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3.A.1.3.2
Three component ABC L-glutamine porter. The basal ATPase activity (ATP hydrolysis in the absence of substrate) is mainly caused by the docking of the closed-unliganded state of GlnH onto the transporter domain of GlnPQ. Unlike glutamine, arginine binds both GlnH domains, but does not trigger their closing. Comparison of the ATPase activity in nanodiscs with glutamine transport in proteoliposomes suggested that the stoichiometry of ATP per substrate is close to two (Lycklama A Nijeholt et al. 2018).

Accession Number:P0AEQ3
Protein Name:Glutamine-binding periplasmic protein GlnH aka B0811 aka GlnBP
Length:248
Molecular Weight:27190.00
Species:Escherichia coli [83333]
Location1 / Topology2 / Orientation3: Periplasm1
Substrate Glutamine

Cross database links:

Genevestigator: P0AEQ3
EchoBASE: EB0381
EcoGene: EG10386
eggNOG: COG0834
HEGENOM: HBG698334
RefSeq: AP_001442.1    NP_415332.1   
Entrez Gene ID: 944872   
Pfam: PF00497   
BioCyc: EcoCyc:GLNH-MONOMER    ECOL168927:B0811-MONOMER   
KEGG: ecj:JW0796    eco:b0811   

Gene Ontology

GO:0030288 C:outer membrane-bounded periplasmic space
GO:0005515 F:protein binding
GO:0005215 F:transporter activity
GO:0006865 P:amino acid transport

References (7)

[1] “Cloning and complete nucleotide sequence of the Escherichia coli glutamine permease operon (glnHPQ).”  Nohno T.et.al.   3027504
[2] “A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.”  Oshima T.et.al.   8905232
[3] “The complete genome sequence of Escherichia coli K-12.”  Blattner F.R.et.al.   9278503
[4] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.”  Hayashi K.et.al.   16738553
[5] “Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.”  Link A.J.et.al.   9298646
[6] “The crystal structure of glutamine-binding protein from Escherichia coli.”  Hsiao C.-D.et.al.   8831790
[7] “The structure of glutamine-binding protein complexed with glutamine at 1.94-A resolution: comparisons with other amino acid binding proteins.”  Sun Y.-J.et.al.   9571045
Structure:
1GGG   1WDN     

External Searches:

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FASTA formatted sequence
1:	MKSVLKVSLA ALTLAFAVSS HAADKKLVVA TDTAFVPFEF KQGDKYVGFD VDLWAAIAKE 
61:	LKLDYELKPM DFSGIIPALQ TKNVDLALAG ITITDERKKA IDFSDGYYKS GLLVMVKANN 
121:	NDVKSVKDLD GKVVAVKSGT GSVDYAKANI KTKDLRQFPN IDNAYMELGT NRADAVLHDT 
181:	PNILYFIKTA GNGQFKAVGD SLEAQQYGIA FPKGSDELRD KVNGALKTLR ENGTYNEIYK 
241:	KWFGTEPK