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P09323 (PTW3C_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
PTS system N-acetylglucosamine-specific EIICBA component
Alternative name(s):
EIICBA-Nag
Short name=EII-Nag

Including the following 3 domains:

  1. N-acetylglucosamine permease IIC component
    Alternative name(s):
    PTS system N-acetylglucosamine-specific EIIC component
  2. N-acetylglucosamine-specific phosphotransferase enzyme IIB component
    EC=2.7.1.69
    Alternative name(s):
    PTS system N-acetylglucosamine-specific EIIB component
  3. N-acetylglucosamine-specific phosphotransferase enzyme IIA component
    EC=2.7.1.-
    Alternative name(s):
    PTS system N-acetylglucosamine-specific EIIA component
Gene names
Name:nagE
Synonyms:pstN
Ordered Locus Names:b0679, JW0665
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length648 AA.
Sequence statusComplete.
Protein existencePredicted

General annotation (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 N-acetylglucosamine transport.

Catalytic activity

Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine.

Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.

Subcellular location

Cell inner membrane; Multi-pass membrane protein Ref.6.

Domain

The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.

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.

The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.

Sequence similarities

Contains 1 PTS EIIA type-1 domain.

Contains 1 PTS EIIB type-1 domain.

Contains 1 PTS EIIC type-1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 648648PTS system N-acetylglucosamine-specific EIICBA component
PRO_0000186475

Regions

Transmembrane16 – 3621Helical; Potential
Transmembrane38 – 5821Helical; Potential
Transmembrane70 – 9021Helical; Potential
Transmembrane92 – 11221Helical; Potential
Transmembrane132 – 15221Helical; Potential
Transmembrane159 – 17921Helical; Potential
Transmembrane192 – 21221Helical; Potential
Transmembrane232 – 25221Helical; Potential
Transmembrane260 – 28021Helical; Potential
Transmembrane282 – 30221Helical; Potential
Transmembrane303 – 32321Helical; Potential
Transmembrane339 – 35921Helical; Potential
Domain1 – 371371PTS EIIC type-1
Domain390 – 47283PTS EIIB type-1
Domain517 – 621105PTS EIIA type-1

Sites

Active site4121Phosphocysteine intermediate; for EIIB activity By similarity
Active site5691Tele-phosphohistidine intermediate; for EIIA activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P09323 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 1E24C97CFCBBAA59

FASTA64868,347
        10         20         30         40         50         60 
MNILGFFQRL GRALQLPIAV LPVAALLLRF GQPDLLNVAF IAQAGGAIFD NLALIFAIGV 

        70         80         90        100        110        120 
ASSWSKDSAG AAALAGAVGY FVLTKAMVTI NPEINMGVLA GIITGLVGGA AYNRWSDIKL 

       130        140        150        160        170        180 
PDFLSFFGGK RFVPIATGFF CLVLAAIFGY VWPPVQHAIH AGGEWIVSAG ALGSGIFGFI 

       190        200        210        220        230        240 
NRLLIPTGLH QVLNTIAWFQ IGEFTNAAGT VFHGDINRFY AGDGTAGMFM SGFFPIMMFG 

       250        260        270        280        290        300 
LPGAALAMYF AAPKERRPMV GGMLLSVAVT AFLTGVTEPL EFLFMFLAPL LYLLHALLTG 

       310        320        330        340        350        360 
ISLFVATLLG IHAGFSFSAG AIDYALMYNL PAASQNVWML LVMGVIFFAI YFVVFSLVIR 

       370        380        390        400        410        420 
MFNLKTPGRE DKEDEIVTEE ANSNTEEGLT QLATNYIAAV GGTDNLKAID ACITRLRLTV 

       430        440        450        460        470        480 
ADSARVNDTM CKRLGASGVV KLNKQTIQVI VGAKAESIGD AMKKVVARGP VAAASAEATP 

       490        500        510        520        530        540 
ATAAPVAKPQ AVPNAVSIAE LVSPITGDVV ALDQVPDEAF ASKAVGDGVA VKPTDKIVVS 

       550        560        570        580        590        600 
PAAGTIVKIF NTNHAFCLET EKGAEIVVHM GIDTVALEGK GFKRLVEEGA QVSAGQPILE 

       610        620        630        640 
MDLDYLNANA RSMISPVVCS NIDDFSGLII KAQGHIVAGQ TPLYEIKK 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequences of the Escherichia coli nagE and nagB genes: the structural genes for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and for glucosamine-6-phosphate deaminase."
Rogers M.J., Ohgi T., Plumbridge J., Soell D.
Gene 62:197-207(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence of cloned enzyme IIN-acetylglucosamine of the phosphoenolpyruvate:N-acetylglucosamine phosphotransferase system of Escherichia coli."
Peri K.G., Waygood E.B.
Biochemistry 27:6054-6061(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19284 Genomic DNA. Translation: AAA24192.1.
U00096 Genomic DNA. Translation: AAC73773.1.
AP009048 Genomic DNA. Translation: BAA35327.1.
PIRWQEC2N. B29895.
RefSeqNP_415205.1. NC_000913.2.
YP_488959.1. NC_007779.1.

3D structure databases

ProteinModelPortalP09323.
SMRP09323. Positions 392-466, 500-648.
ModBaseSearch...

Protein-protein interaction databases

STRING511145.b0679.

Protein family/group databases

TCDB4.A.1.1.2. PTS glucose-glucoside (Glc) family.

Proteomic databases

PaxDbP09323.
PRIDEP09323.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73773; AAC73773; b0679.
BAA35327; BAA35327; BAA35327.
GeneID12932215.
945292.
KEGGecj:Y75_p0658.
eco:b0679.
PATRIC32116545. VBIEscCol129921_0705.

Organism-specific databases

EchoBASEEB0629.
EcoGeneEG10635. nagE.

Phylogenomic databases

eggNOGCOG1263.
HOGENOMHOG000250993.
KOK02802.
K02803.
K02804.
OMAQANLEMI.
ProtClustDBPRK10255.

Enzyme and pathway databases

BioCycEcoCyc:NAGE-MONOMER.
ECOL316407:JW0665-MONOMER.

Gene expression databases

GenevestigatorP09323.

Family and domain databases

Gene3D3.30.1360.60. 1 hit.
InterProIPR011055. Dup_hybrid_motif.
IPR018113. PTrfase_EIIB/Cys_phosph_CS.
IPR001127. PTS_EIIA_1_perm.
IPR001996. PTS_EIIB_1.
IPR003352. PTS_EIIC.
IPR013013. PTS_EIIC_1.
IPR011535. PTS_Glc-like_IIB_component.
IPR010974. PTS_IIBC_nag.
[Graphical view]
PfamPF00358. PTS_EIIA_1. 1 hit.
PF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
SUPFAMSSF51261. Dup_hybrid_motif. 1 hit.
SSF55604. PTS_EIIB. 1 hit.
TIGRFAMsTIGR00826. EIIB_glc. 1 hit.
TIGR00830. PTBA. 1 hit.
TIGR01998. PTS-II-BC-nag. 1 hit.
PROSITEPS51093. PTS_EIIA_TYPE_1. 1 hit.
PS00371. PTS_EIIA_TYPE_1_HIS. 1 hit.
PS51098. PTS_EIIB_TYPE_1. 1 hit.
PS01035. PTS_EIIB_TYPE_1_CYS. 1 hit.
PS51103. PTS_EIIC_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTW3C_ECOLI
AccessionPrimary (citable) accession number: P09323
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 1, 2013
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families