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   04-NOV-2026, entry version 154.
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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; 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.
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_CP009789.1.
DR   PDB; 1A6J; X-ray; 2.35 A; A/B=1-163.
DR   AlphaFoldDB; P69829; -.
DR   BMRB; P69829; -.
DR   SMR; P69829; -.
DR   BioGRID; 4259284; 22.
DR   BioGRID; 852034; 6.
DR   DIP; DIP-10604N; -.
DR   FunCoup; P69829; 255.
DR   IntAct; P69829; 10.
DR   STRING; 511145.b3204; -.
DR   jPOST; P69829; -.
DR   PaxDb; 511145-b3204; -.
DR   EnsemblBacteria; AAC76236; AAC76236; b3204.
DR   GeneID; 67174136; -.
DR   GeneID; 947721; -.
DR   KEGG; ecj:JW3171; -.
DR   KEGG; eco:b3204; -.
DR   KEGG; ecoc:C3026_17435; -.
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; AAFVKMQ; -.
DR   OrthoDB; 95460at2; -.
DR   PhylomeDB; P69829; -.
DR   BioCyc; EcoCyc:EG11682-MONOMER; -.
DR   EvolutionaryTrace; P69829; -.
DR   PRO; PR:P69829; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P69829; -.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IMP:EcoCyc.
DR   GO; GO:0030295; F:protein kinase activator activity; IDA:EcoCyc.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-carbohydrate phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR   CDD; cd00211; PTS_IIA_fru; 1.
DR   FunFam; 3.40.930.10:FF:000003; PTS IIA-like nitrogen regulatory protein PtsN; 1.
DR   Gene3D; 3.40.930.10; Mannitol-specific EII, Chain A; 1.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   InterPro; IPR006320; PTS_Nitro_regul.
DR   InterPro; IPR051541; PTS_SugarTrans_NitroReg.
DR   NCBIfam; TIGR01419; nitro_reg_IIA; 1.
DR   NCBIfam; NF008145; ptsN; 1.
DR   PANTHER; PTHR47738:SF1; NITROGEN REGULATORY PROTEIN; 1.
DR   PANTHER; PTHR47738; PTS SYSTEM FRUCTOSE-LIKE EIIA COMPONENT-RELATED; 1.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 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
//