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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).  Glutamine transporters are effective targets for digestive system malignant tumor treatment (Chu et al. 2024).

Accession Number:P10346
Protein Name:GlnQ aka B0809
Length:240
Molecular Weight:26731.00
Species:Escherichia coli [83333]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Peripheral membrane protein2
Substrate glutamine

Cross database links:

DIP: DIP-9786N
RefSeq: AP_001440.1    NP_415330.1   
Entrez Gene ID: 945435   
Pfam: PF00005   
BioCyc: EcoCyc:GLNQ-MONOMER    ECOL168927:B0809-MONOMER   
KEGG: ecj:JW0794    eco:b0809   

Gene Ontology

GO:0005886 C:plasma membrane
GO:0005524 F:ATP binding
GO:0016887 F:ATPase activity
GO:0005515 F:protein binding
GO:0006865 P:amino acid transport

References (5)

[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] “Protein complexes of the Escherichia coli cell envelope.”  Stenberg F.et.al.   16079137

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MIEFKNVSKH FGPTQVLHNI DLNIAQGEVV VIIGPSGSGK STLLRCINKL EEITSGDLIV 
61:	DGLKVNDPKV DERLIRQEAG MVFQQFYLFP HLTALENVMF GPLRVRGANK EEAEKLAREL 
121:	LAKVGLAERA HHYPSELSGG QQQRVAIARA LAVKPKMMLF DEPTSALDPE LRHEVLKVMQ 
181:	DLAEEGMTMV IVTHEIGFAE KVASRLIFID KGRIAEDGNP QVLIKNPPSQ RLQEFLQHVS