RegulonDB RegulonDB 10.7: Gene Form
   

glnH gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

glnH glnP dps glnQ IHF NtrC NtrC NtrC NtrC IHF anti-anti-terminator anti-terminator terminator glnHp1 glnHp1 glnHp2 glnHp2 TSS_969 TSS_969 TSS_968 TSS_968 TSS_967 TSS_967 TSS_966 TSS_966 glnQp glnQp TSS_965 TSS_965 TSS_964 TSS_964

Gene      
Name: glnH    Texpresso search in the literature
Synonym(s): ECK0800, EG10386, b0811
Genome position(nucleotides): 847258 <-- 848004 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
48.73
External database links:  
ASAP:
ABE-0002771
CGSC:
18271
ECHOBASE:
EB0381
OU-MICROARRAY:
b0811
PORTECO:
glnH
REGULONDB:
b0811
STRING:
511145.b0811
M3D: glnH
COLOMBOS: glnH
PortEco: b0811


Product      
Name: L-glutamine ABC transporter periplasmic binding protein
Synonym(s): GlnBP, GlnH
Sequence: Get amino acid sequence Fasta Format
Cellular location: periplasmic space,membrane
Molecular weight: 27.19
Isoelectric point: 9.033
Motif(s):
 
Type Positions Sequence
112 -> 202 LLVMVKANNNDVKSVKDLDGKVVAVKSGTGSVDYAKANIKTKDLRQFPNIDNAYMELGTNRADAVLHDTPNILYFIKTAGNGQFKAVGDSL
27 -> 244 LVVATDTAFVPFEFKQGDKYVGFDVDLWAAIAKELKLDYELKPMDFSGIIPALQTKNVDLALAGITITDERKKAIDFSDGYYKSGLLVMVKANNNDVKSVKDLDGKVVAVKSGTGSVDYAKANIKTKDLRQFPNIDNAYMELGTNRADAVLHDTPNILYFIKTAGNGQFKAVGDSLEAQQYGIAFPKGSDELRDKVNGALKTLRENGTYNEIYKKWFG
23 -> 106 ADKKLVVATDTAFVPFEFKQGDKYVGFDVDLWAAIAKELKLDYELKPMDFSGIIPALQTKNVDLALAGITITDERKKAIDFSDG
1 -> 22 MKSVLKVSLAALTLAFAVSSHA
107 -> 111 YYKSG

 

Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.5 - biosynthesis of building blocks --> 1.5.1 - amino acids --> 1.5.1.2 - glutamine
  4 - transport --> 4.3 - Primary Active Transporters --> 4.3.A - Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters --> 4.3.A.1 - The ATP-binding Cassette (ABC) Superfamily + ABC-type Uptake Permeases --> 4.3.A.1.p - ABC superfamily, periplasmic binding component
Gene Ontology Terms (GO)  
cellular_component GO:0016020 - membrane
GO:0030288 - outer membrane-bounded periplasmic space
GO:0042597 - periplasmic space
molecular_function GO:0015276 - ligand-gated ion channel activity
GO:0070406 - glutamine binding
biological_process GO:0006865 - amino acid transport
GO:0034220 - ion transmembrane transport
GO:0006868 - glutamine transport
Note(s): Note(s): ...[more].
Reference(s): [1] Bermejo GA., et al., 2010
[2] Loeffler HH., et al., 2009
[3] Pang A., et al., 2003
[4] Pistolesi S., et al., 2012
[5] Su JG., et al., 2007
[6] Tjandra N., et al., 1992
[7] Yu J., et al., 1997
External database links:  
ECOCYC:
GLNH-MONOMER
ECOLIWIKI:
b0811
INTERPRO:
IPR018313
INTERPRO:
IPR001320
INTERPRO:
IPR001638
MODBASE:
P0AEQ3
PDB:
1GGG
PDB:
1WDN
PFAM:
PF00497
PRIDE:
P0AEQ3
PRODB:
PRO_000022787
PROSITE:
PS01039
PROTEINMODELPORTAL:
P0AEQ3
REFSEQ:
NP_415332
SMART:
SM00062
SMART:
SM00079
SMR:
P0AEQ3
SWISSMODEL:
P0AEQ3
UNIPROT:
P0AEQ3


Operon      
Name: glnHPQ         
Operon arrangement:
Transcription unit        Promoter
glnQ
glnHPQ
glnHPQ


Transcriptional Regulation      
Display Regulation             
Activated by: IHF, NtrC
Repressed by: NtrC


RNA cis-regulatory element    
Attenuation: Transcriptional


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_964 846498 reverse nd [RS-EPT-CBR] [8]
  promoter TSS_965 846624 reverse nd [RS-EPT-CBR] [8]
  promoter TSS_966 846763 reverse nd [RS-EPT-CBR] [8]
  promoter TSS_967 846774 reverse nd [RS-EPT-CBR] [8]
  promoter TSS_968 846807 reverse nd [RS-EPT-CBR] [8]
  promoter TSS_969 847113 reverse nd [RS-EPT-CBR] [8]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates



Reference(s)    

 [1] Bermejo GA., Strub MP., Ho C., Tjandra N., 2010, Ligand-free open-closed transitions of periplasmic binding proteins: the case of glutamine-binding protein., Biochemistry 49(9):1893-902

 [2] Loeffler HH., Kitao A., 2009, Collective dynamics of periplasmic glutamine binding protein upon domain closure., Biophys J 97(9):2541-9

 [3] Pang A., Arinaminpathy Y., Sansom MS., Biggin PC., 2003, Interdomain dynamics and ligand binding: molecular dynamics simulations of glutamine binding protein., FEBS Lett 550(1-3):168-74

 [4] Pistolesi S., Tjandra N., 2012, Temperature dependence of molecular interactions involved in defining stability of glutamine binding protein and its complex with L-glutamine., Biochemistry 51(2):643-52

 [5] Su JG., Jiao X., Sun TG., Li CH., Chen WZ., Wang CX., 2007, Analysis of domain movements in glutamine-binding protein with simple models., Biophys J 92(4):1326-35

 [6] Tjandra N., Simplaceanu V., Cottam PF., Ho C., 1992, Multidimensional 1H and 15N NMR investigation of glutamine-binding protein of Escherichia coli., J Biomol NMR 2(2):149-60

 [7] Yu J., Simplaceanu V., Tjandra NL., Cottam PF., Lukin JA., Ho C., 1997, 1H, 13C, and 15N NMR backbone assignments and chemical-shift-derived secondary structure of glutamine-binding protein of Escherichia coli., J Biomol NMR 9(2):167-80

 [8] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.


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