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:	bbp_326

From

Buchnera aphidicola subsp. Baizongia pistaciae

[TaxID: 135842]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0235981100; PubMed=12522265 [NCBI, ExPASy, EBI, Israel, Japan]
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
"Reductive genome evolution in Buchnera aphidicola.";
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).

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 (By similarity).
CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.
SUBCELLULAR LOCATION: Cell 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

AE016826; AAO27048.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_777943.1; -.

3D structure databases

HSSP

P05053; 1O2F. [HSSP ENTRY / PDB]

ModBase

Q89AG6.

Enzyme and pathway databases

BioCyc

BAPH224915:BBP_326-MON; -.

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.
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.
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).

Genome annotation databases

GeneID

1058276; -.

GenomeReviews

AE016826_GR; bbp_326.

KEGG

bab:bbp326; -.

Phylogenomic databases

HOGENOM

Q89AG6; -.

Genome annotation databases

CMR

Q89AG6; bbp_326.

Other

UniRef

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

Keywords

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`	`1 479`	`479`	`PTS system glucose-specific EIICB component.`	`PRO_0000186527`
`TRANSMEM`	`15 35`	`21`	`Potential.`
`TRANSMEM`	`51 71`	`21`	`Potential.`
`TRANSMEM`	`80 100`	`21`	`Potential.`
`TRANSMEM`	`112 132`	`21`	`Potential.`
`TRANSMEM`	`152 172`	`21`	`Potential.`
`TRANSMEM`	`252 272`	`21`	`Potential.`
`TRANSMEM`	`280 300`	`21`	`Potential.`
`TRANSMEM`	`305 325`	`21`	`Potential.`
`TRANSMEM`	`356 376`	`21`	`Potential.`
`DOMAIN`	`1 388`	`388`	`PTS EIIC type-1.`
`DOMAIN`	`399 479`	`81`	`PTS EIIB type-1.`
`ACT_SITE`	`421 421`		`Phosphocysteine intermediate; for EIIB activity (By similarity).`

Sequence information

Length: 479 AA [This is the length of the unprocessed precursor]

Molecular weight: 52157 Da [This is the MW of the unprocessed precursor]

CRC64: FF1B60760B4D9ABD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFKNAFSNLQ KIGRSLMLPV SVLPIAGILL GIGSANFKII PHTISNIMTE AGSSVFSNMP 

        70         80         90        100        110        120 
LIFAIGIALG FTKNDGVSAL AAVVSYGIMT KTLSITIPIF SNLSDINVNQ KYLLDTGILG 

       130        140        150        160        170        180 
GIIAGSISAY IFNTFYRIQL PEYLGFFAGR RFVPIASGLI SIIFGCILSI IWPPIGNVIK 

       190        200        210        220        230        240 
TFSEWAAYQN PTLAFGIYGT VERALVPFGL HHIWNVPFQM QIGEYNNSIG QIFHGDIARY 

       250        260        270        280        290        300 
MAGDSTAGKL SGGFIFKMYG LPFAALAMWH CANKKNKAKI GGIMMSGALT AILTGITEPI 

       310        320        330        340        350        360 
EFSFILVAPI LYVIHAILAG LAFPICILLN MRSGTSFSHG LIDFIVLSGN SNNFWLFPIV 

       370        380        390        400        410        420 
GLFYGILYYG IFYFMIKKFN LKTPGREKSI TYINQKTIKE TALLVISILG GKTNIINLDA 

       430        440        450        460        470 
CITRLRITVL DISKVNQKKL KNLGASGVIV SGSGIQIVFG TQSDHIKTEI DNYMSNTNQ

Q89AG6 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