ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q89A36


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PTM3C_BUCBP
Primary accession number Q89A36
Secondary accession numbers None
Integrated into Swiss-Prot on November 14, 2003
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 45)
Name and origin of the protein
Protein name PTS system mannitol-specific EIICBA component
Synonyms EIICBA-Mtl
EII-Mtl
Includes Mannitol permease IIC component
     (PTS system mannitol-specific EIIC component)
Mannitol-specific phosphotransferase enzyme IIB component
     (EC 2.7.1.69)
     (PTS system mannitol-specific EIIB component)
Mannitol-specific phosphotransferase enzyme IIA component
     (EC 2.7.1.-)
     (PTS system mannitol-specific EIIA component)
Gene name
Name: mtlA
OrderedLocusNames: bbp_517
From
Buchnera aphidicola subsp. Baizongia pistaciae [TaxID: 135842] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0235981100; PubMed=12522265 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Reductive genome evolution in Buchnera aphidicola.";
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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.
  • CATALYTIC ACTIVITY: 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.
  • DOMAIN: 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.
  • DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.
  • PTM: An intramolecular phosphotransfer takes places between His-556 and Cys-385 (By similarity).
  • SIMILARITY: Contains 1 PTS EIIA type-2 domain.
  • SIMILARITY: Contains 1 PTS EIIB type-2 domain.
  • SIMILARITY: Contains 1 PTS EIIC type-2 domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE016826; AAO27220.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_778115.1; -.
3D structure databases
HSSP P00550; 1J6T. [HSSP ENTRY / PDB]
ModBase Q89A36.
Enzyme and pathway databases
BioCyc BAPH224915:BBP_517-MON; -.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0016301; Molecular function: kinase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0008982; Molecular function: protein-N(PI)-phosphohistidine-sugar phosphotransferase activity (inferred from electronic annotation from InterPro).
GO:0005351; Molecular function: sugar:hydrogen symporter activity (inferred from electronic annotation from InterPro).
GO:0009401; Biological process: phosphoenolpyruvate-dependent sugar phosphotransferase system (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR002178; PTS_EIIA_2.
IPR013011; PTS_EIIB_2.
IPR003352; PTS_EIIC.
IPR013014; PTS_EIIC_2.
IPR003501; PTS_IIB_lac.
Graphical view of domain structure.
Gene3D G3DSA:3.40.930.10; PTS_EIIA_2; 1.
Pfam PF00359; PTS_EIIA_2; 1.
PF02378; PTS_EIIC; 1.
PF02302; PTS_IIB; 1.
Pfam graphical view of domain structure.
ProDom PD001689; PTS_EIIA_2; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS51094; PTS_EIIA_TYPE_2; 1.
PS00372; PTS_EIIA_TYPE_2_HIS; 1.
PS51099; PTS_EIIB_TYPE_2; 1.
PS51104; PTS_EIIC_TYPE_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q89A36.
ProtoNet Q89A36.
Genome annotation databases
GeneID 1058455; -.
GenomeReviews AE016826_GR; bbp_517.
KEGG bab:bbp517; -.
Phylogenomic databases
HOGENOM Q89A36; -.
Genome annotation databases
CMR Q89A36; bbp_517.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Complete proteome; Kinase; Membrane; Phosphotransferase system; Sugar transport; Transferase; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   640  640     PTS system mannitol-specific EIICBA component. PRO_0000186613
TRANSMEM   18    38  21     Potential. 
TRANSMEM   52    72  21     Potential. 
TRANSMEM   83   103  21     Potential. 
TRANSMEM   134   154  21     Potential. 
TRANSMEM   161   181  21     Potential. 
TRANSMEM   186   206  21     Potential. 
TRANSMEM   213   233  21     Potential. 
TRANSMEM   269   289  21     Potential. 
TRANSMEM   313   333  21     Potential. 
DOMAIN   12   343  332     PTS EIIC type-2. 
DOMAIN   379   475  97     PTS EIIB type-2. 
DOMAIN   496   638  143     PTS EIIA type-2. 
ACT_SITE   385   385        Phosphocysteine intermediate; for EIIB activity (By similarity). 
ACT_SITE   556   556        Tele-phosphohistidine intermediate; for EIIA activity (By similarity). 
Sequence information
Length: 640 AA [This is the length of the unprocessed precursor] Molecular weight: 70759 Da [This is the MW of the unprocessed precursor] CRC64: A5B76D06E6909C3B [This is a checksum on the sequence]
        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 

Q89A36 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!