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Q9CLY8 (PTM3C_PASMU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. 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 mannitol-specific EIICBA component
Alternative name(s):
EIICBA-Mtl
Short name=EII-Mtl

Including the following 3 domains:

  1. Mannitol permease IIC component
    Alternative name(s):
    PTS system mannitol-specific EIIC component
  2. Mannitol-specific phosphotransferase enzyme IIB component
    EC=2.7.1.69
    Alternative name(s):
    PTS system mannitol-specific EIIB component
  3. Mannitol-specific phosphotransferase enzyme IIA component
    EC=2.7.1.-
    Alternative name(s):
    PTS system mannitol-specific EIIA component
Gene names
Name:mtlA
Ordered Locus Names:PM1061
OrganismPasteurella multocida (strain Pm70) [Complete proteome] [HAMAP]
Taxonomic identifier272843 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Pasteurella

Protein attributes

Sequence length624 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.

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

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

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.

The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.

Post-translational modification

An intramolecular phosphotransfer takes places between His-542 and Cys-378 By similarity.

Sequence similarities

Contains 1 PTS EIIA type-2 domain.

Contains 1 PTS EIIB type-2 domain.

Contains 1 PTS EIIC type-2 domain.

Sequence caution

The sequence AAK03145.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 624624PTS system mannitol-specific EIICBA component
PRO_0000186616

Regions

Transmembrane25 – 4521Helical; Potential
Transmembrane53 – 7321Helical; Potential
Transmembrane79 – 9921Helical; Potential
Transmembrane134 – 15421Helical; Potential
Transmembrane214 – 23421Helical; Potential
Transmembrane246 – 26621Helical; Potential
Transmembrane270 – 29021Helical; Potential
Transmembrane313 – 33321Helical; Potential
Domain13 – 336324PTS EIIC type-2
Domain372 – 46392PTS EIIB type-2
Domain482 – 624143PTS EIIA type-2

Sites

Active site3781Phosphocysteine intermediate; for EIIB activity By similarity
Active site5421Tele-phosphohistidine intermediate; for EIIA activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CLY8 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: EA104312CEE2D891

FASTA62466,550
        10         20         30         40         50         60 
MLSANAKVKV QNFGRFLSNM VMPNIGAFIA WGFITALFIP TGWLPNETLA KLVGPMITYL 

        70         80         90        100        110        120 
LPLLIGYSGG KLIAGERGAV VGAIATAGVI VGTDIPMFLG AMIAGPTGGW AIKRFDKWAD 

       130        140        150        160        170        180 
GKIKSGFEML VNNFSSGIIG MILAILFFWL IGPAVKALST MLAAGVDILV KAHLLPLTSI 

       190        200        210        220        230        240 
FVEPAKILFL NNAINHGIFS PLGIQQSQEF GQSIFFLIEA NPGPGLGVLL AYIIFGKGTA 

       250        260        270        280        290        300 
KQTAGGATII HFFGGIHEIY FPYVLMNPRL LLAVIAGGVS GVFTLVLFNA GLVAPASPGS 

       310        320        330        340        350        360 
IIAVLLMTPQ NAIVGVLASV AIAATVSFVI ASFFLKIQKE ENGHSLEKMQ AASKAMKSGV 

       370        380        390        400        410        420 
QFNTPARYQG VQKIFVACDA GMGSSAMGAS MLRKKVKEAG LAIEVTNCAI NDLPEDAQLV 

       430        440        450        460        470        480 
ITHQDLTLRA KKHTPNAMHF SLNNFLDAHF YDNLVQDLSN TKVADLAKVS TLEPQEAPQT 

       490        500        510        520        530        540 
AFVLTEKQVF LGLKAANKEE AIRFAGERLV ESGFVLPSYV DAMFEREKMV STYLGEGIAV 

       550        560        570        580        590        600 
PHGTIEAKDA VLKTGVVVCQ YPEGVKFNED EEDSIAKLVI GIAAKNNEHL QVVSAITNAL 

       610        620 
DNEDAIRILS ETDDVEKVLA LLKA

« Hide

References

[1]"Complete genomic sequence of Pasteurella multocida Pm70."
May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed: 11248100] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pm70.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE004439 Genomic DNA. Translation: AAK03145.1. Different initiation.
RefSeqNP_245998.1. NC_002663.1.

3D structure databases

ProteinModelPortalQ9CLY8.
SMRQ9CLY8. Positions 371-458, 482-622.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1244408.
GenomeReviewsGene locus PM1061 in contig AE004439_GR.
KEGGpmu:PM1061.
NMPDRfig|272843.1.peg.1061.
PATRIC22871371. VBIPasMul88067_1075.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG296680.
OMAITHKDLT.
ProtClustDBPRK15083.

Enzyme and pathway databases

BioCycPMUL272843:PM1061-MONOMER.

Family and domain databases

InterProIPR016152. PTrfase/Anion_transptr.
IPR002178. PTS_EIIA_2.
IPR013011. PTS_EIIB_2.
IPR003501. PTS_EIIB_2/3.
IPR003352. PTS_EIIC.
IPR013014. PTS_EIIC_2.
IPR004718. PTS_IIC_mtl.
[Graphical view]
Gene3DG3DSA:3.40.930.10. PTS_EIIA_2. 1 hit.
KOK02798.
K02799.
K02800.
PfamPF00359. PTS_EIIA_2. 1 hit.
PF02378. PTS_EIIC. 1 hit.
PF02302. PTS_IIB. 1 hit.
[Graphical view]
SUPFAMSSF55804. PTrfase/Anion_transptr. 1 hit.
TIGRFAMsTIGR00851. MtlA. 1 hit.
PROSITEPS51094. PTS_EIIA_TYPE_2. 1 hit.
PS00372. PTS_EIIA_TYPE_2_HIS. 1 hit.
PS51099. PTS_EIIB_TYPE_2. 1 hit.
PS51104. PTS_EIIC_TYPE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTM3C_PASMU
AccessionPrimary (citable) accession number: Q9CLY8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: January 25, 2012
This is version 82 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

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