GLNB_MYCBO
ID GLNB_MYCBO Reviewed; 112 AA.
AC P64250; A0A1R3Y2L5; Q10960; X2BMG6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Nitrogen regulatory protein P-II;
GN Name=glnB; OrderedLocusNames=BQ2027_MB2943C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU01564.1; -; Genomic_DNA.
DR RefSeq; NP_856588.1; NC_002945.3.
DR RefSeq; WP_003414756.1; NC_002945.4.
DR AlphaFoldDB; P64250; -.
DR SMR; P64250; -.
DR EnsemblBacteria; SIU01564; SIU01564; BQ2027_MB2943C.
DR GeneID; 45426906; -.
DR PATRIC; fig|233413.5.peg.3229; -.
DR OMA; HQIEVNF; -.
DR Proteomes; UP000001419; 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_0000139780"
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