ID   GLNB_RHOCA              Reviewed;         112 AA.
AC   P13556;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Nitrogen regulatory protein P-II;
GN   Name=glnB;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2152916; DOI=10.1128/jb.172.1.53-62.1990;
RA   Kranz R.G., Pace V.M., Caldicott I.M.;
RT   "Inactivation, sequence, and lacZ fusion analysis of a regulatory locus
RT   required for repression of nitrogen fixation genes in Rhodobacter
RT   capsulatus.";
RL   J. Bacteriol. 172:53-62(1990).
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, so activating
CC       the enzyme.
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; U25953; AAA87024.1; -; Genomic_DNA.
DR   EMBL; M28244; AAA26122.1; -; Genomic_DNA.
DR   RefSeq; WP_013067397.1; NZ_VIBE01000013.1.
DR   AlphaFoldDB; P13556; -.
DR   SMR; P13556; -.
DR   IntAct; P13556; 3.
DR   PRIDE; P13556; -.
DR   GeneID; 31490550; -.
DR   OMA; PEWTEEV; -.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006808; P:regulation of nitrogen utilization; IMP:CACAO.
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   Nitrogen fixation; Nucleotide-binding; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..112
FT                   /note="Nitrogen regulatory protein P-II"
FT                   /id="PRO_0000139786"
FT   MOD_RES         51
FT                   /note="O-UMP-tyrosine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
SQ   SEQUENCE   112 AA;  12300 MW;  6E4CA130963B6426 CRC64;
     MKKVEAIIKP FKLDEVKEAL QEAGIQGLSV IEVKGFGRQK GHTELYRGAE YVVDFLPKVK
     IEMVLPDEMV DIAIEAIVGA ARTEKIGDGK IFVSSIEQAI RIRTGETGED AV