(data stored in ACNUC7421 zone)

SWISSPROT: GLNK_ECO57

ID   GLNK_ECO57              Reviewed;         112 AA.
AC   P0AC57; P38504; P77118;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 76.
DE   RecName: Full=Nitrogen regulatory protein P-II 2;
GN   Name=glnK; OrderedLocusNames=Z0562, ECs0504;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: P-II indirectly controls the transcription of the
CC       glutamine synthetase gene (GlnA). P-II prevents NR-II-catalyzed
CC       conversion of NR-I to NR-I-phosphate, the transcriptional
CC       activator of GlnA. When P-II is uridylylated to P-II-UMP, these
CC       events are reversed. When the ratio of Gln to 2-ketoglutarate
CC       decreases, P-II is uridylylated to P-II-UMP, which causes the
CC       deadenylation of glutamine synthetase by GlnE, so activating the
CC       enzyme (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- PTM: Uridylylated/deuridylylated by GlnD. {ECO:0000250}.
CC   -!- PTM: Uridylylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the P(II) protein family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00675}.
DR   EMBL; AE005174; AAG54800.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33927.1; -; Genomic_DNA.
DR   PIR; D85542; D85542.
DR   PIR; H90691; H90691.
DR   RefSeq; NP_308531.1; NC_002695.1.
DR   RefSeq; WP_000780338.1; NZ_MWVM01000009.1.
DR   ProteinModelPortal; P0AC57; -.
DR   SMR; P0AC57; -.
DR   STRING; 155864.Z0562; -.
DR   PRIDE; P0AC57; -.
DR   EnsemblBacteria; AAG54800; AAG54800; Z0562.
DR   EnsemblBacteria; BAB33927; BAB33927; BAB33927.
DR   GeneID; 914607; -.
DR   KEGG; ece:Z0562; -.
DR   KEGG; ecs:ECs0504; -.
DR   PATRIC; fig|386585.9.peg.609; -.
DR   eggNOG; ENOG4108YZA; Bacteria.
DR   eggNOG; COG0347; LUCA.
DR   HOGENOM; HOG000017847; -.
DR   KO; K04752; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006808; P:regulation of nitrogen utilization; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.120; -; 1.
DR   InterPro; IPR002187; N-reg_PII.
DR   InterPro; IPR011322; N-reg_PII-like_a/b.
DR   InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR   InterPro; IPR017918; N-reg_PII_CS.
DR   InterPro; IPR002332; N-reg_PII_urydylation_site.
DR   Pfam; PF00543; P-II; 1.
DR   PIRSF; PIRSF039144; GlnB; 1.
DR   PRINTS; PR00340; PIIGLNB.
DR   SMART; SM00938; P-II; 1.
DR   SUPFAM; SSF54913; SSF54913; 1.
DR   PROSITE; PS00638; PII_GLNB_CTER; 1.
DR   PROSITE; PS51343; PII_GLNB_DOM; 1.
DR   PROSITE; PS00496; PII_GLNB_UMP; 1.
PE   3: Inferred from homology;
DR   PRODOM; P0AC57.
DR   SWISS-2DPAGE; P0AC57.
KW   Complete proteome; Nucleotide-binding; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    112       Nitrogen regulatory protein P-II 2.
FT                                /FTId=PRO_0000139774.
FT   MOD_RES      51     51       O-UMP-tyrosine. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00675}.
SQ   SEQUENCE   112 AA;  12259 MW;  1875CD92C162B537 CRC64;
     MKLVTVIIKP FKLEDVREAL SSIGIQGLTV TEVKGFGRQK GHAELYRGAE YSVNFLPKVK
     IDVAIADDQL DEVIDIVSKA AYTGKIGDGK IFVAELQRVI RIRTGEADEA AL
//

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