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:	BUsg_344

From

Buchnera aphidicola subsp. Schizaphis graminum

[TaxID: 98794]

[HAMAP proteome]

Taxonomy

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

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(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 (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

AE013218; AAM67898.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_660687.1; -.

3D structure databases

HSSP

P05053; 1IBA. [HSSP ENTRY / PDB]

ModBase

Q8K9J0.

Enzyme and pathway databases

BioCyc

BAPH198804:BUSG344-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).

ProtoNet

Q8K9J0.

Genome annotation databases

GeneID

1005590; -.

GenomeReviews

AE013218_GR; BUsg_344.

KEGG

bas:BUsg344; -.

Phylogenomic databases

HOGENOM

Q8K9J0; -.

Genome annotation databases

CMR

Q8K9J0; BUsg_344.

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`	`1 477`	`477`	`PTS system glucose-specific EIICB component.`	`PRO_0000186526`
`TRANSMEM`	`20 40`	`21`	`Potential.`
`TRANSMEM`	`51 71`	`21`	`Potential.`
`TRANSMEM`	`76 96`	`21`	`Potential.`
`TRANSMEM`	`112 132`	`21`	`Potential.`
`TRANSMEM`	`152 172`	`21`	`Potential.`
`TRANSMEM`	`250 270`	`21`	`Potential.`
`TRANSMEM`	`280 300`	`21`	`Potential.`
`TRANSMEM`	`304 324`	`21`	`Potential.`
`TRANSMEM`	`354 374`	`21`	`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: 51941 Da [This is the MW of the unprocessed precursor]

CRC64: 84CA2ABDFEA4CFA2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFKNVFSSLQ KVGKSLMLPV SVLPIAGILL GIGSAHFTLI PEIISQIMAQ TGGSIFSNMP 

        70         80         90        100        110        120 
LIFAIGVALG FSNNDGVAAL AAVVAYSILI QTLSAVELNI LNTDANTIKN KNFSDIGILG 

       130        140        150        160        170        180 
GIIAGAISAY MFNKFYKIQL PEYLGFFAGK RFVPIISGLF AIFVGLILSL IWPSIGNKIQ 

       190        200        210        220        230        240 
IFSEWAAYQN PIIAFSLYGL VERALVPFGL HHIWNVPFQM QIGEYKNSIG QIFHGDIARY 

       250        260        270        280        290        300 
MAGDTTAGNL SGGFIFKMYG LPGAALAIWH TAKKENRKKI GSIMISAALT AFLTGITEPI 

       310        320        330        340        350        360 
EFSFILVAPI LYIIHAILAG LSFPLCIFLN MRAGTSFSHG FIDFIVLSGH SHKIFLFPIV 

       370        380        390        400        410        420 
GICYGLLYYS IFYFLITTFN LKTPGREENK NTVFFRNNIE IAPYIVEALG GKNNIKNLDA 

       430        440        450        460        470 
CITRLRITVS EISKVNEENL KNLGAAGVVI SGSGVQAVFG TRSENIKTAI DEYINNI

Q8K9J0 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