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Protein

Sensory histidine kinase/phosphatase NtrB

Gene

glnL

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Under conditions of nitrogen limitation, NtrB autophosphorylates and transfers the phosphoryl group to NtrC. In the presence of nitrogen, acts as a phosphatase that dephosphorylates and inactivates NtrC.4 Publications

Catalytic activityi

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.2 Publications

Enzyme regulationi

The phosphatase and kinase activities are regulated by the nitrogen regulatory proteins P-II 1 (GlnB) and P-II 2 (GlnK) (PubMed:2874557, PubMed:2574599, PubMed:10074086, PubMed:10231487). GlnB acts by binding to NtrB, leading to activation of the phosphatase activity and inhibition of the kinase activity. Binding of GlnB to NtrB is allosterically controlled by the small-molecule effector 2-ketoglutarate. At low 2-ketoglutarate concentrations, GlnB interacts with NtrB, but not at high 2-ketoglutarate concentrations (PubMed:10074086). Uridylylation of GlnB also prevents interaction with NtrB (PubMed:7961766).5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei329ATPBy similarity1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • phosphoprotein phosphatase activity Source: EcoCyc
  • phosphorelay sensor kinase activity Source: EcoCyc

GO - Biological processi

  • nitrogen fixation Source: UniProtKB-KW
  • phosphorelay signal transduction system Source: EcoCyc
  • protein autophosphorylation Source: EcoCyc
  • regulation of nitrogen compound metabolic process Source: EcoCyc
  • regulation of transcription, DNA-templated Source: InterPro

Keywordsi

Molecular functionHydrolase, Kinase, Transferase
Biological processNitrogen fixation, Two-component regulatory system
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:PROTEIN-NRII

Names & Taxonomyi

Protein namesi
Recommended name:
Sensory histidine kinase/phosphatase NtrBCurated (EC:2.7.13.32 Publications, EC:3.1.3.-2 Publications)
Alternative name(s):
Nitrogen regulation protein NR(II)Curated
Nitrogen regulator II1 Publication
Short name:
NRII1 Publication
Gene namesi
Name:glnL1 Publication
Synonyms:glnR, ntrB1 Publication
Ordered Locus Names:b3869, JW3840
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10387 glnL

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • intracellular Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000748201 – 349Sensory histidine kinase/phosphatase NtrBAdd BLAST349

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei139Phosphohistidine; by autocatalysisPROSITE-ProRule annotation1 Publication1

Post-translational modificationi

Autophosphorylated.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0AFB5
PRIDEiP0AFB5

PTM databases

iPTMnetiP0AFB5

Interactioni

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4262629, 18 interactors
DIPiDIP-9784N
IntActiP0AFB5, 10 interactors
STRINGi316385.ECDH10B_4059

Structurei

Secondary structure

1349
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi195 – 197Combined sources3
Helixi199 – 210Combined sources12
Turni211 – 213Combined sources3
Beta strandi218 – 223Combined sources6
Beta strandi231 – 233Combined sources3
Helixi235 – 253Combined sources19
Helixi254 – 256Combined sources3
Beta strandi258 – 272Combined sources15
Beta strandi275 – 288Combined sources14
Helixi314 – 325Combined sources12
Beta strandi329 – 335Combined sources7
Beta strandi338 – 348Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R62X-ray1.60A190-349[»]
ProteinModelPortaliP0AFB5
SMRiP0AFB5
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AFB5

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 78PASPROSITE-ProRule annotationAdd BLAST74
Domaini136 – 349Histidine kinasePROSITE-ProRule annotationAdd BLAST214

Domaini

The C-terminal ATP-binding domain is required for both kinase and phosphatase activities and contains the GlnB binding site.1 Publication

Phylogenomic databases

eggNOGiENOG4105CUX Bacteria
COG3852 LUCA
HOGENOMiHOG000262169
InParanoidiP0AFB5
KOiK07708
OMAiNIVHNAA
PhylomeDBiP0AFB5

Family and domain databases

CDDicd00075 HATPase_c, 1 hit
cd00082 HisKA, 1 hit
cd00130 PAS, 1 hit
Gene3Di3.30.565.10, 1 hit
InterProiView protein in InterPro
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
IPR005467 His_kinase_dom
IPR003661 HisK_dim/P
IPR036097 HisK_dim/P_sf
IPR000014 PAS
IPR035965 PAS-like_dom_sf
IPR013767 PAS_fold
IPR004358 Sig_transdc_His_kin-like_C
PfamiView protein in Pfam
PF02518 HATPase_c, 1 hit
PF00512 HisKA, 1 hit
PF00989 PAS, 1 hit
PRINTSiPR00344 BCTRLSENSOR
SMARTiView protein in SMART
SM00387 HATPase_c, 1 hit
SM00388 HisKA, 1 hit
SM00091 PAS, 1 hit
SUPFAMiSSF47384 SSF47384, 1 hit
SSF55785 SSF55785, 1 hit
SSF55874 SSF55874, 1 hit
PROSITEiView protein in PROSITE
PS50109 HIS_KIN, 1 hit
PS50112 PAS, 1 hit

Sequencei

Sequence statusi: Complete.

P0AFB5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATGTQPDAG QILNSLINSI LLIDDNLAIH YANPAAQQLL AQSSRKLFGT
60 70 80 90 100
PLPELLSYFS LNIELMQESL EAGQGFTDNE VTLVIDGRSH ILSVTAQRMP
110 120 130 140 150
DGMILLEMAP MDNQRRLSQE QLQHAQQVAA RDLVRGLAHE IKNPLGGLRG
160 170 180 190 200
AAQLLSKALP DPSLLEYTKV IIEQADRLRN LVDRLLGPQL PGTRVTESIH
210 220 230 240 250
KVAERVVTLV SMELPDNVRL IRDYDPSLPE LAHDPDQIEQ VLLNIVRNAL
260 270 280 290 300
QALGPEGGEI ILRTRTAFQL TLHGERYRLA ARIDVEDNGP GIPPHLQDTL
310 320 330 340
FYPMVSGREG GTGLGLSIAR NLIDQHSGKI EFTSWPGHTE FSVYLPIRK
Length:349
Mass (Da):38,556
Last modified:January 1, 1988 - v1
Checksum:i8B6B3BB18B2E2E98
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05173 Genomic DNA Translation: CAA28807.1
L19201 Genomic DNA Translation: AAB03003.1
U00096 Genomic DNA Translation: AAC76866.1
AP009048 Genomic DNA Translation: BAE77440.1
K02176 Genomic DNA Translation: AAA23881.1
PIRiA30377 RGECGL
RefSeqiNP_418305.1, NC_000913.3
WP_000190577.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76866; AAC76866; b3869
BAE77440; BAE77440; BAE77440
GeneIDi948360
KEGGiecj:JW3840
eco:b3869
PATRICifig|1411691.4.peg.2842

Similar proteinsi

Entry informationi

Entry nameiNTRB_ECOLI
AccessioniPrimary (citable) accession number: P0AFB5
Secondary accession number(s): P06712, Q2M8G6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: March 28, 2018
This is version 112 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health