GLNB_HAEIN
ID GLNB_HAEIN Reviewed; 112 AA.
AC P43795;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Nitrogen regulatory protein P-II;
GN Name=glnB; OrderedLocusNames=HI_0337;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC21999.1; -; Genomic_DNA.
DR PIR; F64062; F64062.
DR RefSeq; NP_438501.1; NC_000907.1.
DR RefSeq; WP_005654045.1; NC_000907.1.
DR AlphaFoldDB; P43795; -.
DR SMR; P43795; -.
DR STRING; 71421.HI_0337; -.
DR EnsemblBacteria; AAC21999; AAC21999; HI_0337.
DR KEGG; hin:HI_0337; -.
DR PATRIC; fig|71421.8.peg.354; -.
DR eggNOG; COG0347; Bacteria.
DR HOGENOM; CLU_082268_0_0_6; -.
DR OMA; HQIEVNF; -.
DR PhylomeDB; P43795; -.
DR BioCyc; HINF71421:G1GJ1-353-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IBA:GO_Central.
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"
FT /id="PRO_0000139777"
FT MOD_RES 51
FT /note="O-UMP-tyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
SQ SEQUENCE 112 AA; 12641 MW; B8CD67EFA9381D61 CRC64;
MKKIEAMIKP FKLDDVRESL SDIGISGMTI TEVRGFGRQK GHTELYRGAE YMVDFLPKVK
LEVVVPDELV DQCIEAIIET AQTGKIGDGK IFVYHVERAI RIRTGEENED AI
