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Reviewed, UniProtKB/Swiss-Prot Q8K911 (PTM3C_BUCAP)

Last modified June 16, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 EIICBA component
Alternative name(s):
    EIICBA-Mtl
      Short name=EII-Mtl
Including the following 3 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
    3- Recommended name:
            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: BUsg_552
OrganismBuchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]
Taxonomic identifier98794 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length649 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 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-563 and Cys-386 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 – 649649PTS system mannitol-specific EIICBA component
PRO_0000186612

Regions

Transmembrane20 – 4021 Potential
Transmembrane47 – 6721 Potential
Transmembrane94 – 11421 Potential
Transmembrane134 – 15421 Potential
Transmembrane161 – 18121 Potential
Transmembrane214 – 23421 Potential
Transmembrane245 – 26521 Potential
Transmembrane267 – 28721 Potential
Transmembrane291 – 31121 Potential
Transmembrane316 – 33621 Potential
Domain12 – 340329PTS EIIC type-2
Domain380 – 47293PTS EIIB type-2
Domain503 – 645143PTS EIIA type-2

Sites

Active site3861Phosphocysteine intermediate; for EIIB activity By similarity
Active site5631Tele-phosphohistidine intermediate; for EIIA activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K911-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: B365CE4719C986C0

FASTA64972,358
        10         20         30         40         50         60 
MFRLITLKIQ NFGQFLSNMI MPNISIFITW GIMNSLFLSL DWQYNKIFAQ LISPIIFYLL 

        70         80         90        100        110        120 
PILIGYTGGS LIAGQRGGLL GSITTIGMIT STDMPMFLGG MVAGPLGGWI IKGFDQIIKN 

       130        140        150        160        170        180 
RIKSGFEMLV NNFSIAIIGI FLTIFSFFFI GPFIEGVSKF LGCLIKIIID FNLLPLIAFI 

       190        200        210        220        230        240 
IEPAKVFFLN NAINHGIFSP LGIQEISENK SSLFFLIESN PGPGLGILIA CFFFGKEKSY 

       250        260        270        280        290        300 
KSSGTAAIVQ FLGGIHEIYF SYVLIKPILM ISLILGSMTS IFMLVFFKGG LIAAVSPGSI 

       310        320        330        340        350        360 
LSILAMTKKG LYFANLISIF SSFLISFLSA MLFFKINLGQ KIKNDKSSIQ LFKNNLFPIK 

       370        380        390        400        410        420 
KIGDEKYDFI KKIKNFQKIK NIIIACDAGM GSSAMGASIL RKKIKSNNLT HIYVSNIAIN 

       430        440        450        460        470        480 
LLPKNADLVI THEKLTYLAK KRAPDAQHIS LTNFLDSNFY TSLVKQLDLN KDFFKKNNIQ 

       490        500        510        520        530        540 
DKKDRITQIN IDSHKEIQSK CFFQISDKNI FLNQYAENKK EAIKIVGKHL VAQGYVKKDY 

       550        560        570        580        590        600 
IDAMLDREKI ASTWLGESVA LPHGTIKSKD SILKTGVIFC QFPKGVHFGE TIDDIAYLVI 

       610        620        630        640 
GIAAKNNEHI MVVSNITNAL DDKDVISKLS KTKSVKEVLS YLNVNVKKN 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE013218 Genomic DNA. Translation: AAM68090.1.
RefSeqNP_660879.1.

3D structure databases

HSSPHSSP built from PDB template 1A3A based on UniProtKB P00550.
ModBaseSearch...

Genome annotation databases

GeneID1005638.
GenomeReviewsGene locus BUsg_552 in contig AE013218_GR.
KEGGbas:BUsg552.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8K911.
OMAQ8K911. ITHKDLT.

Enzyme and pathway databases

BioCycBAPH198804:BUSG552-MON.

Family and domain databases

InterProIPR002178. PTS_EIIA_2.
IPR013011. PTS_EIIB_2.
IPR003352. PTS_EIIC.
IPR013014. PTS_EIIC_2.
IPR003501. PTS_IIB_lac.
[Graphical view]
Gene3DG3DSA:3.40.930.10. PTS_EIIA_2. 1 hit.
PfamPF00359. PTS_EIIA_2. 1 hit.
PF02378. PTS_EIIC. 1 hit.
PF02302. PTS_IIB. 1 hit.
[Graphical view]
ProDomPD001689. PTS_EIIA_2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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_BUCAP
AccessionPrimary (citable) accession number: Q8K911
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 1, 2002
Last modified: June 16, 2009
This is version 57 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

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