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P19642 (PTOCB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 130. 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 maltose- and glucose-specific EIICB component

Including the following 2 domains:

  1. Maltose and glucose permease IIC component
    Alternative name(s):
    PTS system maltose- and glucose-specific EIIC component
  2. Maltose- and glucose-specific phosphotransferase enzyme IIB component
    EC=2.7.1.69
    Alternative name(s):
    PTS system maltose- and glucose-specific EIIB component
Gene names
Name:malX
Ordered Locus Names:b1621, JW1613
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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 maltose and glucose transport.

MalX encodes a phosphotransferase system enzyme II that can recognize glucose and maltose as substrates even though these sugars may not represent the natural substrates of the system.

Catalytic activity

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.

Sequence similarities

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 – 530530PTS system maltose- and glucose-specific EIICB component
PRO_0000186657

Regions

Transmembrane22 – 4221Helical; Potential
Transmembrane69 – 8921Helical; Potential
Transmembrane96 – 11621Helical; Potential
Transmembrane138 – 15821Helical; Potential
Transmembrane189 – 20921Helical; Potential
Transmembrane289 – 30921Helical; Potential
Transmembrane321 – 34121Helical; Potential
Transmembrane343 – 36321Helical; Potential
Transmembrane369 – 38921Helical; Potential
Transmembrane399 – 41921Helical; Potential
Domain1 – 431431PTS EIIC type-1
Domain449 – 53082PTS EIIB type-1

Sites

Active site4711Phosphocysteine intermediate; for EIIB activity By similarity

Experimental info

Sequence conflict1441I → Y in AAA24098. Ref.1
Sequence conflict2961P → N in AAA24098. Ref.1
Sequence conflict4321E → R in AAA24098. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P19642 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: 042E9817955975BF

FASTA53056,627
        10         20         30         40         50         60 
MTAKTAPKVT LWEFFQQLGK TFMLPVALLS FCGIMLGIGS SLSSHDVITL IPVLGNPVLQ 

        70         80         90        100        110        120 
AIFTWMSKIG SFAFSFLPVM FCIAIPLGLA RENKGVAAFA GFIGYAVMNL AVNFWLTNKG 

       130        140        150        160        170        180 
ILPTTDAAVL KANNIQSILG IQSIDTGILG AVIAGIIVWM LHERFHNIRL PDALAFFGGT 

       190        200        210        220        230        240 
RFVPIISSLV MGLVGLVIPL VWPIFAMGIS GLGHMINSAG DFGPMLFGTG ERLLLPFGLH 

       250        260        270        280        290        300 
HILVALIRFT DAGGTQEVCG QTVSGALTIF QAQLSCPTTH GFSESATRFL SQGKMPAFLG 

       310        320        330        340        350        360 
GLPGAALAMY HCARPENRHK IKGLLISGLI ACVVGGTTEP LEFLFLFVAP VLYVIHALLT 

       370        380        390        400        410        420 
GLGFTVMSVL GVTIGNTDGN IIDFVVFGIL HGLSTKWYMV PVVAAIWFVV YYVIFRFAIT 

       430        440        450        460        470        480 
RFNLKTPGRD SEVASSIEKA VAGAPGKSGY NVPAILEALG GADNIVSLDN CITRLRLSVK 

       490        500        510        520        530 
DMSLVNVQAL KDNRAIGVVQ LNQHNLQVVI GPQVQSVKDE MAGLMHTVQA 

« Hide

References

« Hide 'large scale' references
[1]"The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltose and an enzyme abolishing the endogenous induction of the maltose system."
Reidl J., Boos W.
J. Bacteriol. 173:4862-4876(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"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.
[4]"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.
[5]"MalI, a novel protein involved in regulation of the maltose system of Escherichia coli, is highly homologous to the repressor proteins GalR, CytR, and LacI."
Reidl J., Roemisch K., Ehrmann M., Boos W.
J. Bacteriol. 171:4888-4899(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-177.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60722 mRNA. Translation: AAA24098.1.
U00096 Genomic DNA. Translation: AAC74693.1.
AP009048 Genomic DNA. Translation: BAA15372.1.
M28539 Genomic DNA. Translation: AAA24103.2. Sequence problems.
PIRG64918.
RefSeqNP_416138.1. NC_000913.2.
YP_489884.1. NC_007779.1.

3D structure databases

ProteinModelPortalP19642.
SMRP19642. Positions 453-521.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-10150N.
IntActP19642. 1 interaction.
MINTMINT-1239961.
STRING511145.b1621.

Protein family/group databases

TCDB4.A.1.1.3. PTS glucose-glucoside (Glc) family.

Proteomic databases

PRIDEP19642.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74693; AAC74693; b1621.
BAA15372; BAA15372; BAA15372.
GeneID12932134.
946009.
KEGGecj:Y75_p1597.
eco:b1621.
PATRIC32118544. VBIEscCol129921_1692.

Organism-specific databases

EchoBASEEB0558.
EcoGeneEG10563. malX.

Phylogenomic databases

eggNOGCOG1263.
HOGENOMHOG000250995.
KOK02790.
K02791.
OMAMSKVGSF.
ProtClustDBPRK10110.

Enzyme and pathway databases

BioCycEcoCyc:MALX-MONOMER.
ECOL316407:JW1613-MONOMER.

Gene expression databases

GenevestigatorP19642.

Family and domain databases

Gene3D3.30.1360.60. 1 hit.
InterProIPR018113. PTrfase_EIIB/Cys_phosph_CS.
IPR004719. PTrfase_sys_maltose/Glc-sp_IIC.
IPR001996. PTS_EIIB_1.
IPR003352. PTS_EIIC.
IPR013013. PTS_EIIC_1.
IPR011535. PTS_Glc-like_IIB_component.
IPR011301. PTS_Mal/Glc-sp_IIBC_component.
[Graphical view]
PfamPF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
SUPFAMSSF55604. PTS_EIIB. 1 hit.
TIGRFAMsTIGR00826. EIIB_glc. 1 hit.
TIGR00852. pts-Glc. 1 hit.
TIGR02004. PTS-IIBC-malX. 1 hit.
PROSITEPS51098. 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 namePTOCB_ECOLI
AccessionPrimary (citable) accession number: P19642
Secondary accession number(s): P77621
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 1, 1997
Last modified: May 1, 2013
This is version 130 of the entry and version 3 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