RS5_ECOLI
ID RS5_ECOLI Reviewed; 167 AA.
AC P0A7W1; O54299; P02356; Q2M6W8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=30S ribosomal protein S5;
DE AltName: Full=Small ribosomal subunit protein uS5 {ECO:0000303|PubMed:24524803};
GN Name=rpsE; Synonyms=spc; OrderedLocusNames=b3303, JW3265;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6222285; DOI=10.1093/nar/11.9.2599;
RA Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.;
RT "The spc ribosomal protein operon of Escherichia coli: sequence and
RT cotranscription of the ribosomal protein genes and a protein export gene.";
RL Nucleic Acids Res. 11:2599-2616(1983).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-167, SUBUNIT, ACETYLATION AT ALA-2, VARIANTS, AND
RP MUTANTS.
RC STRAIN=B, and K;
RX PubMed=363452; DOI=10.1016/0014-5793(78)80059-3;
RA Wittmann-Liebold B., Greuer B.;
RT "The primary structure of protein S5 from the small subunit of the
RT Escherichia coli ribosome.";
RL FEBS Lett. 95:91-98(1978).
RN [5]
RP PROTEIN SEQUENCE OF 15-23, SUBUNIT, AND VARIANT SPECTINOMYCIN RESISTANT.
RC STRAIN=B;
RX PubMed=4273819; DOI=10.1007/bf00333767;
RA DeWilde M., Wittmann-Liebold B.;
RT "Localization of the amino-acid exchange in protein S5 from an Escherichia
RT coli mutant resistant to spectinomycin.";
RL Mol. Gen. Genet. 127:273-276(1973).
RN [6]
RP INVOLVEMENT IN FORMATION OF THE EF-G/RIBOSOME COMPLEX.
RC STRAIN=B/2;
RX PubMed=4346030; DOI=10.1073/pnas.70.1.151;
RA Marsh R.C., Parmeggiani A.;
RT "Requirement of proteins S5 and S9 from 30S subunits for the ribosome-
RT dependent GTPase activity of elongation factor G.";
RL Proc. Natl. Acad. Sci. U.S.A. 70:151-155(1973).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [8]
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 [9]
RP CHARACTERIZATION OF VARIANTS.
RC STRAIN=O17;
RX PubMed=2138078; DOI=10.1002/j.1460-2075.1990.tb08167.x;
RA Bilgin N., Richter A.A., Ehrenberg M., Dahlberg A.E., Kurland C.G.;
RT "Ribosomal RNA and protein mutants resistant to spectinomycin.";
RL EMBO J. 9:735-739(1990).
RN [10]
RP CROSS-LINKING TO MRNA.
RX PubMed=1712292; DOI=10.1002/j.1460-2075.1991.tb07755.x;
RA Rinke-Appel J., Juenke N., Stade K., Brimacombe R.;
RT "The path of mRNA through the Escherichia coli ribosome; site-directed
RT cross-linking of mRNA analogues carrying a photo-reactive label at various
RT points 3' to the decoding site.";
RL EMBO J. 10:2195-2202(1991).
RN [11]
RP ROLE IN MRNA HELICASE ACTIVITY, AND MUTAGENESIS.
RC STRAIN=MRE-600;
RX PubMed=15652481; DOI=10.1016/j.cell.2004.11.042;
RA Takyar S., Hickerson R.P., Noller H.F.;
RT "mRNA helicase activity of the ribosome.";
RL Cell 120:49-58(2005).
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 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 [14]
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 [15]
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 [16]
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 [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX
RP WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=27906160; DOI=10.1038/nature20822;
RA Ma C., Kurita D., Li N., Chen Y., Himeno H., Gao N.;
RT "Mechanistic insights into the alternative translation termination by ArfA
RT and RF2.";
RL Nature 541:550-553(2017).
RN [18]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX
RP WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=27906161; DOI=10.1038/nature20821;
RA Huter P., Mueller C., Beckert B., Arenz S., Berninghausen O., Beckmann R.,
RA Wilson D.N.;
RT "Structural basis for ArfA-RF2-mediated translation termination on mRNAs
RT lacking stop codons.";
RL Nature 541:546-549(2017).
RN [19]
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 [20]
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 S12 plays an important role in translational
CC accuracy. Many suppressors of streptomycin-dependent mutants of protein
CC S12 are found in this protein, some but not all of which decrease
CC translational accuracy (ram, ribosomal ambiguity mutations).
CC {ECO:0000269|PubMed:15652481}.
CC -!- FUNCTION: Located at the back of the 30S subunit body where it
CC stabilizes the conformation of the head with respect to the body.
CC {ECO:0000269|PubMed:15652481}.
CC -!- FUNCTION: The physical location of this protein suggests it may also
CC play a role in mRNA unwinding by the ribosome, possibly by forming part
CC of a processivity clamp. {ECO:0000269|PubMed:15652481}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit (PubMed:363452,
CC PubMed:4273819, PubMed:12809609, PubMed:16272117, PubMed:27934701,
CC PubMed:10094780, PubMed:12244297, PubMed:27906160, PubMed:27906161,
CC PubMed:28077875). Contacts proteins S4 and S8. With proteins S4 and S5
CC encircles the mRNA as it enters the ribosome, which may play a role in
CC mRNA helicase processivity (PubMed:15652481). Can be cross-linked to
CC mRNA (PubMed:1712292). {ECO:0000269|PubMed:10094780,
CC ECO:0000269|PubMed:12244297, ECO:0000269|PubMed:12809609,
CC ECO:0000269|PubMed:15652481, ECO:0000269|PubMed:16272117,
CC ECO:0000269|PubMed:1712292, ECO:0000269|PubMed:27906160,
CC ECO:0000269|PubMed:27906161, ECO:0000269|PubMed:27934701,
CC ECO:0000269|PubMed:28077875, ECO:0000269|PubMed:363452,
CC ECO:0000269|PubMed:4273819}.
CC -!- INTERACTION:
CC P0A7W1; P0A7C2: lexA; NbExp=2; IntAct=EBI-543949, EBI-553416;
CC P0A7W1; P30850: rnb; NbExp=3; IntAct=EBI-543949, EBI-557325;
CC P0A7W1; P0ADZ0: rplW; NbExp=2; IntAct=EBI-543949, EBI-542264;
CC -!- DOMAIN: The N-terminal domain interacts with the head of the 30S
CC subunit; the C-terminal domain interacts with the body and contacts
CC protein S4. The interaction surface between S4 and S5 is involved in
CC control of translational fidelity.
CC -!- MASS SPECTROMETRY: Mass=17514.8; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10094780};
CC -!- MISCELLANEOUS: Altered S5 proteins have been identified in a number of
CC mutants. Some mutations in S5 have been shown to increase translational
CC error frequencies.
CC -!- MISCELLANEOUS: Some mutants in this protein can partially suppress an
CC alanyl-tRNA synthetase mutant.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000305}.
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DR EMBL; X01563; CAA25722.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58100.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76328.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77988.1; -; Genomic_DNA.
DR PIR; B65123; R3EC5.
DR RefSeq; NP_417762.1; NC_000913.3.
DR RefSeq; WP_000940121.1; NZ_STEB01000038.1.
DR PDB; 1EG0; EM; 11.50 A; B=1-148.
DR PDB; 2YKR; EM; 9.80 A; E=10-159.
DR PDB; 3IY8; EM; 14.10 A; E=10-159.
DR PDB; 3J9Y; EM; 3.90 A; e=1-167.
DR PDB; 3J9Z; EM; 3.60 A; SE=2-167.
DR PDB; 3JA1; EM; 3.60 A; SE=2-167.
DR PDB; 3JBU; EM; 3.64 A; E=1-167.
DR PDB; 3JBV; EM; 3.32 A; E=1-167.
DR PDB; 3JCD; EM; 3.70 A; e=1-167.
DR PDB; 3JCE; EM; 3.20 A; e=1-167.
DR PDB; 3JCJ; EM; 3.70 A; k=1-167.
DR PDB; 3JCN; EM; 4.60 A; f=1-159.
DR PDB; 4A2I; EM; 16.50 A; E=10-159.
DR PDB; 4ADV; EM; 13.50 A; E=2-167.
DR PDB; 4U1U; X-ray; 2.95 A; AE/CE=10-159.
DR PDB; 4U1V; X-ray; 3.00 A; AE/CE=10-159.
DR PDB; 4U20; X-ray; 2.90 A; AE/CE=10-159.
DR PDB; 4U24; X-ray; 2.90 A; AE/CE=10-159.
DR PDB; 4U25; X-ray; 2.90 A; AE/CE=10-159.
DR PDB; 4U26; X-ray; 2.80 A; AE/CE=10-159.
DR PDB; 4U27; X-ray; 2.80 A; AE/CE=10-159.
DR PDB; 4V47; EM; 12.30 A; BE=2-167.
DR PDB; 4V48; EM; 11.50 A; BE=2-167.
DR PDB; 4V4H; X-ray; 3.46 A; AE/CE=1-167.
DR PDB; 4V4Q; X-ray; 3.46 A; AE/CE=2-167.
DR PDB; 4V4V; EM; 15.00 A; AE=10-157.
DR PDB; 4V4W; EM; 15.00 A; AE=10-157.
DR PDB; 4V50; X-ray; 3.22 A; AE/CE=2-167.
DR PDB; 4V52; X-ray; 3.21 A; AE/CE=2-167.
DR PDB; 4V53; X-ray; 3.54 A; AE/CE=2-167.
DR PDB; 4V54; X-ray; 3.30 A; AE/CE=2-167.
DR PDB; 4V55; X-ray; 4.00 A; AE/CE=2-167.
DR PDB; 4V56; X-ray; 3.93 A; AE/CE=2-167.
DR PDB; 4V57; X-ray; 3.50 A; AE/CE=2-167.
DR PDB; 4V5B; X-ray; 3.74 A; BE/DE=2-167.
DR PDB; 4V5H; EM; 5.80 A; AE=10-159.
DR PDB; 4V5Y; X-ray; 4.45 A; AE/CE=2-167.
DR PDB; 4V64; X-ray; 3.50 A; AE/CE=2-167.
DR PDB; 4V65; EM; 9.00 A; AS=1-159.
DR PDB; 4V66; EM; 9.00 A; AS=1-159.
DR PDB; 4V69; EM; 6.70 A; AE=10-159.
DR PDB; 4V6C; X-ray; 3.19 A; AE/CE=1-167.
DR PDB; 4V6D; X-ray; 3.81 A; AE/CE=1-167.
DR PDB; 4V6E; X-ray; 3.71 A; AE/CE=1-167.
DR PDB; 4V6K; EM; 8.25 A; BI=1-167.
DR PDB; 4V6L; EM; 13.20 A; AI=1-167.
DR PDB; 4V6M; EM; 7.10 A; AE=2-167.
DR PDB; 4V6N; EM; 12.10 A; BH=2-167.
DR PDB; 4V6O; EM; 14.70 A; AH=2-167.
DR PDB; 4V6P; EM; 13.50 A; AH=2-167.
DR PDB; 4V6Q; EM; 11.50 A; AH=2-167.
DR PDB; 4V6R; EM; 11.50 A; AH=2-167.
DR PDB; 4V6S; EM; 13.10 A; BG=2-167.
DR PDB; 4V6T; EM; 8.30 A; AE=10-159.
DR PDB; 4V6V; EM; 9.80 A; AE=2-167.
DR PDB; 4V6Y; EM; 12.00 A; AE=10-159.
DR PDB; 4V6Z; EM; 12.00 A; AE=10-159.
DR PDB; 4V70; EM; 17.00 A; AE=10-159.
DR PDB; 4V71; EM; 20.00 A; AE=10-159.
DR PDB; 4V72; EM; 13.00 A; AE=10-159.
DR PDB; 4V73; EM; 15.00 A; AE=10-159.
DR PDB; 4V74; EM; 17.00 A; AE=10-159.
DR PDB; 4V75; EM; 12.00 A; AE=10-159.
DR PDB; 4V76; EM; 17.00 A; AE=10-159.
DR PDB; 4V77; EM; 17.00 A; AE=10-159.
DR PDB; 4V78; EM; 20.00 A; AE=10-159.
DR PDB; 4V79; EM; 15.00 A; AE=10-159.
DR PDB; 4V7A; EM; 9.00 A; AE=10-159.
DR PDB; 4V7B; EM; 6.80 A; AE=1-167.
DR PDB; 4V7C; EM; 7.60 A; AE=2-167.
DR PDB; 4V7D; EM; 7.60 A; BE=2-167.
DR PDB; 4V7I; EM; 9.60 A; BE=1-167.
DR PDB; 4V7S; X-ray; 3.25 A; AE/CE=10-159.
DR PDB; 4V7T; X-ray; 3.19 A; AE/CE=10-159.
DR PDB; 4V7U; X-ray; 3.10 A; AE/CE=10-159.
DR PDB; 4V7V; X-ray; 3.29 A; AE/CE=10-159.
DR PDB; 4V85; X-ray; 3.20 A; AE=1-167.
DR PDB; 4V89; X-ray; 3.70 A; AE=1-167.
DR PDB; 4V9C; X-ray; 3.30 A; AE/CE=1-167.
DR PDB; 4V9D; X-ray; 3.00 A; AE/BE=10-159.
DR PDB; 4V9O; X-ray; 2.90 A; BE/DE/FE/HE=1-167.
DR PDB; 4V9P; X-ray; 2.90 A; BE/DE/FE/HE=1-167.
DR PDB; 4WF1; X-ray; 3.09 A; AE/CE=10-159.
DR PDB; 4WOI; X-ray; 3.00 A; AE/DE=1-167.
DR PDB; 4WWW; X-ray; 3.10 A; QE/XE=10-159.
DR PDB; 4YBB; X-ray; 2.10 A; AE/BE=10-164.
DR PDB; 5AFI; EM; 2.90 A; e=1-167.
DR PDB; 5H5U; EM; 3.00 A; l=2-167.
DR PDB; 5IQR; EM; 3.00 A; j=1-167.
DR PDB; 5IT8; X-ray; 3.12 A; AE/BE=10-164.
DR PDB; 5J5B; X-ray; 2.80 A; AE/BE=10-164.
DR PDB; 5J7L; X-ray; 3.00 A; AE/BE=10-164.
DR PDB; 5J88; X-ray; 3.32 A; AE/BE=10-164.
DR PDB; 5J8A; X-ray; 3.10 A; AE/BE=10-164.
DR PDB; 5J91; X-ray; 2.96 A; AE/BE=10-164.
DR PDB; 5JC9; X-ray; 3.03 A; AE/BE=10-164.
DR PDB; 5JTE; EM; 3.60 A; AE=1-167.
DR PDB; 5JU8; EM; 3.60 A; AE=1-167.
DR PDB; 5KCR; EM; 3.60 A; 1e=1-167.
DR PDB; 5KCS; EM; 3.90 A; 1e=1-167.
DR PDB; 5KPS; EM; 3.90 A; 10=1-167.
DR PDB; 5KPV; EM; 4.10 A; 9=1-167.
DR PDB; 5KPW; EM; 3.90 A; 9=1-167.
DR PDB; 5KPX; EM; 3.90 A; 9=1-167.
DR PDB; 5L3P; EM; 3.70 A; e=1-167.
DR PDB; 5LZA; EM; 3.60 A; e=10-166.
DR PDB; 5LZB; EM; 5.30 A; e=10-166.
DR PDB; 5LZC; EM; 4.80 A; e=10-166.
DR PDB; 5LZD; EM; 3.40 A; e=10-166.
DR PDB; 5LZE; EM; 3.50 A; e=10-166.
DR PDB; 5LZF; EM; 4.60 A; e=10-166.
DR PDB; 5MDV; EM; 2.97 A; j=1-167.
DR PDB; 5MDW; EM; 3.06 A; j=1-167.
DR PDB; 5MDY; EM; 3.35 A; j=1-167.
DR PDB; 5MDZ; EM; 3.10 A; j=1-167.
DR PDB; 5ME0; EM; 13.50 A; E=1-167.
DR PDB; 5ME1; EM; 13.50 A; E=1-167.
DR PDB; 5MGP; EM; 3.10 A; e=10-166.
DR PDB; 5MY1; EM; 7.60 A; E=2-167.
DR PDB; 5NO2; EM; 5.16 A; E=10-164.
DR PDB; 5NO3; EM; 5.16 A; E=10-164.
DR PDB; 5NO4; EM; 5.16 A; E=10-164.
DR PDB; 5NP6; EM; 3.60 A; H=10-166.
DR PDB; 5NWY; EM; 2.93 A; 4=1-166.
DR PDB; 5O2R; EM; 3.40 A; e=10-166.
DR PDB; 5U4I; EM; 3.50 A; e=1-167.
DR PDB; 5U4J; EM; 3.70 A; e=1-167.
DR PDB; 5U9F; EM; 3.20 A; E=1-167.
DR PDB; 5U9G; EM; 3.20 A; E=1-167.
DR PDB; 5UYK; EM; 3.90 A; E=10-166.
DR PDB; 5UYL; EM; 3.60 A; E=10-166.
DR PDB; 5UYM; EM; 3.20 A; E=10-166.
DR PDB; 5UYN; EM; 4.00 A; E=10-166.
DR PDB; 5UYP; EM; 3.90 A; E=10-166.
DR PDB; 5UYQ; EM; 3.80 A; E=10-166.
DR PDB; 5UZ4; EM; 5.80 A; E=1-167.
DR PDB; 5WDT; EM; 3.00 A; e=10-166.
DR PDB; 5WE4; EM; 3.10 A; e=10-166.
DR PDB; 5WE6; EM; 3.40 A; e=10-166.
DR PDB; 5WFK; EM; 3.40 A; e=10-166.
DR PDB; 6BU8; EM; 3.50 A; E=10-166.
DR PDB; 6BY1; X-ray; 3.94 A; AE/BE=10-159.
DR PDB; 6C4I; EM; 3.24 A; e=1-167.
DR PDB; 6DNC; EM; 3.70 A; RA=1-167.
DR PDB; 6ENF; EM; 3.20 A; e=10-166.
DR PDB; 6ENJ; EM; 3.70 A; e=10-166.
DR PDB; 6ENU; EM; 3.10 A; e=10-166.
DR PDB; 6GWT; EM; 3.80 A; e=10-166.
DR PDB; 6GXM; EM; 3.80 A; e=10-166.
DR PDB; 6GXN; EM; 3.90 A; e=10-166.
DR PDB; 6GXO; EM; 3.90 A; e=10-166.
DR PDB; 6GXP; EM; 4.40 A; e=10-166.
DR PDB; 6H4N; EM; 3.00 A; e=10-166.
DR PDB; 6H58; EM; 7.90 A; e/ee=10-166.
DR PDB; 6HRM; EM; 2.96 A; j=10-165.
DR PDB; 6I7V; X-ray; 2.90 A; AE/BE=10-159.
DR PDB; 6NQB; EM; 3.80 A; E=10-158.
DR PDB; 6O9J; EM; 3.90 A; e=10-159.
DR PDB; 6O9K; EM; 4.00 A; e=10-159.
DR PDB; 6OFX; EM; 3.30 A; J=10-166.
DR PDB; 6OG7; EM; 3.30 A; J=10-166.
DR PDB; 6ORE; EM; 2.90 A; j=10-165.
DR PDB; 6ORL; EM; 3.50 A; j=10-165.
DR PDB; 6OST; EM; 4.20 A; j=10-165.
DR PDB; 6OT3; EM; 3.90 A; j=10-165.
DR PDB; 6OUO; EM; 3.70 A; j=10-165.
DR PDB; 6Q97; EM; 3.90 A; j=10-165.
DR PDB; 6Q98; EM; 4.30 A; j=1-167.
DR PDB; 6Q9A; EM; 3.70 A; j=10-165.
DR PDB; 6SZS; EM; 3.06 A; e=1-167.
DR PDB; 6TBV; EM; 2.70 A; S051=1-167.
DR PDB; 6TC3; EM; 2.70 A; S051=1-167.
DR PDB; 6VWL; EM; 3.10 A; d=1-167.
DR PDB; 6VWM; EM; 3.40 A; d=1-167.
DR PDB; 6VWN; EM; 3.40 A; d=1-167.
DR PDB; 6W6K; EM; 3.60 A; E=1-167.
DR PDB; 6W77; EM; 3.60 A; E=1-167.
DR PDB; 6W7M; EM; 3.80 A; E=1-167.
DR PDB; 6W7N; EM; 3.40 A; E=1-167.
DR PDB; 6W7W; EM; 3.90 A; D=1-167.
DR PDB; 6WD6; EM; 3.70 A; J=10-166.
DR PDB; 6WDB; EM; 4.00 A; J=10-166.
DR PDB; 6WDC; EM; 4.20 A; J=10-166.
DR PDB; 6WDD; EM; 3.20 A; J=10-166.
DR PDB; 6WDE; EM; 3.00 A; J=10-166.
DR PDB; 6WDF; EM; 3.30 A; J=10-166.
DR PDB; 6WDG; EM; 3.30 A; J=10-166.
DR PDB; 6WDH; EM; 4.30 A; J=10-166.
DR PDB; 6WDI; EM; 4.00 A; J=10-166.
DR PDB; 6WDJ; EM; 3.70 A; J=10-166.
DR PDB; 6WDK; EM; 3.60 A; J=10-166.
DR PDB; 6WDL; EM; 3.70 A; J=10-166.
DR PDB; 6WDM; EM; 3.60 A; J=10-166.
DR PDB; 6WNV; EM; 3.50 A; J=10-166.
DR PDB; 6WNW; EM; 3.20 A; J=10-166.
DR PDB; 6XE0; EM; 6.80 A; D=10-159.
DR PDB; 6XZA; EM; 2.66 A; E1=10-164.
DR PDB; 6XZB; EM; 2.54 A; E1=10-164.
DR PDB; 6Y69; EM; 2.86 A; e=10-166.
DR PDB; 6ZTL; EM; 3.50 A; AE=1-167.
DR PDB; 7ABZ; EM; 3.21 A; j=1-167.
DR PDB; 7AC7; EM; 3.08 A; j=10-165.
DR PDB; 7ACJ; EM; 3.20 A; j=10-165.
DR PDB; 7ACR; EM; 3.44 A; j=10-165.
DR PDB; 7AFI; EM; 3.53 A; E=1-167.
DR PDB; 7AFL; EM; 4.20 A; E=1-167.
DR PDB; 7AFO; EM; 3.93 A; E=1-167.
DR PDB; 7B5K; EM; 2.90 A; e=10-164.
DR PDB; 7BOD; EM; 2.88 A; E=1-167.
DR PDB; 7BOE; EM; 2.90 A; E=1-167.
DR PDB; 7BOF; EM; 2.92 A; E=1-167.
DR PDB; 7BOG; EM; 2.75 A; E=1-167.
DR PDB; 7BOH; EM; 2.82 A; E=1-167.
DR PDB; 7BOI; EM; 2.98 A; E=1-167.
DR PDB; 7D6Z; EM; 3.40 A; l=1-167.
DR PDB; 7D80; EM; 4.10 A; F=1-167.
DR PDB; 7JSS; EM; 3.70 A; J=10-166.
DR PDB; 7JSW; EM; 3.80 A; J=10-166.
DR PDB; 7JSZ; EM; 3.70 A; J=10-166.
DR PDB; 7JT1; EM; 3.30 A; J=10-166.
DR PDB; 7JT2; EM; 3.50 A; J=10-166.
DR PDB; 7JT3; EM; 3.70 A; J=10-166.
DR PDB; 7K50; EM; 3.40 A; J=10-166.
DR PDB; 7K51; EM; 3.50 A; J=10-166.
DR PDB; 7K52; EM; 3.40 A; J=10-166.
DR PDB; 7K53; EM; 3.20 A; J=10-166.
DR PDB; 7K54; EM; 3.20 A; J=10-166.
DR PDB; 7K55; EM; 3.30 A; J=10-166.
DR PDB; 7LV0; EM; 3.20 A; J=10-166.
DR PDB; 7N1P; EM; 2.33 A; SE=1-167.
DR PDB; 7N2C; EM; 2.72 A; SE=1-167.
DR PDB; 7N2U; EM; 2.53 A; SE=1-167.
DR PDB; 7N2V; EM; 2.54 A; SE=1-167.
DR PDB; 7N30; EM; 2.66 A; SE=1-167.
DR PDB; 7N31; EM; 2.69 A; SE=1-167.
DR PDB; 7NAR; EM; 3.00 A; E=1-167.
DR PDB; 7NAS; EM; 3.31 A; E=1-167.
DR PDB; 7NAT; EM; 3.59 A; E=1-167.
DR PDB; 7NAU; EM; 3.78 A; E=1-167.
DR PDB; 7NAV; EM; 4.80 A; E=1-167.
DR PDB; 7NBU; EM; 3.11 A; E=10-165.
DR PDB; 7O19; EM; 2.90 A; AE=1-167.
DR PDB; 7O1A; EM; 2.40 A; AE=1-167.
DR PDB; 7O1C; EM; 2.60 A; AE=1-167.
DR PDB; 7O5H; EM; 3.10 A; E=10-167.
DR PDB; 7OE0; EM; 2.69 A; E=2-167.
DR PDB; 7OE1; EM; 3.05 A; E=2-167.
DR PDB; 7OIZ; EM; 2.90 A; E=1-167.
DR PDB; 7OJ0; EM; 3.50 A; E=1-167.
DR PDB; 7P3K; EM; 2.90 A; E=1-167.
DR PDB; 7PJV; EM; 3.10 A; e=1-167.
DR PDB; 7PJY; EM; 3.10 A; e=1-167.
DR PDB; 7QG8; EM; 3.97 A; 4=4-165.
DR PDB; 7QGH; EM; 4.48 A; 4=4-165.
DR PDB; 7S1I; EM; 2.48 A; G=1-167.
DR PDB; 7S1J; EM; 2.47 A; G=1-167.
DR PDB; 7S1K; EM; 2.42 A; G=1-167.
DR PDB; 7SS9; EM; 3.90 A; J=10-166.
DR PDB; 7SSD; EM; 3.30 A; J=10-166.
DR PDB; 7SSL; EM; 3.80 A; J=10-166.
DR PDB; 7SSN; EM; 3.20 A; J=10-166.
DR PDB; 7SSO; EM; 3.20 A; J=10-166.
DR PDB; 7SSW; EM; 3.80 A; J=10-166.
DR PDB; 7ST2; EM; 2.90 A; J=10-166.
DR PDB; 7ST6; EM; 3.00 A; J=10-166.
DR PDB; 7ST7; EM; 3.20 A; J=10-166.
DR PDBsum; 1EG0; -.
DR PDBsum; 2YKR; -.
DR PDBsum; 3IY8; -.
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; 5UZ4; -.
DR PDBsum; 5WDT; -.
DR PDBsum; 5WE4; -.
DR PDBsum; 5WE6; -.
DR PDBsum; 5WFK; -.
DR PDBsum; 6BU8; -.
DR PDBsum; 6BY1; -.
DR PDBsum; 6C4I; -.
DR PDBsum; 6DNC; -.
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; 6NQB; -.
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; 6Q97; -.
DR PDBsum; 6Q98; -.
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; 7N1P; -.
DR PDBsum; 7N2C; -.
DR PDBsum; 7N2U; -.
DR PDBsum; 7N2V; -.
DR PDBsum; 7N30; -.
DR PDBsum; 7N31; -.
DR PDBsum; 7NAR; -.
DR PDBsum; 7NAS; -.
DR PDBsum; 7NAT; -.
DR PDBsum; 7NAU; -.
DR PDBsum; 7NAV; -.
DR PDBsum; 7NBU; -.
DR PDBsum; 7O19; -.
DR PDBsum; 7O1A; -.
DR PDBsum; 7O1C; -.
DR PDBsum; 7O5H; -.
DR PDBsum; 7OE0; -.
DR PDBsum; 7OE1; -.
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; P0A7W1; -.
DR SMR; P0A7W1; -.
DR BioGRID; 4263408; 155.
DR BioGRID; 852107; 3.
DR ComplexPortal; CPX-3802; 30S small ribosomal subunit.
DR DIP; DIP-10781N; -.
DR IntAct; P0A7W1; 202.
DR MINT; P0A7W1; -.
DR STRING; 511145.b3303; -.
DR iPTMnet; P0A7W1; -.
DR jPOST; P0A7W1; -.
DR PaxDb; P0A7W1; -.
DR PRIDE; P0A7W1; -.
DR EnsemblBacteria; AAC76328; AAC76328; b3303.
DR EnsemblBacteria; BAE77988; BAE77988; BAE77988.
DR GeneID; 67370899; -.
DR GeneID; 947795; -.
DR KEGG; ecj:JW3265; -.
DR KEGG; eco:b3303; -.
DR PATRIC; fig|1411691.4.peg.3428; -.
DR EchoBASE; EB0897; -.
DR eggNOG; COG0098; Bacteria.
DR HOGENOM; CLU_065898_2_2_6; -.
DR InParanoid; P0A7W1; -.
DR OMA; KRGCGSW; -.
DR PhylomeDB; P0A7W1; -.
DR BioCyc; EcoCyc:EG10904-MON; -.
DR BioCyc; MetaCyc:EG10904-MON; -.
DR EvolutionaryTrace; P0A7W1; -.
DR PRO; PR:P0A7W1; -.
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:CAFA.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:1990145; P:maintenance of translational fidelity; IMP:EcoCyc.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IDA:CAFA.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_01307_B; Ribosomal_S5_B; 1.
DR InterPro; IPR000851; Ribosomal_S5.
DR InterPro; IPR005712; Ribosomal_S5_bac-type.
DR InterPro; IPR005324; Ribosomal_S5_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR013810; Ribosomal_S5_N.
DR InterPro; IPR018192; Ribosomal_S5_N_CS.
DR PANTHER; PTHR13718; PTHR13718; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR01021; rpsE_bact; 1.
DR PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Antibiotic resistance;
KW Direct protein sequencing; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:363452"
FT CHAIN 2..167
FT /note="30S ribosomal protein S5"
FT /id="PRO_0000131511"
FT DOMAIN 11..74
FT /note="S5 DRBM"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:363452"
FT VARIANT 20
FT /note="R -> L (in strain: SPCR9; spectinomycin resistant.
FT Not a ram mutation)"
FT VARIANT 21
FT /note="V -> E (in strain: SPCR7; spectinomycin resistant.
FT Not a ram mutation)"
FT VARIANT 22
FT /note="S -> P (in strain: SPCR13 and SPCR15; spectinomycin
FT resistant. Not a ram mutation)"
FT VARIANT 104
FT /note="G -> R (in strain: N-660; suppresses S12
FT streptomycin dependence)"
FT VARIANT 112
FT /note="R -> G (in strain: NEA-314; neamycin resistant)"
FT VARIANT 112
FT /note="R -> L (in strain: N-421 and D-1023; suppresses S12
FT streptomycin-dependence)"
FT VARIANT 112
FT /note="R -> S (in strain: NEA-319; neamycin resistant)"
FT VARIANT 151
FT /note="E -> S (in strain: B)"
FT VARIANT 162..167
FT /note="EEILGK -> G (in strain: 0-1; suppresses an alanyl-
FT tRNA synthetase mutation. Blocks ribosome assembly below 25
FT degrees Celsius)"
FT MUTAGEN 20..29
FT /note="RVSKTVKGGR->AVSKTVKGGA: No effect on mRNA unwinding
FT ability of the ribosome."
FT /evidence="ECO:0000269|PubMed:15652481"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:7OE0"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 45..55
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:7BOF"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:7BOF"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 133..145
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:7O5H"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:7BOG"
SQ SEQUENCE 167 AA; 17603 MW; 0B7EA2CB34018CAB CRC64;
MAHIEKQAGE LQEKLIAVNR VSKTVKGGRI FSFTALTVVG DGNGRVGFGY GKAREVPAAI
QKAMEKARRN MINVALNNGT LQHPVKGVHT GSRVFMQPAS EGTGIIAGGA MRAVLEVAGV
HNVLAKAYGS TNPINVVRAT IDGLENMNSP EMVAAKRGKS VEEILGK
