TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*4.A.1.1.1









Glucose porter (PtsG; GlcA; Umg) (transports D-glucose and α-methyl-D-glucopyranoside).  The IIC domain has been crystallized, and x-ray data to 4.5 Å resolution have been described (Zurbriggen et al. 2010).  The system has been manipulated to engineer increased production of aromatic metabolites (Carmona et al. 2015, Vargas-Tah et al. 2015). The presence or absence of D-glucose reflects the transporter before and after release of the transported glucose into the cytoplasm. The transition associated with substrate release appears to require a subtle structural rearrangement in the region that includes hairpin 1 (Kalbermatter et al. 2017).  Mlc (for makes large colonies) represses transcription of the genes encoding enzyme I, HPr and EIIBCGlc in defined media that lack PTS substrates. When glucose is present, the unphosphorylated form of EIIBCGlc sequesters Mlc to the cell membrane, preventing its interaction with DNA (Plumbridge 2002, Joyet et al. 2013). The Vibrio Mlc functions similarly (Pickering et al. 2014). A small (43 aa) protein, SgrT, acts in tandem with a well-characterized small RNA during metabolic stress, due to the accumulation of cytoplasmic sugar-Ps to help bacterial cells maintain balanced metabolism and continue growing. SgrT acts on the glucose transport system, inhibiting its activity under stress conditions in order to allow cells to utilize alternative carbon sources (Lloyd et al. 2017).

 

Bacteria
Proteobacteria
PtsG/Crr; Glucose IICB/IIA complex of E. coli
*4.A.1.1.2









N-Acetyl glucosamine (NAG) porter (NagE) (Plumbridge 2015).

Bacteria
Proteobacteria
NagE, the IICBANag complex of E. coli
*4.A.1.1.3









Maltose porter (MalX)
Bacteria
Proteobacteria
Maltose IICB complex (MalX) of E. coli
*4.A.1.1.4









The α-glucoside-specific IICB (MalB) (substrates probably include glucosyl-α-fructose disaccharides: trehalurose (α-1,1), turanose (α-1,3), malturose (α-1,4), leucrose (α-1,5) and palatinose (α-1,6)).
Bacteria
Fusobacteria
The α-glucoside IICB, MalB of Fusobacterium mortiferum
*4.A.1.1.5









N-Acetylglucosamine (NAG) porter (PtsBC1C2)(also may facilitate xylose transport) (Saito and Schrempf 2004).

Bacteria
Actinobacteria
The NAG IICC'B complex of Streptomyces olivaceoviridis (IIA not identified)
IICNag (PtsC1)
IIC'Nag (PtsC2)
IIBNag (PtsB)
*4.A.1.1.6









The glucosamine IICBA porter (GamP) (40% identical to 4.A.1.1.2) (Plumbridge 2015). The IIA domain in this protein can transfer the phosphoryl moiety to the maltose, N-acetylglucosamine, sucrose and trehalose PTS systems (MalP, NagP, SacP and TreP, respectively) (Morabbi Heravi and Altenbuchner 2018).

Bacteria
Firmicutes
GamP of Bacillus subtilis (gi2632521)
*4.A.1.1.7









The N-acetylglucosamine IICB porter (NagP; YflF) (45% identical to 4.A.1.1.2) (Plumbridge 2015).

Bacteria
Firmicutes
NagP of Bacillus subtilis (gi2443228)
*4.A.1.1.8









The maltose IICB porter (MalP; GlvC) (56% identical to 4.A.1.1.4) (Yamamoto et al., 2001).

Bacteria
Firmicutes
MalP of Bacillus subtilis (IICBA) (P54715)
*4.A.1.1.9









The glucose IICBA porter (PtsG) 44% identical to 4.A.1.1.1)
Bacteria
Firmicutes
PtsG of Bacillus subtilis (P20166)
*4.A.1.1.10









The α-glucoside-specific IICB, AglB (transports glucose, methyl-α-glucoside, maltitol, isomaltose, trehalulose α(1→1), turanose α(1→3), maltulose α(1→4), leucrose α(1→5), and palatinose α(1→6), but not sucrose (most resembles 4.A.1.1.4 and 4.A.1.1.8) (Pikis et al., 2006)
Bacteria
Proteobacteria
Glucose/α-glucoside IICB complex of Klebsiella pneumoniae (Q9AGA7)
*4.A.1.1.11









The maltose/maltotriose porter, MalT (31% identical to 4.A.1.1.9) (Webb et al., 2007)
Bacteria
Firmicutes
MalT IICBA of Streptococcus mutans (Q8DS05)
*4.A.1.1.12









Maltose/Maltotriose PTS transporter, MalT (Shelburne et al., 2008) 631aas (68% identical to 4.A.1.1.11 from S. mutans
Bacteria
Firmicutes
MalT IICBA of Streptococcus pyogenes (Q48WG5)
*4.A.1.1.13









Glucose porter, GlcA (IICBA). Glucose uptake is inhibited by 2-deoxyglucose and methyl-β-D-glucoside (Christiansen and Hengstenberg, 1999).

Bacteria
Firmicutes
GlcA of Staphylococcus carnosus (Q57071)
*4.A.1.1.14









Glucose porter GlcB (IICBA). Glucose uptake is inhibited by methyl-α-D-glucoside, methyl-β-D-glucoside, p-nitrophenyl-α-D-glucoside, o-nitrophenyl-β-D-glucoside and salicin, but not by 2-deoxyglucose. Mannose and N-acetylglucosamine are not transported (Christiansen and Hengstenberg, 1999).

Bacteria
Firmicutes
GlcB of Staphylococcus carnosus (Q53922)
*4.A.1.1.15









N-acetyl glucosamine-specific PTS permease, GlcNAc IIBC/GlcNAc I-HPr-IIA (Johnson et al. 2008)

Bacteria
Proteobacteria
GlcNAc IIBC/GlcNAc I-HPr-IIA of Pseudomonas aeruginosa
GlcNAc IIBC (Q9HXN4)
GlcNAc I-HPr-IIA (Q9HXN5)
*4.A.1.1.16









PTS uptake porter for sucrose isomers, IICB (Thompson and Pikis 2012).

Bacteria
Fusobacteria
IICB for sucose isomers of Leptotrichia buccalis
*4.A.1.1.17









The Maltose group translocator, MalT of 470 aas and 10 TMSs. Takes up extracellular maltose, releasing maltose-phosphate into the cytoplasm.  The 3-d structure at 2.55 Å resolution has been solved (McCoy et al. 2016; Vastermark and Saier 2016).

MalT of Bacillus cereus
*4.A.1.1.18









Glucose-specific Enzyme IIBC of the PTS, PtsG.  Essential for infectivity and virulence in mice although no other PTS Enzyme II is required (Khajanchi et al. 2016).

Bacteria
Spirochaetes
IIBCGlc (PtsG) of Borrelia burgdorferi
*4.A.1.1.19









PTS α-glucoside transporter, subunit IICB (Francl et al. 2010).

Bacteria
Firmicutes
IICB of Lactobacillus gasseri
*4.A.1.1.20









The N-acetylglucosamine PTS transporter/kinase, NagE2 (416 aas; IIC)/NagF (77 aas; IIB).  The IIA specific for glucose (Crr) is the IIA for this system, and activity depends on Enzyme I and HPr (Nothaft et al. 2010). The genes encoding these enzymes are regulated by two transcription factors, DasR and AtrA, and the system serves as a sensor as well as a transporter/kinase (Nothaft et al. 2010).

Bacteria
Actinobacteria
NagE2F of Streptomyces coelicolor
*4.A.1.1.21









Enzyme IIA of 168 aas.  It is of the glucose type and can phosphorylate maltose via MalP (TC# 4.A..1.1.8), N-acetyl glucosamine via NagP (TC#4.A.1.1.7), sucrose via SacX (TC#4.A.1.2.10) and SacP (TC# 4.A.1.2.9), and trehalose via TreP (TC# 4.A.1.2.8), none of which have their own IIA protein (Morabbi Heravi and Altenbuchner 2018). Other Enzymes IIA could also phosphorlyate these sugars via their respective IIBC proteins.

Bacteria
Firmicutes
PtsA (YpqE) IIA protein of Bacillus subtilis
*4.A.1.2.1









Sucrose porter (ScrA)
Bacteria
Proteobacteria
Sucrose IIBC complex (ScrA) of plasmid pUR400 from Salmonella typhimurium
*4.A.1.2.2









β-Glucoside (salicin, arbutin, cellobiose, etc) group translocator, BglF.  The bgl operon, encoding BglF, is regulated by antitermination when the RNA antiterminator protein, BglG, binds to one of two RAT sites in the mRNA (Gordon et al. 2015).

Bacteria
Proteobacteria
BglF (IIBCAbgl) complex of E. coli
*4.A.1.2.3









β-Glucoside [arbutin-salicin-cellobiose] (ASC) group translocator, AscF (Desai et al. 2010).

Bacteria
Proteobacteria
AscF (IICBAsc complex) of E. coli
*4.A.1.2.4









Trehalose porter, TreB (IIBC) which can take up maltose by facilitated diffusion (Decker et al. 1999).  Can also transport sucrose at a low rate (Steen et al. 2014).

Bacteria
Proteobacteria
Trehalose IIBC complex of E. coli
*4.A.1.2.5









β-glucoside (methyl-β-glucoside, salicin, arbutin) porter, BglF [a V317A or V317M mutation allows it to transport cellobiose as well] (Kotrba et al., 2003)
Bacteria
Actinobacteria
β-glucoside IIBCA (BglF) of Corynebacterium glutamicum
*4.A.1.2.6









β-glucoside (Aesculin/arbutin) porter, BglP (Cote et al., 2000; Cote and Honeyman, 2003)
Bacteria
Firmicutes
β-glucoside IIBCA (BglP) of Streptococcus mutans (AAF89975)
*4.A.1.2.7









N-Acetylmuramic acid porter, MurP (YfeV) (Dahl et al., 2004)
Bacteria
Proteobacteria
N-Acetylmuramate IIBC (MurP or YfeV) of E. coli (P77272)
*4.A.1.2.8









Trehalose porter, IIBC (TreP) (38% identical to 4.A.1.2.4) (Schöck and Dahl 1996; Ujiie et al. 2009).

Bacteria
Firmicutes
TreP of Bacillus subtilis (P39794)
*4.A.1.2.9









Sucrose porter, IIBC (SacP) (55% identical to 4.A.1.2.1)
Bacteria
Firmicutes
SacP of Bacillus subtilis (P05306)
*4.A.1.2.10









Sucrose porter and regulatory sensor, IIBC (SacX) (43% identical to 4.A.1.2.1) (Tortosa and Le Coq 1995). The IIA domains of PtsA, GamP, PtsG and GmuA can all phosphorylate the IIB domain in the SacX sensor (Morabbi Heravi and Altenbuchner 2018).

Bacteria
Firmicutes
SacX of Bacillus subtilis (P15400)
*4.A.1.2.11









Aryl β-glucoside porter, IIBCA (BglP; SytA) (35% identical to 4.A.1.2.2)
Bacteria
Firmicutes
BglP of Bacillus subtilis (P40739)
*4.A.1.2.12









The sucrose porter, PtsS (regulated by SugR which also regulates other enzymes II) (Engels and Wendisch, 2007)
Bacteria
Actinobacteria
PtsS (IIBCA) complex of Corynebacterium glutamicum (Q8NMD6)
*4.A.1.2.13









Trehalose PTS permease IIBC of 494 aas (Ells and Truelstrup Hansen 2011).

Bacteria
Firmicutes
Trehalose IIBC of Listeria monocytogenese
*4.A.1.2.14









PTS beta-glucoside transporter, EIIBCA of 672 aas and 12 predicted TMSs (Francl et al. 2010).

EIIBCA of Lactobacillus gasseri
*4.A.1.2.15









PTS beta-glucoside transporter, EIIBCA of 624 aas and 10 predicted TMSs (Francl et al. 2010).

Bacteria
Firmicutes
EIIBCA of Lactobacillus gasseri
*4.A.1.2.16









PTS beta-glucoside transporter, EIIBCA of 647 aas and 10 predicted TMSs (Francl et al. 2010).

Bacteria
Firmicutes
EIIBCA of Lactobacillus gasseri
*4.A.1.2.17









N-acetylmuramic acid (MurNAc)-selective PTS transport system, MurP, IIBC, of 455 aas and 10 - 12 TMSs.

Bacteria
Firmicutes
MurP of Bacillus velezensis
*4.A.1.2.18









Glucose/fructose/glucosamine/mannose PTS IIABC system, FruA.  FruA phosphorylates the sugar subrates on the 6-hydroxyl group (Mazé et al. 2007).

Bacteria
Actinobacteria
FruA of Bifidobacterium breve