Glucose permease IIC component
     (PTS system glucose-specific EIIC component)
Glucose-specific phosphotransferase enzyme IIB component
     (EC 2.7.1.69)
     (PTS system glucose-specific EIIB component)

Gene name

	Name:	ptsG
	OrderedLocusNames:	c1373

From

Escherichia coli O6

[TaxID: 217992]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
DOI=10.1073/pnas.252529799; PubMed=12471157 [NCBI, ExPASy, EBI, Israel, Japan]
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).

Comments

FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in glucose transport. This enzyme is also a chemoreceptor monitoring the environment for changes in sugar concentration (By similarity).
CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.
SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein (By similarity).
DOMAIN: The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.
DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.
SIMILARITY: Contains 1 PTS EIIB type-1 domain.
SIMILARITY: Contains 1 PTS EIIC type-1 domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE014075; AAN79843.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_753283.1; -.

3D structure databases

SMR

P69787; 400-476.

ModBase

P69787.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005355;	Molecular function: glucose transmembrane transporter activity (inferred from electronic annotation from InterPro).
GO:0016301;	Molecular function: kinase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0008982;	Molecular function: protein-N(PI)-phosphohistidine-sugar phosphotransferase activity (inferred from electronic annotation from InterPro).
GO:0005351;	Molecular function: sugar:hydrogen symporter activity (inferred from electronic annotation from InterPro).
GO:0015758;	Biological process: glucose transport (inferred from electronic annotation from InterPro).
GO:0009401;	Biological process: phosphoenolpyruvate-dependent sugar phosphotransferase system (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001996; PTS_EIIB.
IPR003352; PTS_EIIC.
IPR013013; PTS_EIIC_1.
IPR011535; PTS_Glc-like_IIB_component.
IPR011299; PTS_IIBC_glc.
IPR004719; PTS_IIC_glc.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.1360.60; PTS_EIIB; 1.

Pfam

PF00367; PTS_EIIB; 1.
PF02378; PTS_EIIC; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00826; EIIB_glc; 1.
TIGR00852; pts-Glc; 1.
TIGR02002; PTS-II-BC-glcB; 1.

PROSITE

PS51098; PTS_EIIB_TYPE_1; 1.
PS01035; PTS_EIIB_TYPE_1_CYS; 1.
PS51103; PTS_EIIC_TYPE_1; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P69787.

Genome annotation databases

GeneID

1035072; -.

GenomeReviews

AE014075_GR; c1373.

KEGG

ecc:c1373; -.

Phylogenomic databases

HOGENOM

P69787; -.

Genome annotation databases

CMR

P69787; c1373.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell inner membrane; Cell membrane; Complete proteome; Kinase; Membrane; Phosphotransferase system; Sugar transport; Transferase; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 477`	`477`	`PTS system glucose-specific EIICB component.`	`PRO_0000186529`
`TOPO_DOM`	`1 14`	`14`	`Cytoplasmic (Potential).`
`TRANSMEM`	`15 35`	`21`	`Potential.`
`TOPO_DOM`	`36 50`	`15`	`Periplasmic (Potential).`
`TRANSMEM`	`51 71`	`21`	`Potential.`
`TOPO_DOM`	`72 79`	`8`	`Cytoplasmic (Potential).`
`TRANSMEM`	`80 100`	`21`	`Potential.`
`TOPO_DOM`	`101 111`	`11`	`Periplasmic (Potential).`
`TRANSMEM`	`112 132`	`21`	`Potential.`
`TOPO_DOM`	`133 151`	`19`	`Cytoplasmic (Potential).`
`TRANSMEM`	`152 172`	`21`	`Potential.`
`TOPO_DOM`	`173 190`	`18`	`Periplasmic (Potential).`
`TRANSMEM`	`191 211`	`21`	`Potential.`
`TOPO_DOM`	`212 249`	`38`	`Cytoplasmic (Potential).`
`TRANSMEM`	`250 270`	`21`	`Potential.`
`TOPO_DOM`	`271 279`	`9`	`Periplasmic (Potential).`
`TRANSMEM`	`280 300`	`21`	`Potential.`
`TOPO_DOM`	`301 309`	`9`	`Cytoplasmic (Potential).`
`TRANSMEM`	`310 330`	`21`	`Potential.`
`TOPO_DOM`	`331 355`	`25`	`Periplasmic (Potential).`
`TRANSMEM`	`356 376`	`21`	`Potential.`
`TOPO_DOM`	`377 477`	`101`	`Cytoplasmic (Potential).`
`DOMAIN`	`1 388`	`388`	`PTS EIIC type-1.`
`DOMAIN`	`399 477`	`79`	`PTS EIIB type-1.`
`ACT_SITE`	`421 421`		`Phosphocysteine intermediate; for EIIB activity (By similarity).`

Sequence information

Length: 477 AA [This is the length of the unprocessed precursor]

Molecular weight: 50677 Da [This is the MW of the unprocessed precursor]

CRC64: D97A80FD64B74F73 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFKNAFANLQ KVGKSLMLPV SVLPIAGILL GVGSANFSWL PAVVSHVMAE AGGSVFANMP 

        70         80         90        100        110        120 
LIFAIGVALG FTNNDGVSAL AAVVAYGIMV KTMAVVAPLV LHLPAEEIAS KHLADTGVLG 

       130        140        150        160        170        180 
GIISGAIAAY MFNRFYRIKL PEYLGFFAGK RFVPIISGLA AIFTGVVLSF IWPPIGSAIQ 

       190        200        210        220        230        240 
TFSQWAAYQN PVVAFGIYGF IERCLVPFGL HHIWNVPFQM QIGEYTNAAG QVFHGDIPRY 

       250        260        270        280        290        300 
MAGDPTAGKL SGGFLFKMYG LPAAAIAIWH SAKPENRAKV GGIMISAALT SFLTGITEPI 

       310        320        330        340        350        360 
EFSFMFVAPI LYIIHAILAG LAFPICILLG MRDGTSFSHG LIDFIVLSGN SSKLWLFPIV 

       370        380        390        400        410        420 
GIGYAIVYYT IFRVLIKALD LKTPGREDAT EDAKATGTSE MAPALVAAFG GKENITNLDA 

       430        440        450        460        470 
CITRLRVSVA DVSKVDQAGL KKLGAAGVVV AGSGVQAIFG TKSDNLKTEM DEYIRNH

P69787 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools