ID   GLNB_MYCTO              Reviewed;         112 AA.
AC   P9WN30; L0TB95; P64249; Q10960;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Nitrogen regulatory protein P-II;
GN   Name=glnB; OrderedLocusNames=MT2987;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: In nitrogen-limiting conditions, when the ratio of Gln to 2-
CC       ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP
CC       allows the deadenylation of glutamine synthetase (GS), thus activating
CC       the enzyme. Conversely, in nitrogen excess P-II is deuridylated and
CC       promotes the adenylation of GS. P-II indirectly controls the
CC       transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed
CC       conversion of NR-I to NR-I-phosphate, the transcriptional activator of
CC       glnA. When P-II is uridylylated to P-II-UMP, these events are reversed
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00675}.
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DR   EMBL; AE000516; AAK47313.1; -; Genomic_DNA.
DR   PIR; G70747; G70747.
DR   RefSeq; WP_003414756.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WN30; -.
DR   SMR; P9WN30; -.
DR   EnsemblBacteria; AAK47313; AAK47313; MT2987.
DR   GeneID; 45426906; -.
DR   KEGG; mtc:MT2987; -.
DR   PATRIC; fig|83331.31.peg.3227; -.
DR   HOGENOM; CLU_082268_0_0_11; -.
DR   Proteomes; UP000001020; 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; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..112
FT                   /note="Nitrogen regulatory protein P-II"
FT                   /id="PRO_0000427198"
FT   MOD_RES         51
FT                   /note="O-UMP-tyrosine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
SQ   SEQUENCE   112 AA;  12227 MW;  1AE59B5537CB3894 CRC64;
     MKLITAIVKP FTLDDVKTSL EDAGVLGMTV SEIQGYGRQK GHTEVYRGAE YSVDFVPKVR
     IEVVVDDSIV DKVVDSIVRA ARTGKIGDGK VWVSPVDTIV RVRTGERGHD AL