ID   GLNB_RHORT              Reviewed;         112 AA.
AC   Q53044; Q2RSL0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Nitrogen regulatory protein P-II;
GN   Name=glnB; OrderedLocusNames=Rru_A2085;
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8704966; DOI=10.1099/13500872-142-5-1265;
RA   Johansson M., Nordlund S.;
RT   "Transcription of the glnB and glnA genes in the photosynthetic bacterium
RT   Rhodospirillum rubrum.";
RL   Microbiology 142:1265-1272(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Zhang Y., Ludden P.W., Roberts G.P.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
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; X84158; CAA58963.1; -; Genomic_DNA.
DR   EMBL; AF029703; AAB84167.1; -; Genomic_DNA.
DR   EMBL; CP000230; ABC22885.1; -; Genomic_DNA.
DR   PIR; S52328; S52328.
DR   RefSeq; WP_011389838.1; NC_007643.1.
DR   RefSeq; YP_427172.1; NC_007643.1.
DR   AlphaFoldDB; Q53044; -.
DR   SMR; Q53044; -.
DR   STRING; 269796.Rru_A2085; -.
DR   EnsemblBacteria; ABC22885; ABC22885; Rru_A2085.
DR   KEGG; rru:Rru_A2085; -.
DR   PATRIC; fig|269796.9.peg.2175; -.
DR   eggNOG; COG0347; Bacteria.
DR   HOGENOM; CLU_082268_0_0_5; -.
DR   OMA; YRGTEHV; -.
DR   OrthoDB; 2021322at2; -.
DR   PhylomeDB; Q53044; -.
DR   Proteomes; UP000001929; Chromosome.
DR   GO; GO:0030234; F:enzyme regulator activity; IDA:CACAO.
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; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..112
FT                   /note="Nitrogen regulatory protein P-II"
FT                   /id="PRO_0000139787"
FT   MOD_RES         51
FT                   /note="O-UMP-tyrosine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
SQ   SEQUENCE   112 AA;  12420 MW;  11A3589FC97C4EBC CRC64;
     MKKIEAIIKP FKLDEVKEAL HEIGLQGITV TEAKGFGRQK GHTELYRGAE YVVDFLPKVK
     IELVIEDALV ERAIEAIQQA AQTGRIGDGK IFVYAIEEAI RIRTGERGGD AI