GLNB_SALTY
ID GLNB_SALTY Reviewed; 112 AA.
AC P0A9Z4; P05826;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Nitrogen regulatory protein P-II 1;
GN Name=glnB; OrderedLocusNames=STM2561;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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; AE006468; AAL21455.1; -; Genomic_DNA.
DR RefSeq; NP_461496.1; NC_003197.2.
DR RefSeq; WP_000717694.1; NC_003197.2.
DR AlphaFoldDB; P0A9Z4; -.
DR SMR; P0A9Z4; -.
DR STRING; 99287.STM2561; -.
DR PaxDb; P0A9Z4; -.
DR EnsemblBacteria; AAL21455; AAL21455; STM2561.
DR GeneID; 1254083; -.
DR GeneID; 63941229; -.
DR GeneID; 67416931; -.
DR KEGG; stm:STM2561; -.
DR PATRIC; fig|99287.12.peg.2702; -.
DR HOGENOM; CLU_082268_0_0_6; -.
DR OMA; HQIEVNF; -.
DR PhylomeDB; P0A9Z4; -.
DR PRO; PR:P0A9Z4; -.
DR Proteomes; UP000001014; 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 1"
FT /id="PRO_0000139790"
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
