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Q89A36 (PTM3C_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 65. 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:bbp_517
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length640 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 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.

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-556 and Cys-385 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 640640PTS system mannitol-specific EIICBA component
PRO_0000186613

Regions

Transmembrane18 – 3821Helical; Potential
Transmembrane52 – 7221Helical; Potential
Transmembrane83 – 10321Helical; Potential
Transmembrane134 – 15421Helical; Potential
Transmembrane161 – 18121Helical; Potential
Transmembrane186 – 20621Helical; Potential
Transmembrane213 – 23321Helical; Potential
Transmembrane269 – 28921Helical; Potential
Transmembrane313 – 33321Helical; Potential
Domain12 – 343332PTS EIIC type-2
Domain379 – 47597PTS EIIB type-2
Domain496 – 638143PTS EIIA type-2

Sites

Active site3851Phosphocysteine intermediate; for EIIB activity By similarity
Active site5561Tele-phosphohistidine intermediate; for EIIA activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89A36 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: A5B76D06E6909C3B

FASTA64070,759
        10         20         30         40         50         60 
MSVPMTVKVQ NLGRFLSAMI MPNISVFIAW GIISGLFIKS GWCPNQTLEK VLSPISVYLF 

        70         80         90        100        110        120 
PILIANTGGY LINGKRGAIV GSIAVVGAII STAIPMLLGA MIIGPIGGWI TYYFDKISKY 

       130        140        150        160        170        180 
KVKSGFEMLV NNFSVGILGV LLLFISFLCI GPMIEKLSCF LGYVVNLMIN NHLLPFIAIL 

       190        200        210        220        230        240 
IEPAKIFFLN NVINHGVLFP LGIQEVVKFN KSIFFLIESN PGPGIGVLMA WFFFGCDNIK 

       250        260        270        280        290        300 
KSLKEAIVIQ LFGGIHEIYF PYVLKNPRLI LALILGSITG IFILIVLRGG LISAASPGSI 

       310        320        330        340        350        360 
ISILAMTPKG LYVINLLAII ISFLVSFLVS CMLLKISNRN HYVKGSNTKI EKDNFLINSS 

       370        380        390        400        410        420 
FQKNRTCIKS SLDSHKCIRN IIFACDAGMG SSAVAAGILR NKIHDLNIFN ITVSNAAIDS 

       430        440        450        460        470        480 
IPNFGVDLII THYSLTDRAR KRNSNAKHLS LNSFLDNAFY NELSKYLVEN NLDNNSSILD 

       490        500        510        520        530        540 
FSVRNQNNFS SKKNVFSLTK ENIFLGQIAS SKEEVIRFIG RQLVNQGYVK EEYIEAMLER 

       550        560        570        580        590        600 
EKMMSTWLGE SIALPHGTIQ SKDFILNTGI IFCQFPNGIL FGDDPEDIAH LVIGVAARNN 

       610        620        630        640 
EHIPVVSNIT NILDNNDVIK SLSITKNIDD VLYLFSRKNI

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016826 Genomic DNA. Translation: AAO27220.1.
RefSeqNP_778115.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89A36.
SMRQ89A36. Positions 496-638.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBUCT00000002612; EBBUCP00000002436; EBBUCG00000002612.
GeneID1058455.
GenomeReviewsGene locus bbp_517 in contig AE016826_GR.
KEGGbab:bbp517.
PATRIC21245853. VBIBucAph80364_0512.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000008060.
HOGENOMHBG296680.
OMANEMGDIT.

Enzyme and pathway databases

BioCycBAPH224915:BBP_517-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.
[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.
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_BUCBP
AccessionPrimary (citable) accession number: Q89A36
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 65 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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