Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q4L9Y1 (PTMCB_STAHJ)

Last modified June 16, 2009. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    PTS system mannitol-specific EIICB component
Alternative name(s):
    EIICB-Mtl
      Short name=EII-Mtl
Including the following 2 domains:
    1- Recommended name:
            Mannitol permease IIC component
        Alternative name(s):
            PTS system mannitol-specific EIIC component
    2- Recommended name:
            Mannitol-specific phosphotransferase enzyme IIB component
              EC=2.7.1.69
        Alternative name(s):
            PTS system mannitol-specific EIIB component
Gene names
Name: mtlA
Ordered Locus Names: SH0235
OrganismStaphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]
Taxonomic identifier279808 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein Potential.

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-2 domain.

Contains 1 PTS EIIC type-2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 519519PTS system mannitol-specific EIICB component
PRO_0000186627

Regions

Transmembrane25 – 4521 Potential
Transmembrane55 – 7521 Potential
Transmembrane95 – 11521 Potential
Transmembrane145 – 16521 Potential
Transmembrane168 – 18821 Potential
Transmembrane221 – 24121 Potential
Transmembrane250 – 27223 Potential
Transmembrane277 – 29923 Potential
Transmembrane321 – 34121 Potential
Domain19 – 351333PTS EIIC type-2
Domain425 – 51995PTS EIIB type-2

Sites

Active site4311Phosphocysteine intermediate; for EIIB activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4L9Y1-1 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: A74770C9BEB765A2

FASTA51955,663
        10         20         30         40         50         60 
MAQTETQEKK GLGRKVQAFG SFLSSMIMPN IGAFIAWGFI AAIFIDNGWY PNKELSQLAG 

        70         80         90        100        110        120 
PMITYLIPLL IAFSGGRLIH DLRGGIVAAT ATMGVIVALP DTPMLLGAMI MGPLVGWLMK 

       130        140        150        160        170        180 
KVDQFLQPRT PQGFEMLFNN FSAGILAFIM TILGFKLLAP IMQFIMHILS VAVEFLVHLH 

       190        200        210        220        230        240 
LLPIVSIIVE PAKILFLNNA INHGVFTPLG TDQAASAGQS ILFAIESNPG PGIGILLAYM 

       250        260        270        280        290        300 
IFGKGTAKAT SYGAGIIHFF GGIHEIYFPY VLMRPLLFIA VILGGMTGVA TYQATGFGFK 

       310        320        330        340        350        360 
SPASPGSFIV YCLNAPKGEF LHMVLGVFLA ALVSFVVAAL IMKFTKEPKQ DLEAATAKME 

       370        380        390        400        410        420 
STKGKKSSVS SKLTGATTGT GAAGVAANKA NGEDQNEASS EDEEEDLLDN YNTEDVDAHD 

       430        440        450        460        470        480 
YSNVDHVIFA CDAGMGSSAM GASMLRNKFK KAGISDVNVT NTAINQLPNN AQLVITQKTL 

       490        500        510 
TDRAIKQVPN AIHISVDNFL NSPRYEELLN NLKKDQDKA 

« Hide

References

[1]"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
J. Bacteriol. 187:7292-7308(2005) [PubMed: 16237012] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AP006716 Genomic DNA. Translation: BAE03544.1.
RefSeqYP_252150.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3482069.
GenomeReviewsGene locus SH0235 in contig AP006716_GR.
KEGGsha:SH0235.
NMPDRfig|279808.3.peg.248.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ4L9Y1.
OMAQ4L9Y1. ITHKDLT.

Enzyme and pathway databases

BioCycSHAE279808:SH0235-MON.

Family and domain databases

InterProIPR013011. PTS_EIIB_2.
IPR003352. PTS_EIIC.
IPR013014. PTS_EIIC_2.
IPR003501. PTS_IIB_lac.
IPR004718. PTS_IIC_mtl.
[Graphical view]
PfamPF02378. PTS_EIIC. 1 hit.
PF02302. PTS_IIB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00851. mtlA. 1 hit.
PROSITEPS51099. PTS_EIIB_TYPE_2. 1 hit.
PS51104. PTS_EIIC_TYPE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTMCB_STAHJ
AccessionPrimary (citable) accession number: Q4L9Y1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: August 2, 2005
Last modified: June 16, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents