NUSB_ECOLI
ID NUSB_ECOLI Reviewed; 139 AA.
AC P0A780; P04381; Q2MC10;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Transcription antitermination protein NusB {ECO:0000255|HAMAP-Rule:MF_00073, ECO:0000305};
DE AltName: Full=Antitermination factor NusB {ECO:0000255|HAMAP-Rule:MF_00073, ECO:0000303|PubMed:7678781};
DE AltName: Full=N utilization substance protein B {ECO:0000305};
GN Name=nusB {ECO:0000255|HAMAP-Rule:MF_00073, ECO:0000303|PubMed:7045592};
GN Synonyms=groNB {ECO:0000303|PubMed:6330693},
GN ssyB {ECO:0000303|PubMed:1406588}; OrderedLocusNames=b0416, JW0406;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-8.
RX PubMed=6330693; DOI=10.1093/nar/12.12.4977;
RA Swindle J., Ajioka J., Dawson D., Myers R., Carroll D., Georgopoulos C.;
RT "The nucleotide sequence of the Escherichia coli K12 nusB (groNB) gene.";
RL Nucleic Acids Res. 12:4977-4985(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-11.
RX PubMed=6330694; DOI=10.1093/nar/12.12.4987;
RA Ishii S., Hatada E., Maekawa T., Imamoto F.;
RT "Molecular cloning and nucleotide sequencing of the nusB gene of E. coli.";
RL Nucleic Acids Res. 12:4987-4995(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3019094; DOI=10.1016/0065-227x(86)90022-5;
RA Imamoto F., Nakamura Y.;
RT "Escherichia coli proteins involved in regulation of transcription
RT termination: function, structure, and expression of the nusA and nusB
RT genes.";
RL Adv. Biophys. 21:175-192(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=1406588; DOI=10.1007/bf00538702;
RA Taura T., Ueguchi C., Shiba K., Ito K.;
RT "Insertional disruption of the nusB (ssyB) gene leads to cold-sensitive
RT growth of Escherichia coli and suppression of the secY24 mutation.";
RL Mol. Gen. Genet. 234:429-432(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
RP FUNCTION.
RX PubMed=7045592; DOI=10.1007/bf00330816;
RA Kuroki K., Ishii S., Kano Y., Miyashita T., Nishi K., Imamoto F.;
RT "Involvement of the nusA and nusB gene products in transcription of
RT Escherichia coli tryptophan operon in vitro.";
RL Mol. Gen. Genet. 185:369-371(1982).
RN [9]
RP INTERACTION WITH RIBOSOMAL PROTEIN S10.
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, AND RNA-BINDING.
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 FUNCTION.
RX PubMed=10383769; DOI=10.1046/j.1365-2958.1999.01442.x;
RA Zellars M., Squires C.L.;
RT "Antiterminator-dependent modulation of transcription elongation rates by
RT NusB and NusG.";
RL Mol. Microbiol. 32:1296-1304(1999).
RN [13]
RP FUNCTION, AND INTERACTION WITH RIBOSOMAL PROTEIN S10.
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.
RX PubMed=14973028; DOI=10.1128/jb.186.5.1304-1310.2004;
RA Torres M., Balada J.M., Zellars M., Squires C., Squires C.L.;
RT "In vivo effect of NusB and NusG on rRNA transcription antitermination.";
RL J. Bacteriol. 186:1304-1310(2004).
RN [15]
RP FUNCTION.
RX PubMed=15716433; DOI=10.1128/jb.187.5.1632-1638.2005;
RA Quan S., Zhang N., French S., Squires C.L.;
RT "Transcriptional polarity in rRNA operons of Escherichia coli nusA and nusB
RT mutant strains.";
RL J. Bacteriol. 187:1632-1638(2005).
RN [16]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH RIBOSOMAL PROTEIN S10.
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 [17]
RP STRUCTURE BY NMR, AND DOMAIN.
RX PubMed=9670024; DOI=10.1093/emboj/17.14.4092;
RA Huenges M., Rolz C., Gschwind R., Peteranderl R., Berglechner F.,
RA Richter G., Bacher A., Kessler H., Gemmecker G.;
RT "Solution structure of the antitermination protein NusB of Escherichia
RT coli: a novel all-helical fold for an RNA-binding protein.";
RL EMBO J. 17:4092-4100(1998).
RN [18] {ECO:0007744|PDB:1EY1}
RP STRUCTURE BY NMR, AND SUBUNIT.
RX PubMed=10881193; DOI=10.1038/75869;
RA Altieri A.S., Mazzulla M.J., Horita D.A., Coats R.H., Wingfield P.T.,
RA Das A., Court D.L., Byrd R.A.;
RT "The structure of the transcriptional antiterminator NusB from Escherichia
RT coli.";
RL Nat. Struct. Biol. 7:470-474(2000).
RN [19] {ECO:0007744|PDB:3D3B, ECO:0007744|PDB:3D3C}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH RIBOSOMAL PROTEIN
RP S10, 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: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: Part of the processive rRNA transcription and antitermination
CC complex (rrnTAC). The complex forms an RNA-chaperone ring around the
CC RNA exit tunnel of RNA polymerase (RNAP). It supports rapid
CC transcription and antitermination of rRNA operons, cotranscriptional
CC rRNA folding, and annealing of distal rRNA regions to allow correct
CC ribosome biogenesis (PubMed:32871103). Involved in transcription
CC antitermination. Required for transcription of ribosomal RNA (rRNA)
CC genes. Binds specifically to the boxA antiterminator sequence of the
CC ribosomal RNA (rrn) operons (PubMed:7045592, PubMed:7678781,
CC PubMed:11884128, PubMed:14973028, PubMed:15716433, PubMed:16109710).
CC The affinity of NusB for the boxA RNA sequence is significantly
CC increased in the presence of the ribosomal protein S10
CC (PubMed:16109710, PubMed:11884128). NusB may serve as a loading factor
CC that ensures efficient entry of S10 into the transcription complexes
CC (PubMed:19111659). It also modulates the rrn boxA-mediated
CC transcription elongation rates (PubMed:10383769).
CC {ECO:0000269|PubMed:10383769, ECO:0000269|PubMed:11884128,
CC ECO:0000269|PubMed:14973028, ECO:0000269|PubMed:15716433,
CC ECO:0000269|PubMed:16109710, ECO:0000269|PubMed:19111659,
CC ECO:0000269|PubMed:32871103, ECO:0000269|PubMed:7045592,
CC ECO:0000269|PubMed:7678781}.
CC -!- SUBUNIT: Monomer in solution (PubMed:10881193, PubMed:16109710). Forms
CC a heterodimer with the ribosomal protein S10 (PubMed:1731086,
CC PubMed:11884128, PubMed:16109710, PubMed:19111659). The rRNA
CC transcription and antitermination complex (rrnTAC) consists of RNAP,
CC NusA, NusB, NusE (rpsJ), NusG, SubB, ribosomal protein S4, DNA and
CC precursor rRNA; S4 is more flexible than other subunits
CC (PubMed:32871103). {ECO:0000269|PubMed:10881193,
CC ECO:0000269|PubMed:11884128, ECO:0000269|PubMed:16109710,
CC ECO:0000269|PubMed:1731086, ECO:0000269|PubMed:19111659,
CC ECO:0000269|PubMed:32871103}.
CC -!- INTERACTION:
CC P0A780; P0A7R5: rpsJ; NbExp=6; IntAct=EBI-555387, EBI-544602;
CC -!- DOMAIN: The N-terminal region functions as an arginine-rich RNA-binding
CC motif (ARM). {ECO:0000269|PubMed:9670024}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene causes cold-sensitive
CC cell growth. {ECO:0000269|PubMed:1406588}.
CC -!- SIMILARITY: Belongs to the NusB family. {ECO:0000255|HAMAP-
CC Rule:MF_00073, ECO:0000305}.
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DR EMBL; X00681; CAA25289.1; -; Genomic_DNA.
DR EMBL; X64395; CAA45737.1; -; Genomic_DNA.
DR EMBL; M26839; AAA24228.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40172.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73519.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76196.1; -; Genomic_DNA.
DR PIR; I51822; FJECB.
DR RefSeq; NP_414950.1; NC_000913.3.
DR RefSeq; WP_000801125.1; NZ_STEB01000007.1.
DR PDB; 1EY1; NMR; -; A=1-139.
DR PDB; 3D3B; X-ray; 1.30 A; A=1-139.
DR PDB; 3D3C; X-ray; 2.60 A; A/B/C=1-139.
DR PDB; 3IMQ; X-ray; 2.50 A; A/B/C=3-139.
DR PDB; 5MS0; EM; 9.80 A; L=1-139.
DR PDB; 6TQN; EM; 3.80 A; B=1-139.
DR PDB; 6TQO; EM; 4.00 A; B=1-139.
DR PDBsum; 1EY1; -.
DR PDBsum; 3D3B; -.
DR PDBsum; 3D3C; -.
DR PDBsum; 3IMQ; -.
DR PDBsum; 5MS0; -.
DR PDBsum; 6TQN; -.
DR PDBsum; 6TQO; -.
DR AlphaFoldDB; P0A780; -.
DR SMR; P0A780; -.
DR BioGRID; 4259834; 56.
DR ComplexPortal; CPX-5674; Transcription elongation complex.
DR ComplexPortal; CPX-5780; lambdaN-dependent processive transcription antitermination complex.
DR DIP; DIP-48254N; -.
DR IntAct; P0A780; 12.
DR STRING; 511145.b0416; -.
DR jPOST; P0A780; -.
DR PaxDb; P0A780; -.
DR PRIDE; P0A780; -.
DR EnsemblBacteria; AAC73519; AAC73519; b0416.
DR EnsemblBacteria; BAE76196; BAE76196; BAE76196.
DR GeneID; 67416509; -.
DR GeneID; 945054; -.
DR KEGG; ecj:JW0406; -.
DR KEGG; eco:b0416; -.
DR PATRIC; fig|1411691.4.peg.1861; -.
DR EchoBASE; EB0660; -.
DR eggNOG; COG0781; Bacteria.
DR HOGENOM; CLU_087843_4_1_6; -.
DR InParanoid; P0A780; -.
DR OMA; DRMPVVD; -.
DR PhylomeDB; P0A780; -.
DR BioCyc; EcoCyc:EG10666-MON; -.
DR EvolutionaryTrace; P0A780; -.
DR PRO; PR:P0A780; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008023; C:transcription elongation factor complex; IC:ComplexPortal.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-UniRule.
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:ComplexPortal.
DR Gene3D; 1.10.940.10; -; 1.
DR HAMAP; MF_00073; NusB; 1.
DR InterPro; IPR035926; NusB-like_sf.
DR InterPro; IPR011605; NusB_fam.
DR InterPro; IPR006027; NusB_RsmB_TIM44.
DR PANTHER; PTHR11078; PTHR11078; 1.
DR Pfam; PF01029; NusB; 1.
DR SUPFAM; SSF48013; SSF48013; 1.
DR TIGRFAMs; TIGR01951; nusB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Ribosome biogenesis; RNA-binding; Transcription;
KW Transcription antitermination; Transcription regulation.
FT CHAIN 1..139
FT /note="Transcription antitermination protein NusB"
FT /id="PRO_0000176536"
FT VARIANT 18
FT /note="Y -> D (in nusB5; abolishes antitermination)"
FT CONFLICT 59
FT /note="T -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 4..23
FT /evidence="ECO:0007829|PDB:3D3B"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:3D3B"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1EY1"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:3D3B"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:3D3B"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:3D3B"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:3IMQ"
FT HELIX 79..94
FT /evidence="ECO:0007829|PDB:3D3B"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:3D3B"
FT HELIX 119..134
FT /evidence="ECO:0007829|PDB:3D3B"
SQ SEQUENCE 139 AA; 15689 MW; 0BB912103061243B CRC64;
MKPAARRRAR ECAVQALYSW QLSQNDIADV EYQFLAEQDV KDVDVLYFRE LLAGVATNTA
YLDGLMKPYL SRLLEELGQV EKAVLRIALY ELSKRSDVPY KVAINEAIEL AKSFGAEDSH
KFVNGVLDKA APVIRPNKK
