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Entry: P02359
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ID   RS7_ECOLI               Reviewed;         179 AA.
AC   P02359; Q2M706;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   26-NOV-2014, entry version 168.
DE   RecName: Full=30S ribosomal protein S7;
GN   Name=rpsG; OrderedLocusNames=b3341, JW3303;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
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   [3]
RP   PROTEIN SEQUENCE OF 2-179.
RC   STRAIN=B, and K;
RX   PubMed=385062; DOI=10.1016/S0300-9084(79)80207-2;
RA   Reinbolt J., Tritsch D., Wittmann-Liebold B.;
RT   "The primary structure of ribosomal protein S7 from E. coli strains K
RT   and B.";
RL   Biochimie 61:501-522(1979).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81 AND 148-179.
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
RC   STRAIN=B/R;
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-173.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=1398129; DOI=10.1016/0378-1119(92)90014-G;
RA   Johanson U., Hughes D.;
RT   "Comparison of the complete sequence of the str operon in Salmonella
RT   typhimurium and Escherichia coli.";
RL   Gene 120:93-98(1992).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-156.
RC   STRAIN=L44;
RA   Weigel C.T.O.;
RL   Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   PROTEIN SEQUENCE OF 111-131, 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   CROSS-LINKING TO IF3.
RC   STRAIN=B;
RX   PubMed=7000779;
RA   MacKeen L.A., Kahan L., Wahba A.J., Schwartz I.;
RT   "Photochemical cross-linking of initiation factor-3 to Escherichia
RT   coli 30 S ribosomal subunits.";
RL   J. Biol. Chem. 255:10526-10531(1980).
RN   [10]
RP   CROSS-LINKING TO IF3.
RC   STRAIN=MRE-600;
RX   PubMed=6349681; DOI=10.1021/bi00282a020;
RA   Boileau G., Butler P., Hershey J.W.B., Traut R.R.;
RT   "Direct cross-links between initiation factors 1, 2, and 3 and
RT   ribosomal proteins promoted by 2-iminothiolane.";
RL   Biochemistry 22:3162-3170(1983).
RN   [11]
RP   ROLE IN SUBUNIT ASSEMBLY.
RC   STRAIN=K12 / D10;
RX   PubMed=2461734; DOI=10.1021/bi00418a057;
RA   Nowotny V., Nierhaus K.H.;
RT   "Assembly of the 30S subunit from Escherichia coli ribosomes occurs
RT   via two assembly domains which are initiated by S4 and S7.";
RL   Biochemistry 27:7051-7055(1988).
RN   [12]
RP   MECHANISM OF TRANSLATION REGULATION.
RC   STRAIN=K12;
RX   PubMed=7507167; DOI=10.1016/S0022-2836(05)80020-8;
RA   Saito K., Mattheakis L.C., Nomura M.;
RT   "Post-transcriptional regulation of the str operon in Escherichia
RT   coli. Ribosomal protein S7 inhibits coupled translation of S7 but not
RT   its independent translation.";
RL   J. Mol. Biol. 235:111-124(1994).
RN   [13]
RP   CROSS-LINKING TO THE TRNA CENTRAL FOLD.
RC   STRAIN=MRE-600;
RX   PubMed=8524654; DOI=10.1093/nar/23.22.4635;
RA   Osswald M., Doering T., Brimacombe R.;
RT   "The ribosomal neighbourhood of the central fold of tRNA: cross-links
RT   from position 47 of tRNA located at the A, P or E site.";
RL   Nucleic Acids Res. 23:4635-4641(1995).
RN   [14]
RP   CROSS-LINKING TO MRNA.
RC   STRAIN=B, and K;
RX   PubMed=10606263; DOI=10.1017/S1355838299991550;
RA   Greuer B., Thiede B., Brimacombe R.;
RT   "The cross-link from the upstream region of mRNA to ribosomal protein
RT   S7 is located in the C-terminal peptide: experimental verification of
RT   a prediction from modeling studies.";
RL   RNA 5:1521-1525(1999).
RN   [15]
RP   MUTAGENESIS OF CONSERVED SURFACE RESIDUES.
RC   STRAIN=K;
RX   PubMed=10772857; DOI=10.1006/jmbi.2000.3563;
RA   Fredrick K., Dunny G.M., Noller H.F.;
RT   "Tagging ribosomal protein S7 allows rapid identification of mutants
RT   defective in assembly and function of 30S subunits.";
RL   J. Mol. Biol. 298:379-394(2000).
RN   [16]
RP   MUTAGENESIS OF CONSERVED RESIDUES.
RC   STRAIN=K12;
RX   PubMed=11160889; DOI=10.1093/nar/29.3.677;
RA   Robert F., Brakier-Gingras L.;
RT   "Ribosomal protein S7 from Escherichia coli uses the same determinants
RT   to bind 16S ribosomal RNA and its messenger RNA.";
RL   Nucleic Acids Res. 29:677-682(2001).
RN   [17]
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   [18]
RP   MODELING OF IF-3/30S SUBUNIT INTERACTION.
RX   PubMed=11684020; DOI=10.1016/S1097-2765(01)00356-2;
RA   Dallas A., Noller H.F.;
RT   "Interaction of translation initiation factor 3 with the 30S ribosomal
RT   subunit.";
RL   Mol. Cell 8:855-864(2001).
RN   [19]
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   [20]
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   [21]
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).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds
CC       directly to 16S rRNA where it nucleates assembly of the head
CC       domain of the 30S subunit. Is located at the subunit interface
CC       close to the decoding center, where it has been shown to contact
CC       mRNA. Has been shown to contact tRNA in both the P and E sites; it
CC       probably blocks exit of the E site tRNA.
CC       {ECO:0000269|PubMed:2461734}.
CC   -!- FUNCTION: Protein S7 is also a translational repressor protein; it
CC       regulates the expression of the str operon members to different
CC       degrees by binding to its mRNA. {ECO:0000269|PubMed:2461734}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S9
CC       and S11 (By similarity). Cross-links to IF3 and the P and E site
CC       tRNAs. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P0A707:infC; NbExp=3; IntAct=EBI-543074, EBI-546262;
CC       P37765:rluB; NbExp=3; IntAct=EBI-543074, EBI-561550;
CC       P0A850:tig; NbExp=3; IntAct=EBI-543074, EBI-544862;
CC   -!- MASS SPECTROMETRY: Mass=19888.7; Method=MALDI; Range=2-179;
CC       Evidence={ECO:0000269|PubMed:10094780};
CC   -!- MISCELLANEOUS: The strain K12 sequence is shown.
CC   -!- MISCELLANEOUS: Has been predicted to contact the N-terminal domain
CC       of IF-3 based on footprint studies; exactly how IF-3 interacts
CC       with the 30S subunit is controversial.
CC       {ECO:0000305|PubMed:11684020}.
CC   -!- SIMILARITY: Belongs to the ribosomal protein S7P family.
CC       {ECO:0000305}.
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DR   EMBL; U18997; AAA58138.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76366.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77950.1; -; Genomic_DNA.
DR   EMBL; V00355; CAA23649.1; -; Genomic_DNA.
DR   EMBL; J01689; AAA50990.1; -; Genomic_DNA.
DR   EMBL; X64592; CAA45881.1; -; Genomic_DNA.
DR   EMBL; X65735; CAA46644.1; -; Genomic_DNA.
DR   EMBL; J01688; AAA50989.1; -; Genomic_DNA.
DR   PIR; H65127; R3EC7K.
DR   RefSeq; NP_417800.1; NC_000913.3.
DR   RefSeq; YP_492091.1; NC_007779.1.
DR   PDB; 1EG0; EM; 11.50 A; D=1-146.
DR   PDB; 1M5G; Model; -; G=3-156.
DR   PDB; 1ML5; EM; 14.00 A; J=1-156.
DR   PDB; 1P6G; EM; 12.30 A; G=2-179.
DR   PDB; 1P87; EM; 11.50 A; G=2-179.
DR   PDB; 1VS5; X-ray; 3.46 A; G=1-179.
DR   PDB; 1VS7; X-ray; 3.46 A; G=1-179.
DR   PDB; 2AVY; X-ray; 3.46 A; G=2-179.
DR   PDB; 2AW7; X-ray; 3.46 A; G=2-179.
DR   PDB; 2GY9; EM; 15.00 A; G=20-156.
DR   PDB; 2GYB; EM; 15.00 A; G=20-156.
DR   PDB; 2I2P; X-ray; 3.22 A; G=2-179.
DR   PDB; 2I2U; X-ray; 3.22 A; G=2-179.
DR   PDB; 2QAL; X-ray; 3.21 A; G=2-179.
DR   PDB; 2QAN; X-ray; 3.21 A; G=2-179.
DR   PDB; 2QB9; X-ray; 3.54 A; G=2-179.
DR   PDB; 2QBB; X-ray; 3.54 A; G=2-179.
DR   PDB; 2QBD; X-ray; 3.30 A; G=2-179.
DR   PDB; 2QBF; X-ray; 3.30 A; G=2-179.
DR   PDB; 2QBH; X-ray; 4.00 A; G=2-179.
DR   PDB; 2QBJ; X-ray; 4.00 A; G=2-179.
DR   PDB; 2QOU; X-ray; 3.93 A; G=2-179.
DR   PDB; 2QOW; X-ray; 3.93 A; G=2-179.
DR   PDB; 2QOY; X-ray; 3.50 A; G=2-179.
DR   PDB; 2QP0; X-ray; 3.50 A; G=2-179.
DR   PDB; 2VHO; X-ray; 3.74 A; G=2-179.
DR   PDB; 2VHP; X-ray; 3.74 A; G=2-179.
DR   PDB; 2WWL; EM; 5.80 A; G=3-152.
DR   PDB; 2YKR; EM; 9.80 A; G=2-152.
DR   PDB; 2Z4K; X-ray; 4.45 A; G=2-179.
DR   PDB; 2Z4M; X-ray; 4.45 A; G=2-179.
DR   PDB; 3DF1; X-ray; 3.50 A; G=2-178.
DR   PDB; 3DF3; X-ray; 3.50 A; G=2-178.
DR   PDB; 3E1A; EM; -; U=1-179.
DR   PDB; 3E1C; EM; -; U=1-179.
DR   PDB; 3FIH; EM; 6.70 A; G=3-152.
DR   PDB; 3I1M; X-ray; 3.19 A; G=1-179.
DR   PDB; 3I1O; X-ray; 3.19 A; G=1-179.
DR   PDB; 3I1Q; X-ray; 3.81 A; G=1-179.
DR   PDB; 3I1S; X-ray; 3.81 A; G=1-179.
DR   PDB; 3I1Z; X-ray; 3.71 A; G=1-179.
DR   PDB; 3I21; X-ray; 3.71 A; G=1-179.
DR   PDB; 3IZV; EM; -; K=1-179.
DR   PDB; 3IZW; EM; -; K=1-179.
DR   PDB; 3J00; EM; -; G=2-179.
DR   PDB; 3J0U; EM; 12.10 A; J=2-179.
DR   PDB; 3J0V; EM; 14.70 A; J=2-179.
DR   PDB; 3J0X; EM; 13.50 A; J=2-179.
DR   PDB; 3J0Z; EM; 11.50 A; J=2-179.
DR   PDB; 3J10; EM; 11.50 A; J=2-179.
DR   PDB; 3J13; EM; 13.10 A; I=2-179.
DR   PDB; 3J18; EM; 8.30 A; G=2-152.
DR   PDB; 3J36; EM; 9.80 A; G=2-179.
DR   PDB; 3J4V; EM; 12.00 A; G=3-152.
DR   PDB; 3J4W; EM; 12.00 A; G=3-152.
DR   PDB; 3J4Y; EM; 17.00 A; G=3-152.
DR   PDB; 3J4Z; EM; 20.00 A; G=3-152.
DR   PDB; 3J53; EM; 13.00 A; G=3-152.
DR   PDB; 3J55; EM; 15.00 A; G=3-152.
DR   PDB; 3J57; EM; 17.00 A; G=3-152.
DR   PDB; 3J59; EM; 12.00 A; G=3-152.
DR   PDB; 3J5B; EM; 17.00 A; G=3-152.
DR   PDB; 3J5D; EM; 17.00 A; G=3-152.
DR   PDB; 3J5F; EM; 20.00 A; G=3-152.
DR   PDB; 3J5H; EM; 15.00 A; G=3-152.
DR   PDB; 3J5J; EM; 9.00 A; G=3-152.
DR   PDB; 3J5N; EM; 6.80 A; G=1-179.
DR   PDB; 3J5S; EM; 7.50 A; I=2-152.
DR   PDB; 3J5T; EM; 7.60 A; G=2-179.
DR   PDB; 3J5X; EM; 7.60 A; G=2-179.
DR   PDB; 3KC4; EM; -; G=1-179.
DR   PDB; 3OAQ; X-ray; 3.25 A; G=2-152.
DR   PDB; 3OAR; X-ray; 3.25 A; G=3-152.
DR   PDB; 3OFA; X-ray; 3.19 A; G=2-152.
DR   PDB; 3OFB; X-ray; 3.19 A; G=3-152.
DR   PDB; 3OFO; X-ray; 3.10 A; G=2-152.
DR   PDB; 3OFP; X-ray; 3.10 A; G=3-152.
DR   PDB; 3OFX; X-ray; 3.29 A; G=2-152.
DR   PDB; 3OFY; X-ray; 3.29 A; G=3-152.
DR   PDB; 3OR9; X-ray; 3.30 A; G=1-179.
DR   PDB; 3ORA; X-ray; 3.30 A; G=1-179.
DR   PDB; 3SFS; X-ray; 3.20 A; G=1-156.
DR   PDB; 3UOQ; X-ray; 3.70 A; G=1-179.
DR   PDB; 4A2I; EM; 16.50 A; G=3-152.
DR   PDB; 4ADV; EM; 13.50 A; G=2-179.
DR   PDB; 4GAQ; X-ray; 3.30 A; G=1-179.
DR   PDB; 4GAS; X-ray; 3.30 A; G=1-179.
DR   PDB; 4GD1; X-ray; 3.00 A; G=2-152.
DR   PDB; 4GD2; X-ray; 3.00 A; G=2-152.
DR   PDB; 4KIY; X-ray; 2.90 A; G=1-179.
DR   PDB; 4KJ0; X-ray; 2.90 A; G=1-179.
DR   PDB; 4KJ2; X-ray; 2.90 A; G=1-179.
DR   PDB; 4KJ4; X-ray; 2.90 A; G=1-179.
DR   PDB; 4KJ6; X-ray; 2.90 A; G=1-179.
DR   PDB; 4KJ8; X-ray; 2.90 A; G=1-179.
DR   PDB; 4KJA; X-ray; 2.90 A; G=1-179.
DR   PDB; 4KJC; X-ray; 2.90 A; G=1-179.
DR   PDB; 4PE9; X-ray; 2.95 A; G=2-152.
DR   PDB; 4PEA; X-ray; 2.95 A; G=2-152.
DR   PDB; 4TOL; X-ray; 3.00 A; G=2-152.
DR   PDB; 4TON; X-ray; 3.00 A; G=2-152.
DR   PDB; 4TOU; X-ray; 2.90 A; G=2-152.
DR   PDB; 4TOW; X-ray; 2.90 A; G=2-152.
DR   PDB; 4TP0; X-ray; 2.90 A; G=2-152.
DR   PDB; 4TP2; X-ray; 2.90 A; G=2-152.
DR   PDB; 4TP4; X-ray; 2.90 A; G=2-152.
DR   PDB; 4TP6; X-ray; 2.90 A; G=2-152.
DR   PDB; 4TP8; X-ray; 2.80 A; G=2-152.
DR   PDB; 4TPA; X-ray; 2.80 A; G=2-152.
DR   PDB; 4TPC; X-ray; 2.80 A; G=2-152.
DR   PDB; 4TPE; X-ray; 2.80 A; G=2-152.
DR   PDBsum; 1EG0; -.
DR   PDBsum; 1M5G; -.
DR   PDBsum; 1ML5; -.
DR   PDBsum; 1P6G; -.
DR   PDBsum; 1P87; -.
DR   PDBsum; 1VS5; -.
DR   PDBsum; 1VS7; -.
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; 3DF1; -.
DR   PDBsum; 3DF3; -.
DR   PDBsum; 3E1A; -.
DR   PDBsum; 3E1C; -.
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; 3J0U; -.
DR   PDBsum; 3J0V; -.
DR   PDBsum; 3J0X; -.
DR   PDBsum; 3J0Z; -.
DR   PDBsum; 3J10; -.
DR   PDBsum; 3J13; -.
DR   PDBsum; 3J18; -.
DR   PDBsum; 3J36; -.
DR   PDBsum; 3J4V; -.
DR   PDBsum; 3J4W; -.
DR   PDBsum; 3J4Y; -.
DR   PDBsum; 3J4Z; -.
DR   PDBsum; 3J53; -.
DR   PDBsum; 3J55; -.
DR   PDBsum; 3J57; -.
DR   PDBsum; 3J59; -.
DR   PDBsum; 3J5B; -.
DR   PDBsum; 3J5D; -.
DR   PDBsum; 3J5F; -.
DR   PDBsum; 3J5H; -.
DR   PDBsum; 3J5J; -.
DR   PDBsum; 3J5N; -.
DR   PDBsum; 3J5S; -.
DR   PDBsum; 3J5T; -.
DR   PDBsum; 3J5X; -.
DR   PDBsum; 3KC4; -.
DR   PDBsum; 3OAQ; -.
DR   PDBsum; 3OAR; -.
DR   PDBsum; 3OFA; -.
DR   PDBsum; 3OFB; -.
DR   PDBsum; 3OFO; -.
DR   PDBsum; 3OFP; -.
DR   PDBsum; 3OFX; -.
DR   PDBsum; 3OFY; -.
DR   PDBsum; 3OR9; -.
DR   PDBsum; 3ORA; -.
DR   PDBsum; 3SFS; -.
DR   PDBsum; 3UOQ; -.
DR   PDBsum; 4A2I; -.
DR   PDBsum; 4ADV; -.
DR   PDBsum; 4GAQ; -.
DR   PDBsum; 4GAS; -.
DR   PDBsum; 4GD1; -.
DR   PDBsum; 4GD2; -.
DR   PDBsum; 4KIY; -.
DR   PDBsum; 4KJ0; -.
DR   PDBsum; 4KJ2; -.
DR   PDBsum; 4KJ4; -.
DR   PDBsum; 4KJ6; -.
DR   PDBsum; 4KJ8; -.
DR   PDBsum; 4KJA; -.
DR   PDBsum; 4KJC; -.
DR   PDBsum; 4PE9; -.
DR   PDBsum; 4PEA; -.
DR   PDBsum; 4TOL; -.
DR   PDBsum; 4TON; -.
DR   PDBsum; 4TOU; -.
DR   PDBsum; 4TOW; -.
DR   PDBsum; 4TP0; -.
DR   PDBsum; 4TP2; -.
DR   PDBsum; 4TP4; -.
DR   PDBsum; 4TP6; -.
DR   PDBsum; 4TP8; -.
DR   PDBsum; 4TPA; -.
DR   PDBsum; 4TPC; -.
DR   PDBsum; 4TPE; -.
DR   ProteinModelPortal; P02359; -.
DR   SMR; P02359; 2-179.
DR   DIP; DIP-10783N; -.
DR   IntAct; P02359; 151.
DR   MINT; MINT-1236482; -.
DR   STRING; 511145.b3341; -.
DR   ChEMBL; CHEMBL2363135; -.
DR   DrugBank; DB00759; Tetracycline.
DR   PhosSite; P0810434; -.
DR   PaxDb; P02359; -.
DR   PRIDE; P02359; -.
DR   EnsemblBacteria; AAC76366; AAC76366; b3341.
DR   EnsemblBacteria; BAE77950; BAE77950; BAE77950.
DR   GeneID; 12933477; -.
DR   GeneID; 947846; -.
DR   KEGG; ecj:Y75_p3835; -.
DR   KEGG; eco:b3341; -.
DR   PATRIC; 32122114; VBIEscCol129921_3434.
DR   EchoBASE; EB0899; -.
DR   EcoGene; EG10906; rpsG.
DR   eggNOG; COG0049; -.
DR   HOGENOM; HOG000039067; -.
DR   InParanoid; P02359; -.
DR   KO; K02992; -.
DR   OMA; ALGMRWL; -.
DR   OrthoDB; EOG6P5ZKW; -.
DR   PhylomeDB; P02359; -.
DR   BioCyc; EcoCyc:EG10906-MONOMER; -.
DR   BioCyc; ECOL316407:JW3303-MONOMER; -.
DR   EvolutionaryTrace; P02359; -.
DR   PRO; PR:P02359; -.
DR   Genevestigator; P02359; -.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:EcoCyc.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; IDA:EcoCyc.
DR   GO; GO:0019843; F:rRNA binding; IDA:EcoCyc.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0017148; P:negative regulation of translation; IDA:EcoCyc.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IDA:EcoCyc.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.455.10; -; 1.
DR   HAMAP; MF_00480_B; Ribosomal_S7_B; 1.
DR   InterPro; IPR000235; Ribosomal_S5/S7.
DR   InterPro; IPR005717; Ribosomal_S7_bac/org-type.
DR   InterPro; IPR020606; Ribosomal_S7_CS.
DR   InterPro; IPR023798; Ribosomal_S7_dom.
DR   PANTHER; PTHR11205; PTHR11205; 1.
DR   Pfam; PF00177; Ribosomal_S7; 1.
DR   PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1.
DR   SUPFAM; SSF47973; SSF47973; 1.
DR   TIGRFAMs; TIGR01029; rpsG_bact; 1.
DR   PROSITE; PS00052; RIBOSOMAL_S7; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; tRNA-binding.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:385062}.
FT   CHAIN         2    179       30S ribosomal protein S7.
FT                                /FTId=PRO_0000124259.
FT   VARIANT     157    179       Missing (in strain: B and L44).
FT   MUTAGEN       2     18       Missing: Defective in ribosome assembly;
FT                                accumulates to abnormally high levels on
FT                                polysomes; significantly decreases
FT                                affinity for its own mRNA.
FT   MUTAGEN      36     36       K->A,E: Defective in ribosome assembly.
FT   MUTAGEN     116    116       M->G: Significantly decreases affinity
FT                                for its own mRNA.
FT   CONFLICT     92     92       Missing (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   TURN         16     18       {ECO:0000244|PDB:4TP8}.
FT   HELIX        21     30       {ECO:0000244|PDB:4TP8}.
FT   HELIX        32     34       {ECO:0000244|PDB:4TPA}.
FT   HELIX        36     54       {ECO:0000244|PDB:4TP8}.
FT   HELIX        59     69       {ECO:0000244|PDB:4TP8}.
FT   STRAND       72     76       {ECO:0000244|PDB:4TP8}.
FT   STRAND       78     80       {ECO:0000244|PDB:2I2P}.
FT   STRAND       81     83       {ECO:0000244|PDB:4TP8}.
FT   STRAND       87     90       {ECO:0000244|PDB:4TP8}.
FT   HELIX        93    109       {ECO:0000244|PDB:4TP8}.
FT   STRAND      113    115       {ECO:0000244|PDB:4TP8}.
FT   HELIX       116    128       {ECO:0000244|PDB:4TP8}.
FT   HELIX       133    144       {ECO:0000244|PDB:4TP8}.
FT   TURN        145    147       {ECO:0000244|PDB:4TP8}.
FT   HELIX       148    151       {ECO:0000244|PDB:4TPA}.
SQ   SEQUENCE   179 AA;  20019 MW;  8627DB380C4A9C0D CRC64;
     MPRRRVIGQR KILPDPKFGS ELLAKFVNIL MVDGKKSTAE SIVYSALETL AQRSGKSELE
     AFEVALENVR PTVEVKSRRV GGSTYQVPVE VRPVRRNALA MRWIVEAARK RGDKSMALRL
     ANELSDAAEN KGTAVKKRED VHRMAEANKA FAHYRWLSLR SFSHQAGASS KQPALGYLN
//
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