GLNB_ECO57
ID GLNB_ECO57 Reviewed; 112 AA.
AC P0A9Z3; P05826;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Nitrogen regulatory protein P-II 1;
GN Name=glnB; OrderedLocusNames=Z3829, ECs3419;
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., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA 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., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT 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 glutamine
CC synthetase gene (GlnA). P-II prevents NR-II-catalyzed conversion of NR-
CC I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II
CC is uridylylated to P-II-UMP, these events are reversed. When the ratio
CC of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP,
CC which causes the deadenylation of glutamine synthetase by GlnE, so
CC activating the enzyme (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- PTM: Uridylylated/deuridylylated by GlnD. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC ProRule:PRU00675}.
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DR EMBL; AE005174; AAG57667.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36842.1; -; Genomic_DNA.
DR PIR; C91056; C91056.
DR RefSeq; NP_311446.1; NC_002695.1.
DR RefSeq; WP_000717694.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A9Z3; -.
DR SMR; P0A9Z3; -.
DR STRING; 155864.EDL933_3718; -.
DR EnsemblBacteria; AAG57667; AAG57667; Z3829.
DR EnsemblBacteria; BAB36842; BAB36842; ECs_3419.
DR GeneID; 63941229; -.
DR GeneID; 67416931; -.
DR GeneID; 914897; -.
DR KEGG; ece:Z3829; -.
DR KEGG; ecs:ECs_3419; -.
DR PATRIC; fig|386585.9.peg.3573; -.
DR eggNOG; COG0347; Bacteria.
DR HOGENOM; CLU_082268_0_0_6; -.
DR OMA; HQIEVNF; -.
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 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 PANTHER; PTHR30115; PTHR30115; 1.
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;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..112
FT /note="Nitrogen regulatory protein P-II 1"
FT /id="PRO_0000139773"
FT MOD_RES 51
FT /note="O-UMP-tyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
SQ SEQUENCE 112 AA; 12425 MW; D1A4158A2F225042 CRC64;
MKKIDAIIKP FKLDDVREAL AEVGITGMTV TEVKGFGRQK GHTELYRGAE YMVDFLPKVK
IEIVVPDDIV DTCVDTIIRT AQTGKIGDGK IFVFDVARVI RIRTGEEDDA AI
