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P45604 (PTW3C_KLEPN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismKlebsiella pneumoniae
Taxonomic identifier573 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella

Protein attributes

Sequence length651 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

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 – 651651PTS system N-acetylglucosamine-specific EIICBA component
PRO_0000186476

Regions

Transmembrane16 – 3621Helical; Potential
Transmembrane40 – 6021Helical; Potential
Transmembrane70 – 9021Helical; Potential
Transmembrane92 – 11221Helical; Potential
Transmembrane132 – 15221Helical; Potential
Transmembrane165 – 18521Helical; Potential
Transmembrane192 – 21221Helical; Potential
Transmembrane232 – 25221Helical; Potential
Transmembrane264 – 28421Helical; Potential
Transmembrane285 – 30521Helical; Potential
Transmembrane308 – 32821Helical; Potential
Transmembrane339 – 35921Helical; Potential
Domain1 – 371371PTS EIIC type-1
Domain390 – 47283PTS EIIB type-1
Domain519 – 623105PTS EIIA type-1

Sites

Active site4121Phosphocysteine intermediate; for EIIB activity By similarity
Active site5711Tele-phosphohistidine intermediate; for EIIA activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P45604 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 3D8D8ADFF4BD48ED

FASTA65168,180
        10         20         30         40         50         60 
MNILGFFQRL GRALQLPIAV LPVAALLLRF GQPDLLNVPF IAQAGGAIFD NLALIFAIGV 

        70         80         90        100        110        120 
ASSWSKDNAG SAALAGAVGY FVMTKAMVTI NPEINMGVLA GIITGLVAGA VYNRWAGIKL 

       130        140        150        160        170        180 
PDFLSFFGGK RFVPIATGFF CLILAAIFGY VWPPVQHAIH SGGEWIVSAG ALGSGIFGFI 

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

       250        260        270        280        290        300 
LPGAALAMYL AAPKARRPMV GGMLLSVAIT AFLTGVTEPL EFLFLFLAPL LYLLHAVLTG 

       310        320        330        340        350        360 
ISLFIATALG IHAGFSFSAG AIDYVLMYSL PAASKNVWML LVMGVVFFFV YFLLFSAVIR 

       370        380        390        400        410        420 
MFNLKTPGRE DKAADVVTEE ANSNTEEGLT QLATSYIAAV GGTDNLKAID ACITRLRLTV 

       430        440        450        460        470        480 
GDSAKVNDAA CKRLGASGVV KLNKQTIQVI VGAKAESIGD EMKKVVTRGP VAAAAAAPAG 

       490        500        510        520        530        540 
NVATAAPAAK PQAVANAKTV ESLVSPITGD VVALEQVPDE AFASKAVGDG IAVKPTDNIV 

       550        560        570        580        590        600 
VAPAAGTVVK IFNTNHAFCL ETNNGAEIVV HMGIDTVALE GKGFKRLVEE GTDVKAGEPI 

       610        620        630        640        650 
LEMDLDFLNA NARSMISPVV CSNSDDYSAL VILASGKVVA GQTPLYEIKG K

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References

[1]"Comparison of the sequences of the nagE operons from Klebsiella pneumoniae and Escherichia coli K12: enhanced variability of the enzyme IIN-acetylglucosamine in regions connecting functional domains."
Vogler A.P., Lengeler J.W.
Mol. Gen. Genet. 230:270-276(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 1033-5P14 / KAY2026.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X63289 Genomic DNA. Translation: CAA44923.1.
PIRS18607.

3D structure databases

ProteinModelPortalP45604.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_KLEPN
AccessionPrimary (citable) accession number: P45604
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 3, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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