ID   GLNB_SHIFL              Reviewed;         112 AA.
AC   P0A9Z6; P05826;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Nitrogen regulatory protein P-II 1;
GN   Name=glnB; OrderedLocusNames=SF2600, S2772;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN44097.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17921.1; -; Genomic_DNA.
DR   RefSeq; NP_708390.1; NC_004337.2.
DR   RefSeq; WP_000717694.1; NZ_WPGW01000021.1.
DR   AlphaFoldDB; P0A9Z6; -.
DR   SMR; P0A9Z6; -.
DR   STRING; 198214.SF2600; -.
DR   PRIDE; P0A9Z6; -.
DR   EnsemblBacteria; AAN44097; AAN44097; SF2600.
DR   EnsemblBacteria; AAP17921; AAP17921; S2772.
DR   GeneID; 1025665; -.
DR   GeneID; 63941229; -.
DR   GeneID; 67416931; -.
DR   KEGG; sfl:SF2600; -.
DR   KEGG; sfx:S2772; -.
DR   PATRIC; fig|198214.7.peg.3105; -.
DR   HOGENOM; CLU_082268_0_0_6; -.
DR   OMA; HQIEVNF; -.
DR   OrthoDB; 2021322at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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_0000139791"
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