About Products Protein Database Contact

glnB

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Cyanidium caldarium
Length
113 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase, so activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.602 kDa
Sequence
MFSKLEAIIRPFKLEEVKVRLMTFGVPGITVTNVMGCGKQIGGIERSKGVEYDSELIEKVKIEIVVMNEHIDELIEIIINAVWTGEIGDGKIFVSPVSSVIRIRTQDKDLDAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
Length
112 amino acids
Function
P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.479 kDa
Sequence
MKKVEAIIRPFKLDEVKIALVNAGIVGMTVSEVRGFGRQKGQTERYRGSEYTVEFLQKLKVEIVVDDNQVDMVVDKIIAAARTGEIGDGKIFISPVEQVIRIRTGEKNTEAV

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Pasteurella multocida (strain Pm70)
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (GlnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.684 kDa
Sequence
MKKIEAIIKPFKLDDVRESLSDVGITGMTVTEVRGFGRQKGHTELYRGAEYMVDFLPKVKMEIVVTDEQVDQCIEAIMETAQTGKIGDGKIFVYDVERVIRIRTGEENEDAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Porphyra purpurea
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase, so activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.32 kDa
Sequence
MKKIEAIIRPFKLNEVKLALVKGGIGGMTVVKVSGFGRQKGQTERYKGSEYSIDIIDKIKIEIIVSDDKVNSITEIIIKTAKTGEIGDGKIFISDVEQVIRIRTNDLNSAAL

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Pyropia yezoensis
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase, so activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.581 kDa
Sequence
MKKIEAIIRPFKLNEVKLALVKEGIGGMTVIKVSGFGRQKGQTERYKGSEYSIDIIDKIKIEIIISDDKVEKIVETIIKASKTGEIGDGKIFISSIERVIRIRTNDLNFEAL

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Rhizobium etli (strain CFN 42 / ATCC 51251)
Length
112 amino acids
Function
In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.178 kDa
Sequence
MKIVMAIIKPFKLDEVREALTAIGIQGLTVTEVKGYGRQKGHTEIYRGTEYAVSFLPKLKIEIAVASELVDRAVEAIAASAKTGQIGDGKIFVYSIDHAVRIRTGETDSEAL

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Length
112 amino acids
Function
In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.2 kDa
Sequence
MKKIEAIIKPFKLDEVKEALQEAGLQGITVTEAKGFGRQKGHTELYRGAEYVVDFLPKVKIEVVLGDDAVEGAIEAIRKAAQTGRIGDGKIFVSNIEEVVRIRTGETGMDAV

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Rhizobium meliloti (strain 1021)
Length
112 amino acids
Function
In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed.
Similarity
Belongs to the P(II) protein family.
Mass
12.281 kDa
Sequence
MKKIEAIIKPFKLDEVKEALQEVGLQGITVTEAKGFGRQKGHTELYRGAEYVVDFLPKVKVEVVLADENAEAVIEAIRNAAQTGRIGDGKIFVSNVEEVIRIRTGETGLDAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Rhodobacter capsulatus
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase, so activating the enzyme.
Similarity
Belongs to the P(II) protein family.
Mass
12.3 kDa
Sequence
MKKVEAIIKPFKLDEVKEALQEAGIQGLSVIEVKGFGRQKGHTELYRGAEYVVDFLPKVKIEMVLPDEMVDIAIEAIVGAARTEKIGDGKIFVSSIEQAIRIRTGETGEDAV

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase, so activating the enzyme.
Similarity
Belongs to the P(II) protein family.
Mass
12.42 kDa
Sequence
MKKIEAIIKPFKLDEVKEALHEIGLQGITVTEAKGFGRQKGHTELYRGAEYVVDFLPKVKIELVIEDALVERAIEAIQQAAQTGRIGDGKIFVYAIEEAIRIRTGERGGDAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Rhodobacter sphaeroides
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase, so activating the enzyme.
Similarity
Belongs to the P(II) protein family.
Mass
12.1 kDa
Sequence
MKKIEAIIKPFKLDEVKEALQAAGVQGLSVTEVKGFGRQKGHTELYRGAAYVVDFLPKVKIEVVLADDMVEAAVEAIVSASRTDKIGDGKIFISPVEQAIRIRTGETGEDAV

Gene
glnB
Protein
Nitrogen regulatory protein P-II 1
Organism
Salmonella typhi
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (GlnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.425 kDa
Sequence
MKKIDAIIKPFKLDDVREALAEVGITGMTVTEVKGFGRQKGHTELYRGAEYMVDFLPKVKIEIVVPDDIVDTCVDTIIRTAQTGKIGDGKIFVFDVARVIRIRTGEEDDAAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II 1
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (GlnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.425 kDa
Sequence
MKKIDAIIKPFKLDDVREALAEVGITGMTVTEVKGFGRQKGHTELYRGAEYMVDFLPKVKIEIVVPDDIVDTCVDTIIRTAQTGKIGDGKIFVFDVARVIRIRTGEEDDAAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II 1
Organism
Shigella flexneri
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (GlnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.425 kDa
Sequence
MKKIDAIIKPFKLDDVREALAEVGITGMTVTEVKGFGRQKGHTELYRGAEYMVDFLPKVKIEIVVPDDIVDTCVDTIIRTAQTGKIGDGKIFVFDVARVIRIRTGEEDDAAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Synechococcus elongatus (strain PCC 7942)
Length
112 amino acids
Function
P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme.
Similarity
Belongs to the P(II) protein family.
Mass
12.391 kDa
Sequence
MKKIEAIIRPFKLDEVKIALVNAGIVGMTVSEVRGFGRQKGQTERYRGSEYTVEFLQKLKLEIVVEDAQVDTVIDKIVAAARTGEIGDGKIFVSPVDQTIRIRTGEKNADAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Length
112 amino acids
Function
P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme.
Similarity
Belongs to the P(II) protein family.
Mass
12.391 kDa
Sequence
MKKIEAIIRPFKLDEVKIALVNAGIVGMTVSEVRGFGRQKGQTERYRGSEYTVEFLQKLKLEIVVEDAQVDTVIDKIVAAARTGEIGDGKIFVSPVDQTIRIRTGEKNADAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Length
112 amino acids
Function
P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.397 kDa
Sequence
MKKVEAIIRPFKLDEVKIALVNAGIVGMTVSEVRGFGRQKGQTERYRGSEYTVEFLQKLKIEIVVDEGQVDMVVDKLVSAARTGEIGDGKIFISPVDSVVRIRTGEKDTEAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
Length
112 amino acids
Function
P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.479 kDa
Sequence
MKKVEAIIRPFKLDEVKIALVNAGIVGMTVSEVRGFGRQKGQTERYRGSEYTVEFLQKLKVEIVVDDNQVDMVVDKIIAAARTGEIGDGKIFISPVEQVIRIRTGEKNTEAV

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Pasteurella multocida (strain Pm70)
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (GlnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.684 kDa
Sequence
MKKIEAIIKPFKLDDVRESLSDVGITGMTVTEVRGFGRQKGHTELYRGAEYMVDFLPKVKMEIVVTDEQVDQCIEAIMETAQTGKIGDGKIFVYDVERVIRIRTGEENEDAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Porphyra purpurea
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase, so activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.32 kDa
Sequence
MKKIEAIIRPFKLNEVKLALVKGGIGGMTVVKVSGFGRQKGQTERYKGSEYSIDIIDKIKIEIIVSDDKVNSITEIIIKTAKTGEIGDGKIFISDVEQVIRIRTNDLNSAAL

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Pyropia yezoensis
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase, so activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.581 kDa
Sequence
MKKIEAIIRPFKLNEVKLALVKEGIGGMTVIKVSGFGRQKGQTERYKGSEYSIDIIDKIKIEIIISDDKVEKIVETIIKASKTGEIGDGKIFISSIERVIRIRTNDLNFEAL

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Rhizobium etli (strain CFN 42 / ATCC 51251)
Length
112 amino acids
Function
In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.178 kDa
Sequence
MKIVMAIIKPFKLDEVREALTAIGIQGLTVTEVKGYGRQKGHTEIYRGTEYAVSFLPKLKIEIAVASELVDRAVEAIAASAKTGQIGDGKIFVYSIDHAVRIRTGETDSEAL

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Length
112 amino acids
Function
In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.2 kDa
Sequence
MKKIEAIIKPFKLDEVKEALQEAGLQGITVTEAKGFGRQKGHTELYRGAEYVVDFLPKVKIEVVLGDDAVEGAIEAIRKAAQTGRIGDGKIFVSNIEEVVRIRTGETGMDAV

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Rhizobium meliloti (strain 1021)
Length
112 amino acids
Function
In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed.
Similarity
Belongs to the P(II) protein family.
Mass
12.281 kDa
Sequence
MKKIEAIIKPFKLDEVKEALQEVGLQGITVTEAKGFGRQKGHTELYRGAEYVVDFLPKVKVEVVLADENAEAVIEAIRNAAQTGRIGDGKIFVSNVEEVIRIRTGETGLDAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Rhodobacter capsulatus
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase, so activating the enzyme.
Similarity
Belongs to the P(II) protein family.
Mass
12.3 kDa
Sequence
MKKVEAIIKPFKLDEVKEALQEAGIQGLSVIEVKGFGRQKGHTELYRGAEYVVDFLPKVKIEMVLPDEMVDIAIEAIVGAARTEKIGDGKIFVSSIEQAIRIRTGETGEDAV

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase, so activating the enzyme.
Similarity
Belongs to the P(II) protein family.
Mass
12.42 kDa
Sequence
MKKIEAIIKPFKLDEVKEALHEIGLQGITVTEAKGFGRQKGHTELYRGAEYVVDFLPKVKIELVIEDALVERAIEAIQQAAQTGRIGDGKIFVYAIEEAIRIRTGERGGDAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Rhodobacter sphaeroides
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase, so activating the enzyme.
Similarity
Belongs to the P(II) protein family.
Mass
12.1 kDa
Sequence
MKKIEAIIKPFKLDEVKEALQAAGVQGLSVTEVKGFGRQKGHTELYRGAAYVVDFLPKVKIEVVLADDMVEAAVEAIVSASRTDKIGDGKIFISPVEQAIRIRTGETGEDAV

Gene
glnB
Protein
Nitrogen regulatory protein P-II 1
Organism
Salmonella typhi
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (GlnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.425 kDa
Sequence
MKKIDAIIKPFKLDDVREALAEVGITGMTVTEVKGFGRQKGHTELYRGAEYMVDFLPKVKIEIVVPDDIVDTCVDTIIRTAQTGKIGDGKIFVFDVARVIRIRTGEEDDAAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II 1
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (GlnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.425 kDa
Sequence
MKKIDAIIKPFKLDDVREALAEVGITGMTVTEVKGFGRQKGHTELYRGAEYMVDFLPKVKIEIVVPDDIVDTCVDTIIRTAQTGKIGDGKIFVFDVARVIRIRTGEEDDAAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II 1
Organism
Shigella flexneri
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (GlnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.425 kDa
Sequence
MKKIDAIIKPFKLDDVREALAEVGITGMTVTEVKGFGRQKGHTELYRGAEYMVDFLPKVKIEIVVPDDIVDTCVDTIIRTAQTGKIGDGKIFVFDVARVIRIRTGEEDDAAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Synechococcus elongatus (strain PCC 7942)
Length
112 amino acids
Function
P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme.
Similarity
Belongs to the P(II) protein family.
Mass
12.391 kDa
Sequence
MKKIEAIIRPFKLDEVKIALVNAGIVGMTVSEVRGFGRQKGQTERYRGSEYTVEFLQKLKLEIVVEDAQVDTVIDKIVAAARTGEIGDGKIFVSPVDQTIRIRTGEKNADAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Length
112 amino acids
Function
P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme.
Similarity
Belongs to the P(II) protein family.
Mass
12.391 kDa
Sequence
MKKIEAIIRPFKLDEVKIALVNAGIVGMTVSEVRGFGRQKGQTERYRGSEYTVEFLQKLKLEIVVEDAQVDTVIDKIVAAARTGEIGDGKIFVSPVDQTIRIRTGEKNADAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Length
112 amino acids
Function
P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.397 kDa
Sequence
MKKVEAIIRPFKLDEVKIALVNAGIVGMTVSEVRGFGRQKGQTERYRGSEYTVEFLQKLKIEIVVDEGQVDMVVDKLVSAARTGEIGDGKIFISPVDSVVRIRTGEKDTEAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Aquifex aeolicus (strain VF5)
Length
112 amino acids
Function
In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.497 kDa
Sequence
MKKIEAIIKPFKLDEVKDALVEIGIGGMTVTEVKGFGQQKGHTEIYRGTEYVIDFLPKVKIEVVVRDEDVEKVVETIVKTAQTGRVGDGKIFIIPVEDVIRIRTGERGEQAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Azospirillum brasilense
Length
112 amino acids
Function
In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed.
Similarity
Belongs to the P(II) protein family.
Mass
12.371 kDa
Sequence
MKKIEAIIKPFKLDEVKEALHEVGIKGITVTEAKGFGRQKGHTELYRGAEYVVDFLPKVKIEVVMEDSLVERAIEAIQQAAHTGRIGDGKIFVTPVEEVVRIRTGEKGGDAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Length
112 amino acids
Function
In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed.
Similarity
Belongs to the P(II) protein family.
Mass
12.349 kDa
Sequence
MKKIEAIIKPFKLDEVKEALQEVGLQGITVTEAKGFGRQKGHAELYRGAEYIVDFLPKVKIEIVIGDDLVERAIDAIRRAAQTGRIGDGKIFVSNIEEAIRIRTGESGLDAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II 1
Organism
Escherichia coli O157:H7
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (GlnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.425 kDa
Sequence
MKKIDAIIKPFKLDDVREALAEVGITGMTVTEVKGFGRQKGHTELYRGAEYMVDFLPKVKIEIVVPDDIVDTCVDTIIRTAQTGKIGDGKIFVFDVARVIRIRTGEEDDAAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II 1
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (GlnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.425 kDa
Sequence
MKKIDAIIKPFKLDDVREALAEVGITGMTVTEVKGFGRQKGHTELYRGAEYMVDFLPKVKIEIVVPDDIVDTCVDTIIRTAQTGKIGDGKIFVFDVARVIRIRTGEEDDAAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II 1
Organism
Escherichia coli (strain K12)
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme.
Similarity
Belongs to the P(II) protein family.
Mass
12.425 kDa
Sequence
MKKIDAIIKPFKLDDVREALAEVGITGMTVTEVKGFGRQKGHTELYRGAEYMVDFLPKVKIEIVVPDDIVDTCVDTIIRTAQTGKIGDGKIFVFDVARVIRIRTGEEDDAAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Length
112 amino acids
Function
P-II indirectly controls the transcription of the glutamine synthetase gene (GlnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.641 kDa
Sequence
MKKIEAMIKPFKLDDVRESLSDIGISGMTITEVRGFGRQKGHTELYRGAEYMVDFLPKVKLEVVVPDELVDQCIEAIIETAQTGKIGDGKIFVYHVERAIRIRTGEENEDAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Klebsiella oxytoca
Length
112 amino acids
Function
In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed.
Similarity
Belongs to the P(II) protein family.
Mass
12.429 kDa
Sequence
MKKIDAIIKPFKLDDVREALAEVGITGMTVTEVKGFGRQKGHTELYRGAEYMVDFLPKVKIEIVVTDDIVDTCVDTIIRTAQTGKIGDGKIFVFDVARVIRIRTGEEDDAAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Microchaete diplosiphon
Length
112 amino acids
Function
P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.479 kDa
Sequence
MKKVEAIIRPFKLDEVKIALVNAGIVGMTVSEVRGFGRQKGQTERYRGSEYTVEFLQKLKVEIVVEDNQVDMVVDKIIAAARTGEIGDGKIFISPVEQVVRIRTGEKNTEAV

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Length
112 amino acids
Function
In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.227 kDa
Sequence
MKLITAIVKPFTLDDVKTSLEDAGVLGMTVSEIQGYGRQKGHTEVYRGAEYSVDFVPKVRIEVVVDDSIVDKVVDSIVRAARTGKIGDGKVWVSPVDTIVRVRTGERGHDAL

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Length
112 amino acids
Function
In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.227 kDa
Sequence
MKLITAIVKPFTLDDVKTSLEDAGVLGMTVSEIQGYGRQKGHTEVYRGAEYSVDFVPKVRIEVVVDDSIVDKVVDSIVRAARTGKIGDGKVWVSPVDTIVRVRTGERGHDAL

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Length
112 amino acids
Function
In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed (By similarity).
Similarity
Belongs to the P(II) protein family.
Mass
12.227 kDa
Sequence
MKLITAIVKPFTLDDVKTSLEDAGVLGMTVSEIQGYGRQKGHTEVYRGAEYSVDFVPKVRIEVVVDDSIVDKVVDSIVRAARTGKIGDGKVWVSPVDTIVRVRTGERGHDAL

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Rhizobium leguminosarum bv. viciae
Length
111 amino acids
Function
In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed.
Similarity
Belongs to the P(II) protein family.
Mass
12.081 kDa
Sequence
MKKIEAIIKPFKLDEVRSPSGVGLQGITVTEAKGFGRQKGHTELYRGAEYVVDFLPKVKVEVVLADENAEAVIEAIRKAAQTGRIGDGKIFVSNVEEVIRIRTGETGIDAI

Gene
glnB
Protein
Nitrogen regulatory protein P-II
Organism
Rhizobium leguminosarum bv. viciae
Length
111 amino acids
Function
In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed.
Similarity
Belongs to the P(II) protein family.
Mass
12.081 kDa
Sequence
MKKIEAIIKPFKLDEVRSPSGVGLQGITVTEAKGFGRQKGHTELYRGAEYVVDFLPKVKVEVVLADENAEAVIEAIRKAAQTGRIGDGKIFVSNVEEVIRIRTGETGIDAI