REGN_LAMBD
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 25-MAY-2022, entry version 108.
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 Caudovirales; Siphoviridae; Lambdavirus.
OX NCBI_TaxID=10710;
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 PDBsum; 1QFQ; -.
DR PDBsum; 5LM7; -.
DR PDBsum; 5MS0; -.
DR PDBsum; 6GOV; -.
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; Genome.
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:0035613; F:RNA stem-loop binding; IMP:CAFA.
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; IC:ComplexPortal.
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.
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
