NUSG_ECOLI
ID NUSG_ECOLI Reviewed; 181 AA.
AC P0AFG0; P16921; Q2M8R8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Transcription termination/antitermination protein NusG {ECO:0000255|HAMAP-Rule:MF_00948};
GN Name=nusG {ECO:0000255|HAMAP-Rule:MF_00948};
GN OrderedLocusNames=b3982, JW3945;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2137819; DOI=10.1128/jb.172.3.1621-1627.1990;
RA Downing W.L., Sullivan S.L., Gottesman M.E., Dennis P.P.;
RT "Sequence and transcriptional pattern of the essential Escherichia coli
RT secE-nusG operon.";
RL J. Bacteriol. 172:1621-1627(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 2-5.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [6]
RP PROTEIN SEQUENCE OF 3-12, FUNCTION, AND INTERACTION WITH RNA POLYMERASE AND
RP RHO FACTOR.
RX PubMed=1532577; DOI=10.1016/s0021-9258(18)42655-5;
RA Li J., Horwitz R., McCracken S., Greenblatt J.;
RT "NusG, a new Escherichia coli elongation factor involved in transcriptional
RT antitermination by the N protein of phage lambda.";
RL J. Biol. Chem. 267:6012-6019(1992).
RN [7]
RP FUNCTION.
RX PubMed=1547498; DOI=10.1016/0092-8674(92)90041-a;
RA Sullivan S.L., Gottesman M.E.;
RT "Requirement for E. coli NusG protein in factor-dependent transcription
RT termination.";
RL Cell 68:989-994(1992).
RN [8]
RP FUNCTION.
RX PubMed=7505669;
RA Nehrke K.W., Zalatan F., Platt T.;
RT "NusG alters rho-dependent termination of transcription in vitro
RT independent of kinetic coupling.";
RL Gene Expr. 3:119-133(1993).
RN [9]
RP FUNCTION, AND INTERACTION WITH RHO FACTOR.
RX PubMed=8422985; DOI=10.1101/gad.7.1.161;
RA Li J., Mason S.W., Greenblatt J.;
RT "Elongation factor NusG interacts with termination factor rho to regulate
RT termination and antitermination of transcription.";
RL Genes Dev. 7:161-172(1993).
RN [10]
RP FUNCTION.
RX PubMed=7868616; DOI=10.1128/jb.177.5.1388-1392.1995;
RA Burova E., Hung S.C., Sagitov V., Stitt B.L., Gottesman M.E.;
RT "Escherichia coli NusG protein stimulates transcription elongation rates in
RT vivo and in vitro.";
RL J. Bacteriol. 177:1388-1392(1995).
RN [11]
RP FUNCTION.
RX PubMed=7761393; DOI=10.1073/pnas.92.11.4738;
RA Burns C.M., Richardson J.P.;
RT "NusG is required to overcome a kinetic limitation to Rho function at an
RT intragenic terminator.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4738-4742(1995).
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, SUBUNIT, AND INTERACTION WITH RHO.
RX PubMed=10820031; DOI=10.1021/bi992658z;
RA Pasman Z., von Hippel P.H.;
RT "Regulation of rho-dependent transcription termination by NusG is specific
RT to the Escherichia coli elongation complex.";
RL Biochemistry 39:5573-5585(2000).
RN [14]
RP FUNCTION IN RRNA TRANSCRIPTION ANTITERMINATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
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 STRUCTURE BY NMR OF 123-181, INTERACTION WITH RPSJ, AND DOMAIN.
RX PubMed=20413501; DOI=10.1126/science.1184953;
RA Burmann B.M., Schweimer K., Luo X., Wahl M.C., Stitt B.L., Gottesman M.E.,
RA Rosch P.;
RT "A NusE:NusG complex links transcription and translation.";
RL Science 328:501-504(2010).
RN [16] {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). Participates in transcription
CC elongation, termination and antitermination. In the absence of Rho,
CC increases the rate of transcription elongation by the RNAP, probably by
CC partially suppressing pausing. In the presence of Rho, modulates most
CC Rho-dependent termination events by interacting with the RNAP to render
CC the complex more susceptible to the termination activity of Rho. May be
CC required to overcome a kinetic limitation of Rho to function at certain
CC terminators. Also involved in ribosomal RNA and phage lambda N-mediated
CC transcriptional antitermination. {ECO:0000255|HAMAP-Rule:MF_00948,
CC ECO:0000269|PubMed:10383769, ECO:0000269|PubMed:10820031,
CC ECO:0000269|PubMed:14973028, ECO:0000269|PubMed:1532577,
CC ECO:0000269|PubMed:1547498, ECO:0000269|PubMed:32871103,
CC ECO:0000269|PubMed:7505669, ECO:0000269|PubMed:7761393,
CC ECO:0000269|PubMed:7868616, ECO:0000269|PubMed:8422985}.
CC -!- SUBUNIT: Monomer. Interacts with the transcription termination factor
CC Rho and with RNAP. One NusG monomer forms a stable complex with a Rho
CC hexamer. Binds directly, but weakly, to the core enzyme of RNAP. Also
CC interacts with RpsJ (NusE). The rRNA transcription and antitermination
CC complex (rrnTAC) consists of RNAP, NusA, NusB, NusE (rpsJ), NusG, SubB,
CC ribosomal protein S4, DNA and precursor rRNA; S4 is more flexible than
CC other subunits (PubMed:32871103). {ECO:0000255|HAMAP-Rule:MF_00948,
CC ECO:0000269|PubMed:10820031, ECO:0000269|PubMed:1532577,
CC ECO:0000269|PubMed:20413501, ECO:0000269|PubMed:32871103,
CC ECO:0000269|PubMed:8422985}.
CC -!- INTERACTION:
CC P0AFG0; P0ACJ8: crp; NbExp=2; IntAct=EBI-369628, EBI-547513;
CC P0AFG0; P0AG30: rho; NbExp=8; IntAct=EBI-369628, EBI-545468;
CC -!- DOMAIN: The N-terminal domain interacts with RNAP and the C-terminal
CC domain binds either to Rho or to RpsJ (NusE). These domains are
CC separated by a flexible linker. {ECO:0000269|PubMed:20413501}.
CC -!- SIMILARITY: Belongs to the NusG family. {ECO:0000255|HAMAP-
CC Rule:MF_00948}.
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DR EMBL; M30610; AAA24622.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43080.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76956.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77338.1; -; Genomic_DNA.
DR PIR; B35139; TWECNG.
DR RefSeq; NP_418409.1; NC_000913.3.
DR RefSeq; WP_001287516.1; NZ_STEB01000045.1.
DR PDB; 2JVV; NMR; -; A=1-181.
DR PDB; 2K06; NMR; -; A=1-123.
DR PDB; 2KVQ; NMR; -; G=123-181.
DR PDB; 5MS0; EM; 9.80 A; F=1-181.
DR PDB; 6C6U; EM; 3.70 A; N=1-181.
DR PDB; 6DUQ; X-ray; 3.70 A; M/N/O/P/Q/R/S/T/U/V/W/X=125-181.
DR PDB; 6TQN; EM; 3.80 A; G=1-181.
DR PDB; 6TQO; EM; 4.00 A; G=1-181.
DR PDB; 6XAV; EM; 7.70 A; L=1-181.
DR PDB; 6XE0; EM; 6.80 A; V=1-181.
DR PDB; 6Z9P; EM; 3.90 A; G=1-181.
DR PDB; 6Z9Q; EM; 5.70 A; G=1-181.
DR PDB; 6Z9R; EM; 4.10 A; G=1-181.
DR PDBsum; 2JVV; -.
DR PDBsum; 2K06; -.
DR PDBsum; 2KVQ; -.
DR PDBsum; 5MS0; -.
DR PDBsum; 6C6U; -.
DR PDBsum; 6DUQ; -.
DR PDBsum; 6TQN; -.
DR PDBsum; 6TQO; -.
DR PDBsum; 6XAV; -.
DR PDBsum; 6XE0; -.
DR PDBsum; 6Z9P; -.
DR PDBsum; 6Z9Q; -.
DR PDBsum; 6Z9R; -.
DR AlphaFoldDB; P0AFG0; -.
DR BMRB; P0AFG0; -.
DR SMR; P0AFG0; -.
DR BioGRID; 4259510; 11.
DR BioGRID; 852779; 4.
DR ComplexPortal; CPX-5674; Transcription elongation complex.
DR ComplexPortal; CPX-5780; lambdaN-dependent processive transcription antitermination complex.
DR DIP; DIP-31860N; -.
DR IntAct; P0AFG0; 61.
DR MINT; P0AFG0; -.
DR STRING; 511145.b3982; -.
DR SWISS-2DPAGE; P0AFG0; -.
DR jPOST; P0AFG0; -.
DR PaxDb; P0AFG0; -.
DR PRIDE; P0AFG0; -.
DR EnsemblBacteria; AAC76956; AAC76956; b3982.
DR EnsemblBacteria; BAE77338; BAE77338; BAE77338.
DR GeneID; 66672107; -.
DR GeneID; 948485; -.
DR KEGG; ecj:JW3945; -.
DR KEGG; eco:b3982; -.
DR PATRIC; fig|1411691.4.peg.2730; -.
DR EchoBASE; EB0661; -.
DR eggNOG; COG0250; Bacteria.
DR HOGENOM; CLU_067287_1_0_6; -.
DR InParanoid; P0AFG0; -.
DR OMA; DGPFNGF; -.
DR PhylomeDB; P0AFG0; -.
DR BioCyc; EcoCyc:EG10667-MON; -.
DR EvolutionaryTrace; P0AFG0; -.
DR PRO; PR:P0AFG0; -.
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:0006354; P:DNA-templated transcription, elongation; IEA:UniProtKB-UniRule.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IDA:EcoCyc.
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 DisProt; DP01496; -.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 3.30.70.940; -; 1.
DR HAMAP; MF_00948; NusG; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR006645; NGN_dom.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR043425; NusG-like.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR001062; Transcrpt_antiterm_NusG.
DR InterPro; IPR015869; Transcrpt_antiterm_NusG_bac_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR30265; PTHR30265; 1.
DR PANTHER; PTHR30265:SF2; PTHR30265:SF2; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF02357; NusG; 1.
DR PRINTS; PR00338; NUSGTNSCPFCT.
DR SMART; SM00739; KOW; 1.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF82679; SSF82679; 1.
DR TIGRFAMs; TIGR00922; nusG; 1.
DR PROSITE; PS01014; NUSG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Ribosome biogenesis; Transcription; Transcription antitermination;
KW Transcription regulation; Transcription termination.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9600841"
FT CHAIN 2..181
FT /note="Transcription termination/antitermination protein
FT NusG"
FT /id="PRO_0000113926"
FT DOMAIN 130..161
FT /note="KOW"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00948"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:2K06"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:2K06"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:2K06"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:2K06"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:2K06"
FT STRAND 86..99
FT /evidence="ECO:0007829|PDB:2K06"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:2K06"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:2JVV"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:2JVV"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:2JVV"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:2JVV"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:2JVV"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:2JVV"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:2JVV"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:2JVV"
SQ SEQUENCE 181 AA; 20532 MW; B3AF94284CC17B04 CRC64;
MSEAPKKRWY VVQAFSGFEG RVATSLREHI KLHNMEDLFG EVMVPTEEVV EIRGGQRRKS
ERKFFPGYVL VQMVMNDASW HLVRSVPRVM GFIGGTSDRP APISDKEVDA IMNRLQQVGD
KPRPKTLFEP GEMVRVNDGP FADFNGVVEE VDYEKSRLKV SVSIFGRATP VELDFSQVEK
A
