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Q46072 (PTN3B_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 92. 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 mannose-specific EIIBCA component
Alternative name(s):
EII-Man/EIII-Man
EIIBCA-Man

Including the following 3 domains:

  1. Mannose-specific phosphotransferase enzyme IIB component
    EC=2.7.1.69
    Alternative name(s):
    PTS system mannose-specific EIIB component
  2. Mannose permease IIC component
    Alternative name(s):
    PTS system mannose-specific EIIC component
  3. Mannose-specific phosphotransferase enzyme IIA component
    EC=2.7.1.-
    Alternative name(s):
    PTS system mannose-specific EIIA component
Gene names
Name:ptsM
Synonyms:ptsG
Ordered Locus Names:Cgl1360, cg1537
OrganismCorynebacterium glutamicum (Brevibacterium flavum)
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length683 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 mannose 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 membrane; Multi-pass membrane protein Probable.

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.

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

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 – 683683PTS system mannose-specific EIIBCA component
PRO_0000186645

Regions

Transmembrane126 – 14621Helical; Potential
Transmembrane162 – 18221Helical; Potential
Transmembrane193 – 21321Helical; Potential
Transmembrane225 – 24521Helical; Potential
Transmembrane260 – 28021Helical; Potential
Transmembrane303 – 32321Helical; Potential
Transmembrane344 – 36421Helical; Potential
Transmembrane376 – 39621Helical; Potential
Transmembrane409 – 42921Helical; Potential
Transmembrane442 – 46221Helical; Potential
Domain1 – 8989PTS EIIB type-1
Domain117 – 476360PTS EIIC type-1
Domain550 – 654105PTS EIIA type-1

Sites

Active site281Phosphocysteine intermediate; for EIIB activity By similarity
Active site6021Tele-phosphohistidine intermediate; for EIIA activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q46072 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0B42CAEC60828075

FASTA68372,571
        10         20         30         40         50         60 
MASKLTTTSQ HILENLGGPD NITSMTHCAT RLRFQVKDQS IVDQQEIDSD PSVLGVVPQG 

        70         80         90        100        110        120 
STGMQVVMGG SVANYYQEIL KLDGMKHFAD GEATESSSKK EYGGVRGKYS WIDYAFEFLS 

       130        140        150        160        170        180 
DTFRPILWAL LGASLIITLL VLADTFGLQD FRAPMDEQPD TYVFLHSMWR SVFYFLPIMV 

       190        200        210        220        230        240 
GATAARKLGA NEWIGAAIPA ALLTPEFLAL GSAGDTVTVF GLPMVLNDYS GQVFPPLIAA 

       250        260        270        280        290        300 
IGLYWVEKGL KKIIPEAVQM VFVPFFSLLI MIPATAFLLG PFGIGVGNGI SNLLEAINNF 

       310        320        330        340        350        360 
SPFILSIVIP LLYPFLVPLG LHWPLNAIMI QNINTLGYDF IQGPMGAWNF ACFGLVTGVF 

       370        380        390        400        410        420 
LLSIKERNKA MRQVSLGGML AGLLGGISEP SLYGVLLRFK KTYFRLLPGC LAGGIVMGIF 

       430        440        450        460        470        480 
DIKAYAFVFT SLLTIPAMDP WLGYTIGIAV AFFVSMFLVL ALDYRSNEER DEARAKVAAD 

       490        500        510        520        530        540 
KQAEEDLKAE ANATPAAPVA AAGAGAGAGA GAAAGAATAV AAKPKLAAGE VVDIVSPLEG 

       550        560        570        580        590        600 
KAIPLSEVPD PIFAAGKLGP GIAIQPTGNT VVAPADATVI LVQKSGHAVA LRLDSGVEIL 

       610        620        630        640        650        660 
VHVGLDTVQL GGEGFTVHVE RRQQVKAGDP LITFDADFIR SKDLPLITPV VVSNAAKFGE 

       670        680 
IEGIPADQAN SSTTVIKVNG KNE 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the gene encoding the Corynebacterium glutamicum mannose enzyme II and analyses of the deduced protein sequence."
Lee J.K., Sung M.H., Yoon K.H., Yu J.H., Oh T.K.
FEMS Microbiol. Lett. 119:137-145(1994) [PubMed: 8039653] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L18874 Genomic DNA. Translation: AAA53546.1.
BA000036 Genomic DNA. Translation: BAB98753.1.
BX927152 Genomic DNA. Translation: CAF21369.1.
RefSeqNP_600576.1. NC_003450.3.
YP_225645.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ46072.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1019335.
3344282.
GenomeReviewsGene locus Cgl1360 in contig BA000036_GR.
Gene locus cg1537 in contig BX927147_GR.
KEGGcgb:cg1537.
cgl:NCgl1305.
PATRIC21494755. VBICorGlu203724_1327.

Phylogenomic databases

HOGENOMHBG673521.
OMAANEWIGA.
PhylomeDBQ46072.
ProtClustDBCLSK633359.

Enzyme and pathway databases

BioCycCGLU196627:CG1537-MONOMER.

Family and domain databases

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.
[Graphical view]
Gene3DG3DSA:3.30.1360.60. PTS_EIIB. 1 hit.
KOK02755.
K02756.
K02757.
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.
TIGRFAMsTIGR00830. PTBA. 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 namePTN3B_CORGL
AccessionPrimary (citable) accession number: Q46072
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: November 1, 1996
Last modified: January 25, 2012
This is version 92 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