NUSA_ECOLI
ID NUSA_ECOLI Reviewed; 495 AA.
AC P0AFF6; P03003; Q2M941;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Transcription termination/antitermination protein NusA {ECO:0000255|HAMAP-Rule:MF_00945};
DE AltName: Full=N utilization substance protein A;
DE AltName: Full=Transcription termination/antitermination L factor {ECO:0000303|PubMed:6154941};
GN Name=nusA {ECO:0000255|HAMAP-Rule:MF_00945};
GN OrderedLocusNames=b3169, JW3138;
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=6326058; DOI=10.1093/nar/12.7.3333;
RA Ishii S., Ihara M., Maekawa T., Nakamura Y., Uchida H., Imamoto F.;
RT "The nucleotide sequence of the cloned nusA gene and its flanking region of
RT Escherichia coli.";
RL Nucleic Acids Res. 12:3333-3342(1984).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=3027511; DOI=10.1007/bf00430455;
RA Saito M., Tsugawa A., Egawa K., Nakamura Y.;
RT "Revised sequence of the nusA gene of Escherichia coli and identification
RT of nusA11 (ts) and nusA1 mutations which cause changes in a hydrophobic
RT amino acid cluster.";
RL Mol. Gen. Genet. 205:380-382(1986).
RN [3]
RP SEQUENCE REVISION, PARTIAL PROTEIN SEQUENCE, INDUCTION, AND MUTAGENESIS OF
RP ARG-104; GLY-181; LEU-183 AND GLU-212.
RX PubMed=1847365; DOI=10.1128/jb.173.4.1492-1501.1991;
RA Ito K., Egawa K., Nakamura Y.;
RT "Genetic interaction between the beta' subunit of RNA polymerase and the
RT arginine-rich domain of Escherichia coli nusA protein.";
RL J. Bacteriol. 173:1492-1501(1991).
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 1-13.
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 IDENTIFICATION AS L FACTOR, AND INTERACTION WITH N PROTEIN.
RX PubMed=6154941; DOI=10.1073/pnas.77.4.1991;
RA Greenblatt J., Li J., Adhya S., Friedman D.I., Baron L.S., Redfield B.,
RA Kung H.F., Weissbach H.;
RT "L factor that is required for beta-galactosidase synthesis is the nusA
RT gene product involved in transcription termination.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:1991-1994(1980).
RN [8]
RP FUNCTION, AND INTERACTION WITH RNA POLYMERASE.
RX PubMed=6263495; DOI=10.1016/0092-8674(81)90332-9;
RA Greenblatt J., Li J.;
RT "Interaction of the sigma factor and the nusA gene protein of E. coli with
RT RNA polymerase in the initiation-termination cycle of transcription.";
RL Cell 24:421-428(1981).
RN [9]
RP FUNCTION.
RX PubMed=6265785; DOI=10.1038/292215a0;
RA Greenblatt J., McLimont M., Hanly S.;
RT "Termination of transcription by nusA gene protein of Escherichia coli.";
RL Nature 292:215-220(1981).
RN [10]
RP INDUCTION BY COLD-SHOCK.
RC STRAIN=CSH142;
RX PubMed=8898389; DOI=10.1111/j.1365-2958.1996.tb02582.x;
RA Jones P.G., Inouye M.;
RT "RbfA, a 30S ribosomal binding factor, is a cold-shock protein whose
RT absence triggers the cold-shock response.";
RL Mol. Microbiol. 21:1207-1218(1996).
RN [11]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=6199039; DOI=10.1021/bi00297a004;
RA Schmidt M.C., Chamberlin M.J.;
RT "Amplification and isolation of Escherichia coli nusA protein and studies
RT of its effects on in vitro RNA chain elongation.";
RL Biochemistry 23:197-203(1984).
RN [12]
RP INTERACTION WITH RHO.
RX PubMed=6096352; DOI=10.1016/s0021-9258(17)42501-4;
RA Schmidt M.C., Chamberlin M.J.;
RT "Binding of rho factor to Escherichia coli RNA polymerase mediated by nusA
RT protein.";
RL J. Biol. Chem. 259:15000-15002(1984).
RN [13]
RP INDUCTION.
RX PubMed=2987884; DOI=10.1093/nar/13.9.3371;
RA Plumbridge J.A., Dondon J., Nakamura Y., Grunberg-Manago M.;
RT "Effect of NusA protein on expression of the nusA,infB operon in E. coli.";
RL Nucleic Acids Res. 13:3371-3388(1985).
RN [14]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=2821282; DOI=10.1016/0022-2836(87)90486-4;
RA Schmidt M.C., Chamberlin M.J.;
RT "nusA protein of Escherichia coli is an efficient transcription termination
RT factor for certain terminator sites.";
RL J. Mol. Biol. 195:809-818(1987).
RN [15]
RP SUBUNIT, AND INTERACTION WITH RNA POLYMERASE.
RX PubMed=1856861; DOI=10.1016/0022-2836(91)90015-x;
RA Gill S.C., Weitzel S.E., von Hippel P.H.;
RT "Escherichia coli sigma 70 and NusA proteins. I. Binding interactions with
RT core RNA polymerase in solution and within the transcription complex.";
RL J. Mol. Biol. 220:307-324(1991).
RN [16]
RP FUNCTION, AND INTERACTION WITH NASCENT RNA.
RX PubMed=7536848; DOI=10.1016/s0022-2836(05)80136-6;
RA Liu K., Hanna M.M.;
RT "NusA contacts nascent RNA in Escherichia coli transcription complexes.";
RL J. Mol. Biol. 247:547-558(1995).
RN [17]
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 [18]
RP FUNCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=9139668; DOI=10.1074/jbc.272.19.12265;
RA Vogel U., Jensen K.F.;
RT "NusA is required for ribosomal antitermination and for modulation of the
RT transcription elongation rate of both antiterminated RNA and mRNA.";
RL J. Biol. Chem. 272:12265-12271(1997).
RN [19]
RP FUNCTION.
RX PubMed=11719185; DOI=10.1016/s0092-8674(01)00582-7;
RA Gusarov I., Nudler E.;
RT "Control of intrinsic transcription termination by N and NusA: the basic
RT mechanisms.";
RL Cell 107:437-449(2001).
RN [20]
RP SUBCELLULAR LOCATION.
RX PubMed=17272300; DOI=10.1093/nar/gkl1158;
RA Watt R.M., Wang J., Leong M., Kung H.F., Cheah K.S., Liu D., Danchin A.,
RA Huang J.D.;
RT "Visualizing the proteome of Escherichia coli: an efficient and versatile
RT method for labeling chromosomal coding DNA sequences (CDSs) with
RT fluorescent protein genes.";
RL Nucleic Acids Res. 35:E37-E37(2007).
RN [21]
RP FUNCTION IN DNA REPAIR, AND DISRUPTION PHENOTYPE.
RX PubMed=20696893; DOI=10.1073/pnas.1005203107;
RA Cohen S.E., Lewis C.A., Mooney R.A., Kohanski M.A., Collins J.J.,
RA Landick R., Walker G.C.;
RT "Roles for the transcription elongation factor NusA in both DNA repair and
RT damage tolerance pathways in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:15517-15522(2010).
RN [22]
RP REVIEW, FUNCTION, AND DOMAIN.
RX PubMed=21922055; DOI=10.4161/trns.2.3.15671;
RA Burmann B.M., Rosch P.;
RT "The role of E. coli Nus-factors in transcription regulation and
RT transcription:translation coupling: From structure to mechanism.";
RL Transcription 2:130-134(2011).
RN [23]
RP FUNCTION, INTERACTION WITH SUHB, INTERACTION WITH RPOA, AND DOMAIN.
RX PubMed=31127279; DOI=10.1093/nar/gkz442;
RA Dudenhoeffer B.R., Schneider H., Schweimer K., Knauer S.H.;
RT "SuhB is an integral part of the ribosomal antitermination complex and
RT interacts with NusA.";
RL Nucleic Acids Res. 47:6504-6518(2019).
RN [24]
RP INTERACTION WITH ESCHERICHIA PHAGE LAMBDA ANTITERMINATION PROTEIN Q
RP (MICROBIAL INFECTION).
RX PubMed=32313022; DOI=10.1038/s41598-020-63523-5;
RA Dudenhoeffer B.R., Borggraefe J., Schweimer K., Knauer S.H.;
RT "NusA directly interacts with antitermination factor Q from phage lambda.";
RL Sci. Rep. 10:6607-6607(2020).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 352-421, AND DOMAIN.
RX PubMed=15365170; DOI=10.1073/pnas.0405883101;
RA Bonin I., Muhlberger R., Bourenkov G.P., Huber R., Bacher A., Richter G.,
RA Wahl M.C.;
RT "Structural basis for the interaction of Escherichia coli NusA with protein
RT N of phage lambda.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13762-13767(2004).
RN [26]
RP STRUCTURE BY NMR OF 351-426, AND DOMAIN.
RX PubMed=15987884; DOI=10.1110/ps.051372205;
RA Eisenmann A., Schwarz S., Prasch S., Schweimer K., Rosch P.;
RT "The E. coli NusA carboxy-terminal domains are structurally similar and
RT show specific RNAP- and lambdaN interaction.";
RL Protein Sci. 14:2018-2029(2005).
RN [27]
RP STRUCTURE BY NMR OF 424-495.
RA Prasch S., Schweimer K., Roesch P.;
RT "structural basis of transcription elongation control: the NusA-aCTD
RT complex.";
RL Submitted (JAN-2008) to the PDB data bank.
RN [28]
RP STRUCTURE BY NMR OF 1-125.
RA Jurk M., Schweimer K., Roesch P.;
RT "Solution structure of the aminoterminal domain of E. coli NusA.";
RL Submitted (APR-2010) to the PDB data bank.
RN [29] {ECO:0007744|PDB:6IB8}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 427-495 IN COMPLEX WITH SUHB,
RP FUNCTION, SUBUNIT, INTERACTION WITH RPOA, INTERACTION WITH SUHB, AND
RP DOMAIN.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=31020314; DOI=10.1093/nar/gkz290;
RA Huang Y.H., Said N., Loll B., Wahl M.C.;
RT "Structural basis for the function of SuhB as a transcription factor in
RT ribosomal RNA synthesis.";
RL Nucleic Acids Res. 47:6488-6503(2019).
RN [30] {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 both
CC transcription termination and antitermination. Involved in a variety of
CC cellular termination and antitermination processes, such as Rho-
CC dependent transcriptional termination and intrinsic termination
CC (PubMed:31020314). Domain AR2 interacts with a large number of other
CC proteins and may serve as a platform to recruit these factors for
CC transcriptional regulation (PubMed:31127279). Involved in phage lambda
CC N-mediated transcriptional antitermination. Also important for
CC coordinating the cellular responses to DNA damage by coupling the
CC processes of nucleotide excision repair and translesion synthesis to
CC transcription. {ECO:0000255|HAMAP-Rule:MF_00945,
CC ECO:0000269|PubMed:11719185, ECO:0000269|PubMed:20696893,
CC ECO:0000269|PubMed:21922055, ECO:0000269|PubMed:2821282,
CC ECO:0000269|PubMed:31020314, ECO:0000269|PubMed:31127279,
CC ECO:0000269|PubMed:32871103, ECO:0000269|PubMed:6199039,
CC ECO:0000269|PubMed:6263495, ECO:0000269|PubMed:6265785,
CC ECO:0000269|PubMed:7536848, ECO:0000269|PubMed:9139668}.
CC -!- SUBUNIT: Monomer. Binds directly to the core enzyme of the DNA-
CC dependent RNA polymerase (RNAP) (PubMed:6263495, PubMed:1856861).
CC Interacts with nascent RNA (PubMed:7536848). Interacts with the
CC termination Rho factor (PubMed:6096352). Interacts with the phage
CC lambda N protein (PubMed:6154941). Interacts with SuhB via the AR2
CC domain, crystallizes as a 2:1 SuhB:NusA heterotrimer. 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:31020314, PubMed:31127279). NusG and the alpha-CTD of RNAP
CC interact with the AR2 domain (PubMed:31127279). {ECO:0000255|HAMAP-
CC Rule:MF_00945, ECO:0000269|PubMed:1856861, ECO:0000269|PubMed:31020314,
CC ECO:0000269|PubMed:31127279, ECO:0000269|PubMed:6096352,
CC ECO:0000269|PubMed:6154941, ECO:0000269|PubMed:6263495,
CC ECO:0000269|PubMed:7536848}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via N-terminus and AR2
CC domain) with Escherichia phage lambda antitermination protein Q; this
CC interaction (AR2 domain) releases the autoinhibition of NusA.
CC {ECO:0000269|PubMed:32313022}.
CC -!- INTERACTION:
CC P0AFF6; Q47155: dinB; NbExp=3; IntAct=EBI-551571, EBI-1037359;
CC P0AFF6; P0A8U6: metJ; NbExp=3; IntAct=EBI-551571, EBI-555272;
CC P0AFF6; P0A7Z4: rpoA; NbExp=7; IntAct=EBI-551571, EBI-544985;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00945,
CC ECO:0000269|PubMed:17272300}. Note=Colocalizes with nucleoids.
CC -!- INDUCTION: In response to low temperature. Negatively autoregulated.
CC Induced by cold shock (42 to 15 degrees Celsius) (at protein level)
CC (PubMed:8898389). {ECO:0000269|PubMed:1847365,
CC ECO:0000269|PubMed:2987884, ECO:0000269|PubMed:8898389}.
CC -!- DOMAIN: The N-terminal region interacts with RNAP (PubMed:21922055).
CC The central region is composed of 3 RNA binding domains, S1, KH 1 and
CC KH 2. The C-terminal region contains 2 acidic repeats, AR1 and AR2,
CC which bind to protein N from phage lambda during antitermination. AR2
CC interacts with SuhB and RNAP alpha subunit C-terminal domain (rpoA);
CC AR2 cannot bind to both simultaneously (PubMed:31020314,
CC PubMed:31127279). SuhB, NusG and the alpha-CTD of RNAP all interact
CC with the AR2 domain and can displace the AR2 domain from the SSK domain
CC (S1, KH1 and KH2) of NusA (PubMed:31127279).
CC {ECO:0000269|PubMed:15365170, ECO:0000269|PubMed:15987884,
CC ECO:0000269|PubMed:21922055, ECO:0000269|PubMed:31020314,
CC ECO:0000269|PubMed:31127279}.
CC -!- DISRUPTION PHENOTYPE: Mutants are sensitive to DNA-damaging agents.
CC {ECO:0000269|PubMed:20696893}.
CC -!- SIMILARITY: Belongs to the NusA family. {ECO:0000255|HAMAP-
CC Rule:MF_00945}.
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DR EMBL; X00513; CAA25200.1; -; Genomic_DNA.
DR EMBL; U18997; AAA57972.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76203.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77215.1; -; Genomic_DNA.
DR PIR; E65107; FJEC.
DR RefSeq; NP_417638.1; NC_000913.3.
DR RefSeq; WP_001031057.1; NZ_STEB01000012.1.
DR PDB; 1U9L; X-ray; 1.90 A; A/B=352-421.
DR PDB; 1WCL; NMR; -; A=351-426.
DR PDB; 1WCN; NMR; -; A=426-495.
DR PDB; 2JZB; NMR; -; B=424-495.
DR PDB; 2KWP; NMR; -; A=1-125.
DR PDB; 5LM9; X-ray; 2.14 A; A=101-426.
DR PDB; 5MS0; EM; 9.80 A; M=1-495.
DR PDB; 6FLQ; EM; 4.10 A; F=1-495.
DR PDB; 6IB8; X-ray; 1.65 A; C=427-495.
DR PDB; 6TQN; EM; 3.80 A; A=1-495.
DR PDB; 6TQO; EM; 4.00 A; A=1-495.
DR PDB; 6XAS; EM; 3.80 A; G=1-495.
DR PDB; 6XAV; EM; 7.70 A; G=1-495.
DR PDB; 6Z9P; EM; 3.90 A; A=1-495.
DR PDB; 6Z9Q; EM; 5.70 A; A=1-495.
DR PDB; 6Z9R; EM; 4.10 A; A=1-495.
DR PDB; 6Z9S; EM; 4.40 A; A=1-495.
DR PDB; 6Z9T; EM; 4.10 A; A=1-495.
DR PDB; 7ADB; EM; 4.40 A; A=1-495.
DR PDB; 7ADC; EM; 4.00 A; A=1-495.
DR PDB; 7ADD; EM; 4.30 A; A=1-495.
DR PDB; 7ADE; EM; 4.20 A; A=1-495.
DR PDBsum; 1U9L; -.
DR PDBsum; 1WCL; -.
DR PDBsum; 1WCN; -.
DR PDBsum; 2JZB; -.
DR PDBsum; 2KWP; -.
DR PDBsum; 5LM9; -.
DR PDBsum; 5MS0; -.
DR PDBsum; 6FLQ; -.
DR PDBsum; 6IB8; -.
DR PDBsum; 6TQN; -.
DR PDBsum; 6TQO; -.
DR PDBsum; 6XAS; -.
DR PDBsum; 6XAV; -.
DR PDBsum; 6Z9P; -.
DR PDBsum; 6Z9Q; -.
DR PDBsum; 6Z9R; -.
DR PDBsum; 6Z9S; -.
DR PDBsum; 6Z9T; -.
DR PDBsum; 7ADB; -.
DR PDBsum; 7ADC; -.
DR PDBsum; 7ADD; -.
DR PDBsum; 7ADE; -.
DR AlphaFoldDB; P0AFF6; -.
DR BMRB; P0AFF6; -.
DR SMR; P0AFF6; -.
DR BioGRID; 4261878; 15.
DR BioGRID; 851995; 1.
DR ComplexPortal; CPX-5674; Transcription elongation complex.
DR ComplexPortal; CPX-5780; lambdaN-dependent processive transcription antitermination complex.
DR DIP; DIP-47857N; -.
DR IntAct; P0AFF6; 45.
DR STRING; 511145.b3169; -.
DR SWISS-2DPAGE; P0AFF6; -.
DR jPOST; P0AFF6; -.
DR PaxDb; P0AFF6; -.
DR PRIDE; P0AFF6; -.
DR EnsemblBacteria; AAC76203; AAC76203; b3169.
DR EnsemblBacteria; BAE77215; BAE77215; BAE77215.
DR GeneID; 66672929; -.
DR GeneID; 947682; -.
DR KEGG; ecj:JW3138; -.
DR KEGG; eco:b3169; -.
DR PATRIC; fig|1411691.4.peg.3561; -.
DR EchoBASE; EB0659; -.
DR eggNOG; COG0195; Bacteria.
DR HOGENOM; CLU_029242_0_0_6; -.
DR InParanoid; P0AFF6; -.
DR OMA; MDIDMSA; -.
DR PhylomeDB; P0AFF6; -.
DR BioCyc; EcoCyc:EG10665-MON; -.
DR EvolutionaryTrace; P0AFF6; -.
DR PRO; PR:P0AFF6; -.
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:0001000; F:bacterial-type RNA polymerase core enzyme binding; IDA:CAFA.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IDA:CAFA.
DR GO; GO:0051259; P:protein complex oligomerization; IDA:CACAO.
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; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1480.10; -; 1.
DR Gene3D; 3.30.300.20; -; 2.
DR HAMAP; MF_00945_B; NusA_B; 1.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR025249; KH_dom_NusA-like.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR030842; NusA_bac.
DR InterPro; IPR036555; NusA_N_sf.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR013735; TF_NusA_N.
DR InterPro; IPR010214; Tscrpt_termin_fac_NusA_C_rpt.
DR InterPro; IPR010213; Tscrpt_termination_fac_NusA.
DR PANTHER; PTHR22648; PTHR22648; 1.
DR Pfam; PF13184; KH_5; 1.
DR Pfam; PF08529; NusA_N; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF47794; SSF47794; 2.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF54814; SSF54814; 2.
DR SUPFAM; SSF69705; SSF69705; 1.
DR TIGRFAMs; TIGR01953; NusA; 1.
DR TIGRFAMs; TIGR01954; nusA_Cterm_rpt; 2.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Host-virus interaction;
KW Reference proteome; Repeat; Ribosome biogenesis; RNA-binding;
KW Stress response; Transcription; Transcription antitermination;
KW Transcription regulation; Transcription termination.
FT CHAIN 1..495
FT /note="Transcription termination/antitermination protein
FT NusA"
FT /id="PRO_0000181965"
FT DOMAIN 135..200
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00945"
FT DOMAIN 230..293
FT /note="KH 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00945"
FT DOMAIN 302..368
FT /note="KH 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00945"
FT REPEAT 364..414
FT /note="1"
FT REPEAT 439..489
FT /note="2"
FT REGION 1..137
FT /note="N-terminal domain (NTD) interacts with RNAP"
FT /evidence="ECO:0000305|PubMed:21922055"
FT REGION 345..426
FT /note="Acidic repeat 1 (AR1)"
FT /evidence="ECO:0000305|PubMed:21922055"
FT REGION 364..489
FT /note="2 X 51 AA approximate repeats"
FT REGION 427..495
FT /note="Acidic repeat 2 (AR2), required for interaction with
FT SuhB, interacts with RNAP subunit alpha (rpoA), NusG"
FT /evidence="ECO:0000269|PubMed:31020314,
FT ECO:0000269|PubMed:31127279, ECO:0000305|PubMed:21922055"
FT MUTAGEN 104
FT /note="R->H: In nusA10-1."
FT /evidence="ECO:0000269|PubMed:1847365"
FT MUTAGEN 181
FT /note="G->D: In nusa11; inability to terminate
FT transcription normally at termination sites."
FT /evidence="ECO:0000269|PubMed:1847365"
FT MUTAGEN 183
FT /note="L->R: In nusA1; restricts lambda growth by
FT preventing antitermination activity of lambda N protein."
FT /evidence="ECO:0000269|PubMed:1847365"
FT MUTAGEN 212
FT /note="E->K: In nusA10-2."
FT /evidence="ECO:0000269|PubMed:1847365"
FT CONFLICT 167..191
FT /note="MLPRENFRPGDRVRGVLYSVRPEAR -> SCRVKTFALATAFVACSIPFARN
FT G (in Ref. 1; CAA25200)"
FT /evidence="ECO:0000305"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:2KWP"
FT HELIX 20..39
FT /evidence="ECO:0007829|PDB:2KWP"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:2KWP"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:2KWP"
FT STRAND 55..65
FT /evidence="ECO:0007829|PDB:2KWP"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:2KWP"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2KWP"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:2KWP"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:2KWP"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2KWP"
FT HELIX 110..132
FT /evidence="ECO:0007829|PDB:5LM9"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:5LM9"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:5LM9"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:5LM9"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:5LM9"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:5LM9"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:5LM9"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:5LM9"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:5LM9"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:5LM9"
FT STRAND 220..229
FT /evidence="ECO:0007829|PDB:5LM9"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:5LM9"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:5LM9"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:5LM9"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:5LM9"
FT HELIX 257..265
FT /evidence="ECO:0007829|PDB:5LM9"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:5LM9"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:5LM9"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:5LM9"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:5LM9"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:5LM9"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:5LM9"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:5LM9"
FT HELIX 314..318
FT /evidence="ECO:0007829|PDB:5LM9"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:5LM9"
FT HELIX 323..332
FT /evidence="ECO:0007829|PDB:5LM9"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:5LM9"
FT HELIX 354..363
FT /evidence="ECO:0007829|PDB:1U9L"
FT HELIX 367..375
FT /evidence="ECO:0007829|PDB:1U9L"
FT HELIX 381..386
FT /evidence="ECO:0007829|PDB:1U9L"
FT HELIX 389..392
FT /evidence="ECO:0007829|PDB:1U9L"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:1WCL"
FT HELIX 400..417
FT /evidence="ECO:0007829|PDB:1U9L"
FT HELIX 432..435
FT /evidence="ECO:0007829|PDB:6IB8"
FT HELIX 442..450
FT /evidence="ECO:0007829|PDB:6IB8"
FT HELIX 456..460
FT /evidence="ECO:0007829|PDB:6IB8"
FT HELIX 464..467
FT /evidence="ECO:0007829|PDB:6IB8"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:1WCN"
FT HELIX 475..489
FT /evidence="ECO:0007829|PDB:6IB8"
FT TURN 491..493
FT /evidence="ECO:0007829|PDB:2JZB"
SQ SEQUENCE 495 AA; 54871 MW; 7D4DD019172FBAD0 CRC64;
MNKEILAVVE AVSNEKALPR EKIFEALESA LATATKKKYE QEIDVRVQID RKSGDFDTFR
RWLVVDEVTQ PTKEITLEAA RYEDESLNLG DYVEDQIESV TFDRITTQTA KQVIVQKVRE
AERAMVVDQF REHEGEIITG VVKKVNRDNI SLDLGNNAEA VILREDMLPR ENFRPGDRVR
GVLYSVRPEA RGAQLFVTRS KPEMLIELFR IEVPEIGEEV IEIKAAARDP GSRAKIAVKT
NDKRIDPVGA CVGMRGARVQ AVSTELGGER IDIVLWDDNP AQFVINAMAP ADVASIVVDE
DKHTMDIAVE AGNLAQAIGR NGQNVRLASQ LSGWELNVMT VDDLQAKHQA EAHAAIDTFT
KYLDIDEDFA TVLVEEGFST LEELAYVPMK ELLEIEGLDE PTVEALRERA KNALATIAQA
QEESLGDNKP ADDLLNLEGV DRDLAFKLAA RGVCTLEDLA EQGIDDLADI EGLTDEKAGA
LIMAARNICW FGDEA
