ID   REGN_LAMBD              Reviewed;         107 AA.
AC   P03045; Q38647;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 3.
DT   10-JUN-2026, entry version 117.
DE   RecName: Full=Antitermination protein N;
DE   AltName: Full=Regulatory protein N;
DE            Short=PN;
GN   Name=N; OrderedLocusNames=lambdap49;
OS   Escherichia phage lambda (Bacteriophage lambda).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudoviricetes incertae sedis; Lambdavirus; Lambdavirus lambda.
OX   NCBI_TaxID=2681611;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2821265; DOI=10.1016/0022-2836(87)90245-2;
RA   Schauer A.T., Carver D.L., Bigelow B., Baron L.S., Friedman D.I.;
RT   "Lambda N antitermination system: functional analysis of phage interactions
RT   with the host NusA protein.";
RL   J. Mol. Biol. 194:679-690(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6221115; DOI=10.1016/0022-2836(82)90546-0;
RA   Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B.;
RT   "Nucleotide sequence of bacteriophage lambda DNA.";
RL   J. Mol. Biol. 162:729-773(1982).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6458018; DOI=10.1093/nar/9.18.4639;
RA   Ineichen K., Shepherd J.C.W., Bickle T.A.;
RT   "The DNA sequence of the phage lambda genome between PL and the gene bet.";
RL   Nucleic Acids Res. 9:4639-4653(1981).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=43815; DOI=10.1016/0378-1119(79)90011-8;
RA   Franklin N.C., Bennett G.N.;
RT   "The N protein of bacteriophage lambda, defined by its DNA sequence, is
RT   highly basic.";
RL   Gene 8:107-119(1979).
RN   [5]
RP   INTERACTION WITH HOST NUSA.
RX   PubMed=10564494; DOI=10.1046/j.1365-2958.1999.01618.x;
RA   Mah T.F., Li J., Davidson A.R., Greenblatt J.;
RT   "Functional importance of regions in Escherichia coli elongation factor
RT   NusA that interact with RNA polymerase, the bacteriophage lambda N protein
RT   and RNA.";
RL   Mol. Microbiol. 34:523-537(1999).
RN   [6]
RP   REVIEW ON FUNCTION.
RX   PubMed=12167155; DOI=10.1046/j.1365-2443.2002.00563.x;
RA   Nudler E., Gottesman M.E.;
RT   "Transcription termination and anti-termination in E. coli.";
RL   Genes Cells 7:755-768(2002).
RN   [7]
RP   FUNCTION.
RX   PubMed=24711367; DOI=10.1093/nar/gku203;
RA   Parks A.R., Court C., Lubkowska L., Jin D.J., Kashlev M., Court D.L.;
RT   "Bacteriophage lambda N protein inhibits transcription slippage by
RT   Escherichia coli RNA polymerase.";
RL   Nucleic Acids Res. 42:5823-5829(2014).
RN   [8]
RP   STRUCTURE BY NMR OF 2-34.
RX   PubMed=10759866; DOI=10.1046/j.1432-1327.2000.01251.x;
RA   Scharpf M., Sticht H., Schweimer K., Boehm M., Hoffmann S., Rosch P.;
RT   "Antitermination in bacteriophage lambda. The structure of the N36 peptide-
RT   boxB RNA complex.";
RL   Eur. J. Biochem. 267:2397-2408(2000).
CC   -!- FUNCTION: Plays a role as a transcriptional antitermination factor that
CC       allows the virus to initiate its lytic phase. Activates expression of
CC       the delayed viral early genes by modifying host RNA polymerase (RNAP)
CC       into a form that is resistant to termination signals. This
CC       antitermination function requires the host NusA protein which serves to
CC       stabilize the interaction between antitermination protein N and host
CC       RNA polymerase. {ECO:0000269|PubMed:24711367}.
CC   -!- SUBUNIT: Interacts with host nusA. {ECO:0000269|PubMed:10564494}.
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DR   EMBL; J02459; AAA96578.1; -; Genomic_DNA.
DR   EMBL; M29653; AAA32249.1; -; Genomic_DNA.
DR   PIR; D94614; VNBPL.
DR   RefSeq; NP_040625.1; NC_001416.1.
DR   PDB; 1QFQ; NMR; -; B=2-36.
DR   PDB; 5LM7; X-ray; 3.35 A; F/N=1-84.
DR   PDB; 5MS0; EM; 9.80 A; N=3-86.
DR   PDB; 6GOV; EM; 3.70 A; N=1-107.
DR   PDB; 7A4F; EM; 3.50 A; AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/CA/CB/CC/CD/CE/CF/CG/CH/CI/CJ=5-22, AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/CA/CB/CC/CD/CE/CF/CG/CH/CI/CJ=30-82.
DR   PDB; 7A4G; EM; 4.20 A; AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO=5-22, AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO=30-82.
DR   PDB; 7A4H; EM; 4.50 A; AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO=5-22, AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO=30-82.
DR   PDB; 7A4I; EM; 7.04 A; 0A/0B/0C/0D/1A/1B/1C/1D/2A/2B/2C/2D/3A/3B/3C/3D/4A/4B/4C/4D/5A/5B/5C/5D/6A/6B/6C/6D/7A/7B=5-22, 0A/0B/0C/0D/1A/1B/1C/1D/2A/2B/2C/2D/3A/3B/3C/3D/4A/4B/4C/4D/5A/5B/5C/5D/6A/6B/6C/6D/7A/7B=30-82.
DR   PDB; 7A4J; EM; 3.04 A; 0A/0B/0C/0D/1A/1B/1C/1D/2A/2B/2C/2D/3A/3B/3C/3D/4A/4B/4C/4D/5A/5B/5C/5D/6A/6B/6C/6D/7A/7B=5-22, 0A/0B/0C/0D/1A/1B/1C/1D/2A/2B/2C/2D/3A/3B/3C/3D/4A/4B/4C/4D/5A/5B/5C/5D/6A/6B/6C/6D/7A/7B=30-82.
DR   EMDB; EMD-3561; -.
DR   SMR; P03045; -.
DR   ComplexPortal; CPX-5780; lambdaN-dependent processive transcription antitermination complex.
DR   IntAct; P03045; 7.
DR   GeneID; 2703540; -.
DR   KEGG; vg:2703540; -.
DR   EvolutionaryTrace; P03045; -.
DR   Proteomes; UP000001711; Segment.
DR   GO; GO:0001000; F:bacterial-type RNA polymerase core enzyme binding; IMP:CAFA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; EXP:DisProt.
DR   GO; GO:0070063; F:RNA polymerase binding; IDA:DisProt.
DR   GO; GO:0035613; F:RNA stem-loop binding; IMP:CAFA.
DR   GO; GO:0003727; F:single-stranded RNA binding; EXP:DisProt.
DR   GO; GO:0001072; F:transcription antitermination factor activity, RNA binding; IMP:CAFA.
DR   GO; GO:0006353; P:DNA-templated transcription termination; IEA:UniProtKB-KW.
DR   GO; GO:0032784; P:regulation of DNA-templated transcription elongation; NAS:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:DisProt.
DR   GO; GO:0031564; P:transcription antitermination; IDA:ComplexPortal.
DR   DisProt; DP00005; -.
DR   InterPro; IPR020952; Antiterm_prot_N_Arg-rich.
DR   Pfam; PF11438; N36; 1.
DR   PDBsum; 1QFQ; -.
DR   PDBsum; 5LM7; -.
DR   PDBsum; 5MS0; -.
DR   PDBsum; 6GOV; -.
DR   PDBsum; 7A4F; -.
DR   PDBsum; 7A4G; -.
DR   PDBsum; 7A4H; -.
DR   PDBsum; 7A4I; -.
DR   PDBsum; 7A4J; -.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Reference proteome; Transcription;
KW   Transcription regulation; Transcription termination.
FT   CHAIN           1..107
FT                   /note="Antitermination protein N"
FT                   /id="PRO_0000077583"
FT   REGION          85..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        35
FT                   /note="R -> L (in Ref. 1; AAA32249)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..10
FT                   /evidence="ECO:0007829|PDB:5LM7"
FT   HELIX           12..19
FT                   /evidence="ECO:0007829|PDB:5LM7"
FT   HELIX           23..25
FT                   /evidence="ECO:0007829|PDB:1QFQ"
FT   STRAND          26..29
FT                   /evidence="ECO:0007829|PDB:1QFQ"
FT   TURN            32..34
FT                   /evidence="ECO:0007829|PDB:5LM7"
FT   HELIX           47..52
FT                   /evidence="ECO:0007829|PDB:5LM7"
FT   HELIX           58..78
FT                   /evidence="ECO:0007829|PDB:5LM7"
SQ   SEQUENCE   107 AA;  12298 MW;  F1EBAA32F3A1FE21 CRC64;
     MDAQTRRRER RAEKQAQWKA ANPLLVGVSA KPVNRPILSL NRKPKSRVES ALNPIDLTVL
     AEYHKQIESN LQRIERKNQR TWYSKPGERG ITCSGRQKIK GKSIPLI
//