GLNB_SYNE7
ID GLNB_SYNE7 Reviewed; 112 AA.
AC P0A3F4; P80016; Q31RG6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Nitrogen regulatory protein P-II;
DE AltName: Full=PII signal transducing protein;
GN Name=glnB; OrderedLocusNames=Synpcc7942_0321;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1905010; DOI=10.1073/pnas.88.11.4565;
RA Tsinoremas N.F., Castets A.M., Harrison M.A., Allen J.F.,
RA Tandeau de Marsac N.;
RT "Photosynthetic electron transport controls nitrogen assimilation in
RT cyanobacteria by means of posttranslational modification of the glnB gene
RT product.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4565-4569(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION.
RX PubMed=8282715; DOI=10.1128/jb.176.1.84-91.1994;
RA Forchhammer K., Tandeau de Marsac N.;
RT "The PII protein in the cyanobacterium Synechococcus sp. strain PCC 7942 is
RT modified by serine phosphorylation and signals the cellular N-status.";
RL J. Bacteriol. 176:84-91(1994).
RN [4]
RP PHOSPHORYLATION AT SER-49.
RX PubMed=7592328; DOI=10.1128/jb.177.20.5812-5817.1995;
RA Forchhammer K., Tandeau de Marsac N.;
RT "Phosphorylation of the PII protein (glnB gene product) in the
RT cyanobacterium Synechococcus sp. strain PCC 7942: analysis of in vitro
RT kinase activity.";
RL J. Bacteriol. 177:5812-5817(1995).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=14646076; DOI=10.1107/s0907444903019589;
RA Xu Y., Carr P.D., Clancy P., Garcia-Dominguez M., Forchhammer K.,
RA Florencio F., Vasudevan S.G., Tandeau de Marsac N., Ollis D.L.;
RT "The structures of the PII proteins from the cyanobacteria Synechococcus
RT sp. PCC 7942 and Synechocystis sp. PCC 6803.";
RL Acta Crystallogr. D 59:2183-2190(2003).
CC -!- FUNCTION: P-II indirectly controls the transcription of the GS gene
CC (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-
CC phosphate, the transcriptional activator of glnA. When P-II is
CC phosphorylated, these events are reversed. In nitrogen-limiting
CC conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is
CC phosphorylated which allows the deadenylation of glutamine synthetase
CC (GS), thus activating the enzyme.
CC -!- SUBUNIT: Homotrimer.
CC -!- INTERACTION:
CC P0A3F4; Q6V1L5: argB; NbExp=12; IntAct=EBI-700889, EBI-700898;
CC P0A3F4; P0A3F4: glnB; NbExp=5; IntAct=EBI-700889, EBI-700889;
CC P0A3F4; Q7X386: Synpcc7942_2061; NbExp=9; IntAct=EBI-700889, EBI-700982;
CC P0A3F4; Q8DGS1: tlr2243; Xeno; NbExp=8; IntAct=EBI-700889, EBI-7629960;
CC -!- PTM: Phosphorylation dependent on the nitrogen source and spectral
CC light quality. {ECO:0000269|PubMed:7592328,
CC ECO:0000269|PubMed:8282715}.
CC -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC ProRule:PRU00675}.
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DR EMBL; M62447; AAA27312.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB56353.1; -; Genomic_DNA.
DR PIR; A39696; A39696.
DR RefSeq; WP_011243504.1; NC_007604.1.
DR PDB; 1QY7; X-ray; 2.00 A; A/B/C=1-112.
DR PDB; 2JJ4; X-ray; 3.46 A; D/E/F=1-112.
DR PDB; 2V5H; X-ray; 2.75 A; G/H/I/J/K/L=1-112.
DR PDB; 2XBP; X-ray; 1.20 A; A=1-112.
DR PDB; 2XG8; X-ray; 3.20 A; A/B/C=1-112.
DR PDB; 2XUL; X-ray; 2.20 A; A/B/C/D/E/F=1-112.
DR PDB; 2XZW; X-ray; 1.95 A; A/B/C/D/E/F/G/H/I=1-112.
DR PDB; 4AFF; X-ray; 1.05 A; A=1-112.
DR PDB; 4C3K; X-ray; 3.10 A; A/B/C/D/E/F=1-112.
DR PDB; 4C3L; X-ray; 1.60 A; A=1-112.
DR PDB; 4C3M; X-ray; 2.15 A; A/B/C=1-112.
DR PDBsum; 1QY7; -.
DR PDBsum; 2JJ4; -.
DR PDBsum; 2V5H; -.
DR PDBsum; 2XBP; -.
DR PDBsum; 2XG8; -.
DR PDBsum; 2XUL; -.
DR PDBsum; 2XZW; -.
DR PDBsum; 4AFF; -.
DR PDBsum; 4C3K; -.
DR PDBsum; 4C3L; -.
DR PDBsum; 4C3M; -.
DR AlphaFoldDB; P0A3F4; -.
DR SMR; P0A3F4; -.
DR DIP; DIP-35002N; -.
DR IntAct; P0A3F4; 9.
DR MINT; P0A3F4; -.
DR STRING; 1140.Synpcc7942_0321; -.
DR iPTMnet; P0A3F4; -.
DR PRIDE; P0A3F4; -.
DR EnsemblBacteria; ABB56353; ABB56353; Synpcc7942_0321.
DR KEGG; syf:Synpcc7942_0321; -.
DR eggNOG; COG0347; Bacteria.
DR HOGENOM; CLU_082268_0_0_3; -.
DR OMA; HQIEVNF; -.
DR OrthoDB; 2021322at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0321-MON; -.
DR EvolutionaryTrace; P0A3F4; -.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW 3D-structure; Nucleotide-binding; Phosphoprotein; Transcription;
KW Transcription regulation.
FT CHAIN 1..112
FT /note="Nitrogen regulatory protein P-II"
FT /id="PRO_0000139794"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:7592328"
FT MOD_RES 51
FT /note="O-UMP-tyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
FT CONFLICT 83
FT /note="T -> P (in Ref. 1; AAA27312)"
FT /evidence="ECO:0000305"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:4AFF"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:4AFF"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:4AFF"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:4AFF"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:2XZW"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2XBP"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:2XBP"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:4AFF"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:4AFF"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:4AFF"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2XG8"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:4AFF"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2XZW"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:4AFF"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:4AFF"
SQ SEQUENCE 112 AA; 12391 MW; 5F44B64CBFF3C559 CRC64;
MKKIEAIIRP FKLDEVKIAL VNAGIVGMTV SEVRGFGRQK GQTERYRGSE YTVEFLQKLK
LEIVVEDAQV DTVIDKIVAA ARTGEIGDGK IFVSPVDQTI RIRTGEKNAD AI
