PTSN_ECOLI
ID PTSN_ECOLI Reviewed; 163 AA.
AC P69829; P31222; Q2M908;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Nitrogen regulatory protein;
DE AltName: Full=Enzyme IIA-NTR;
DE AltName: Full=PTS system EIIA component;
DE AltName: Full=Phosphotransferase enzyme IIA component;
GN Name=ptsN; Synonyms=rpoP, yhbI; OrderedLocusNames=b3204, JW3171;
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 CHARACTERIZATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7876255; DOI=10.1074/jbc.270.9.4822;
RA Powell B.S., Court D.L., Inada T., Nakamura Y., Michotey V., Cui X.,
RA Reizer A., Saier M.H. Jr., Reizer J.;
RT "Novel proteins of the phosphotransferase system encoded within the rpoN
RT operon of Escherichia coli. Enzyme IIANtr affects growth on organic
RT nitrogen and the conditional lethality of an erats mutant.";
RL J. Biol. Chem. 270:4822-4839(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8444818; DOI=10.1128/jb.175.5.1550-1551.1993;
RA Imaishi H., Gomada M., Inouye S., Nakazawa A.;
RT "Physical map location of the rpoN gene of Escherichia coli.";
RL J. Bacteriol. 175:1550-1551(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8025669; DOI=10.1099/13500872-140-5-1035;
RA Jones D.H.A., Franklin C.F.H., Thomas C.M.;
RT "Molecular analysis of the operon which encodes the RNA polymerase sigma
RT factor sigma 54 of Escherichia coli.";
RL Microbiology 140:1035-1043(1994).
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 X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9636714; DOI=10.1006/jmbi.1998.1753;
RA Bordo D., van Monfort R.L., Pijning T., Kalk K.H., Reizer J.,
RA Saier M.H. Jr., Dijkstra B.W.;
RT "The three-dimensional structure of the nitrogen regulatory protein IIANtr
RT from Escherichia coli.";
RL J. Mol. Biol. 279:245-255(1998).
CC -!- FUNCTION: Seems to have a role in regulating nitrogen assimilation.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P69829; P21865: kdpD; NbExp=4; IntAct=EBI-547017, EBI-1123100;
CC P69829; P0AGI8: trkA; NbExp=3; IntAct=EBI-547017, EBI-1132371;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: The EIIA domain is phosphorylated by phospho-NPr on a histidyl
CC residue.
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DR EMBL; U12684; AAB60165.1; -; Genomic_DNA.
DR EMBL; D12938; BAA02317.1; -; Genomic_DNA.
DR EMBL; Z27094; CAA81619.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58006.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76236.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77248.1; -; Genomic_DNA.
DR PIR; I76720; I76720.
DR RefSeq; NP_417671.1; NC_000913.3.
DR RefSeq; WP_000183676.1; NZ_STEB01000012.1.
DR PDB; 1A6J; X-ray; 2.35 A; A/B=1-163.
DR PDBsum; 1A6J; -.
DR AlphaFoldDB; P69829; -.
DR BMRB; P69829; -.
DR SMR; P69829; -.
DR BioGRID; 4259284; 21.
DR BioGRID; 852034; 6.
DR DIP; DIP-10604N; -.
DR IntAct; P69829; 10.
DR STRING; 511145.b3204; -.
DR jPOST; P69829; -.
DR PaxDb; P69829; -.
DR PRIDE; P69829; -.
DR EnsemblBacteria; AAC76236; AAC76236; b3204.
DR EnsemblBacteria; BAE77248; BAE77248; BAE77248.
DR GeneID; 67415962; -.
DR GeneID; 947721; -.
DR KEGG; ecj:JW3171; -.
DR KEGG; eco:b3204; -.
DR PATRIC; fig|1411691.4.peg.3527; -.
DR EchoBASE; EB1633; -.
DR eggNOG; COG1762; Bacteria.
DR HOGENOM; CLU_072531_5_2_6; -.
DR InParanoid; P69829; -.
DR OMA; FDAPDEQ; -.
DR PhylomeDB; P69829; -.
DR BioCyc; EcoCyc:EG11682-MON; -.
DR EvolutionaryTrace; P69829; -.
DR PRO; PR:P69829; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004857; F:enzyme inhibitor activity; IMP:EcoCyc.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030295; F:protein kinase activator activity; IDA:EcoCyc.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0032412; P:regulation of ion transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0010243; P:response to organonitrogen compound; IMP:EcoCyc.
DR CDD; cd00211; PTS_IIA_fru; 1.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR InterPro; IPR006320; PTS_Nitro_regul.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR SUPFAM; SSF55804; SSF55804; 1.
DR TIGRFAMs; TIGR01419; nitro_reg_IIA; 1.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Kinase; Reference proteome; Transferase.
FT CHAIN 1..163
FT /note="Nitrogen regulatory protein"
FT /id="PRO_0000186694"
FT DOMAIN 12..156
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 73
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1A6J"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:1A6J"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:1A6J"
FT HELIX 28..43
FT /evidence="ECO:0007829|PDB:1A6J"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:1A6J"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:1A6J"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1A6J"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1A6J"
FT STRAND 84..94
FT /evidence="ECO:0007829|PDB:1A6J"
FT STRAND 104..113
FT /evidence="ECO:0007829|PDB:1A6J"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1A6J"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:1A6J"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:1A6J"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:1A6J"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:1A6J"
SQ SEQUENCE 163 AA; 17960 MW; 57240CF2C550AC80 CRC64;
MTNNDTTLQL SSVLNRECTR SRVHCQSKKR ALEIISELAA KQLSLPPQVV FEAILTREKM
GSTGIGNGIA IPHGKLEEDT LRAVGVFVQL ETPIAFDAID NQPVDLLFAL LVPADQTKTH
LHTLSLVAKR LADKTICRRL RAAQSDEELY QIITDTEGTP DEA
