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30S ribosomal protein S12 (Small ribosomal subunit protein uS12)

 RS12_ECOLI              Reviewed;         124 AA.
P0A7S3; P02367; Q2M707; Q9F5N3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
13-FEB-2019, entry version 150.
RecName: Full=30S ribosomal protein S12;
AltName: Full=Small ribosomal subunit protein uS12 {ECO:0000303|PubMed:24524803};
Name=rpsL; Synonyms=strA; OrderedLocusNames=b3342, JW3304;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
PRELIMINARY PROTEIN SEQUENCE OF 2-124, AND SUBUNIT.
STRAIN=K;
PubMed=320034; DOI=10.1016/0014-5793(77)80004-5;
Funatsu G., Yaguchi M., Wittmann-Liebold B.;
"Primary structure of protein S12 from the small Escherichia coli
ribosomal subunit.";
FEBS Lett. 73:12-17(1977).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=6989816;
Post L.E., Nomura M.;
"DNA sequences from the str operon of Escherichia coli.";
J. Biol. Chem. 255:4660-4666(1980).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS STREPTOMYCIN
RESISTANT.
STRAIN=B/R WP2;
PubMed=1552908; DOI=10.1007/BF00299141;
Timms A.R., Steingrimsdottir H., Lehmann A.R., Bridges B.A.;
"Mutant sequences in the rpsL gene of Escherichia coli B/r:
mechanistic implications for spontaneous and ultraviolet light
mutagenesis.";
Mol. Gen. Genet. 232:89-96(1992).
[4]
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT STREPTOMYCIN RESISTANT.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574, and K12 / W3110 / ZK126;
Kharat A.S., Blot M.;
"Nucleotide information of the rpsL150 allele of MC4100, strain of
Escherichia coli.";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[6]
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
STRAIN=K12;
PubMed=151587; DOI=10.1016/0092-8674(78)90096-X;
Post L.E., Arfsten A.E., Reusser F., Nomura M.;
"DNA sequences of promoter regions for the str and spc ribosomal
protein operons in E. coli.";
Cell 15:215-229(1978).
[8]
PROTEIN SEQUENCE OF 2-11, CROSS-LINKING TO RRNA, AND SUBUNIT.
STRAIN=MRE-600;
PubMed=7556101;
Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.;
"Protein-rRNA binding features and their structural and functional
implications in ribosomes as determined by cross-linking studies.";
EMBO J. 14:4578-4588(1995).
[9]
EFFECT OF MUTATIONS ON RRNA FOLDING.
STRAIN=UD1A1;
PubMed=2477554; DOI=10.1016/0022-2836(89)90509-3;
Allen P.N., Noller H.F.;
"Mutations in ribosomal proteins S4 and S12 influence the higher order
structure of 16 S ribosomal RNA.";
J. Mol. Biol. 208:457-468(1989).
[10]
MUTAGENESIS OF LEU-57 AND LYS-88.
STRAIN=K12;
PubMed=10209746; DOI=10.1046/j.1365-2958.1999.01307.x;
Toivonen J.M., Boocock M.R., Jacobs H.T.;
"Modelling in Escherichia coli of mutations in mitoribosomal protein
S12: novel mutant phenotypes of rpsL.";
Mol. Microbiol. 31:1735-1746(1999).
[11]
METHYLTHIOLATION AT ASP-89.
PubMed=8844851; DOI=10.1002/pro.5560050816;
Kowalak J.A., Walsh K.A.;
"Beta-methylthio-aspartic acid: identification of a novel
posttranslational modification in ribosomal protein S12 from
Escherichia coli.";
Protein Sci. 5:1625-1632(1996).
[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]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[14]
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).
[15]
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).
[16]
STRUCTURE BY ELECTRON MICROSCOPY (11 ANGSTROMS) OF KIRROMYCIN-STALLED
RIBOSOMES COMPLEXED WITH EF-TU/AMINOACYL-TRNA/GTP, AND SUBUNIT.
PubMed=12093756; DOI=10.1093/emboj/cdf326;
Valle M., Sengupta J., Swami N.K., Grassucci R.A., Burkhardt N.,
Nierhaus K.H., Agrawal R.K., Frank J.;
"Cryo-EM reveals an active role for aminoacyl-tRNA in the
accommodation process.";
EMBO J. 21:3557-3567(2002).
[17]
STRUCTURE BY ELECTRON MICROSCOPY (13 ANGSTROMS) OF KIRROMYCIN-STALLED
RIBOSOMES COMPLEXED WITH EF-TU/AMINOACYL-TRNA/GTP, AND SUBUNIT.
STRAIN=MRE-600;
PubMed=12379845; DOI=10.1038/nsb859;
Stark H., Rodnina M.V., Wieden H.-J., Zemlin F., Wintermeyer W.,
Van Heel M.;
"Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in
the codon-recognition complex.";
Nat. Struct. Biol. 9:849-854(2002).
[18]
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).
[19]
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).
[20]
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).
[21]
STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 70S RIBOSOME IN
COMPLEX WITH ARFA AND RF2, INTERACTION WITH ARFA, 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).
[22] {ECO:0000244|PDB:5MGP}
STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 2-124 OF 70S
RIBOSOME IN COMPLEX WITH ARFA AND RF2, INTERACTION WITH 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).
[23]
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).
[24]
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 S5 plays an important role in translational
accuracy.
-!- FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that
are involved in tRNA selection in the A site and with the mRNA
backbone. Located at the interface of the 30S and 50S subunits, it
traverses the body of the 30S subunit contacting proteins on the
other side and probably holding the rRNA structure together. The
combined cluster of proteins S8, S12 and S17 appears to hold
together the shoulder and platform of the 30S subunit (By
similarity). {ECO:0000250|UniProtKB:Q5SHN3,
ECO:0000269|PubMed:7556101}.
-!- FUNCTION: Cryo-EM studies suggest that S12 contacts the EF-Tu
bound tRNA in the A-site during codon-recognition. This contact is
most likely broken as the aminoacyl-tRNA moves into the peptidyl
transferase center in the 50S subunit.
{ECO:0000305|PubMed:12093756}.
-!- SUBUNIT: Part of the 30S ribosomal subunit (PubMed:320034,
PubMed:7556101, PubMed:12809609, PubMed:16272117, PubMed:27934701,
PubMed:10094780, PubMed:12093756, PubMed:12379845,
PubMed:12244297, PubMed:27906160, PubMed:27906161). Contacts
proteins S8 and S17. Interacts with ArfA (PubMed:27906160,
PubMed:27906161). May interact with IF1 in the 30S initiation
complex (By similarity). {ECO:0000250|UniProtKB:Q5SHN3,
ECO:0000269|PubMed:10094780, ECO:0000269|PubMed:12093756,
ECO:0000269|PubMed:12244297, ECO:0000269|PubMed:12379845,
ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:16272117,
ECO:0000269|PubMed:27906160, ECO:0000269|PubMed:27906161,
ECO:0000269|PubMed:27934701, ECO:0000269|PubMed:320034,
ECO:0000269|PubMed:7556101}.
-!- INTERACTION:
P0A8A8:rimP; NbExp=3; IntAct=EBI-543960, EBI-561065;
-!- MASS SPECTROMETRY: Mass=13651.3; Method=MALDI; Range=2-124;
Evidence={ECO:0000269|PubMed:10094780};
-!- MISCELLANEOUS: At least 19 substitutions or deletions in 11 codons
can promote streptomycin resistance, dependence or
pseudodependence; all but one of the streptomycin resistant
mutations (K42R) are associated with hyperaccurate translation and
thus reduced translational efficiency.
{ECO:0000269|PubMed:1552908, ECO:0000269|Ref.5}.
-!- MISCELLANEOUS: The streptomycin sensitive allele is dominant to
resistant alleles.
-!- SIMILARITY: Belongs to the universal ribosomal protein uS12
family. {ECO:0000305}.
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EMBL; V00355; CAA23648.1; -; Genomic_DNA.
EMBL; U18997; AAA58139.1; -; Genomic_DNA.
EMBL; U00096; AAC76367.1; -; Genomic_DNA.
EMBL; AP009048; BAE77949.1; -; Genomic_DNA.
EMBL; AF312716; AAG30936.1; -; Genomic_DNA.
EMBL; AF312717; AAG30937.1; -; Genomic_DNA.
EMBL; V00354; CAA23647.1; -; Genomic_DNA.
EMBL; J01688; AAA50988.1; -; Genomic_DNA.
PIR; S13738; R3EC12.
RefSeq; NP_417801.1; NC_000913.3.
RefSeq; WP_000246815.1; NZ_CP011343.2.
PDB; 1M5G; Model; -; L=2-124.
PDB; 1MJ1; EM; 13.00 A; O=5-123.
PDB; 1ZN1; EM; 14.10 A; L=28-124.
PDB; 2YKR; EM; 9.80 A; L=2-124.
PDB; 3DEG; EM; -; D=2-124.
PDB; 3EP2; EM; -; L=2-124.
PDB; 3EQ3; EM; -; L=2-124.
PDB; 3EQ4; EM; -; L=2-124.
PDB; 3J0D; EM; 11.10 A; I=2-124.
PDB; 3J0E; EM; 9.90 A; F=2-124.
PDB; 3J9Y; EM; 3.90 A; l=1-124.
PDB; 3J9Z; EM; 3.60 A; SL=2-124.
PDB; 3JA1; EM; 3.60 A; SL=2-124.
PDB; 3JBU; EM; 3.64 A; L=1-124.
PDB; 3JBV; EM; 3.32 A; L=1-124.
PDB; 3JCD; EM; 3.70 A; l=1-124.
PDB; 3JCE; EM; 3.20 A; l=1-124.
PDB; 3JCJ; EM; 3.70 A; t=1-124.
PDB; 3JCN; EM; 4.60 A; o=1-124.
PDB; 4A2I; EM; 16.50 A; L=2-124.
PDB; 4ADV; EM; 13.50 A; L=2-124.
PDB; 4U1U; X-ray; 2.95 A; AL/CL=2-124.
PDB; 4U1V; X-ray; 3.00 A; AL/CL=2-124.
PDB; 4U20; X-ray; 2.90 A; AL/CL=2-124.
PDB; 4U24; X-ray; 2.90 A; AL/CL=2-124.
PDB; 4U25; X-ray; 2.90 A; AL/CL=2-124.
PDB; 4U26; X-ray; 2.80 A; AL/CL=2-124.
PDB; 4U27; X-ray; 2.80 A; AL/CL=2-124.
PDB; 4V47; EM; 12.30 A; BL=2-124.
PDB; 4V48; EM; 11.50 A; BL=2-124.
PDB; 4V4H; X-ray; 3.46 A; AL/CL=1-124.
PDB; 4V4Q; X-ray; 3.46 A; AL/CL=2-124.
PDB; 4V4V; EM; 15.00 A; AL=23-123.
PDB; 4V4W; EM; 15.00 A; AL=23-123.
PDB; 4V50; X-ray; 3.22 A; AL/CL=2-124.
PDB; 4V52; X-ray; 3.21 A; AL/CL=2-124.
PDB; 4V53; X-ray; 3.54 A; AL/CL=2-124.
PDB; 4V54; X-ray; 3.30 A; AL/CL=2-124.
PDB; 4V55; X-ray; 4.00 A; AL/CL=2-124.
PDB; 4V56; X-ray; 3.93 A; AL/CL=2-124.
PDB; 4V57; X-ray; 3.50 A; AL/CL=2-124.
PDB; 4V5B; X-ray; 3.74 A; BL/DL=2-124.
PDB; 4V5H; EM; 5.80 A; AL=2-124.
PDB; 4V5Y; X-ray; 4.45 A; AL/CL=2-124.
PDB; 4V64; X-ray; 3.50 A; AL/CL=2-124.
PDB; 4V65; EM; 9.00 A; AD=1-124.
PDB; 4V66; EM; 9.00 A; AD=1-124.
PDB; 4V69; EM; 6.70 A; AL=2-124.
PDB; 4V6C; X-ray; 3.19 A; AL/CL=1-124.
PDB; 4V6D; X-ray; 3.81 A; AL/CL=1-124.
PDB; 4V6E; X-ray; 3.71 A; AL/CL=1-124.
PDB; 4V6K; EM; 8.25 A; BP=1-124.
PDB; 4V6L; EM; 13.20 A; AP=1-124.
PDB; 4V6M; EM; 7.10 A; AL=2-124, AO=2-89.
PDB; 4V6N; EM; 12.10 A; BO=2-124.
PDB; 4V6O; EM; 14.70 A; AO=2-124.
PDB; 4V6P; EM; 13.50 A; AO=2-124.
PDB; 4V6Q; EM; 11.50 A; AO=2-124.
PDB; 4V6R; EM; 11.50 A; AO=2-124.
PDB; 4V6S; EM; 13.10 A; BN=2-124.
PDB; 4V6T; EM; 8.30 A; AL=2-124.
PDB; 4V6V; EM; 9.80 A; AL=2-124.
PDB; 4V6Y; EM; 12.00 A; AL=1-124.
PDB; 4V6Z; EM; 12.00 A; AL=1-124.
PDB; 4V70; EM; 17.00 A; AL=1-124.
PDB; 4V71; EM; 20.00 A; AL=1-124.
PDB; 4V72; EM; 13.00 A; AL=1-124.
PDB; 4V73; EM; 15.00 A; AL=1-124.
PDB; 4V74; EM; 17.00 A; AL=1-124.
PDB; 4V75; EM; 12.00 A; AL=1-124.
PDB; 4V76; EM; 17.00 A; AL=1-124.
PDB; 4V77; EM; 17.00 A; AL=1-124.
PDB; 4V78; EM; 20.00 A; AL=1-124.
PDB; 4V79; EM; 15.00 A; AL=1-124.
PDB; 4V7A; EM; 9.00 A; AL=1-124.
PDB; 4V7B; EM; 6.80 A; AL=1-124.
PDB; 4V7C; EM; 7.60 A; AL=2-124.
PDB; 4V7D; EM; 7.60 A; BL=2-124.
PDB; 4V7I; EM; 9.60 A; BL=1-124.
PDB; 4V7S; X-ray; 3.25 A; AL/CL=2-124.
PDB; 4V7T; X-ray; 3.19 A; AL/CL=2-124.
PDB; 4V7U; X-ray; 3.10 A; AL/CL=2-124.
PDB; 4V7V; X-ray; 3.29 A; AL/CL=2-124.
PDB; 4V85; X-ray; 3.20 A; L=1-124.
PDB; 4V89; X-ray; 3.70 A; AL=1-124.
PDB; 4V9C; X-ray; 3.30 A; AL/CL=1-124.
PDB; 4V9D; X-ray; 3.00 A; AL/BL=2-124.
PDB; 4V9O; X-ray; 2.90 A; BL/DL/FL/HL=1-124.
PDB; 4V9P; X-ray; 2.90 A; BL/DL/FL/HL=1-124.
PDB; 4WF1; X-ray; 3.09 A; AL/CL=2-124.
PDB; 4WOI; X-ray; 3.00 A; AL/DL=1-124.
PDB; 4WWW; X-ray; 3.10 A; QL/XL=2-124.
PDB; 4YBB; X-ray; 2.10 A; AL/BL=2-124.
PDB; 5AFI; EM; 2.90 A; l=1-124.
PDB; 5H5U; EM; 3.00 A; s=2-124.
PDB; 5IQR; EM; 3.00 A; q=1-124.
PDB; 5IT8; X-ray; 3.12 A; AL/BL=2-124.
PDB; 5J5B; X-ray; 2.80 A; AL/BL=2-124.
PDB; 5J7L; X-ray; 3.00 A; AL/BL=2-124.
PDB; 5J88; X-ray; 3.32 A; AL/BL=2-124.
PDB; 5J8A; X-ray; 3.10 A; AL/BL=2-124.
PDB; 5J91; X-ray; 2.96 A; AL/BL=2-124.
PDB; 5JC9; X-ray; 3.03 A; AL/BL=2-124.
PDB; 5JTE; EM; 3.60 A; AL=1-124.
PDB; 5JU8; EM; 3.60 A; AL=1-124.
PDB; 5KCR; EM; 3.60 A; 1l=1-124.
PDB; 5KCS; EM; 3.90 A; 1l=1-124.
PDB; 5KPS; EM; 3.90 A; 17=1-124.
PDB; 5KPV; EM; 4.10 A; 16=1-124.
PDB; 5KPW; EM; 3.90 A; 16=1-124.
PDB; 5KPX; EM; 3.90 A; 16=1-124.
PDB; 5L3P; EM; 3.70 A; l=1-124.
PDB; 5LZA; EM; 3.60 A; l=2-124.
PDB; 5LZB; EM; 5.30 A; l=2-124.
PDB; 5LZC; EM; 4.80 A; l=2-124.
PDB; 5LZD; EM; 3.40 A; l=2-124.
PDB; 5LZE; EM; 3.50 A; l=2-124.
PDB; 5LZF; EM; 4.60 A; l=2-124.
PDB; 5MDV; EM; 2.97 A; q=1-124.
PDB; 5MDW; EM; 3.06 A; q=1-124.
PDB; 5MDY; EM; 3.35 A; q=1-124.
PDB; 5MDZ; EM; 3.10 A; q=1-124.
PDB; 5ME0; EM; 13.50 A; L=2-124.
PDB; 5ME1; EM; 13.50 A; L=2-124.
PDB; 5MGP; EM; 3.10 A; l=2-124.
PDB; 5MY1; EM; 7.60 A; L=2-124.
PDB; 5NO2; EM; 5.16 A; L=2-15.
PDB; 5NO3; EM; 5.16 A; L=2-15.
PDB; 5NO4; EM; 5.16 A; L=2-15.
PDB; 5NP6; EM; 3.60 A; O=2-124.
PDB; 5NWY; EM; 2.93 A; B=1-124.
PDB; 5O2R; EM; 3.40 A; l=2-124.
PDB; 5U4I; EM; 3.50 A; l=2-124.
PDB; 5U4J; EM; 3.70 A; l=1-124.
PDB; 5U9F; EM; 3.20 A; L=1-124.
PDB; 5U9G; EM; 3.20 A; L=1-124.
PDB; 5UYK; EM; 3.90 A; L=2-124.
PDB; 5UYL; EM; 3.60 A; L=2-124.
PDB; 5UYM; EM; 3.20 A; L=2-124.
PDB; 5UYN; EM; 4.00 A; L=2-124.
PDB; 5UYP; EM; 3.90 A; L=2-124.
PDB; 5UYQ; EM; 3.80 A; L=2-124.
PDB; 5WDT; EM; 3.00 A; l=2-122.
PDB; 5WE4; EM; 3.10 A; l=2-122.
PDB; 5WE6; EM; 3.40 A; l=2-122.
PDB; 5WFK; EM; 3.40 A; l=2-122.
PDB; 6BU8; EM; 3.50 A; L=2-124.
PDB; 6C4I; EM; 3.24 A; l=1-124.
PDB; 6ENF; EM; 3.20 A; l=2-124.
PDB; 6ENJ; EM; 3.70 A; l=2-124.
PDB; 6ENU; EM; 3.10 A; l=2-124.
PDB; 6GWT; EM; 3.80 A; l=2-124.
PDB; 6GXM; EM; 3.80 A; l=2-124.
PDB; 6GXN; EM; 3.90 A; l=2-124.
PDB; 6GXO; EM; 3.90 A; l=2-124.
PDB; 6GXP; EM; 4.40 A; l=2-124.
PDB; 6H4N; EM; 3.00 A; l=2-124.
PDB; 6H58; EM; 7.90 A; l/ll=2-124.
PDB; 6HRM; EM; 2.96 A; q=2-124.
PDB; 6I7V; X-ray; 2.90 A; AL/BL=2-124.
PDBsum; 1M5G; -.
PDBsum; 1MJ1; -.
PDBsum; 1ZN1; -.
PDBsum; 2YKR; -.
PDBsum; 3DEG; -.
PDBsum; 3EP2; -.
PDBsum; 3EQ3; -.
PDBsum; 3EQ4; -.
PDBsum; 3J0D; -.
PDBsum; 3J0E; -.
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; 5WDT; -.
PDBsum; 5WE4; -.
PDBsum; 5WE6; -.
PDBsum; 5WFK; -.
PDBsum; 6BU8; -.
PDBsum; 6C4I; -.
PDBsum; 6ENF; -.
PDBsum; 6ENJ; -.
PDBsum; 6ENU; -.
PDBsum; 6GWT; -.
PDBsum; 6GXM; -.
PDBsum; 6GXN; -.
PDBsum; 6GXO; -.
PDBsum; 6GXP; -.
PDBsum; 6H4N; -.
PDBsum; 6H58; -.
PDBsum; 6HRM; -.
PDBsum; 6I7V; -.
DisProt; DP00145; -.
ProteinModelPortal; P0A7S3; -.
SMR; P0A7S3; -.
BioGrid; 852156; 1.
ComplexPortal; CPX-3802; 30S small ribosomal subunit.
DIP; DIP-35806N; -.
IntAct; P0A7S3; 29.
STRING; 316385.ECDH10B_p2; -.
DrugBank; DB00479; Amikacin.
DrugBank; DB06696; Arbekacin.
DrugBank; DB00452; Framycetin.
DrugBank; DB00798; Gentamicin.
DrugBank; DB04729; GENTAMICIN C1A.
DrugBank; DB01172; Kanamycin.
DrugBank; DB00994; Neomycin.
DrugBank; DB00955; Netilmicin.
DrugBank; DB03615; Ribostamycin.
DrugBank; DB00919; Spectinomycin.
DrugBank; DB01082; Streptomycin.
DrugBank; DB00560; Tigecycline.
DrugBank; DB00684; Tobramycin.
iPTMnet; P0A7S3; -.
EPD; P0A7S3; -.
jPOST; P0A7S3; -.
PaxDb; P0A7S3; -.
PRIDE; P0A7S3; -.
EnsemblBacteria; AAC76367; AAC76367; b3342.
EnsemblBacteria; BAE77949; BAE77949; BAE77949.
GeneID; 34154647; -.
GeneID; 947845; -.
KEGG; ecj:JW3304; -.
KEGG; eco:b3342; -.
PATRIC; fig|1411691.4.peg.3389; -.
EchoBASE; EB0904; -.
EcoGene; EG10911; rpsL.
eggNOG; COG0048; LUCA.
HOGENOM; HOG000040063; -.
InParanoid; P0A7S3; -.
KO; K02950; -.
PhylomeDB; P0A7S3; -.
BioCyc; EcoCyc:EG10911-MONOMER; -.
BioCyc; ECOL316407:JW3304-MONOMER; -.
BioCyc; MetaCyc:EG10911-MONOMER; -.
EvolutionaryTrace; P0A7S3; -.
PRO; PR:P0A7S3; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:EcoliWiki.
GO; GO:0034336; F:misfolded RNA binding; IDA:EcoCyc.
GO; GO:0019843; F:rRNA binding; IDA:EcoCyc.
GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
GO; GO:0000372; P:Group I intron splicing; IDA:EcoCyc.
GO; GO:1990145; P:maintenance of translational fidelity; IMP:EcoCyc.
GO; GO:0033120; P:positive regulation of RNA splicing; IDA:EcoCyc.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
GO; GO:0034337; P:RNA folding; IDA:EcoCyc.
GO; GO:0006412; P:translation; IMP:EcoCyc.
CDD; cd03368; Ribosomal_S12; 1.
HAMAP; MF_00403_B; Ribosomal_S12_B; 1.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR006032; Ribosomal_S12/S23.
InterPro; IPR005679; Ribosomal_S12_bac.
PANTHER; PTHR11652; PTHR11652; 1.
Pfam; PF00164; Ribosom_S12_S23; 1.
PIRSF; PIRSF002133; Ribosomal_S12/S23; 1.
PRINTS; PR01034; RIBOSOMALS12.
SUPFAM; SSF50249; SSF50249; 1.
TIGRFAMs; TIGR00981; rpsL_bact; 1.
PROSITE; PS00055; RIBOSOMAL_S12; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Antibiotic resistance; Complete proteome;
Direct protein sequencing; Methylation; Reference proteome;
Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
tRNA-binding.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7556101}.
CHAIN 2 124 30S ribosomal protein S12.
/FTId=PRO_0000146219.
MOD_RES 89 89 3-methylthioaspartic acid.
{ECO:0000269|PubMed:8844851}.
MOD_RES 108 108 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
VARIANT 43 43 K -> R (confers streptomycin resistance
but not hyperaccurate translation).
MUTAGEN 57 57 L->H: Protein is not incorporated into
ribosomes. {ECO:0000269|PubMed:10209746}.
MUTAGEN 88 88 K->Q: Confers low-level resistance to
streptomycin and a 15% decrease in the
translational elongation rate.
{ECO:0000269|PubMed:10209746}.
HELIX 4 9 {ECO:0000244|PDB:4U26}.
TURN 24 26 {ECO:0000244|PDB:4U27}.
STRAND 30 36 {ECO:0000244|PDB:4U26}.
STRAND 37 40 {ECO:0000244|PDB:4V50}.
STRAND 43 45 {ECO:0000244|PDB:4V6C}.
STRAND 52 57 {ECO:0000244|PDB:4U26}.
TURN 58 60 {ECO:0000244|PDB:4V54}.
STRAND 62 66 {ECO:0000244|PDB:4U26}.
STRAND 69 71 {ECO:0000244|PDB:4WF1}.
STRAND 79 84 {ECO:0000244|PDB:4U26}.
STRAND 90 92 {ECO:0000244|PDB:4U27}.
STRAND 95 97 {ECO:0000244|PDB:4U26}.
STRAND 99 101 {ECO:0000244|PDB:4U1V}.
TURN 114 118 {ECO:0000244|PDB:4U26}.
SEQUENCE 124 AA; 13737 MW; 94A57F4C4FF0FC5E CRC64;
MATVNQLVRK PRARKVAKSN VPALEACPQK RGVCTRVYTT TPKKPNSALR KVCRVRLTNG
FEVTSYIGGE GHNLQEHSVI LIRGGRVKDL PGVRYHTVRG ALDCSGVKDR KQARSKYGVK
RPKA


Related products :

Catalog number Product name Quantity
30-186 Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPS12 is the 28S subunit protein that belongs to the ribosomal protein S12P family. The protein is a ke 0.05 mg
29-214 RPL9 is a ribosomal protein that is a component of the 60S subunit. RPL9 belongs to the L6P family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal pro 0.1 mg
29-215 RPL9 is a ribosomal protein that is a component of the 60S subunit. RPL9 belongs to the L6P family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal pro 0.1 mg
EIAAB35293 39S ribosomal protein L27 homolog,39S ribosomal protein L41, mitochondrial,Bcl-2-interacting mitochondrial ribosomal protein L41,BMRP,Cell proliferation-inducing gene 3 protein,Homo sapiens,Human,L41m
29-216 RPL6 is a ribosomal protein that is a component of the 60S subunit. RPL6 belongs to the L6E family of ribosomal proteins. It is located in the cytoplasm. The protein can bind specifically to domain C 0.1 mg
26-118 Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPL39 is a 39S subunit protein. Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes 0.05 mg
EIAAB35298 28S ribosomal protein S32, mitochondrial,39S ribosomal protein L31, mitochondrial,39S ribosomal protein L42, mitochondrial,Homo sapiens,HSPC204,Human,L31mt,L42mt,MRPL31,MRP-L31,MRPL42,MRP-L42,MRPS32,M
EIAAB35296 28S ribosomal protein S32, mitochondrial,39S ribosomal protein L31, mitochondrial,39S ribosomal protein L42, mitochondrial,D10Ertd322e,L31mt,L42mt,Mouse,MRP-L31,Mrpl42,MRP-L42,Mrps32,MRP-S32,Mus muscu
29-101 Mammalian mitochondrial ribosomal proteins help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPS15 is 0.1 mg
29-221 RPL32 is a ribosomal protein that is a component of the 60S subunit. RPL32 belongs to the L32E family of ribosomal proteins. It is located in the cytoplasm. Although some studies have mapped this gene 0.1 mg
EIAAB35182 Mouse,Mus musculus,Probable ribosome biogenesis protein RLP24,Ribosomal L24 domain-containing protein 1,Ribosomal protein L24-like,Rsl24d1
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EIAAB36079 40S ribosomal protein S2,40S ribosomal protein S4,Homo sapiens,Human,Protein LLRep3,RPS2,RPS4
18-783-75538 RABBIT ANTI RIBOSOMAL S6 KINASE 2 (C-TERMINAL) - RIBOSOMAL PROTEIN S6 KINASE ALPHA-2; EC 2.7.11.1; S6K-alpha 2; 90 kDa ribosomal protein S6 kinase 2; p90-RSK 2; Ribosomal S6 kinase 3; RSK-3; pp90RSK3; 0.1 ml
EIAAB34981 60S ribosomal protein L22,EAP,EBER-associated protein,Epstein-Barr virus small RNA-associated protein,Heparin-binding protein HBp15,Homo sapiens,Human,RPL22
EIAAB33379 60S ribosomal protein L39 pseudogene 5,Homo sapiens,Human,Putative 60S ribosomal protein L39-like 5,RPL39P5
EIAAB35154 60S acidic ribosomal protein P0,60S ribosomal protein L10E,Arbp,Rat,Rattus norvegicus,Rplp0
EIAAB35158 60S acidic ribosomal protein P0,60S ribosomal protein L10E,Homo sapiens,Human,RPLP0
EIAAB35156 60S acidic ribosomal protein P0,60S ribosomal protein L10E,Arbp,Mouse,Mus musculus,Rplp0
27-821 Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit a 0.05 mg
29-467 Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit a 0.05 mg
26-705 Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit a 0.05 mg
EIAAB35157 60S acidic ribosomal protein P0,60S ribosomal protein L10E,Bos taurus,Bovine,RPLP0
EIAAB35108 60S ribosomal protein L1,60S ribosomal protein L4,Homo sapiens,Human,RPL1,RPL4
EIAAB35072 60S ribosomal protein L36a,60S ribosomal protein L44,Rat,Rattus norvegicus,Rpl36a,Rpl44

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Pathways :
WP210: Cytoplasmic Ribosomal Proteins
WP1566: Citrate cycle (TCA cycle)
WP1644: DNA replication
WP1663: Homologous recombination
WP1672: Mismatch repair
WP1693: Purine metabolism
WP1694: Pyrimidine metabolism
WP2272: Pathogenic Escherichia coli infection
WP2292: Chemokine signaling pathway
WP1049: G Protein Signaling Pathways
WP1071: Cytoplasmic Ribosomal Proteins
WP1165: G Protein Signaling Pathways
WP1187: Cytoplasmic Ribosomal Proteins
WP1239: Cytoplasmic Ribosomal Proteins
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP163: Cytoplasmic Ribosomal Proteins
WP1650: Fluorobenzoate degradation

Related Genes :
[rpsL strA b3342 JW3304] 30S ribosomal protein S12 (Small ribosomal subunit protein uS12)
[rpsL TTHA1697] 30S ribosomal protein S12
[rpsL fun strA BSU01100] 30S ribosomal protein S12 (BS12)
[rpsA ssyF b0911 JW0894] 30S ribosomal protein S1 (Bacteriophage Q beta RNA-directed RNA polymerase subunit I) (Small ribosomal subunit protein bS1)
[rpsM b3298 JW3260] 30S ribosomal protein S13 (Small ribosomal subunit protein uS13)
[rpsG b3341 JW3303] 30S ribosomal protein S7 (Small ribosomal subunit protein uS7)
[rps12-A; rps12-B] Plastid 30S ribosomal protein S12
[rpsS b3316 JW3278] 30S ribosomal protein S19 (Small ribosomal subunit protein uS19)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[rpsI b3230 JW3199] 30S ribosomal protein S9 (Small ribosomal subunit protein uS9)
[rbfA P15B yhbB b3167 JW3136] 30S ribosome-binding factor (Protein P15B) (Ribosome-binding factor A) (RbfA)
[rpsD BSU29660] 30S ribosomal protein S4 (BS4)
[rpsD rps4 TTHA1665] 30S ribosomal protein S4
[rsgA engC yjeQ b4161 JW4122] Small ribosomal subunit biogenesis GTPase RsgA (EC 3.6.1.-)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]

Bibliography :