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4.A.2.1.2
Mannitol porter (MtlA) (mannitol-1-P forming), the mannitol IICBA complex.  The enzyme-transporter has been alterred genetically, sequenced, purified, reconstituted and characterized (Jacobson et al. 1983, Leonard and Saier 1983, Lee and Saier 1983, Manayan et al. 1988). Intramolecular phosphoryl transfer between the A and B domains of IIMtl is rate-limited by chemistry and not by the rate of formation or dissociation of a stereospecific complex in which the active sites are optimally apposed (Suh et al. 2007). Substrates, in addition to D-mannitol, include D-glucitol (D-sorbitol), D-2-amino-2-deoxymannitol, D-2-deoxymannitol and D-arabitol (D-arabinitol) (Jacobson et al. 1983).

Accession Number:P00550
Protein Name:PTMA aka MTLA aka B3599
Length:637
Molecular Weight:67972.00
Species:Escherichia coli [83333]
Number of TMSs:10
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Multi-pass membrane protein2
Substrate D-mannitol

Cross database links:

DIP: DIP-10267N
RefSeq: AP_004193.1    NP_418056.1   
Entrez Gene ID: 948118   
Pfam: PF00359    PF02378    PF02302   
BioCyc: EcoCyc:MTLA-MONOMER    ECOL168927:B3599-MONOMER   
KEGG: ecj:JW3573    eco:b3599   

Gene Ontology

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:0005351 F:sugar:hydrogen symporter activity
GO:0009401 P:phosphoenolpyruvate-dependent sugar phospho...

References (9)

[1] “Mannitol-specific enzyme II of the bacterial phosphotransferase system. III. The nucleotide sequence of the permease gene.”  Lee C.A.et.al.   6309813
[2] “Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes.”  Sofia H.J.et.al.   8041620
[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] “Nucleotide sequence of the mannitol (mtl) operon in Escherichia coli.”  Davis T.et.al.   3135464
[6] “S-phosphocysteine and phosphohistidine are intermediates in the phosphoenolpyruvate-dependent mannitol transport catalyzed by Escherichia coli EIIMtl.”  Pas H.H.et.al.   3142516
[7] “Membrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusions.”  Sugiyama J.E.et.al.   1946374
[8] “Global topology analysis of the Escherichia coli inner membrane proteome.”  Daley D.O.et.al.   15919996
[9] “The structure of the Escherichia coli phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active site.”  van Montfort R.L.M.et.al.   9551558
Structure:
1A3A   1J6T   1VKR   1VRV   2FEW     

External Searches:

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence 
1:	MSSDIKIKVQ SFGRFLSNMV MPNIGAFIAW GIITALFIPT GWLPNETLAK LVGPMITYLL 
61:	PLLIGYTGGK LVGGERGGVV GAITTMGVIV GADMPMFLGS MIAGPLGGWC IKHFDRWVDG 
121:	KIKSGFEMLV NNFSAGIIGM ILAILAFLGI GPIVEALSKM LAAGVNFMVV HDMLPLASIF 
181:	VEPAKILFLN NAINHGIFSP LGIQQSHELG KSIFFLIEAN PGPGMGVLLA YMFFGRGSAK 
241:	QSAGGAAIIH FLGGIHEIYF PYVLMNPRLI LAVILGGMTG VFTLTILGGG LVSPASPGSI 
301:	LAVLAMTPKG AYFANIAGVC AAMAVSFVVS AILLKTSKVK EEDDIEAATR RMQDMKAESK 
361:	GASPLSAGDV TNDLSHVRKI IVACDAGMGS SAMGAGVLRK KIQDAGLSQI SVTNSAINNL 
421:	PPDVDLVITH RDLTERAMRQ VPQAQHISLT NFLDSGLYTS LTERLVAAQR HTANEEKVKD 
481:	SLKDSFDDSS ANLFKLGAEN IFLGRKAATK EEAIRFAGEQ LVKGGYVEPE YVQAMLDREK 
541:	LTPTYLGESI AVPHGTVEAK DRVLKTGVVF CQYPEGVRFG EEEDDIARLV IGIAARNNEH 
601:	IQVITSLTNA LDDESVIERL AHTTSVDEVL ELLAGRK