RS10_ECOLI
ID RS10_ECOLI Reviewed; 103 AA.
AC P0A7R5; P02364; Q2M6Y6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=30S ribosomal protein S10 {ECO:0000255|HAMAP-Rule:MF_00508};
DE AltName: Full=Small ribosomal subunit protein uS10 {ECO:0000303|PubMed:24524803};
DE AltName: Full=Transcription termination/antitermination protein NusE {ECO:0000305};
GN Name=rpsJ; Synonyms=nusE; OrderedLocusNames=b3321, JW3283;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP PROTEIN SEQUENCE, AND SUBUNIT.
RX PubMed=7007073; DOI=10.1016/0014-5793(80)81277-4;
RA Yaguchi M., Roy C., Wittmann H.G.;
RT "The primary structure of protein S10 from the small ribosomal subunit of
RT Escherichia coli.";
RL FEBS Lett. 121:113-116(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7037196; DOI=10.1016/0092-8674(81)90303-2;
RA Olins P.O., Nomura M.;
RT "Regulation of the S10 ribosomal protein operon in E. coli: nucleotide
RT sequence at the start of the operon.";
RL Cell 26:205-211(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3892488; DOI=10.1093/nar/13.12.4521;
RA Zurawski G., Zurawski S.M.;
RT "Structure of the Escherichia coli S10 ribosomal protein operon.";
RL Nucleic Acids Res. 13:4521-4526(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [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 [6]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RC STRAIN=ECOR 30;
RA Noorani S.M., Lindahl L., Zengel J.M.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION.
RX PubMed=6759118; DOI=10.1111/j.1432-1033.1982.tb06982.x;
RA Riehl N., Remy P., Ebel J.P., Ehresmann B.;
RT "Crosslinking of N-acetyl-phenylalanyl [s4U]tRNAPhe to protein S10 in the
RT ribosomal P site.";
RL Eur. J. Biochem. 128:427-433(1982).
RN [9]
RP INTERACTION WITH NUSB.
RX PubMed=1731086; DOI=10.1016/0022-2836(92)90715-v;
RA Mason S.W., Li J., Greenblatt J.;
RT "Direct interaction between two Escherichia coli transcription
RT antitermination factors, NusB and ribosomal protein S10.";
RL J. Mol. Biol. 223:55-66(1992).
RN [10]
RP FUNCTION IN ANTITERMINATION.
RX PubMed=7678781; DOI=10.1016/0092-8674(93)90665-d;
RA Nodwell J.R., Greenblatt J.;
RT "Recognition of boxA antiterminator RNA by the E. coli antitermination
RT factors NusB and ribosomal protein S10.";
RL Cell 72:261-268(1993).
RN [11]
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 [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 FUNCTION IN ANTITERMINATION, AND INTERACTION WITH NUSB.
RX PubMed=11884128; DOI=10.1006/jmbi.2001.5388;
RA Luettgen H., Robelek R., Muehlberger R., Diercks T., Schuster S.C.,
RA Koehler P., Kessler H., Bacher A., Richter G.;
RT "Transcriptional regulation by antitermination. Interaction of RNA with
RT NusB protein and NusB/NusE protein complex of Escherichia coli.";
RL J. Mol. Biol. 316:875-885(2002).
RN [14]
RP FUNCTION, INTERACTION WITH NUSB, AND RNA-BINDING.
RX PubMed=16109710; DOI=10.1074/jbc.m507146200;
RA Greive S.J., Lins A.F., von Hippel P.H.;
RT "Assembly of an RNA-protein complex. Binding of NusB and NusE (S10)
RT proteins to boxA RNA nucleates the formation of the antitermination complex
RT involved in controlling rRNA transcription in Escherichia coli.";
RL J. Biol. Chem. 280:36397-36408(2005).
RN [15]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [16]
RP 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 [17] {ECO:0007744|PDB:4V47}
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 [18] {ECO:0007744|PDB:4V4Q}
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 [19] {ECO:0007744|PDB:3D3B, ECO:0007744|PDB:3D3C}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH NUSB, AND FUNCTION.
RX PubMed=19111659; DOI=10.1016/j.molcel.2008.10.028;
RA Luo X., Hsiao H.H., Bubunenko M., Weber G., Court D.L., Gottesman M.E.,
RA Urlaub H., Wahl M.C.;
RT "Structural and functional analysis of the E. coli NusB-S10 transcription
RT antitermination complex.";
RL Mol. Cell 32:791-802(2008).
RN [20] {ECO:0007744|PDB:5H5U}
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 [21] {ECO:0007744|PDB:5MGP}
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 [22] {ECO:0007744|PDB:5MDV, ECO:0007744|PDB:5MDW, ECO:0007744|PDB:5MDY, ECO:0007744|PDB:5MDZ}
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 [23] {ECO:0007744|PDB:5U4I}
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).
RN [24] {ECO:0007744|PDB:6TQN, ECO:0007744|PDB:6TQO}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF RRNA
RP TRANSCRIPTION-ELONGATION-ANTITERMINATION COMPLEXES WITH AND WITHOUT S4,
RP FUNCTION, AND SUBUNIT.
RX PubMed=32871103; DOI=10.1016/j.molcel.2020.08.010;
RA Huang Y.H., Hilal T., Loll B., Buerger J., Mielke T., Boettcher C.,
RA Said N., Wahl M.C.;
RT "Structure-Based Mechanisms of a Molecular RNA Polymerase/Chaperone Machine
RT Required for Ribosome Biosynthesis.";
RL Mol. Cell 0:0-0(2020).
CC -!- FUNCTION: Involved in the binding of tRNA to the ribosomes
CC (PubMed:6759118). Part of the processive rRNA transcription and
CC antitermination complex (rrnTAC). The complex forms an RNA-chaperone
CC ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports
CC rapid transcription and antitermination of rRNA operons,
CC cotranscriptional rRNA folding, and annealing of distal rRNA regions to
CC allow correct ribosome biogenesis (PubMed:32871103). In complex with
CC NusB is involved in the regulation of ribosomal RNA (rRNA) biosynthesis
CC by transcriptional antitermination. S10 binds RNA non-specifically and
CC increases the affinity of NusB for the boxA RNA sequence
CC (PubMed:7678781, PubMed:11884128, PubMed:16109710). S10 may constitute
CC the critical antitermination component of the NusB-S10 complex
CC (PubMed:19111659). {ECO:0000269|PubMed:11884128,
CC ECO:0000269|PubMed:16109710, ECO:0000269|PubMed:19111659,
CC ECO:0000269|PubMed:32871103, ECO:0000269|PubMed:6759118,
CC ECO:0000269|PubMed:7678781}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit (PubMed:10094780,
CC PubMed:12244297, PubMed:12809609, PubMed:16272117, PubMed:27906160,
CC PubMed:27906161, PubMed:27934701, PubMed:28077875, PubMed:7007073). Can
CC also form a heterodimer with the transcription antitermination protein
CC NusB (PubMed:1731086, PubMed:11884128, PubMed:16109710,
CC PubMed:19111659). Binding of S10 to NusB is mutually exclusive with its
CC incorporation into the ribosome (PubMed:19111659). The rRNA
CC transcription and antitermination complex (rrnTAC) consists of RNAP,
CC NusA, NusB, NusE (this protein), NusG, SubB, ribosomal protein S4, DNA
CC and precursor rRNA; S4 is more flexible than other subunits
CC (PubMed:32871103). {ECO:0000269|PubMed:10094780,
CC ECO:0000269|PubMed:11884128, ECO:0000269|PubMed:12244297,
CC ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:16109710,
CC ECO:0000269|PubMed:16272117, ECO:0000269|PubMed:1731086,
CC ECO:0000269|PubMed:19111659, ECO:0000269|PubMed:27906160,
CC ECO:0000269|PubMed:27906161, ECO:0000269|PubMed:27934701,
CC ECO:0000269|PubMed:28077875, ECO:0000269|PubMed:32871103,
CC ECO:0000269|PubMed:7007073}.
CC -!- INTERACTION:
CC P0A7R5; P0A780: nusB; NbExp=6; IntAct=EBI-544602, EBI-555387;
CC P0A7R5; P0AA43: rsuA; NbExp=3; IntAct=EBI-544602, EBI-557810;
CC -!- MASS SPECTROMETRY: Mass=11734.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10094780};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS10 family.
CC {ECO:0000255|HAMAP-Rule:MF_00508, ECO:0000305}.
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DR EMBL; V00344; CAA23633.1; -; Genomic_DNA.
DR EMBL; X02613; CAA26459.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58118.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76346.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77970.1; -; Genomic_DNA.
DR EMBL; AF058450; AAC14290.1; -; Genomic_DNA.
DR PIR; A02720; R3EC10.
DR RefSeq; NP_417780.1; NC_000913.3.
DR RefSeq; WP_001181004.1; NZ_STEB01000038.1.
DR PDB; 2KVQ; NMR; -; E=1-45, E=68-103.
DR PDB; 2YKR; EM; 9.80 A; J=5-102.
DR PDB; 3D3B; X-ray; 1.30 A; J=1-45, J=68-103.
DR PDB; 3D3C; X-ray; 2.60 A; J/K/L=1-45, J/K/L=68-103.
DR PDB; 3IMQ; X-ray; 2.50 A; J/K/L=1-103.
DR PDB; 3J9Y; EM; 3.90 A; j=1-103.
DR PDB; 3J9Z; EM; 3.60 A; SJ=1-103.
DR PDB; 3JA1; EM; 3.60 A; SJ=1-103.
DR PDB; 3JBU; EM; 3.64 A; J=1-103.
DR PDB; 3JBV; EM; 3.32 A; J=1-103.
DR PDB; 3JCD; EM; 3.70 A; j=1-103.
DR PDB; 3JCE; EM; 3.20 A; j=1-103.
DR PDB; 3JCJ; EM; 3.70 A; r=1-102.
DR PDB; 3JCN; EM; 4.60 A; m=1-102.
DR PDB; 3W1Y; X-ray; 2.30 A; C=1-103.
DR PDB; 4A2I; EM; 16.50 A; J=5-102.
DR PDB; 4ADV; EM; 13.50 A; J=1-103.
DR PDB; 4U1U; X-ray; 2.95 A; AJ/CJ=5-102.
DR PDB; 4U1V; X-ray; 3.00 A; AJ/CJ=5-102.
DR PDB; 4U20; X-ray; 2.90 A; AJ/CJ=5-102.
DR PDB; 4U24; X-ray; 2.90 A; AJ/CJ=5-102.
DR PDB; 4U25; X-ray; 2.90 A; AJ/CJ=5-102.
DR PDB; 4U26; X-ray; 2.80 A; AJ/CJ=5-102.
DR PDB; 4U27; X-ray; 2.80 A; AJ/CJ=5-102.
DR PDB; 4V47; EM; 12.30 A; BJ=1-103.
DR PDB; 4V48; EM; 11.50 A; BJ=1-103.
DR PDB; 4V4H; X-ray; 3.46 A; AJ/CJ=1-103.
DR PDB; 4V4Q; X-ray; 3.46 A; AJ/CJ=1-103.
DR PDB; 4V4V; EM; 15.00 A; AJ=5-100.
DR PDB; 4V4W; EM; 15.00 A; AJ=5-100.
DR PDB; 4V50; X-ray; 3.22 A; AJ/CJ=1-103.
DR PDB; 4V52; X-ray; 3.21 A; AJ/CJ=1-103.
DR PDB; 4V53; X-ray; 3.54 A; AJ/CJ=1-103.
DR PDB; 4V54; X-ray; 3.30 A; AJ/CJ=1-103.
DR PDB; 4V55; X-ray; 4.00 A; AJ/CJ=1-103.
DR PDB; 4V56; X-ray; 3.93 A; AJ/CJ=1-103.
DR PDB; 4V57; X-ray; 3.50 A; AJ/CJ=1-103.
DR PDB; 4V5B; X-ray; 3.74 A; BJ/DJ=1-103.
DR PDB; 4V5H; EM; 5.80 A; AJ=5-102.
DR PDB; 4V5Y; X-ray; 4.45 A; AJ/CJ=1-103.
DR PDB; 4V64; X-ray; 3.50 A; AJ/CJ=1-103.
DR PDB; 4V65; EM; 9.00 A; AX=1-103.
DR PDB; 4V66; EM; 9.00 A; AX=1-103.
DR PDB; 4V69; EM; 6.70 A; AJ=5-102.
DR PDB; 4V6C; X-ray; 3.19 A; AJ/CJ=1-103.
DR PDB; 4V6D; X-ray; 3.81 A; AJ/CJ=1-103.
DR PDB; 4V6E; X-ray; 3.71 A; AJ/CJ=1-103.
DR PDB; 4V6K; EM; 8.25 A; BN=1-103.
DR PDB; 4V6L; EM; 13.20 A; AN=1-103.
DR PDB; 4V6M; EM; 7.10 A; AJ=1-103.
DR PDB; 4V6N; EM; 12.10 A; BM=1-103.
DR PDB; 4V6O; EM; 14.70 A; AM=1-103.
DR PDB; 4V6P; EM; 13.50 A; AM=1-103.
DR PDB; 4V6Q; EM; 11.50 A; AM=1-103.
DR PDB; 4V6R; EM; 11.50 A; AM=1-103.
DR PDB; 4V6S; EM; 13.10 A; BL=1-103.
DR PDB; 4V6T; EM; 8.30 A; AJ=5-102.
DR PDB; 4V6V; EM; 9.80 A; AJ=1-103.
DR PDB; 4V6Y; EM; 12.00 A; AJ=5-102.
DR PDB; 4V6Z; EM; 12.00 A; AJ=5-102.
DR PDB; 4V70; EM; 17.00 A; AJ=5-102.
DR PDB; 4V71; EM; 20.00 A; AJ=5-102.
DR PDB; 4V72; EM; 13.00 A; AJ=5-102.
DR PDB; 4V73; EM; 15.00 A; AJ=5-102.
DR PDB; 4V74; EM; 17.00 A; AJ=5-102.
DR PDB; 4V75; EM; 12.00 A; AJ=5-102.
DR PDB; 4V76; EM; 17.00 A; AJ=5-102.
DR PDB; 4V77; EM; 17.00 A; AJ=5-102.
DR PDB; 4V78; EM; 20.00 A; AJ=5-102.
DR PDB; 4V79; EM; 15.00 A; AJ=5-102.
DR PDB; 4V7A; EM; 9.00 A; AJ=5-102.
DR PDB; 4V7B; EM; 6.80 A; AJ=1-103.
DR PDB; 4V7C; EM; 7.60 A; AJ=1-103.
DR PDB; 4V7D; EM; 7.60 A; BJ=1-103.
DR PDB; 4V7I; EM; 9.60 A; BJ=1-103.
DR PDB; 4V7S; X-ray; 3.25 A; AJ/CJ=5-102.
DR PDB; 4V7T; X-ray; 3.19 A; AJ/CJ=5-102.
DR PDB; 4V7U; X-ray; 3.10 A; AJ/CJ=5-102.
DR PDB; 4V7V; X-ray; 3.29 A; AJ/CJ=5-102.
DR PDB; 4V85; X-ray; 3.20 A; AJ=1-103.
DR PDB; 4V89; X-ray; 3.70 A; AJ=1-103.
DR PDB; 4V9C; X-ray; 3.30 A; AJ/CJ=1-103.
DR PDB; 4V9D; X-ray; 3.00 A; AJ/BJ=5-102.
DR PDB; 4V9O; X-ray; 2.90 A; BJ/DJ/FJ/HJ=1-103.
DR PDB; 4V9P; X-ray; 2.90 A; BJ/DJ/FJ/HJ=1-103.
DR PDB; 4WF1; X-ray; 3.09 A; AJ/CJ=5-102.
DR PDB; 4WOI; X-ray; 3.00 A; AJ/DJ=1-103.
DR PDB; 4WWW; X-ray; 3.10 A; QJ/XJ=5-102.
DR PDB; 4YBB; X-ray; 2.10 A; AJ/BJ=4-102.
DR PDB; 5AFI; EM; 2.90 A; j=1-103.
DR PDB; 5H5U; EM; 3.00 A; q=1-103.
DR PDB; 5IQR; EM; 3.00 A; o=1-103.
DR PDB; 5IT8; X-ray; 3.12 A; AJ/BJ=4-102.
DR PDB; 5J5B; X-ray; 2.80 A; AJ/BJ=4-102.
DR PDB; 5J7L; X-ray; 3.00 A; AJ/BJ=4-102.
DR PDB; 5J88; X-ray; 3.32 A; AJ/BJ=4-102.
DR PDB; 5J8A; X-ray; 3.10 A; AJ/BJ=4-102.
DR PDB; 5J91; X-ray; 2.96 A; AJ/BJ=4-102.
DR PDB; 5JC9; X-ray; 3.03 A; AJ/BJ=4-102.
DR PDB; 5JTE; EM; 3.60 A; AJ=1-103.
DR PDB; 5JU8; EM; 3.60 A; AJ=1-103.
DR PDB; 5KCR; EM; 3.60 A; 1j=1-103.
DR PDB; 5KCS; EM; 3.90 A; 1j=1-103.
DR PDB; 5KPS; EM; 3.90 A; 15=1-103.
DR PDB; 5KPV; EM; 4.10 A; 14=1-103.
DR PDB; 5KPW; EM; 3.90 A; 14=1-103.
DR PDB; 5KPX; EM; 3.90 A; 14=1-103.
DR PDB; 5L3P; EM; 3.70 A; j=1-103.
DR PDB; 5LZA; EM; 3.60 A; j=5-102.
DR PDB; 5LZB; EM; 5.30 A; j=5-102.
DR PDB; 5LZC; EM; 4.80 A; j=5-102.
DR PDB; 5LZD; EM; 3.40 A; j=5-102.
DR PDB; 5LZE; EM; 3.50 A; j=5-102.
DR PDB; 5LZF; EM; 4.60 A; j=5-102.
DR PDB; 5MDV; EM; 2.97 A; o=1-103.
DR PDB; 5MDW; EM; 3.06 A; o=1-103.
DR PDB; 5MDY; EM; 3.35 A; o=1-103.
DR PDB; 5MDZ; EM; 3.10 A; o=1-103.
DR PDB; 5ME0; EM; 13.50 A; J=1-103.
DR PDB; 5ME1; EM; 13.50 A; J=1-103.
DR PDB; 5MGP; EM; 3.10 A; j=5-102.
DR PDB; 5MS0; EM; 9.80 A; E=4-103.
DR PDB; 5MY1; EM; 7.60 A; J=1-103.
DR PDB; 5NO2; EM; 5.16 A; J=4-102.
DR PDB; 5NO3; EM; 5.16 A; J=4-102.
DR PDB; 5NO4; EM; 5.16 A; J=4-102.
DR PDB; 5NP6; EM; 3.60 A; M=5-102.
DR PDB; 5NWY; EM; 2.93 A; 9=1-103.
DR PDB; 5O2R; EM; 3.40 A; j=5-102.
DR PDB; 5U4I; EM; 3.50 A; j=1-103.
DR PDB; 5U9F; EM; 3.20 A; J=1-103.
DR PDB; 5U9G; EM; 3.20 A; J=1-103.
DR PDB; 5UYK; EM; 3.90 A; J=5-102.
DR PDB; 5UYL; EM; 3.60 A; J=5-102.
DR PDB; 5UYM; EM; 3.20 A; J=5-102.
DR PDB; 5UYN; EM; 4.00 A; J=5-102.
DR PDB; 5UYP; EM; 3.90 A; J=5-102.
DR PDB; 5UYQ; EM; 3.80 A; J=5-102.
DR PDB; 5UZ4; EM; 5.80 A; J=1-103.
DR PDB; 5WDT; EM; 3.00 A; j=5-102.
DR PDB; 5WE4; EM; 3.10 A; j=5-102.
DR PDB; 5WE6; EM; 3.40 A; j=5-102.
DR PDB; 5WFK; EM; 3.40 A; j=5-102.
DR PDB; 6BU8; EM; 3.50 A; J=5-102.
DR PDB; 6BY1; X-ray; 3.94 A; AJ/BJ=5-102.
DR PDB; 6C4I; EM; 3.24 A; j=1-103.
DR PDB; 6ENF; EM; 3.20 A; j=5-102.
DR PDB; 6ENJ; EM; 3.70 A; j=5-102.
DR PDB; 6ENU; EM; 3.10 A; j=5-102.
DR PDB; 6GWT; EM; 3.80 A; j=5-102.
DR PDB; 6GXM; EM; 3.80 A; j=5-102.
DR PDB; 6GXN; EM; 3.90 A; j=5-102.
DR PDB; 6GXO; EM; 3.90 A; j=5-102.
DR PDB; 6GXP; EM; 4.40 A; j=5-102.
DR PDB; 6H4N; EM; 3.00 A; j=5-102.
DR PDB; 6H58; EM; 7.90 A; j/jj=5-102.
DR PDB; 6HRM; EM; 2.96 A; o=5-103.
DR PDB; 6I7V; X-ray; 2.90 A; AJ/BJ=5-102.
DR PDB; 6NQB; EM; 3.80 A; J=5-102.
DR PDB; 6O9J; EM; 3.90 A; j=5-102.
DR PDB; 6O9K; EM; 4.00 A; j=5-102.
DR PDB; 6OFX; EM; 3.30 A; O=5-102.
DR PDB; 6OG7; EM; 3.30 A; O=5-102.
DR PDB; 6ORE; EM; 2.90 A; o=5-103.
DR PDB; 6ORL; EM; 3.50 A; o=5-103.
DR PDB; 6OST; EM; 4.20 A; o=5-103.
DR PDB; 6OT3; EM; 3.90 A; o=5-103.
DR PDB; 6OUO; EM; 3.70 A; o=5-103.
DR PDB; 6Q97; EM; 3.90 A; o=5-103.
DR PDB; 6Q98; EM; 4.30 A; o=1-103.
DR PDB; 6Q9A; EM; 3.70 A; o=5-103.
DR PDB; 6SZS; EM; 3.06 A; j=1-103.
DR PDB; 6TBV; EM; 2.70 A; S101=1-103.
DR PDB; 6TC3; EM; 2.70 A; S101=1-103.
DR PDB; 6TQN; EM; 3.80 A; E=1-103.
DR PDB; 6TQO; EM; 4.00 A; E=1-103.
DR PDB; 6VWL; EM; 3.10 A; i=1-103.
DR PDB; 6VWM; EM; 3.40 A; i=1-103.
DR PDB; 6VWN; EM; 3.40 A; i=1-103.
DR PDB; 6W6K; EM; 3.60 A; J=1-103.
DR PDB; 6W77; EM; 3.60 A; J=1-103.
DR PDB; 6W7M; EM; 3.80 A; J=1-103.
DR PDB; 6W7N; EM; 3.40 A; J=1-103.
DR PDB; 6WD6; EM; 3.70 A; O=5-102.
DR PDB; 6WDB; EM; 4.00 A; O=5-102.
DR PDB; 6WDC; EM; 4.20 A; O=5-102.
DR PDB; 6WDD; EM; 3.20 A; O=5-102.
DR PDB; 6WDE; EM; 3.00 A; O=5-102.
DR PDB; 6WDF; EM; 3.30 A; O=5-102.
DR PDB; 6WDG; EM; 3.30 A; O=5-102.
DR PDB; 6WDH; EM; 4.30 A; O=5-102.
DR PDB; 6WDI; EM; 4.00 A; O=5-102.
DR PDB; 6WDJ; EM; 3.70 A; O=5-102.
DR PDB; 6WDK; EM; 3.60 A; O=5-102.
DR PDB; 6WDL; EM; 3.70 A; O=5-102.
DR PDB; 6WDM; EM; 3.60 A; O=5-102.
DR PDB; 6WNV; EM; 3.50 A; O=5-102.
DR PDB; 6WNW; EM; 3.20 A; O=5-102.
DR PDB; 6XE0; EM; 6.80 A; I=5-102.
DR PDB; 6XZA; EM; 2.66 A; J1=4-102.
DR PDB; 6XZB; EM; 2.54 A; J1=4-102.
DR PDB; 6Y69; EM; 2.86 A; j=5-102.
DR PDB; 6ZTL; EM; 3.50 A; AJ=1-103.
DR PDB; 7ABZ; EM; 3.21 A; o=5-102.
DR PDB; 7AC7; EM; 3.08 A; o=5-103.
DR PDB; 7ACJ; EM; 3.20 A; o=5-103.
DR PDB; 7ACR; EM; 3.44 A; o=5-103.
DR PDB; 7AF3; EM; 2.82 A; J=1-103.
DR PDB; 7AF5; EM; 2.96 A; J=1-103.
DR PDB; 7AF8; EM; 2.75 A; J=1-103.
DR PDB; 7AFA; EM; 2.95 A; J=1-103.
DR PDB; 7AFD; EM; 3.44 A; J=1-103.
DR PDB; 7AFH; EM; 3.59 A; J=1-103.
DR PDB; 7AFK; EM; 4.90 A; J=1-103.
DR PDB; 7AFN; EM; 3.86 A; J=1-103.
DR PDB; 7B5K; EM; 2.90 A; j=4-102.
DR PDB; 7BOE; EM; 2.90 A; J=1-103.
DR PDB; 7BOH; EM; 2.82 A; J=1-103.
DR PDB; 7D6Z; EM; 3.40 A; q=1-103.
DR PDB; 7D80; EM; 4.10 A; K=1-103.
DR PDB; 7JSS; EM; 3.70 A; O=5-102.
DR PDB; 7JSW; EM; 3.80 A; O=5-102.
DR PDB; 7JSZ; EM; 3.70 A; O=5-102.
DR PDB; 7JT1; EM; 3.30 A; O=5-102.
DR PDB; 7JT2; EM; 3.50 A; O=5-102.
DR PDB; 7JT3; EM; 3.70 A; O=5-102.
DR PDB; 7K50; EM; 3.40 A; O=5-102.
DR PDB; 7K51; EM; 3.50 A; O=5-102.
DR PDB; 7K52; EM; 3.40 A; O=5-102.
DR PDB; 7K53; EM; 3.20 A; O=5-102.
DR PDB; 7K54; EM; 3.20 A; O=5-102.
DR PDB; 7K55; EM; 3.30 A; O=5-102.
DR PDB; 7LV0; EM; 3.20 A; O=5-102.
DR PDB; 7N1P; EM; 2.33 A; SJ=1-103.
DR PDB; 7N2C; EM; 2.72 A; SJ=1-103.
DR PDB; 7N2U; EM; 2.53 A; SJ=1-103.
DR PDB; 7N2V; EM; 2.54 A; SJ=1-103.
DR PDB; 7N30; EM; 2.66 A; SJ=1-103.
DR PDB; 7N31; EM; 2.69 A; SJ=1-103.
DR PDB; 7NAR; EM; 3.00 A; J=1-103.
DR PDB; 7NAT; EM; 3.59 A; J=1-103.
DR PDB; 7NAU; EM; 3.78 A; J=1-103.
DR PDB; 7NAV; EM; 4.80 A; J=1-103.
DR PDB; 7NBU; EM; 3.11 A; J=5-102.
DR PDB; 7O19; EM; 2.90 A; AJ=1-103.
DR PDB; 7O1A; EM; 2.40 A; AJ=1-103.
DR PDB; 7O1C; EM; 2.60 A; AJ=1-103.
DR PDB; 7OE0; EM; 2.69 A; J=1-103.
DR PDB; 7OE1; EM; 3.05 A; J=1-103.
DR PDB; 7P3K; EM; 2.90 A; J=1-103.
DR PDB; 7PJV; EM; 3.10 A; j=1-103.
DR PDB; 7PJY; EM; 3.10 A; j=1-103.
DR PDB; 7QG8; EM; 3.97 A; 9=1-103.
DR PDB; 7SS9; EM; 3.90 A; O=5-102.
DR PDB; 7SSD; EM; 3.30 A; O=5-102.
DR PDB; 7SSL; EM; 3.80 A; O=5-102.
DR PDB; 7SSN; EM; 3.20 A; O=5-102.
DR PDB; 7SSO; EM; 3.20 A; O=5-102.
DR PDB; 7SSW; EM; 3.80 A; O=5-102.
DR PDB; 7ST2; EM; 2.90 A; O=5-102.
DR PDB; 7ST6; EM; 3.00 A; O=5-102.
DR PDB; 7ST7; EM; 3.20 A; O=5-102.
DR PDBsum; 2KVQ; -.
DR PDBsum; 2YKR; -.
DR PDBsum; 3D3B; -.
DR PDBsum; 3D3C; -.
DR PDBsum; 3IMQ; -.
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; 3W1Y; -.
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; 5MS0; -.
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; 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; 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; 6TQN; -.
DR PDBsum; 6TQO; -.
DR PDBsum; 6VWL; -.
DR PDBsum; 6VWM; -.
DR PDBsum; 6VWN; -.
DR PDBsum; 6W6K; -.
DR PDBsum; 6W77; -.
DR PDBsum; 6W7M; -.
DR PDBsum; 6W7N; -.
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; 7AF3; -.
DR PDBsum; 7AF5; -.
DR PDBsum; 7AF8; -.
DR PDBsum; 7AFA; -.
DR PDBsum; 7AFD; -.
DR PDBsum; 7AFH; -.
DR PDBsum; 7AFK; -.
DR PDBsum; 7AFN; -.
DR PDBsum; 7B5K; -.
DR PDBsum; 7BOE; -.
DR PDBsum; 7BOH; -.
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; 7NAT; -.
DR PDBsum; 7NAU; -.
DR PDBsum; 7NAV; -.
DR PDBsum; 7NBU; -.
DR PDBsum; 7O19; -.
DR PDBsum; 7O1A; -.
DR PDBsum; 7O1C; -.
DR PDBsum; 7OE0; -.
DR PDBsum; 7OE1; -.
DR PDBsum; 7P3K; -.
DR PDBsum; 7PJV; -.
DR PDBsum; 7PJY; -.
DR PDBsum; 7QG8; -.
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; P0A7R5; -.
DR SMR; P0A7R5; -.
DR BioGRID; 852128; 1.
DR ComplexPortal; CPX-3802; 30S small ribosomal subunit.
DR ComplexPortal; CPX-5674; Transcription elongation complex.
DR ComplexPortal; CPX-5780; lambdaN-dependent processive transcription antitermination complex.
DR DIP; DIP-35797N; -.
DR IntAct; P0A7R5; 135.
DR STRING; 511145.b3321; -.
DR DrugBank; DB00698; Nitrofurantoin.
DR MoonProt; P0A7R5; -.
DR jPOST; P0A7R5; -.
DR PaxDb; P0A7R5; -.
DR PRIDE; P0A7R5; -.
DR EnsemblBacteria; AAC76346; AAC76346; b3321.
DR EnsemblBacteria; BAE77970; BAE77970; BAE77970.
DR GeneID; 67415362; -.
DR GeneID; 947816; -.
DR KEGG; ecj:JW3283; -.
DR KEGG; eco:b3321; -.
DR PATRIC; fig|1411691.4.peg.3410; -.
DR EchoBASE; EB0902; -.
DR eggNOG; COG0051; Bacteria.
DR HOGENOM; CLU_122625_1_3_6; -.
DR InParanoid; P0A7R5; -.
DR OMA; QFEIRVH; -.
DR PhylomeDB; P0A7R5; -.
DR BioCyc; EcoCyc:EG10909-MON; -.
DR BioCyc; MetaCyc:EG10909-MON; -.
DR EvolutionaryTrace; P0A7R5; -.
DR PRO; PR:P0A7R5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:EcoliWiki.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0008023; C:transcription elongation factor complex; IC:ComplexPortal.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0001072; F:transcription antitermination factor activity, RNA binding; IDA:EcoCyc.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IC:ComplexPortal.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0031564; P:transcription antitermination; IDA:EcoCyc.
DR Gene3D; 3.30.70.600; -; 1.
DR HAMAP; MF_00508; Ribosomal_S10; 1.
DR InterPro; IPR001848; Ribosomal_S10.
DR InterPro; IPR018268; Ribosomal_S10_CS.
DR InterPro; IPR027486; Ribosomal_S10_dom.
DR InterPro; IPR036838; Ribosomal_S10_dom_sf.
DR PANTHER; PTHR11700; PTHR11700; 1.
DR Pfam; PF00338; Ribosomal_S10; 1.
DR PRINTS; PR00971; RIBOSOMALS10.
DR SMART; SM01403; Ribosomal_S10; 1.
DR SUPFAM; SSF54999; SSF54999; 1.
DR TIGRFAMs; TIGR01049; rpsJ_bact; 1.
DR PROSITE; PS00361; RIBOSOMAL_S10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Ribosome biogenesis; RNA-binding;
KW Transcription; Transcription antitermination; Transcription regulation.
FT CHAIN 1..103
FT /note="30S ribosomal protein S10"
FT /id="PRO_0000146529"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:3D3B"
FT HELIX 15..30
FT /evidence="ECO:0007829|PDB:3D3B"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:3D3B"
FT STRAND 35..45
FT /evidence="ECO:0007829|PDB:3D3B"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:3D3B"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:3D3B"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:3D3B"
SQ SEQUENCE 103 AA; 11736 MW; DAEB35A2557F1D59 CRC64;
MQNQRIRIRL KAFDHRLIDQ ATAEIVETAK RTGAQVRGPI PLPTRKERFT VLISPHVNKD
ARDQYEIRTH LRLVDIVEPT EKTVDALMRL DLAAGVDVQI SLG
