Skip Header

Contribute Send feedback
Read comments (?) or add your own

P50976 (PTLCB_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PTS system lactose-specific EIICB component
Alternative name(s):
EIICB-Lac
Short name=EII-Lac

Including the following 2 domains:

  1. Lactose permease IIC component
    Alternative name(s):
    PTS system lactose-specific EIIC component
  2. Lactose-specific phosphotransferase enzyme IIB component
    EC=2.7.1.69
    Alternative name(s):
    PTS system lactose-specific EIIB component
Gene names
Name:lacE
Ordered Locus Names:SMU_1491
OrganismStreptococcus mutans [Complete proteome] [HAMAP]
Taxonomic identifier1309 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length568 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 lactose transport.

Catalytic activity

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

Subcellular location

Cell membrane; Multi-pass membrane protein Probable.

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-3 domain.

Contains 1 PTS EIIC type-3 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 568568PTS system lactose-specific EIICB component
PRO_0000186595

Regions

Transmembrane30 – 5021Helical; Potential
Transmembrane65 – 8521Helical; Potential
Transmembrane103 – 12321Helical; Potential
Transmembrane128 – 14821Helical; Potential
Transmembrane183 – 20321Helical; Potential
Transmembrane222 – 24221Helical; Potential
Transmembrane246 – 26621Helical; Potential
Transmembrane283 – 30321Helical; Potential
Transmembrane339 – 35921Helical; Potential
Transmembrane381 – 40121Helical; Potential
Domain8 – 409402PTS EIIC type-3
Domain465 – 568104PTS EIIB type-3

Sites

Active site4721Phosphocysteine intermediate; for EIIB activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P50976 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: A129FDD14282EAAE

FASTA56861,420
        10         20         30         40         50         60 
MNTLIAQIEK GKPFFEKISR NIYLRAIRDG FISAMPVILF SSIFLLIAYV PNIFGFTWPK 

        70         80         90        100        110        120 
GIENMLMTPY NYTMGIIGFL VAGTTAKSLT DSMNRQLEKT NQINFISTML ASMAGFLIMA 

       130        140        150        160        170        180 
ADPAKEGGFL SAFMGTKGLL TAFIAAFITV NVYKICVKNN VTIRMPEEVP PNISQVFKDI 

       190        200        210        220        230        240 
FPFAFSIIIL YAIQLAIKAV IGVNVAQSIG TLLAPLFSAA DGYLGITIIF GAYALFWFVG 

       250        260        270        280        290        300 
IHGPSIVEPA IAAITYSNVE LNAHLIHAGQ HADKVITSGT QMFIVTMGGT GATLVVPFMF 

       310        320        330        340        350        360 
MWLCKSKRNK AIGRASVVPT FFGVNEPILF GAPIVLNPVF FIPFILAPIV NVWIFKFFVD 

       370        380        390        400        410        420 
TLGMNSFFAN LPWTTPGPIG IVLGTGFAVL SFVLAALLIL VDTVIYYPFV KVYDEQILAE 

       430        440        450        460        470        480 
EAEGKSSSDA LKEKVAANFD TKKADAILEG AESKEEPATH AITEETNVLV LCAGGGTSGL 

       490        500        510        520        530        540 
LANALNKAAE EYGAPVKAAA GSYGAHREIL DQYQLVILAP QVASNYEDMK AETDKLGIKL 

       550        560 
AKTEGAQYIG LTRDGKGALA FVEEQFKD

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide and deduced amino acid sequences of the lacR, lacABCD, and lacFE genes encoding the repressor, tagatose 6-phosphate gene cluster, and sugar-specific phosphotransferase system components of the lactose operon of Streptococcus mutans."
Rosey E.L., Stewart G.C.
J. Bacteriol. 174:6159-6170(1992) [PubMed: 1400164] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 700611 / UA130 / Serotype c.
[2]"Isolation, characterization and nucleotide sequence of the Streptococcus mutans lactose-specific enzyme II (lacE) gene of the PTS and the phospho-beta-galactosidase (lacG) gene."
Honeyman A.L., Curtiss R. III
J. Gen. Microbiol. 139:2685-2694(1993) [PubMed: 8277252] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 700611 / UA130 / Serotype c.
[3]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed: 12397186] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159 / Serotype c.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L18993 Unassigned DNA. Translation: AAA16449.1.
AE014133 Genomic DNA. Translation: AAN59145.1.
RefSeqNP_721839.1. NC_004350.2.

3D structure databases

ProteinModelPortalP50976.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000013759; EBSTRP00000013241; EBSTRG00000013759.
GeneID1028733.
GenomeReviewsGene locus SMU_1491 in contig AE014133_GR.
KEGGsmu:SMU_1491.
NMPDRfig|210007.1.peg.1352.
PATRIC19664997. VBIStrMut61772_1327.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000026586.
HOGENOMHBG337916.
OMAWSKDIEN.
ProtClustDBCLSK877288.

Enzyme and pathway databases

BioCycSMUT210007:SMU_1491-MONOMER.

Family and domain databases

InterProIPR014350. PTrfase_system_EIIB_3_subgr.
IPR003501. PTS_EIIB_2/3.
IPR013012. PTS_EIIB_3.
IPR003352. PTS_EIIC.
IPR004501. PTS_IIC_lac.
IPR004801. PTS_IIC_lac_spec.
[Graphical view]
KOK02787.
K02788.
PfamPF02378. PTS_EIIC. 1 hit.
PF02302. PTS_IIB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00394. Lac_pts_IIC. 1 hit.
TIGR00410. LacE. 1 hit.
TIGR00853. Pts-lac. 1 hit.
PROSITEPS51100. PTS_EIIB_TYPE_3. 1 hit.
PS51105. PTS_EIIC_TYPE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTLCB_STRMU
AccessionPrimary (citable) accession number: P50976
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 25, 2012
This is version 90 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents