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30S ribosomal protein S5 (Small ribosomal subunit protein uS5)

 RS5_ECOLI               Reviewed;         167 AA.
P0A7W1; O54299; P02356; Q2M6W8;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 136.
RecName: Full=30S ribosomal protein S5;
AltName: Full=Small ribosomal subunit protein uS5 {ECO:0000303|PubMed:24524803};
Name=rpsE; Synonyms=spc; OrderedLocusNames=b3303, JW3265;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=6222285; DOI=10.1093/nar/11.9.2599;
Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.;
"The spc ribosomal protein operon of Escherichia coli: sequence and
cotranscription of the ribosomal protein genes and a protein export
gene.";
Nucleic Acids Res. 11:2599-2616(1983).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
PROTEIN SEQUENCE OF 2-167, SUBUNIT, ACETYLATION AT ALA-2, VARIANTS,
AND MUTANTS.
STRAIN=B, and K;
PubMed=363452; DOI=10.1016/0014-5793(78)80059-3;
Wittmann-Liebold B., Greuer B.;
"The primary structure of protein S5 from the small subunit of the
Escherichia coli ribosome.";
FEBS Lett. 95:91-98(1978).
[5]
PROTEIN SEQUENCE OF 15-23, SUBUNIT, AND VARIANT SPECTINOMYCIN
RESISTANT.
STRAIN=B;
PubMed=4273819; DOI=10.1007/BF00333767;
DeWilde M., Wittmann-Liebold B.;
"Localization of the amino-acid exchange in protein S5 from an
Escherichia coli mutant resistant to spectinomycin.";
Mol. Gen. Genet. 127:273-276(1973).
[6]
INVOLVEMENT IN FORMATION OF THE EF-G/RIBOSOME COMPLEX.
STRAIN=B/2;
PubMed=4346030; DOI=10.1073/pnas.70.1.151;
Marsh R.C., Parmeggiani A.;
"Requirement of proteins S5 and S9 from 30S subunits for the ribosome-
dependent GTPase activity of elongation factor G.";
Proc. Natl. Acad. Sci. U.S.A. 70:151-155(1973).
[7]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[8]
NOMENCLATURE.
PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
Williamson J.R., Wilson D., Yonath A., Yusupov M.;
"A new system for naming ribosomal proteins.";
Curr. Opin. Struct. Biol. 24:165-169(2014).
[9]
CHARACTERIZATION OF VARIANTS.
STRAIN=O17;
PubMed=2138078;
Bilgin N., Richter A.A., Ehrenberg M., Dahlberg A.E., Kurland C.G.;
"Ribosomal RNA and protein mutants resistant to spectinomycin.";
EMBO J. 9:735-739(1990).
[10]
CROSS-LINKING TO MRNA.
PubMed=1712292;
Rinke-Appel J., Juenke N., Stade K., Brimacombe R.;
"The path of mRNA through the Escherichia coli ribosome; site-directed
cross-linking of mRNA analogues carrying a photo-reactive label at
various points 3' to the decoding site.";
EMBO J. 10:2195-2202(1991).
[11]
ROLE IN MRNA HELICASE ACTIVITY, AND MUTAGENESIS.
STRAIN=MRE-600;
PubMed=15652481; DOI=10.1016/j.cell.2004.11.042;
Takyar S., Hickerson R.P., Noller H.F.;
"mRNA helicase activity of the ribosome.";
Cell 120:49-58(2005).
[12]
MASS SPECTROMETRY, AND SUBUNIT.
STRAIN=K12 / ATCC 25404 / DSM 5698 / NCIMB 11290;
PubMed=10094780; DOI=10.1006/abio.1998.3077;
Arnold R.J., Reilly J.P.;
"Observation of Escherichia coli ribosomal proteins and their
posttranslational modifications by mass spectrometry.";
Anal. Biochem. 269:105-112(1999).
[13]
REVIEW ON TRANSLATIONAL ACCURACY.
Kurland C.G., Hughes D., Ehrenberg M.;
"Limitations of translational accuracy.";
(In) Neidhardt F.C., Curtiss R. III, Ingraham J.L., Lin E.C.C.,
Low K.B. Magasanik B., Reznikoff W.S., Riley M., Schaechter M.,
Umbarger H.E. (eds.);
Escherichia coli and Salmonella: Cellular and molecular biology (2nd
ed.), pp.979-1004, American Society for Microbiology Press, Washington
D.C. (1996).
[14]
3D-STRUCTURE MODELING, AND SUBUNIT.
PubMed=12244297; DOI=10.1038/nsb841;
Tung C.-S., Joseph S., Sanbonmatsu K.Y.;
"All-atom homology model of the Escherichia coli 30S ribosomal
subunit.";
Nat. Struct. Biol. 9:750-755(2002).
[15]
STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS), AND SUBUNIT.
STRAIN=MRE-600;
PubMed=12809609; DOI=10.1016/S0092-8674(03)00427-6;
Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M.,
Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S.,
Frank J.;
"Study of the structural dynamics of the E. coli 70S ribosome using
real-space refinement.";
Cell 113:789-801(2003).
[16]
X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME
STRUCTURES, AND SUBUNIT.
STRAIN=MRE-600;
PubMed=16272117; DOI=10.1126/science.1117230;
Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W.,
Vila-Sanjurjo A., Holton J.M., Cate J.H.D.;
"Structures of the bacterial ribosome at 3.5 A resolution.";
Science 310:827-834(2005).
[17]
STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 70S RIBOSOME IN
COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
PubMed=27906160; DOI=10.1038/nature20822;
Ma C., Kurita D., Li N., Chen Y., Himeno H., Gao N.;
"Mechanistic insights into the alternative translation termination by
ArfA and RF2.";
Nature 541:550-553(2017).
[18]
STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 70S RIBOSOME IN
COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
PubMed=27906161; DOI=10.1038/nature20821;
Huter P., Mueller C., Beckert B., Arenz S., Berninghausen O.,
Beckmann R., Wilson D.N.;
"Structural basis for ArfA-RF2-mediated translation termination on
mRNAs lacking stop codons.";
Nature 541:546-549(2017).
[19]
STRUCTURE BY ELECTRON MICROSCOPY (2.97 ANGSTROMS) OF 70S RIBOSOME IN
COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
PubMed=27934701; DOI=10.1126/science.aai9127;
James N.R., Brown A., Gordiyenko Y., Ramakrishnan V.;
"Translational termination without a stop codon.";
Science 354:1437-1440(2016).
[20]
STRUCTURE BY ELECTRON MICROSCOPY (3.52 ANGSTROMS) OF 70S RIBOSOME IN
COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
PubMed=28077875; DOI=10.1038/nature21053;
Zeng F., Chen Y., Remis J., Shekhar M., Phillips J.C., Tajkhorshid E.,
Jin H.;
"Structural basis of co-translational quality control by ArfA and RF2
bound to ribosome.";
Nature 541:554-557(2017).
-!- FUNCTION: With S4 and S12 plays an important role in translational
accuracy. Many suppressors of streptomycin-dependent mutants of
protein S12 are found in this protein, some but not all of which
decrease translational accuracy (ram, ribosomal ambiguity
mutations). {ECO:0000269|PubMed:15652481}.
-!- FUNCTION: Located at the back of the 30S subunit body where it
stabilizes the conformation of the head with respect to the body.
{ECO:0000269|PubMed:15652481}.
-!- FUNCTION: The physical location of this protein suggests it may
also play a role in mRNA unwinding by the ribosome, possibly by
forming part of a processivity clamp.
{ECO:0000269|PubMed:15652481}.
-!- SUBUNIT: Part of the 30S ribosomal subunit (PubMed:363452,
PubMed:4273819, PubMed:12809609, PubMed:16272117, PubMed:27934701,
PubMed:10094780, PubMed:12244297, PubMed:27906160,
PubMed:27906161, PubMed:28077875). Contacts proteins S4 and S8.
With proteins S4 and S5 encircles the mRNA as it enters the
ribosome, which may play a role in mRNA helicase processivity
(PubMed:15652481). Can be cross-linked to mRNA (PubMed:1712292).
{ECO:0000269|PubMed:10094780, ECO:0000269|PubMed:12244297,
ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:15652481,
ECO:0000269|PubMed:16272117, ECO:0000269|PubMed:1712292,
ECO:0000269|PubMed:27906160, ECO:0000269|PubMed:27906161,
ECO:0000269|PubMed:27934701, ECO:0000269|PubMed:28077875,
ECO:0000269|PubMed:363452, ECO:0000269|PubMed:4273819}.
-!- INTERACTION:
P0A7C2:lexA; NbExp=2; IntAct=EBI-543949, EBI-553416;
P30850:rnb; NbExp=3; IntAct=EBI-543949, EBI-557325;
P0ADZ0:rplW; NbExp=2; IntAct=EBI-543949, EBI-542264;
-!- DOMAIN: The N-terminal domain interacts with the head of the 30S
subunit; the C-terminal domain interacts with the body and
contacts protein S4. The interaction surface between S4 and S5 is
involved in control of translational fidelity.
-!- MASS SPECTROMETRY: Mass=17514.8; Method=MALDI; Range=2-167;
Evidence={ECO:0000269|PubMed:10094780};
-!- MISCELLANEOUS: Altered S5 proteins have been identified in a
number of mutants. Some mutations in S5 have been shown to
increase translational error frequencies.
-!- MISCELLANEOUS: Some mutants in this protein can partially suppress
an alanyl-tRNA synthetase mutant.
-!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
{ECO:0000305}.
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EMBL; X01563; CAA25722.1; -; Genomic_DNA.
EMBL; U18997; AAA58100.1; -; Genomic_DNA.
EMBL; U00096; AAC76328.1; -; Genomic_DNA.
EMBL; AP009048; BAE77988.1; -; Genomic_DNA.
PIR; B65123; R3EC5.
RefSeq; NP_417762.1; NC_000913.3.
RefSeq; WP_000940121.1; NZ_LN832404.1.
PDB; 1EG0; EM; 11.50 A; B=1-148.
PDB; 1M5G; Model; -; E=10-159.
PDB; 2YKR; EM; 9.80 A; E=10-159.
PDB; 3J9Y; EM; 3.90 A; e=1-167.
PDB; 3J9Z; EM; 3.60 A; SE=2-167.
PDB; 3JA1; EM; 3.60 A; SE=2-167.
PDB; 3JBU; EM; 3.64 A; E=1-167.
PDB; 3JBV; EM; 3.32 A; E=1-167.
PDB; 3JCD; EM; 3.70 A; e=1-167.
PDB; 3JCE; EM; 3.20 A; e=1-167.
PDB; 3JCJ; EM; 3.70 A; k=1-167.
PDB; 3JCN; EM; 4.60 A; f=1-159.
PDB; 4A2I; EM; 16.50 A; E=10-159.
PDB; 4ADV; EM; 13.50 A; E=2-167.
PDB; 4U1U; X-ray; 2.95 A; AE/CE=10-159.
PDB; 4U1V; X-ray; 3.00 A; AE/CE=10-159.
PDB; 4U20; X-ray; 2.90 A; AE/CE=10-159.
PDB; 4U24; X-ray; 2.90 A; AE/CE=10-159.
PDB; 4U25; X-ray; 2.90 A; AE/CE=10-159.
PDB; 4U26; X-ray; 2.80 A; AE/CE=10-159.
PDB; 4U27; X-ray; 2.80 A; AE/CE=10-159.
PDB; 4V47; EM; 12.30 A; BE=2-167.
PDB; 4V48; EM; 11.50 A; BE=2-167.
PDB; 4V4H; X-ray; 3.46 A; AE/CE=1-167.
PDB; 4V4Q; X-ray; 3.46 A; AE/CE=2-167.
PDB; 4V4V; EM; 15.00 A; AE=10-157.
PDB; 4V4W; EM; 15.00 A; AE=10-157.
PDB; 4V50; X-ray; 3.22 A; AE/CE=2-167.
PDB; 4V52; X-ray; 3.21 A; AE/CE=2-167.
PDB; 4V53; X-ray; 3.54 A; AE/CE=2-167.
PDB; 4V54; X-ray; 3.30 A; AE/CE=2-167.
PDB; 4V55; X-ray; 4.00 A; AE/CE=2-167.
PDB; 4V56; X-ray; 3.93 A; AE/CE=2-167.
PDB; 4V57; X-ray; 3.50 A; AE/CE=2-167.
PDB; 4V5B; X-ray; 3.74 A; BE/DE=2-167.
PDB; 4V5H; EM; 5.80 A; AE=10-159.
PDB; 4V5Y; X-ray; 4.45 A; AE/CE=2-167.
PDB; 4V64; X-ray; 3.50 A; AE/CE=2-167.
PDB; 4V65; EM; 9.00 A; AS=1-159.
PDB; 4V66; EM; 9.00 A; AS=1-159.
PDB; 4V69; EM; 6.70 A; AE=10-159.
PDB; 4V6C; X-ray; 3.19 A; AE/CE=1-167.
PDB; 4V6D; X-ray; 3.81 A; AE/CE=1-167.
PDB; 4V6E; X-ray; 3.71 A; AE/CE=1-167.
PDB; 4V6K; EM; 8.25 A; BI=1-167.
PDB; 4V6L; EM; 13.20 A; AI=1-167.
PDB; 4V6M; EM; 7.10 A; AE=2-167.
PDB; 4V6N; EM; 12.10 A; BH=2-167.
PDB; 4V6O; EM; 14.70 A; AH=2-167.
PDB; 4V6P; EM; 13.50 A; AH=2-167.
PDB; 4V6Q; EM; 11.50 A; AH=2-167.
PDB; 4V6R; EM; 11.50 A; AH=2-167.
PDB; 4V6S; EM; 13.10 A; BG=2-167.
PDB; 4V6T; EM; 8.30 A; AE=10-159.
PDB; 4V6V; EM; 9.80 A; AE=2-167.
PDB; 4V6Y; EM; 12.00 A; AE=10-159.
PDB; 4V6Z; EM; 12.00 A; AE=10-159.
PDB; 4V70; EM; 17.00 A; AE=10-159.
PDB; 4V71; EM; 20.00 A; AE=10-159.
PDB; 4V72; EM; 13.00 A; AE=10-159.
PDB; 4V73; EM; 15.00 A; AE=10-159.
PDB; 4V74; EM; 17.00 A; AE=10-159.
PDB; 4V75; EM; 12.00 A; AE=10-159.
PDB; 4V76; EM; 17.00 A; AE=10-159.
PDB; 4V77; EM; 17.00 A; AE=10-159.
PDB; 4V78; EM; 20.00 A; AE=10-159.
PDB; 4V79; EM; 15.00 A; AE=10-159.
PDB; 4V7A; EM; 9.00 A; AE=10-159.
PDB; 4V7B; EM; 6.80 A; AE=1-167.
PDB; 4V7C; EM; 7.60 A; AE=2-167.
PDB; 4V7D; EM; 7.60 A; BE=2-167.
PDB; 4V7I; EM; 9.60 A; BE=1-167.
PDB; 4V7S; X-ray; 3.25 A; AE/CE=10-159.
PDB; 4V7T; X-ray; 3.19 A; AE/CE=10-159.
PDB; 4V7U; X-ray; 3.10 A; AE/CE=10-159.
PDB; 4V7V; X-ray; 3.29 A; AE/CE=10-159.
PDB; 4V85; X-ray; 3.20 A; E=1-167.
PDB; 4V89; X-ray; 3.70 A; AE=1-167.
PDB; 4V9C; X-ray; 3.30 A; AE/CE=1-167.
PDB; 4V9D; X-ray; 3.00 A; AE/BE=10-159.
PDB; 4V9O; X-ray; 2.90 A; BE/DE/FE/HE=1-167.
PDB; 4V9P; X-ray; 2.90 A; BE/DE/FE/HE=1-167.
PDB; 4WF1; X-ray; 3.09 A; AE/CE=10-159.
PDB; 4WOI; X-ray; 3.00 A; AE/DE=1-167.
PDB; 4WWW; X-ray; 3.10 A; QE/XE=10-159.
PDB; 4YBB; X-ray; 2.10 A; AE/BE=10-164.
PDB; 5AFI; EM; 2.90 A; e=1-167.
PDB; 5H5U; EM; 3.00 A; l=2-167.
PDB; 5IQR; EM; 3.00 A; j=1-167.
PDB; 5IT8; X-ray; 3.12 A; AE/BE=10-164.
PDB; 5J5B; X-ray; 2.80 A; AE/BE=10-164.
PDB; 5J7L; X-ray; 3.00 A; AE/BE=10-164.
PDB; 5J88; X-ray; 3.32 A; AE/BE=10-164.
PDB; 5J8A; X-ray; 3.10 A; AE/BE=10-164.
PDB; 5J91; X-ray; 2.96 A; AE/BE=10-164.
PDB; 5JC9; X-ray; 3.03 A; AE/BE=10-164.
PDB; 5JTE; EM; 3.60 A; AE=1-167.
PDB; 5JU8; EM; 3.60 A; AE=1-167.
PDB; 5KCR; EM; 3.60 A; 1e=1-167.
PDB; 5KCS; EM; 3.90 A; 1e=1-167.
PDB; 5KPS; EM; 3.90 A; 10=1-167.
PDB; 5KPV; EM; 4.10 A; 9=1-167.
PDB; 5KPW; EM; 3.90 A; 9=1-167.
PDB; 5KPX; EM; 3.90 A; 9=1-167.
PDB; 5L3P; EM; 3.70 A; e=1-167.
PDB; 5LZA; EM; 3.60 A; e=10-166.
PDB; 5LZB; EM; 5.30 A; e=10-166.
PDB; 5LZC; EM; 4.80 A; e=10-166.
PDB; 5LZD; EM; 3.40 A; e=10-166.
PDB; 5LZE; EM; 3.50 A; e=10-166.
PDB; 5LZF; EM; 4.60 A; e=10-166.
PDB; 5MDV; EM; 2.97 A; j=1-167.
PDB; 5MDW; EM; 3.06 A; j=1-167.
PDB; 5MDY; EM; 3.35 A; j=1-167.
PDB; 5MDZ; EM; 3.10 A; j=1-167.
PDB; 5ME0; EM; 13.50 A; E=1-167.
PDB; 5ME1; EM; 13.50 A; E=1-167.
PDB; 5MGP; EM; 3.10 A; e=10-166.
PDB; 5MY1; EM; 7.60 A; E=2-167.
PDB; 5NO2; EM; 5.16 A; E=10-164.
PDB; 5NO3; EM; 5.16 A; E=10-164.
PDB; 5NO4; EM; 5.16 A; E=10-164.
PDB; 5NP6; EM; 3.60 A; H=10-166.
PDB; 5NWY; EM; 2.93 A; 4=1-166.
PDB; 5O2R; EM; 3.40 A; e=10-166.
PDB; 5U4I; EM; 3.50 A; e=1-167.
PDB; 5U4J; EM; 3.70 A; e=1-167.
PDB; 5U9F; EM; 3.20 A; E=1-167.
PDB; 5U9G; EM; 3.20 A; E=1-167.
PDB; 5UYK; EM; 3.90 A; E=10-166.
PDB; 5UYL; EM; 3.60 A; E=10-166.
PDB; 5UYM; EM; 3.20 A; E=10-166.
PDB; 5UYN; EM; 4.00 A; E=10-166.
PDB; 5UYP; EM; 3.90 A; E=10-166.
PDB; 5UYQ; EM; 3.80 A; E=10-166.
PDB; 5UZ4; EM; 5.80 A; E=1-167.
PDBsum; 1EG0; -.
PDBsum; 1M5G; -.
PDBsum; 2YKR; -.
PDBsum; 3J9Y; -.
PDBsum; 3J9Z; -.
PDBsum; 3JA1; -.
PDBsum; 3JBU; -.
PDBsum; 3JBV; -.
PDBsum; 3JCD; -.
PDBsum; 3JCE; -.
PDBsum; 3JCJ; -.
PDBsum; 3JCN; -.
PDBsum; 4A2I; -.
PDBsum; 4ADV; -.
PDBsum; 4U1U; -.
PDBsum; 4U1V; -.
PDBsum; 4U20; -.
PDBsum; 4U24; -.
PDBsum; 4U25; -.
PDBsum; 4U26; -.
PDBsum; 4U27; -.
PDBsum; 4V47; -.
PDBsum; 4V48; -.
PDBsum; 4V4H; -.
PDBsum; 4V4Q; -.
PDBsum; 4V4V; -.
PDBsum; 4V4W; -.
PDBsum; 4V50; -.
PDBsum; 4V52; -.
PDBsum; 4V53; -.
PDBsum; 4V54; -.
PDBsum; 4V55; -.
PDBsum; 4V56; -.
PDBsum; 4V57; -.
PDBsum; 4V5B; -.
PDBsum; 4V5H; -.
PDBsum; 4V5Y; -.
PDBsum; 4V64; -.
PDBsum; 4V65; -.
PDBsum; 4V66; -.
PDBsum; 4V69; -.
PDBsum; 4V6C; -.
PDBsum; 4V6D; -.
PDBsum; 4V6E; -.
PDBsum; 4V6K; -.
PDBsum; 4V6L; -.
PDBsum; 4V6M; -.
PDBsum; 4V6N; -.
PDBsum; 4V6O; -.
PDBsum; 4V6P; -.
PDBsum; 4V6Q; -.
PDBsum; 4V6R; -.
PDBsum; 4V6S; -.
PDBsum; 4V6T; -.
PDBsum; 4V6V; -.
PDBsum; 4V6Y; -.
PDBsum; 4V6Z; -.
PDBsum; 4V70; -.
PDBsum; 4V71; -.
PDBsum; 4V72; -.
PDBsum; 4V73; -.
PDBsum; 4V74; -.
PDBsum; 4V75; -.
PDBsum; 4V76; -.
PDBsum; 4V77; -.
PDBsum; 4V78; -.
PDBsum; 4V79; -.
PDBsum; 4V7A; -.
PDBsum; 4V7B; -.
PDBsum; 4V7C; -.
PDBsum; 4V7D; -.
PDBsum; 4V7I; -.
PDBsum; 4V7S; -.
PDBsum; 4V7T; -.
PDBsum; 4V7U; -.
PDBsum; 4V7V; -.
PDBsum; 4V85; -.
PDBsum; 4V89; -.
PDBsum; 4V9C; -.
PDBsum; 4V9D; -.
PDBsum; 4V9O; -.
PDBsum; 4V9P; -.
PDBsum; 4WF1; -.
PDBsum; 4WOI; -.
PDBsum; 4WWW; -.
PDBsum; 4YBB; -.
PDBsum; 5AFI; -.
PDBsum; 5H5U; -.
PDBsum; 5IQR; -.
PDBsum; 5IT8; -.
PDBsum; 5J5B; -.
PDBsum; 5J7L; -.
PDBsum; 5J88; -.
PDBsum; 5J8A; -.
PDBsum; 5J91; -.
PDBsum; 5JC9; -.
PDBsum; 5JTE; -.
PDBsum; 5JU8; -.
PDBsum; 5KCR; -.
PDBsum; 5KCS; -.
PDBsum; 5KPS; -.
PDBsum; 5KPV; -.
PDBsum; 5KPW; -.
PDBsum; 5KPX; -.
PDBsum; 5L3P; -.
PDBsum; 5LZA; -.
PDBsum; 5LZB; -.
PDBsum; 5LZC; -.
PDBsum; 5LZD; -.
PDBsum; 5LZE; -.
PDBsum; 5LZF; -.
PDBsum; 5MDV; -.
PDBsum; 5MDW; -.
PDBsum; 5MDY; -.
PDBsum; 5MDZ; -.
PDBsum; 5ME0; -.
PDBsum; 5ME1; -.
PDBsum; 5MGP; -.
PDBsum; 5MY1; -.
PDBsum; 5NO2; -.
PDBsum; 5NO3; -.
PDBsum; 5NO4; -.
PDBsum; 5NP6; -.
PDBsum; 5NWY; -.
PDBsum; 5O2R; -.
PDBsum; 5U4I; -.
PDBsum; 5U4J; -.
PDBsum; 5U9F; -.
PDBsum; 5U9G; -.
PDBsum; 5UYK; -.
PDBsum; 5UYL; -.
PDBsum; 5UYM; -.
PDBsum; 5UYN; -.
PDBsum; 5UYP; -.
PDBsum; 5UYQ; -.
PDBsum; 5UZ4; -.
ProteinModelPortal; P0A7W1; -.
SMR; P0A7W1; -.
BioGrid; 4263408; 155.
DIP; DIP-10781N; -.
IntAct; P0A7W1; 193.
MINT; MINT-6478202; -.
STRING; 316385.ECDH10B_3478; -.
iPTMnet; P0A7W1; -.
PaxDb; P0A7W1; -.
PRIDE; P0A7W1; -.
EnsemblBacteria; AAC76328; AAC76328; b3303.
EnsemblBacteria; BAE77988; BAE77988; BAE77988.
GeneID; 31655992; -.
GeneID; 947795; -.
KEGG; ecj:JW3265; -.
KEGG; eco:b3303; -.
PATRIC; fig|1411691.4.peg.3428; -.
EchoBASE; EB0897; -.
EcoGene; EG10904; rpsE.
eggNOG; COG0098; LUCA.
HOGENOM; HOG000072595; -.
InParanoid; P0A7W1; -.
KO; K02988; -.
PhylomeDB; P0A7W1; -.
BioCyc; EcoCyc:EG10904-MONOMER; -.
BioCyc; MetaCyc:EG10904-MONOMER; -.
EvolutionaryTrace; P0A7W1; -.
PRO; PR:P0A7W1; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:CAFA.
GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
GO; GO:1990145; P:maintenance of translational fidelity; IMP:EcoCyc.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
GO; GO:0000028; P:ribosomal small subunit assembly; IDA:CAFA.
Gene3D; 3.30.230.10; -; 1.
HAMAP; MF_01307_B; Ribosomal_S5_B; 1.
InterPro; IPR000851; Ribosomal_S5.
InterPro; IPR005712; Ribosomal_S5_bac-type.
InterPro; IPR005324; Ribosomal_S5_C.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
InterPro; IPR013810; Ribosomal_S5_N.
InterPro; IPR018192; Ribosomal_S5_N_CS.
PANTHER; PTHR13718; PTHR13718; 1.
Pfam; PF00333; Ribosomal_S5; 1.
Pfam; PF03719; Ribosomal_S5_C; 1.
SUPFAM; SSF54211; SSF54211; 1.
TIGRFAMs; TIGR01021; rpsE_bact; 1.
PROSITE; PS00585; RIBOSOMAL_S5; 1.
PROSITE; PS50881; S5_DSRBD; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Antibiotic resistance; Complete proteome;
Direct protein sequencing; Reference proteome; Ribonucleoprotein;
Ribosomal protein; RNA-binding; rRNA-binding.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:363452}.
CHAIN 2 167 30S ribosomal protein S5.
/FTId=PRO_0000131511.
DOMAIN 11 74 S5 DRBM.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:363452}.
VARIANT 20 20 R -> L (in strain: SPCR9; spectinomycin
resistant. Not a ram mutation).
VARIANT 21 21 V -> E (in strain: SPCR7; spectinomycin
resistant. Not a ram mutation).
VARIANT 22 22 S -> P (in strain: SPCR13 and SPCR15;
spectinomycin resistant. Not a ram
mutation).
VARIANT 104 104 G -> R (in strain: N-660; suppresses S12
streptomycin dependence).
VARIANT 112 112 R -> G (in strain: NEA-314; neamycin
resistant).
VARIANT 112 112 R -> L (in strain: N-421 and D-1023;
suppresses S12 streptomycin-dependence).
VARIANT 112 112 R -> S (in strain: NEA-319; neamycin
resistant).
VARIANT 151 151 E -> S (in strain: B).
VARIANT 162 167 EEILGK -> G (in strain: 0-1; suppresses
an alanyl-tRNA synthetase mutation.
Blocks ribosome assembly below 25 degrees
Celsius).
MUTAGEN 20 29 RVSKTVKGGR->AVSKTVKGGA: No effect on mRNA
unwinding ability of the ribosome.
{ECO:0000269|PubMed:15652481}.
STRAND 13 22 {ECO:0000244|PDB:4U26}.
STRAND 26 28 {ECO:0000244|PDB:4V9D}.
STRAND 31 40 {ECO:0000244|PDB:4U26}.
STRAND 42 44 {ECO:0000244|PDB:4U26}.
STRAND 46 49 {ECO:0000244|PDB:4U26}.
STRAND 52 55 {ECO:0000244|PDB:4U26}.
HELIX 56 68 {ECO:0000244|PDB:4U26}.
STRAND 69 72 {ECO:0000244|PDB:4U27}.
STRAND 78 80 {ECO:0000244|PDB:4U20}.
STRAND 85 89 {ECO:0000244|PDB:4U26}.
STRAND 92 97 {ECO:0000244|PDB:4U26}.
STRAND 101 103 {ECO:0000244|PDB:4V9O}.
TURN 109 111 {ECO:0000244|PDB:4U26}.
HELIX 112 118 {ECO:0000244|PDB:4U26}.
STRAND 120 123 {ECO:0000244|PDB:4V50}.
STRAND 124 129 {ECO:0000244|PDB:4U26}.
HELIX 133 146 {ECO:0000244|PDB:4U26}.
HELIX 150 152 {ECO:0000244|PDB:4V9O}.
HELIX 153 156 {ECO:0000244|PDB:4U26}.
SEQUENCE 167 AA; 17603 MW; 0B7EA2CB34018CAB CRC64;
MAHIEKQAGE LQEKLIAVNR VSKTVKGGRI FSFTALTVVG DGNGRVGFGY GKAREVPAAI
QKAMEKARRN MINVALNNGT LQHPVKGVHT GSRVFMQPAS EGTGIIAGGA MRAVLEVAGV
HNVLAKAYGS TNPINVVRAT IDGLENMNSP EMVAAKRGKS VEEILGK


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