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UniProtKB/Swiss-Prot entry P28008


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

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Entry information
Entry name PTMCB_STACA
Primary accession number P28008
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on February 1, 1996 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 69)
Name and origin of the protein
Protein name PTS system mannitol-specific EIICB component
Synonyms EIICB-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)
Gene name
Name: mtlA
From
Staphylococcus carnosus [TaxID: 1281] 
Taxonomy Bacteria; Firmicutes; Bacillales; Staphylococcus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1551396 [NCBI, ExPASy, EBI, Israel, Japan]
Fischer R., Hengstenberg W.;
"Mannitol-specific enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus carnosus. Sequence and expression in Escherichia coli and structural comparison with the enzyme IImannitol of Escherichia coli.";
Eur. J. Biochem. 204:963-969(1992).
[2]
SEQUENCE REVISION.
Hengstenberg W.;
Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
[3]
ACTIVE SITE CYS-432.
PubMed=7588734 [NCBI, ExPASy, EBI, Israel, Japan]
Pogge von Strandmann R., Weigt C., Fischer R., Meyer H.E., Kalbitzer H.R., Hengstenberg W.;
"Expression, purification and characterization of the enzyme II mannitol-specific domain from Staphylococcus carnosus and determination of the active-site cysteine residue.";
Eur. J. Biochem. 233:116-122(1995).
Comments
  • FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant 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: Homodimer.
  • SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein (Potential).
  • INDUCTION: By mannitol.
  • 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.
  • 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
X56333; CAA39769.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S68193; S22385.
3D structure databases
ModBase P28008.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005886; Cellular component: plasma membrane (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 IPR013011; PTS_EIIB_2.
IPR003352; PTS_EIIC.
IPR013014; PTS_EIIC_2.
IPR003501; PTS_IIB_lac.
IPR004718; PTS_IIC_mtl.
Graphical view of domain structure.
Pfam PF02378; PTS_EIIC; 1.
PF02302; PTS_IIB; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00851; mtlA; 1.
PROSITE PS51099; PTS_EIIB_TYPE_2; 1.
PS51104; PTS_EIIC_TYPE_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P28008.
ProtoNet P28008.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Membrane; Phosphoprotein; 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   518  518     PTS system mannitol-specific EIICB component. PRO_0000186626
TRANSMEM   26    46  21     Potential. 
TRANSMEM   56    76  21     Potential. 
TRANSMEM   96   116  21     Potential. 
TRANSMEM   142   162  21     Potential. 
TRANSMEM   169   189  21     Potential. 
TRANSMEM   222   242  21     Potential. 
TRANSMEM   276   296  21     Potential. 
TRANSMEM   322   342  21     Potential. 
DOMAIN   20   352  333     PTS EIIC type-2. 
DOMAIN   426   518  93     PTS EIIB type-2. 
ACT_SITE   432   432        Phosphocysteine intermediate. 
Sequence information
Length: 518 AA [This is the length of the unprocessed precursor] Molecular weight: 55686 Da [This is the MW of the unprocessed precursor] CRC64: A0DE0B9E4BA74FA5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDTMSNSQQN KGIGRKVQAF GSFLSSMIMP NIGAFIAWGF IAAIFIDNGW FPNKDLAQLA 

        70         80         90        100        110        120 
GPMITYLIPL LIAFSGGRLI HDLRGGIIAA TATMGVIVAL PDTPMLLGAM IMGPLVGWLM 

       130        140        150        160        170        180 
KKTDEFVQPR TPQGFEMLFN NFSAGILGFI MTIFGFEVLA PIMKFIMHIL SVGVEALVHA 

       190        200        210        220        230        240 
HLLPLVSILV EPAKIVFLNN AINHGVFTPL GADQAAHAGQ SILYTIESNP GPGIGVLIAY 

       250        260        270        280        290        300 
MIFGKGTAKA TSYGAGIIQF FGGIHEIYFP YVLMRPLLFV SVILGGMTGV ATYSLLDFGF 

       310        320        330        340        350        360 
KTPASPGSII VYAINAPKGE FLHMLTGVVL AALVSFVVSA LILKFTKDPK QDLAEATAQM 

       370        380        390        400        410        420 
EATKGKKSSV ASKLSAKDDN KAADNKTAET TTATAASNKA EDKDSDELLD DYNTEDVDAH 

       430        440        450        460        470        480 
NYNNVDHVIF ACDAGMGSSA MGASMLRNKF KNAGLENIQV TNTAINQLPK NAQLVITQKK 

       490        500        510 
LTDRAIKQSP DAIHISVENF LNSPRYEELI NNLKEDQD 

P28008 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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