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UniProtKB/Swiss-Prot entry P00550


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

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Entry information
Entry name PTM3C_ECOLI
Primary accession number P00550
Secondary accession number Q2M7R2
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    October 14, 2008 (Entry version 108)
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: b3599, JW3573
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6309813 [NCBI, ExPASy, EBI, Israel, Japan]
Lee C.A., Saier M.H. Jr.;
"Mannitol-specific enzyme II of the bacterial phosphotransferase system. III. The nucleotide sequence of the permease gene.";
J. Biol. Chem. 258:10761-10767(1983).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1093/nar/22.13.2576; PubMed=8041620 [NCBI, ExPASy, EBI, Israel, Japan]
Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes.";
Nucleic Acids Res. 22:2576-2586(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 619-637.
STRAIN=K12;
PubMed=3135464 [NCBI, ExPASy, EBI, Israel, Japan]
Davis T., Yamada M., Elgort M., Saier M.H. Jr.;
"Nucleotide sequence of the mannitol (mtl) operon in Escherichia coli.";
Mol. Microbiol. 2:405-412(1988).
[6]
PHOSPHORYLATION AT HIS-554.
DOI=10.1021/bi00416a002; PubMed=3142516 [NCBI, ExPASy, EBI, Israel, Japan]
Pas H.H., Robillard G.T.;
"S-phosphocysteine and phosphohistidine are intermediates in the phosphoenolpyruvate-dependent mannitol transport catalyzed by Escherichia coli EIIMtl.";
Biochemistry 27:5835-5839(1988).
[7]
TOPOLOGY.
PubMed=1946374 [NCBI, ExPASy, EBI, Israel, Japan]
Sugiyama J.E., Mahmoodian S., Jacobson G.R.;
"Membrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusions.";
Proc. Natl. Acad. Sci. U.S.A. 88:9603-9607(1991).
[8]
SUBCELLULAR LOCATION.
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.1109730; PubMed=15919996 [NCBI, ExPASy, EBI, Israel, Japan]
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane proteome.";
Science 308:1321-1323(2005).
[9]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 490-637.
DOI=10.1016/S0969-2126(98)00039-2; PubMed=9551558 [NCBI, ExPASy, EBI, Israel, Japan]
van Montfort R.L.M., Pijning T., Kalk K.H., Hangyi I., Kouwijzer M.L.C.E., Robillard G.T., Dijkstra B.W.;
"The structure of the Escherichia coli phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active site.";
Structure 6:377-388(1998).
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.
  • 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.
  • SUBUNIT: Homodimer.
  • INTERACTION:
    P0A6F5:groL; NbExp=1; IntAct=EBI-547239, EBI-543750;
  • SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
  • 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-554 and Cys-384.
  • 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
V01503; CAA24748.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00039; AAB18576.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76623.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77694.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X06794; CAA29953.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A00661; WQEC2M.
RefSeq AP_004193.1; -.
NP_418056.1; -.
3D structure databases
PDB
1A3A; X-ray; 1.80 A; A/B/C/D=491-637.[ExPASy / RCSB / EBI]
1J6T; NMR; -; A=491-637.[ExPASy / RCSB / EBI]
1VKR; NMR; -; A=366-489.[ExPASy / RCSB / EBI]
1VRV; NMR; -; A=375-475.[ExPASy / RCSB / EBI]
2FEW; NMR; -; A=491-637, B=375-475.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A3A; -.
1J6T; -.
1VKR; -.
1VRV; -.
2FEW; -.
ModBase P00550.
Protein-protein interaction databases
DIP DIP:10267N; -.
IntAct P00550; -.
Enzyme and pathway databases
BioCyc EcoCyc:MTLA-MON; -.
Organism-specific databases
EchoBASE EB0610; -.
EcoGene EG10615; mtlA.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
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.
IPR004718; PTS_IIC_mtl.
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]
TIGRFAMs TIGR00851; mtlA; 1.
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 P00550.
ProtoNet P00550.
Genome annotation databases
GeneID 948118; -.
GenomeReviews U00096_GR; b3599.
AP009048_GR; JW3573.
KEGG ecj:JW3573; -.
eco:b3599; -.
Phylogenomic databases
HOGENOM P00550; -.
Other
LinkHub P00550; -.
Genome annotation databases
CMR P00550; b3599.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell inner membrane; 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   637  637     PTS system mannitol-specific EIICBA component. PRO_0000186614
TOPO_DOM   1    24  24     Cytoplasmic (Potential). 
TRANSMEM   25    44  20     Probable. 
TOPO_DOM   45    50  6     Periplasmic (Potential). 
TRANSMEM   51    69  19     Probable. 
TOPO_DOM   70   134  65     Cytoplasmic (Potential). 
TRANSMEM   135   154  20     Probable. 
TOPO_DOM   155   165  11     Periplasmic (Potential). 
TRANSMEM   166   184  19     Probable. 
TOPO_DOM   185   273  89     Cytoplasmic (Potential). 
TRANSMEM   274   291  18     Probable. 
TOPO_DOM   292   313  22     Periplasmic (Potential). 
TRANSMEM   314   333  20     Probable. 
TOPO_DOM   334   637  304     Cytoplasmic (Probable). 
DOMAIN   12   341  330     PTS EIIC type-2. 
DOMAIN   378   473  96     PTS EIIB type-2. 
DOMAIN   494   636  143     PTS EIIA type-2. 
ACT_SITE   384   384        Phosphocysteine intermediate; for EIIB activity. 
ACT_SITE   554   554        Tele-phosphohistidine intermediate; for EIIA activity. 
STRAND   379   389  11      
HELIX   390   404  15      
STRAND   410   416  7      
STRAND   425   430  6      
HELIX   431   440  10      
STRAND   444   450  7      
HELIX   455   470  16      
HELIX   498   500  3      
HELIX   510   523  14      
HELIX   530   541  12      
STRAND   545   547  3      
HELIX   557   562  6      
STRAND   563   565  3      
STRAND   567   578  12      
STRAND   580   582  3      
STRAND   586   594  9      
TURN   597   599  3      
HELIX   600   610  11      
HELIX   614   622  9      
HELIX   626   632  7      
TURN   633   635  3      
Sequence information
Length: 637 AA [This is the length of the unprocessed precursor] Molecular weight: 67972 Da [This is the MW of the unprocessed precursor] CRC64: A992992D534BF98D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSDIKIKVQ SFGRFLSNMV MPNIGAFIAW GIITALFIPT GWLPNETLAK LVGPMITYLL 

        70         80         90        100        110        120 
PLLIGYTGGK LVGGERGGVV GAITTMGVIV GADMPMFLGS MIAGPLGGWC IKHFDRWVDG 

       130        140        150        160        170        180 
KIKSGFEMLV NNFSAGIIGM ILAILAFLGI GPIVEALSKM LAAGVNFMVV HDMLPLASIF 

       190        200        210        220        230        240 
VEPAKILFLN NAINHGIFSP LGIQQSHELG KSIFFLIEAN PGPGMGVLLA YMFFGRGSAK 

       250        260        270        280        290        300 
QSAGGAAIIH FLGGIHEIYF PYVLMNPRLI LAVILGGMTG VFTLTILGGG LVSPASPGSI 

       310        320        330        340        350        360 
LAVLAMTPKG AYFANIAGVC AAMAVSFVVS AILLKTSKVK EEDDIEAATR RMQDMKAESK 

       370        380        390        400        410        420 
GASPLSAGDV TNDLSHVRKI IVACDAGMGS SAMGAGVLRK KIQDAGLSQI SVTNSAINNL 

       430        440        450        460        470        480 
PPDVDLVITH RDLTERAMRQ VPQAQHISLT NFLDSGLYTS LTERLVAAQR HTANEEKVKD 

       490        500        510        520        530        540 
SLKDSFDDSS ANLFKLGAEN IFLGRKAATK EEAIRFAGEQ LVKGGYVEPE YVQAMLDREK 

       550        560        570        580        590        600 
LTPTYLGESI AVPHGTVEAK DRVLKTGVVF CQYPEGVRFG EEEDDIARLV IGIAARNNEH 

       610        620        630 
IQVITSLTNA LDDESVIERL AHTTSVDEVL ELLAGRK 

P00550 in FASTA format

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