RegulonDB

Gene
Name:	glnB
Synonym(s):	ECK2550, EG10384, b2553
Genome position(nucleotides):	2687070 <-- 2687408
Strand:	reverse
Sequence:	Get nucleotide sequence FastaFormat
GC content %:	51.03
External database links:

ASAP:	ABE-0008398
CGSC:	32933
ECHOBASE:	EB0379
ECOLIHUB:	glnB
OU-MICROARRAY:	b2553
STRING:	511145.b2553
COLOMBOS:	glnB

Product

Name:

nitrogen regulatory protein PII-1

Synonym(s):

GlnB, PII, PII-1, [protein PII], regulatory protein P-II, regulation of nitrogen metabolism and fatty acid biosynthesis, unmodified PII

Sequence:

Get amino acid sequence Fasta Format

Cellular location:

cytosol

Molecular weight:

12.425

Isoelectric point:

4.952

Motif(s):

Type	Positions	Sequence	Comment
	1 -> 108	MKKIDAIIKPFKLDDVREALAEVGITGMTVTEVKGFGRQKGHTELYRGAEYMVDFLPKVKIEIVVPDDIVDTCVDTIIRTAQTGKIGDGKIFVFDVARVIRIRTGEED
	2 -> 8	KKIDAII
	10 -> 23	PFKLDDVREALAEV
	19 -> 19	A	UniProt: In Ref. 1; AAA23883..
	27 -> 36	GMTVTEVKGF

Type	Positions	Sequence	Comment
	1 -> 108	MKKIDAIIKPFKLDDVREALAEVGITGMTVTEVKGFGRQKGHTELYRGAEYMVDFLPKVKIEIVVPDDIVDTCVDTIIRTAQTGKIGDGKIFVFDVARVIRIRTGEED
	2 -> 8	KKIDAII
	10 -> 23	PFKLDDVREALAEV
	19 -> 19	A	UniProt: In Ref. 1; AAA23883..
	27 -> 36	GMTVTEVKGF
	29 -> 29	T	experimental mutation T → M results in defects in interaction with protein receptors and/or effectors (see \|CITS: [9209053]\|) for details
	37 -> 55	GRQKGHTELYRGAEYMVDF
	39 -> 39	Q	experimental mutation Q → E results in defects in interaction with protein receptors and/or effectors (see \|CITS: [9209053]\|) for details
	40 -> 40	K	experimental mutation K → N results in defects in interaction with protein receptors and/or effectors (see \|CITS: [9209053]\|) for details
	41 -> 41	G	experimental mutation G → A results in defective uridylylation
	47 -> 53	RGAEYMV	experimental mutation Δ47-53 results in defects in uridylylation and in interaction with protein receptors
	49 -> 49	A	experimental mutation A → P results in severe defect in interaction with NtrB
	50 -> 50	E	experimental mutation E → Q results in defective uridylylation
	51 -> 51	Y	experimental mutation Y → F results in defective uridylylation
	53 -> 53	V	experimental mutation V → G results in defects in interaction with protein receptors
	56 -> 65	LPKVKIEIVV
	67 -> 81	DDIVDTCVDTIIRTA
	81 -> 82	AQ	UniProt: In Ref. 1; AAA23883..
	82 -> 90	QTGKIGDGK
	83 -> 83	T	experimental mutation T → N results in defects in interaction with protein receptors and/or effectors (see \|CITS: [9209053]\|) for details
	84 -> 90	GKIGDGK
	89 -> 89	G	experimental mutation G → A results in severe defects in interaction with protein receptors and effectors (see \|CITS: [9209053]\|) for details
	90 -> 90	K	experimental mutation K → R results in defects in interaction with protein receptors and/or effectors (see \|CITS: [9209053]\|) for details
	91 -> 95	IFVFD
	96 -> 112	VARVIRIRTGEEDDAAI
	97 -> 102	ARVIRI
	106 -> 109	EEDD

Classification:

Multifun Terms (GenProtEC)
		1 - metabolism --> 1.5 - biosynthesis of building blocks --> 1.5.1 - amino acids --> 1.5.1.2 - glutamine
		1 - metabolism --> 1.5 - biosynthesis of building blocks --> 1.5.4 - fatty acids and phosphatidic acid
		1 - metabolism --> 1.8 - metabolism of other compounds --> 1.8.3 - nitrogen metabolism
		3 - regulation --> 3.1 - type of regulation --> 3.1.3 - posttranscriptional --> 3.1.3.3 - inhibition / activation of enzymes
Gene Ontology Terms (GO)
	cellular_component	GO:0005829 - cytosol
	molecular_function	GO:0005515 - protein binding GO:0008047 - enzyme activator activity GO:0030234 - enzyme regulator activity GO:0000166 - nucleotide binding GO:0005524 - ATP binding GO:0042802 - identical protein binding GO:0036094 - small molecule binding
	biological_process	GO:0050790 - regulation of catalytic activity GO:0006808 - regulation of nitrogen utilization GO:0042304 - regulation of fatty acid biosynthetic process

Evidence:

[EXP-IMP] Inferred from mutant phenotype
[IDA-PURIFIED-PROTEIN-NH] Assay of protein purified to homogeneity from its native host

Reference(s):

[1] Atkinson MR., et al., 1994
[2] Gerhardt EC., et al., 2015
[3] Jiang P., et al., 1999
[4] Jiang P., et al., 1997

External database links:

ALPHAFOLD:

DIP:

ECOCYC:

ECOLIWIKI:

INTERPRO:

INTERPRO:

INTERPRO:

INTERPRO:

INTERPRO:

MODBASE:

PANTHER:

PDB:

PDB:

PDB:

PFAM:

PRIDE:

PRINTS:

PRODB:

PROSITE:

PROSITE:

PROSITE:

REFSEQ:

SMART:

SMR:

UNIPROT:

Transcriptional Regulation
	Display Regulation
Repressed by:	PurR

Reference(s)
[1] Atkinson MR., Kamberov ES., Weiss RL., Ninfa AJ., 1994, Reversible uridylylation of the Escherichia coli PII signal transduction protein regulates its ability to stimulate the dephosphorylation of the transcription factor nitrogen regulator I (NRI or NtrC)., J Biol Chem 269(45):28288-93
[2] Gerhardt EC., Rodrigues TE., Muller-Santos M., Pedrosa FO., Souza EM., Forchhammer K., Huergo LF., 2015, The bacterial signal transduction protein GlnB regulates the committed step in fatty acid biosynthesis by acting as a dissociable regulatory subunit of acetyl-CoA carboxylase., Mol Microbiol 95(6):1025-35
[3] Jiang P., Ninfa AJ., 1999, Regulation of autophosphorylation of Escherichia coli nitrogen regulator II by the PII signal transduction protein., J Bacteriol 181(6):1906-11
[4] Jiang P., Zucker P., Atkinson MR., Kamberov ES., Tirasophon W., Chandran P., Schefke BR., Ninfa AJ., 1997, Structure/function analysis of the PII signal transduction protein of Escherichia coli: genetic separation of interactions with protein receptors., J Bacteriol 179(13):4342-53