TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


4.A.6.1.1
The mannose (glucose, 2-deoxyglucose, glucosamine, N-acetylglucosamine, N-acetylmannosamine, mannosamine and fructose) PTS porter/group translocator, ManXYZ (Rephaeli and Saier 1980; Plumbridge 2015). Catalyzes xylose facilitated diffusion in lactobacilli. The order of D-sugar substrate affinities is: glucose > mannose > 2-deoxyglucose > N-acetylglucosamine > glucosamine > N-acetylmannosamine > mannosamine > fructose (Rephaeli and Saier 1980).  The mechanism appears to be rapid equilibrium, random, bi-bi sequential (Rephaeli and Saier 1980). L-sugars are not transported. This system is allostericallly inhibited by a complex of DicB (62 aas, P09557) and MinC (231 aas, P18186) (Jeckelmann and Erni 2020). At the transcriptional level, the manXYZ operon is regulated by the Mlc transcriptional regulator, and at the translational level it is regulated by the DicF small RNA that is complementary to manXYZ (Jeckelmann and Erni 2020). The 3-d structure of the IIC/IID complex revealed that the N- and C-terminal halves form the transport and scaffold domains, respectively (Liu et al. 2019).  Two 3-helix bundles are mixed by an intersubunit helix swap yielding tight intersubunit contacts with a novel fold. An "elevator" mechanism has been proposed in which the transport domain moves vertically or rotates relative to a stationary scaffold domain, where both the transport and scaffold domains consist of α-helices of both the IIC aqnd IID domains. Only the IIC and IID proteins, not hte IIAB protein are required for lambda phage infectivity (Esquinas-Rychen and Erni 2001).  

Accession Number:P69797
Protein Name:PTNA aka MANX aka PTSL aka GPTB aka B1817
Length:323
Molecular Weight:35048.00
Species:Escherichia coli [83333]
Location1 / Topology2 / Orientation3: Cytoplasm1 / Peripheral membrane protein2
Substrate 2-amino-2-deoxy-D-glucopyranose, D-glucosamine, aldehydo-D-mannosamine, keto-D-fructose, D-glucopyranose, D-mannopyranose

Cross database links:

DIP: DIP-35846N
RefSeq: AP_002436.1    NP_416331.1   
Entrez Gene ID: 946334   
Pfam: PF03610    PF03830   
BioCyc: EcoCyc:MANX-MONOMER    ECOL168927:B1817-MONOMER   
KEGG: ecj:JW1806    eco:b1817   

Gene Ontology

GO:0005737 C:cytoplasm
GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0016301 F:kinase activity
GO:0005515 F:protein binding
GO:0008982 F:protein-N(PI)-phosphohistidine-sugar phosph...
GO:0009401 P:phosphoenolpyruvate-dependent sugar phospho...

References (10)

[1] “The mannose permease of Escherichia coli consists of three different proteins. Amino acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage lambda DNA.”  Erni B.et.al.   2951378
[2] “A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map.”  Itoh T.et.al.   9097040
[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] “Protein complexes of the Escherichia coli cell envelope.”  Stenberg F.et.al.   16079137
[7] “Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.”  Zhang J.et.al.   18723842
[8] “Structure of the IIA domain of the mannose transporter from Escherichia coli at 1.7-A resolution.”  Nunn R.S.et.al.   8676384
[9] “Predicted topology of the N-terminal domain of the hydrophilic subunit of the mannose transporter of Escherichia coli.”  Markovic-Housley Z.et.al.   8131846
[10] “Secondary structure of the IIB domain of the Escherichia coli mannose transporter, a new fold in the class of alpha/beta twisted open-sheet structures.”  Gschwind R.M.et.al.   9074635
Structure:
1PDO   1VRC   1VSQ   2JZH   2JZN   2JZO     

External Searches:

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence
1:	MTIAIVIGTH GWAAEQLLKT AEMLLGEQEN VGWIDFVPGE NAETLIEKYN AQLAKLDTTK 
61:	GVLFLVDTWG GSPFNAASRI VVDKEHYEVI AGVNIPMLVE TLMARDDDPS FDELVALAVE 
121:	TGREGVKALK AKPVEKAAPA PAAAAPKAAP TPAKPMGPND YMVIGLARID DRLIHGQVAT 
181:	RWTKETNVSR IIVVSDEVAA DTVRKTLLTQ VAPPGVTAHV VDVAKMIRVY NNPKYAGERV 
241:	MLLFTNPTDV ERLVEGGVKI TSVNVGGMAF RQGKTQVNNA VSVDEKDIEA FKKLNARGIE 
301:	LEVRKVSTDP KLKMMDLISK IDK