 4V75; EM; 12.00 A; AL=1-124.
DR PDB; 4V76; EM; 17.00 A; AL=1-124.
DR PDB; 4V77; EM; 17.00 A; AL=1-124.
DR PDB; 4V78; EM; 20.00 A; AL=1-124.
DR PDB; 4V79; EM; 15.00 A; AL=1-124.
DR PDB; 4V7A; EM; 9.00 A; AL=1-124.
DR PDB; 4V7B; EM; 6.80 A; AL=1-124.
DR PDB; 4V7C; EM; 7.60 A; AL=2-124.
DR PDB; 4V7D; EM; 7.60 A; BL=2-124.
DR PDB; 4V7I; EM; 9.60 A; BL=1-124.
DR PDB; 4V7S; X-ray; 3.25 A; AL/CL=2-124.
DR PDB; 4V7T; X-ray; 3.19 A; AL/CL=2-124.
DR PDB; 4V7U; X-ray; 3.10 A; AL/CL=2-124.
DR PDB; 4V7V; X-ray; 3.29 A; AL/CL=2-124.
DR PDB; 4V85; X-ray; 3.20 A; AL=1-124.
DR PDB; 4V89; X-ray; 3.70 A; AL=1-124.
DR PDB; 4V9C; X-ray; 3.30 A; AL/CL=1-124.
DR PDB; 4V9D; X-ray; 3.00 A; AL/BL=2-124.
DR PDB; 4V9O; X-ray; 2.90 A; BL/DL/FL/HL=1-124.
DR PDB; 4V9P; X-ray; 2.90 A; BL/DL/FL/HL=1-124.
DR PDB; 4WF1; X-ray; 3.09 A; AL/CL=2-124.
DR PDB; 4WOI; X-ray; 3.00 A; AL/DL=1-124.
DR PDB; 4WWW; X-ray; 3.10 A; QL/XL=2-124.
DR PDB; 4YBB; X-ray; 2.10 A; AL/BL=2-124.
DR PDB; 5AFI; EM; 2.90 A; l=1-124.
DR PDB; 5H5U; EM; 3.00 A; s=2-124.
DR PDB; 5IQR; EM; 3.00 A; q=1-124.
DR PDB; 5IT8; X-ray; 3.12 A; AL/BL=2-124.
DR PDB; 5J5B; X-ray; 2.80 A; AL/BL=2-124.
DR PDB; 5J7L; X-ray; 3.00 A; AL/BL=2-124.
DR PDB; 5J88; X-ray; 3.32 A; AL/BL=2-124.
DR PDB; 5J8A; X-ray; 3.10 A; AL/BL=2-124.
DR PDB; 5J91; X-ray; 2.96 A; AL/BL=2-124.
DR PDB; 5JC9; X-ray; 3.03 A; AL/BL=2-124.
DR PDB; 5JTE; EM; 3.60 A; AL=1-124.
DR PDB; 5JU8; EM; 3.60 A; AL=1-124.
DR PDB; 5KCR; EM; 3.60 A; 1l=1-124.
DR PDB; 5KCS; EM; 3.90 A; 1l=1-124.
DR PDB; 5KPS; EM; 3.90 A; 17=1-124.
DR PDB; 5KPV; EM; 4.10 A; 16=1-124.
DR PDB; 5KPW; EM; 3.90 A; 16=1-124.
DR PDB; 5KPX; EM; 3.90 A; 16=1-124.
DR PDB; 5L3P; EM; 3.70 A; l=1-124.
DR PDB; 5LZA; EM; 3.60 A; l=2-124.
DR PDB; 5LZB; EM; 5.30 A; l=2-124.
DR PDB; 5LZC; EM; 4.80 A; l=2-124.
DR PDB; 5LZD; EM; 3.40 A; l=2-124.
DR PDB; 5LZE; EM; 3.50 A; l=2-124.
DR PDB; 5LZF; EM; 4.60 A; l=2-124.
DR PDB; 5MDV; EM; 2.97 A; q=1-124.
DR PDB; 5MDW; EM; 3.06 A; q=1-124.
DR PDB; 5MDY; EM; 3.35 A; q=1-124.
DR PDB; 5MDZ; EM; 3.10 A; q=1-124.
DR PDB; 5ME0; EM; 13.50 A; L=2-124.
DR PDB; 5ME1; EM; 13.50 A; L=2-124.
DR PDB; 5MGP; EM; 3.10 A; l=2-124.
DR PDB; 5MY1; EM; 7.60 A; L=2-124.
DR PDB; 5NO2; EM; 5.16 A; L=2-15.
DR PDB; 5NO3; EM; 5.16 A; L=2-15.
DR PDB; 5NO4; EM; 5.16 A; L=2-15.
DR PDB; 5NP6; EM; 3.60 A; O=2-124.
DR PDB; 5NWY; EM; 2.93 A; B=1-124.
DR PDB; 5O2R; EM; 3.40 A; l=2-124.
DR PDB; 5U4I; EM; 3.50 A; l=2-124.
DR PDB; 5U4J; EM; 3.70 A; l=1-124.
DR PDB; 5U9F; EM; 3.20 A; L=1-124.
DR PDB; 5U9G; EM; 3.20 A; L=1-124.
DR PDB; 5UYK; EM; 3.90 A; L=2-124.
DR PDB; 5UYL; EM; 3.60 A; L=2-124.
DR PDB; 5UYM; EM; 3.20 A; L=2-124.
DR PDB; 5UYN; EM; 4.00 A; L=2-124.
DR PDB; 5UYP; EM; 3.90 A; L=2-124.
DR PDB; 5UYQ; EM; 3.80 A; L=2-124.
DR PDB; 5WDT; EM; 3.00 A; l=2-122.
DR PDB; 5WE4; EM; 3.10 A; l=2-122.
DR PDB; 5WE6; EM; 3.40 A; l=2-122.
DR PDB; 5WFK; EM; 3.40 A; l=2-122.
DR PDB; 6BU8; EM; 3.50 A; L=2-124.
DR PDB; 6BY1; X-ray; 3.94 A; AL/BL=2-124.
DR PDB; 6C4I; EM; 3.24 A; l=1-124.
DR PDB; 6ENF; EM; 3.20 A; l=2-124.
DR PDB; 6ENJ; EM; 3.70 A; l=2-124.
DR PDB; 6ENU; EM; 3.10 A; l=2-124.
DR PDB; 6GWT; EM; 3.80 A; l=2-124.
DR PDB; 6GXM; EM; 3.80 A; l=2-124.
DR PDB; 6GXN; EM; 3.90 A; l=2-124.
DR PDB; 6GXO; EM; 3.90 A; l=2-124.
DR PDB; 6GXP; EM; 4.40 A; l=2-124.
DR PDB; 6H4N; EM; 3.00 A; l=2-124.
DR PDB; 6H58; EM; 7.90 A; l/ll=2-124.
DR PDB; 6HRM; EM; 2.96 A; q=2-124.
DR PDB; 6I7V; X-ray; 2.90 A; AL/BL=2-124.
DR PDB; 6O9J; EM; 3.90 A; l=2-124.
DR PDB; 6O9K; EM; 4.00 A; l=2-124.
DR PDB; 6OFX; EM; 3.30 A; Q=2-124.
DR PDB; 6OG7; EM; 3.30 A; Q=2-124.
DR PDB; 6ORE; EM; 2.90 A; q=2-124.
DR PDB; 6ORL; EM; 3.50 A; q=2-124.
DR PDB; 6OST; EM; 4.20 A; q=2-124.
DR PDB; 6OT3; EM; 3.90 A; q=2-88.
DR PDB; 6OUO; EM; 3.70 A; q=2-88.
DR PDB; 6Q9A; EM; 3.70 A; q=2-123.
DR PDB; 6SZS; EM; 3.06 A; l=1-124.
DR PDB; 6TBV; EM; 2.70 A; S121=1-124.
DR PDB; 6TC3; EM; 2.70 A; S121=1-124.
DR PDB; 6VWL; EM; 3.10 A; k=1-124.
DR PDB; 6VWM; EM; 3.40 A; k=1-124.
DR PDB; 6VWN; EM; 3.40 A; k=1-124.
DR PDB; 6W6K; EM; 3.60 A; L=1-124.
DR PDB; 6W77; EM; 3.60 A; L=1-124.
DR PDB; 6W7M; EM; 3.80 A; L=1-124.
DR PDB; 6W7N; EM; 3.40 A; L=1-124.
DR PDB; 6W7W; EM; 3.90 A; K=1-124.
DR PDB; 6WD6; EM; 3.70 A; Q=2-124.
DR PDB; 6WDB; EM; 4.00 A; Q=2-124.
DR PDB; 6WDC; EM; 4.20 A; Q=2-124.
DR PDB; 6WDD; EM; 3.20 A; Q=2-124.
DR PDB; 6WDE; EM; 3.00 A; Q=2-124.
DR PDB; 6WDF; EM; 3.30 A; Q=2-124.
DR PDB; 6WDG; EM; 3.30 A; Q=2-124.
DR PDB; 6WDH; EM; 4.30 A; Q=2-124.
DR PDB; 6WDI; EM; 4.00 A; Q=2-124.
DR PDB; 6WDJ; EM; 3.70 A; Q=2-124.
DR PDB; 6WDK; EM; 3.60 A; Q=2-124.
DR PDB; 6WDL; EM; 3.70 A; Q=2-124.
DR PDB; 6WDM; EM; 3.60 A; Q=2-124.
DR PDB; 6WNV; EM; 3.50 A; Q=2-124.
DR PDB; 6WNW; EM; 3.20 A; Q=2-124.
DR PDB; 6XE0; EM; 6.80 A; K=2-124.
DR PDB; 6XZA; EM; 2.66 A; L1=2-124.
DR PDB; 6XZB; EM; 2.54 A; L1=2-124.
DR PDB; 6Y69; EM; 2.86 A; l=2-124.
DR PDB; 6ZTL; EM; 3.50 A; AL=1-124.
DR PDB; 7ABZ; EM; 3.21 A; q=2-124.
DR PDB; 7AC7; EM; 3.08 A; q=2-124.
DR PDB; 7ACJ; EM; 3.20 A; q=2-123.
DR PDB; 7ACR; EM; 3.44 A; q=2-123.
DR PDB; 7AFI; EM; 3.53 A; L=1-124.
DR PDB; 7AFL; EM; 4.20 A; L=1-124.
DR PDB; 7AFO; EM; 3.93 A; L=1-124.
DR PDB; 7B5K; EM; 2.90 A; l=2-124.
DR PDB; 7BOD; EM; 2.88 A; L=1-124.
DR PDB; 7BOE; EM; 2.90 A; L=1-124.
DR PDB; 7BOF; EM; 2.92 A; L=1-124.
DR PDB; 7BOG; EM; 2.75 A; L=1-124.
DR PDB; 7BOH; EM; 2.82 A; L=1-124.
DR PDB; 7BOI; EM; 2.98 A; L=1-124.
DR PDB; 7D6Z; EM; 3.40 A; s=1-124.
DR PDB; 7D80; EM; 4.10 A; M=1-124.
DR PDB; 7JSS; EM; 3.70 A; Q=2-124.
DR PDB; 7JSW; EM; 3.80 A; Q=2-124.
DR PDB; 7JSZ; EM; 3.70 A; Q=2-124.
DR PDB; 7JT1; EM; 3.30 A; Q=2-124.
DR PDB; 7JT2; EM; 3.50 A; Q=2-124.
DR PDB; 7JT3; EM; 3.70 A; Q=2-124.
DR PDB; 7K50; EM; 3.40 A; Q=2-124.
DR PDB; 7K51; EM; 3.50 A; Q=2-124.
DR PDB; 7K52; EM; 3.40 A; Q=2-124.
DR PDB; 7K53; EM; 3.20 A; Q=2-124.
DR PDB; 7K54; EM; 3.20 A; Q=2-124.
DR PDB; 7K55; EM; 3.30 A; Q=2-124.
DR PDB; 7LV0; EM; 3.20 A; Q=2-124.
DR PDB; 7NAR; EM; 3.00 A; L=1-124.
DR PDB; 7NAS; EM; 3.31 A; L=1-124.
DR PDB; 7NAT; EM; 3.59 A; L=1-124.
DR PDB; 7NAU; EM; 3.78 A; L=1-124.
DR PDB; 7NAV; EM; 4.80 A; L=1-124.
DR PDB; 7NBU; EM; 3.11 A; L=2-124.
DR PDB; 7NWT; EM; 2.66 A; q=1-124.
DR PDB; 7O19; EM; 2.90 A; AL=1-124.
DR PDB; 7O1A; EM; 2.40 A; AL=1-124.
DR PDB; 7O1C; EM; 2.60 A; AL=1-124.
DR PDB; 7O5H; EM; 3.10 A; L=2-124.
DR PDB; 7OE0; EM; 2.69 A; L=2-124.
DR PDB; 7OE1; EM; 3.05 A; L=2-124.
DR PDB; 7OI0; EM; 2.76 A; L=2-124.
DR PDB; 7OIZ; EM; 2.90 A; L=1-124.
DR PDB; 7OJ0; EM; 3.50 A; L=1-124.
DR PDB; 7P3K; EM; 2.90 A; L=1-124.
DR PDB; 7PJV; EM; 3.10 A; l=1-124.
DR PDB; 7PJY; EM; 3.10 A; l=1-124.
DR PDB; 7QG8; EM; 3.97 A; E=1-124.
DR PDB; 7QGH; EM; 4.48 A; B=1-124.
DR PDB; 7S1I; EM; 2.48 A; t=1-124.
DR PDB; 7S1J; EM; 2.47 A; t=1-124.
DR PDB; 7S1K; EM; 2.42 A; t=1-124.
DR PDB; 7SS9; EM; 3.90 A; Q=2-124.
DR PDB; 7SSD; EM; 3.30 A; Q=2-124.
DR PDB; 7SSL; EM; 3.80 A; Q=2-124.
DR PDB; 7SSN; EM; 3.20 A; Q=2-124.
DR PDB; 7SSO; EM; 3.20 A; Q=2-124.
DR PDB; 7SSW; EM; 3.80 A; Q=2-124.
DR PDB; 7ST2; EM; 2.90 A; Q=2-124.
DR PDB; 7ST6; EM; 3.00 A; Q=2-124.
DR PDB; 7ST7; EM; 3.20 A; Q=2-124.
DR PDBsum; 1MJ1; -.
DR PDBsum; 1ZN1; -.
DR PDBsum; 2YKR; -.
DR PDBsum; 3DEG; -.
DR PDBsum; 3EP2; -.
DR PDBsum; 3EQ3; -.
DR PDBsum; 3EQ4; -.
DR PDBsum; 3IY8; -.
DR PDBsum; 3J0D; -.
DR PDBsum; 3J0E; -.
DR PDBsum; 3J9Y; -.
DR PDBsum; 3J9Z; -.
DR PDBsum; 3JA1; -.
DR PDBsum; 3JBU; -.
DR PDBsum; 3JBV; -.
DR PDBsum; 3JCD; -.
DR PDBsum; 3JCE; -.
DR PDBsum; 3JCJ; -.
DR PDBsum; 3JCN; -.
DR PDBsum; 4A2I; -.
DR PDBsum; 4ADV; -.
DR PDBsum; 4U1U; -.
DR PDBsum; 4U1V; -.
DR PDBsum; 4U20; -.
DR PDBsum; 4U24; -.
DR PDBsum; 4U25; -.
DR PDBsum; 4U26; -.
DR PDBsum; 4U27; -.
DR PDBsum; 4V47; -.
DR PDBsum; 4V48; -.
DR PDBsum; 4V4H; -.
DR PDBsum; 4V4Q; -.
DR PDBsum; 4V4V; -.
DR PDBsum; 4V4W; -.
DR PDBsum; 4V50; -.
DR PDBsum; 4V52; -.
DR PDBsum; 4V53; -.
DR PDBsum; 4V54; -.
DR PDBsum; 4V55; -.
DR PDBsum; 4V56; -.
DR PDBsum; 4V57; -.
DR PDBsum; 4V5B; -.
DR PDBsum; 4V5H; -.
DR PDBsum; 4V5Y; -.
DR PDBsum; 4V64; -.
DR PDBsum; 4V65; -.
DR PDBsum; 4V66; -.
DR PDBsum; 4V69; -.
DR PDBsum; 4V6C; -.
DR PDBsum; 4V6D; -.
DR PDBsum; 4V6E; -.
DR PDBsum; 4V6K; -.
DR PDBsum; 4V6L; -.
DR PDBsum; 4V6M; -.
DR PDBsum; 4V6N; -.
DR PDBsum; 4V6O; -.
DR PDBsum; 4V6P; -.
DR PDBsum; 4V6Q; -.
DR PDBsum; 4V6R; -.
DR PDBsum; 4V6S; -.
DR PDBsum; 4V6T; -.
DR PDBsum; 4V6V; -.
DR PDBsum; 4V6Y; -.
DR PDBsum; 4V6Z; -.
DR PDBsum; 4V70; -.
DR PDBsum; 4V71; -.
DR PDBsum; 4V72; -.
DR PDBsum; 4V73; -.
DR PDBsum; 4V74; -.
DR PDBsum; 4V75; -.
DR PDBsum; 4V76; -.
DR PDBsum; 4V77; -.
DR PDBsum; 4V78; -.
DR PDBsum; 4V79; -.
DR PDBsum; 4V7A; -.
DR PDBsum; 4V7B; -.
DR PDBsum; 4V7C; -.
DR PDBsum; 4V7D; -.
DR PDBsum; 4V7I; -.
DR PDBsum; 4V7S; -.
DR PDBsum; 4V7T; -.
DR PDBsum; 4V7U; -.
DR PDBsum; 4V7V; -.
DR PDBsum; 4V85; -.
DR PDBsum; 4V89; -.
DR PDBsum; 4V9C; -.
DR PDBsum; 4V9D; -.
DR PDBsum; 4V9O; -.
DR PDBsum; 4V9P; -.
DR PDBsum; 4WF1; -.
DR PDBsum; 4WOI; -.
DR PDBsum; 4WWW; -.
DR PDBsum; 4YBB; -.
DR PDBsum; 5AFI; -.
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; 5JTE; -.
DR PDBsum; 5JU8; -.
DR PDBsum; 5KCR; -.
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; 5ME0; -.
DR PDBsum; 5ME1; -.
DR PDBsum; 5MGP; -.
DR PDBsum; 5MY1; -.
DR PDBsum; 5NO2; -.
DR PDBsum; 5NO3; -.
DR PDBsum; 5NO4; -.
DR PDBsum; 5NP6; -.
DR PDBsum; 5NWY; -.
DR PDBsum; 5O2R; -.
DR PDBsum; 5U4I; -.
DR PDBsum; 5U4J; -.
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; 6GWT; -.
DR PDBsum; 6GXM; -.
DR PDBsum; 6GXN; -.
DR PDBsum; 6GXO; -.
DR PDBsum; 6GXP; -.
DR PDBsum; 6H4N; -.
DR PDBsum; 6H58; -.
DR PDBsum; 6HRM; -.
DR PDBsum; 6I7V; -.
DR PDBsum; 6O9J; -.
DR PDBsum; 6O9K; -.
DR PDBsum; 6OFX; -.
DR PDBsum; 6OG7; -.
DR PDBsum; 6ORE; -.
DR PDBsum; 6ORL; -.
DR PDBsum; 6OST; -.
DR PDBsum; 6OT3; -.
DR PDBsum; 6OUO; -.
DR PDBsum; 6Q9A; -.
DR PDBsum; 6SZS; -.
DR PDBsum; 6TBV; -.
DR PDBsum; 6TC3; -.
DR PDBsum; 6VWL; -.
DR PDBsum; 6VWM; -.
DR PDBsum; 6VWN; -.
DR PDBsum; 6W6K; -.
DR PDBsum; 6W77; -.
DR PDBsum; 6W7M; -.
DR PDBsum; 6W7N; -.
DR PDBsum; 6W7W; -.
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; 6WNV; -.
DR PDBsum; 6WNW; -.
DR PDBsum; 6XE0; -.
DR PDBsum; 6XZA; -.
DR PDBsum; 6XZB; -.
DR PDBsum; 6Y69; -.
DR PDBsum; 6ZTL; -.
DR PDBsum; 7ABZ; -.
DR PDBsum; 7AC7; -.
DR PDBsum; 7ACJ; -.
DR PDBsum; 7ACR; -.
DR PDBsum; 7AFI; -.
DR PDBsum; 7AFL; -.
DR PDBsum; 7AFO; -.
DR PDBsum; 7B5K; -.
DR PDBsum; 7BOD; -.
DR PDBsum; 7BOE; -.
DR PDBsum; 7BOF; -.
DR PDBsum; 7BOG; -.
DR PDBsum; 7BOH; -.
DR PDBsum; 7BOI; -.
DR PDBsum; 7D6Z; -.
DR PDBsum; 7D80; -.
DR PDBsum; 7JSS; -.
DR PDBsum; 7JSW; -.
DR PDBsum; 7JSZ; -.
DR PDBsum; 7JT1; -.
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; 7NAR; -.
DR PDBsum; 7NAS; -.
DR PDBsum; 7NAT; -.
DR PDBsum; 7NAU; -.
DR PDBsum; 7NAV; -.
DR PDBsum; 7NBU; -.
DR PDBsum; 7NWT; -.
DR PDBsum; 7O19; -.
DR PDBsum; 7O1A; -.
DR PDBsum; 7O1C; -.
DR PDBsum; 7O5H; -.
DR PDBsum; 7OE0; -.
DR PDBsum; 7OE1; -.
DR PDBsum; 7OI0; -.
DR PDBsum; 7OIZ; -.
DR PDBsum; 7OJ0; -.
DR PDBsum; 7P3K; -.
DR PDBsum; 7PJV; -.
DR PDBsum; 7PJY; -.
DR PDBsum; 7QG8; -.
DR PDBsum; 7QGH; -.
DR PDBsum; 7S1I; -.
DR PDBsum; 7S1J; -.
DR PDBsum; 7S1K; -.
DR PDBsum; 7SS9; -.
DR PDBsum; 7SSD; -.
DR PDBsum; 7SSL; -.
DR PDBsum; 7SSN; -.
DR PDBsum; 7SSO; -.
DR PDBsum; 7SSW; -.
DR PDBsum; 7ST2; -.
DR PDBsum; 7ST6; -.
DR PDBsum; 7ST7; -.
DR AlphaFoldDB; P0A7S3; -.
DR SMR; P0A7S3; -.
DR BioGRID; 852156; 1.
DR ComplexPortal; CPX-3802; 30S small ribosomal subunit.
DR DIP; DIP-35806N; -.
DR IntAct; P0A7S3; 45.
DR STRING; 511145.b3342; -.
DR DrugBank; DB00479; Amikacin.
DR DrugBank; DB06696; Arbekacin.
DR DrugBank; DB00452; Framycetin.
DR DrugBank; DB00798; Gentamicin.
DR DrugBank; DB04729; Gentamicin C1a.
DR DrugBank; DB01172; Kanamycin.
DR DrugBank; DB00994; Neomycin.
DR DrugBank; DB00955; Netilmicin.
DR DrugBank; DB03615; Ribostamycin.
DR DrugBank; DB00919; Spectinomycin.
DR DrugBank; DB01082; Streptomycin.
DR DrugBank; DB00560; Tigecycline.
DR DrugCentral; P0A7S3; -.
DR iPTMnet; P0A7S3; -.
DR jPOST; P0A7S3; -.
DR PaxDb; P0A7S3; -.
DR PRIDE; P0A7S3; -.
DR EnsemblBacteria; AAC76367; AAC76367; b3342.
DR EnsemblBacteria; BAE77949; BAE77949; BAE77949.
DR GeneID; 64727495; -.
DR GeneID; 67463992; -.
DR GeneID; 947845; -.
DR KEGG; ecj:JW3304; -.
DR KEGG; eco:b3342; -.
DR PATRIC; fig|1411691.4.peg.3389; -.
DR EchoBASE; EB0904; -.
DR eggNOG; COG0048; Bacteria.
DR HOGENOM; CLU_104295_1_2_6; -.
DR InParanoid; P0A7S3; -.
DR OMA; SPALEKC; -.
DR PhylomeDB; P0A7S3; -.
DR BioCyc; EcoCyc:EG10911-MON; -.
DR BioCyc; MetaCyc:EG10911-MON; -.
DR EvolutionaryTrace; P0A7S3; -.
DR PRO; PR:P0A7S3; -.
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:0022627; C:cytosolic small ribosomal subunit; IDA:EcoliWiki.
DR GO; GO:0005840; C:ribosome; IBA:GO_Central.
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; IDA:CAFA.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0000372; P:Group I intron splicing; IDA:EcoCyc.
DR GO; GO:1990145; P:maintenance of translational fidelity; IMP: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 CDD; cd03368; Ribosomal_S12; 1.
DR DisProt; DP00145; -.
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;
KW Direct protein sequencing; Methylation; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7556101"
FT CHAIN 2..124
FT /note="30S ribosomal protein S12"
FT /id="PRO_0000146219"
FT MOD_RES 89
FT /note="3-methylthioaspartic acid"
FT /evidence="ECO:0000269|PubMed:8844851"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT VARIANT 43
FT /note="K -> R (confers streptomycin resistance but not
FT hyperaccurate translation)"
FT MUTAGEN 57
FT /note="L->H: Protein is not incorporated into ribosomes."
FT /evidence="ECO:0000269|PubMed:10209746"
FT MUTAGEN 88
FT /note="K->Q: Confers low-level resistance to streptomycin
FT and a 15% decrease in the translational elongation rate."
FT /evidence="ECO:0000269|PubMed:10209746"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:7BOD"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:7OE1"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:7NAS"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:7OE0"
SQ SEQUENCE 124 AA; 13737 MW; 94A57F4C4FF0FC5E CRC64;
MATVNQLVRK PRARKVAKSN VPALEACPQK RGVCTRVYTT TPKKPNSALR KVCRVRLTNG
FEVTSYIGGE GHNLQEHSVI LIRGGRVKDL PGVRYHTVRG ALDCSGVKDR KQARSKYGVK
RPKA
