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Q02420 (PTMA_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 90. 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:
Mannitol-specific phosphotransferase enzyme IIA component

EC=2.7.1.-
Alternative name(s):
EIIA-Mtl
EIII-Mtl
PTS system mannitol-specific EIIA component
Gene names
Name:mtlF
Synonyms:mtlA2
Ordered Locus Names:SMU_1183
OrganismStreptococcus mutans serotype c (strain ATCC 700610 / UA159) [Complete proteome] [HAMAP]
Taxonomic identifier210007 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length145 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 mannitol transport By similarity.

Catalytic activity

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

Subunit structure

Homotrimer.

Subcellular location

Cytoplasm Potential.

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-2 domain.

Ontologies

Keywords
   Biological processPhosphotransferase system
Sugar transport
Transport
   Cellular componentCytoplasm
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionkinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

sugar:hydrogen symporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 145145Mannitol-specific phosphotransferase enzyme IIA component
PRO_0000186644

Regions

Domain1 – 144144PTS EIIA type-2

Sites

Active site611Tele-phosphohistidine intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q02420 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 684973EEE46409C3

FASTA14515,878
        10         20         30         40         50         60 
MEFQKDLIKL NQHFPDKEAA IRFCGQLLAD GGYVEPAYID AMIQRDKELS VYMGNFIAIP 

        70         80         90        100        110        120 
HGTDDAKKDV LKSGITVVQV PDGVNFGTED DPQVATVLFG IAGIGDEHLQ IIQNISIFCA 

       130        140 
DVDNVVKLAD AQTEDEVVKL LSQVN 

« Hide

References

« Hide 'large scale' references
[1]"Isolation, characterization, and nucleotide sequence of the Streptococcus mutans mannitol-phosphate dehydrogenase gene and the mannitol-specific factor III gene of the phosphoenolpyruvate phosphotransferase system."
Honeyman A.L., Curtiss R. III
Infect. Immun. 60:3369-3375(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 700611 / UA130 / Serotype c.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF210133 Genomic DNA. Translation: AAA26941.1.
AE014133 Genomic DNA. Translation: AAN58873.1.
PIRB44798.
RefSeqNP_721567.1. NC_004350.2.

3D structure databases

ProteinModelPortalQ02420.
ModBaseSearch...

Protein-protein interaction databases

STRING210007.SMU.1183.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN58873; AAN58873; SMU_1183.
GeneID1028483.
KEGGsmu:SMU_1183.
PATRIC19664457. VBIStrMut61772_1061.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4668.
KOK02798.
OMAINQNFSN.
ProtClustDBCLSK696971.

Family and domain databases

Gene3D3.40.930.10. 1 hit.
InterProIPR016152. PTrfase/Anion_transptr.
IPR002178. PTS_EIIA_2.
[Graphical view]
PfamPF00359. PTS_EIIA_2. 1 hit.
[Graphical view]
SUPFAMSSF55804. PTrfase/Anion_transptr. 1 hit.
PROSITEPS51094. PTS_EIIA_TYPE_2. 1 hit.
PS00372. PTS_EIIA_TYPE_2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTMA_STRMU
AccessionPrimary (citable) accession number: Q02420
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 1, 2013
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