GLNB_SYNY3
ID GLNB_SYNY3 Reviewed; 112 AA.
AC Q55247;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Nitrogen regulatory protein P-II;
DE AltName: Full=PII signal transducing protein;
GN Name=glnB; OrderedLocusNames=ssl0707;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9426594; DOI=10.1023/a:1005846626187;
RA Garcia-Dominguez M., Florencio F.J.;
RT "Nitrogen availability and electron transport control the expression of
RT glnB gene (encoding PII protein) in the cyanobacterium Synechocystis sp.
RT PCC 6803.";
RL Plant Mol. Biol. 35:723-734(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP PROTEIN SEQUENCE OF 1-20.
RX PubMed=9298645; DOI=10.1002/elps.1150180806;
RA Sazuka T., Ohara O.;
RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT PCC6803: linking 130 protein spots with their respective genes.";
RL Electrophoresis 18:1252-1258(1997).
RN [4]
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q55247; P73148: sll0985; NbExp=5; IntAct=EBI-906365, EBI-906297;
CC -!- PTM: Phosphorylation dependent on the nitrogen source and spectral
CC light quality. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the P(II) protein family. {ECO:0000255|PROSITE-
CC ProRule:PRU00675}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA18533.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X97496; CAA66127.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA18533.1; ALT_INIT; Genomic_DNA.
DR PIR; S76404; S76404.
DR PDB; 1UL3; X-ray; 2.00 A; A/B/C/D=1-112.
DR PDBsum; 1UL3; -.
DR AlphaFoldDB; Q55247; -.
DR SMR; Q55247; -.
DR IntAct; Q55247; 3.
DR STRING; 1148.1653621; -.
DR PaxDb; Q55247; -.
DR EnsemblBacteria; BAA18533; BAA18533; BAA18533.
DR KEGG; syn:ssl0707; -.
DR eggNOG; COG0347; Bacteria.
DR InParanoid; Q55247; -.
DR OMA; HQIEVNF; -.
DR PhylomeDB; Q55247; -.
DR EvolutionaryTrace; Q55247; -.
DR Proteomes; UP000001425; 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..112
FT /note="Nitrogen regulatory protein P-II"
FT /id="PRO_0000139795"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MOD_RES 51
FT /note="O-UMP-tyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00675"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:1UL3"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1UL3"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:1UL3"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:1UL3"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:1UL3"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:1UL3"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1UL3"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:1UL3"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1UL3"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1UL3"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1UL3"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1UL3"
SQ SEQUENCE 112 AA; 12397 MW; F9ABD0F5C173B799 CRC64;
MKKVEAIIRP FKLDEVKIAL VNAGIVGMTV SEVRGFGRQK GQTERYRGSE YTVEFLQKLK
IEIVVDEGQV DMVVDKLVSA ARTGEIGDGK IFISPVDSVV RIRTGEKDTE AI
