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UniProtKB/Swiss-Prot entry P69797


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

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Entry information
Entry name PTNAB_ECOLI
Primary accession number P69797
Secondary accession numbers P08186 Q47350
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 47)
Name and origin of the protein
Protein name PTS system mannose-specific EIIAB component
Synonym EIIAB-Man
Includes Mannose-specific phosphotransferase enzyme IIA component
     (EC 2.7.1.-)
     (PTS system mannose-specific EIIA component)
     (EIII-Man)
Mannose-specific phosphotransferase enzyme IIB component
     (EC 2.7.1.69)
     (PTS system mannose-specific EIIB component)
Gene name
Name: manX
Synonyms: gptB, ptsL
OrderedLocusNames: b1817, JW1806
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].
STRAIN=K12;
Saris P.E.J., Liljestroem P., Palva E.T.;
"Nucleotide sequence of manX(ptsL) encoding the enzyme III(Man) (II-A(Man)) function in the phosphotransferase system of Escherichia coli K-12.";
FEMS Microbiol. Lett. 49:69-73(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2951378 [NCBI, ExPASy, EBI, Israel, Japan]
Erni B., Zanolari B., Kocher H.P.;
"The mannose permease of Escherichia coli consists of three different proteins. Amino acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage lambda DNA.";
J. Biol. Chem. 262:5238-5247(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.6.379; PubMed=9097040 [NCBI, ExPASy, EBI, Israel, Japan]
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.;
"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map.";
DNA Res. 3:379-392(1996).
[4]
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).
[5]
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).
[6]
PROTEIN SEQUENCE OF 2-13.
STRAIN=K12 / EMG2;
DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[7]
SUBCELLULAR LOCATION.
STRAIN=BL21-DE3;
DOI=10.1074/jbc.M506479200; PubMed=16079137 [NCBI, ExPASy, EBI, Israel, Japan]
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.;
"Protein complexes of the Escherichia coli cell envelope.";
J. Biol. Chem. 280:34409-34419(2005).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55 AND LYS-234, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M800187-MCP200; PubMed=18723842 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved modification in E. coli.";
Mol. Cell. Proteomics 0:0-0(2008).
[9]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-134.
DOI=10.1006/jmbi.1996.0335; PubMed=8676384 [NCBI, ExPASy, EBI, Israel, Japan]
Nunn R.S., Markovic-Housley Z., Genovesio-Taverne J.-C., Fluekiger K., Rizkallah P.J., Jansonius J.N., Schirmer T., Erni B.;
"Structure of the IIA domain of the mannose transporter from Escherichia coli at 1.7-A resolution.";
J. Mol. Biol. 259:502-511(1996).
[10]
STRUCTURE BY NMR OF 1-121.
DOI=10.1016/0014-5793(94)80138-X; PubMed=8131846 [NCBI, ExPASy, EBI, Israel, Japan]
Markovic-Housley Z., Balbach J., Stolz B., Genovesio-Taverne J.-C.;
"Predicted topology of the N-terminal domain of the hydrophilic subunit of the mannose transporter of Escherichia coli.";
FEBS Lett. 340:202-206(1994).
[11]
STRUCTURE BY NMR OF 156-323.
DOI=10.1016/S0014-5793(97)00084-7; PubMed=9074635 [NCBI, ExPASy, EBI, Israel, Japan]
Gschwind R.M., Gemmecker G., Leutner M., Kessler H., Gutknecht R., Lanz R., Fluekiger K., Erni B.;
"Secondary structure of the IIB domain of the Escherichia coli mannose transporter, a new fold in the class of alpha/beta twisted open-sheet structures.";
FEBS Lett. 404:45-50(1997).
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 mannose 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.
  • INTERACTION:
    P0ACN7:cytR; NbExp=1; IntAct=EBI-554089, EBI-1125696;
  • SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral membrane protein.
  • DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.
  • 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 EIIA type-4 domain.
  • SIMILARITY: Contains 1 PTS EIIB type-4 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
M36404; AAA24110.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J02699; AAA24443.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74887.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15624.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A30286; WQECM3.
RefSeq AP_002436.1; -.
NP_416331.1; -.
3D structure databases
PDB
1PDO; X-ray; 1.70 A; A=1-133.[ExPASy / RCSB / EBI]
1VRC; NMR; -; A/B=1-133.[ExPASy / RCSB / EBI]
1VSQ; NMR; -; A/B=2-134, C=159-323.[ExPASy / RCSB / EBI]
2JZH; NMR; -; A=154-323.[ExPASy / RCSB / EBI]
2JZN; NMR; -; A/B=2-134, C=159-323.[ExPASy / RCSB / EBI]
2JZO; NMR; -; A/B=2-134, D=159-323.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1PDO; -.
1VRC; -.
1VSQ; -.
2JZH; -.
2JZN; -.
2JZO; -.
ModBase P69797.
Protein-protein interaction databases
IntAct P69797; -.
Enzyme and pathway databases
BioCyc EcoCyc:MANX-MON; -.
2D gel databases
SWISS-2DPAGE P69797; -.
Organism-specific databases
EchoBASE EB0562; -.
EcoGene EG10567; manX.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
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:0016301; Molecular function: kinase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
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 UniProtKB-KW).
GO:0009401; Biological process: phosphoenolpyruvate-dependent sugar phosphotransferase system (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR004701; PTS_EIIA_fruc.
IPR013789; PTS_EIIA_fruc_sub.
IPR004720; PTS_IIB_sorb.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.510; PTS_EIIA_fruc; 1.
G3DSA:3.40.35.10; PTS_IIB_sorb; 1.
Pfam PF03610; EIIA-man; 1.
PF03830; PTSIIB_sorb; 1.
Pfam graphical view of domain structure.
ProDom PD008332; PTSIIB_sorb; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00824; EIIA-man; 1.
TIGR00854; pts-sorbose; 1.
PROSITE PS51096; PTS_EIIA_TYPE_4; 1.
PS51101; PTS_EIIB_TYPE_4; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P69797.
Genome annotation databases
GeneID 946334; -.
GenomeReviews U00096_GR; b1817.
AP009048_GR; JW1806.
KEGG ecj:JW1806; -.
eco:b1817; -.
Phylogenomic databases
HOGENOM P69797; -.
Other
LinkHub P69797; -.
Genome annotation databases
CMR P69797; b1817.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; Membrane; Phosphotransferase system; Sugar transport; Transferase; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   323  322     PTS system mannose-specific EIIAB component. PRO_0000186653
DOMAIN   2   124  123     PTS EIIA type-4. 
DOMAIN   157   320  164     PTS EIIB type-4. 
REGION   137   155  19     Hinge. 
ACT_SITE   10    10        Tele-phosphohistidine intermediate; for EIIA activity (By similarity). 
ACT_SITE   175   175        Pros-phosphohistidine intermediate; for EIIB activity (By similarity). 
MOD_RES   55    55        N6-acetyllysine. 
MOD_RES   234   234        N6-acetyllysine. 
CONFLICT   2    23        TIAIVIGTHGWAAEQLLKTAEM -> GWGCRAGCLKRQKW (in Ref. 1; AAA24110). 
CONFLICT   35    35        D -> N (in Ref. 1; AAA24110). 
CONFLICT   101   101        T -> R (in Ref. 1; AAA24110). 
CONFLICT   142   142        A -> G (in Ref. 1; AAA24110). 
STRAND   4     8  5      
HELIX   13    25  13      
STRAND   29    34  6      
HELIX   42    53  12      
STRAND   62    68  7      
HELIX   72    81  10      
STRAND   87    92  6      
HELIX   95   105  11      
HELIX   111   124  14      
STRAND   163   170  8      
HELIX   178   185  8      
STRAND   189   194  6      
HELIX   196   199  4      
HELIX   202   210  9      
STRAND   217   221  5      
HELIX   223   230  8      
HELIX   233   235  3      
STRAND   239   246  8      
HELIX   247   255  9      
STRAND   261   267  7      
STRAND   274   276  3      
STRAND   278   280  3      
HELIX   285   296  12      
STRAND   300   303  4      
HELIX   314   319  6      
Sequence information
Length: 323 AA [This is the length of the unprocessed precursor] Molecular weight: 35048 Da [This is the MW of the unprocessed precursor] CRC64: A446B79421B8C040 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTIAIVIGTH GWAAEQLLKT AEMLLGEQEN VGWIDFVPGE NAETLIEKYN AQLAKLDTTK 

        70         80         90        100        110        120 
GVLFLVDTWG GSPFNAASRI VVDKEHYEVI AGVNIPMLVE TLMARDDDPS FDELVALAVE 

       130        140        150        160        170        180 
TGREGVKALK AKPVEKAAPA PAAAAPKAAP TPAKPMGPND YMVIGLARID DRLIHGQVAT 

       190        200        210        220        230        240 
RWTKETNVSR IIVVSDEVAA DTVRKTLLTQ VAPPGVTAHV VDVAKMIRVY NNPKYAGERV 

       250        260        270        280        290        300 
MLLFTNPTDV ERLVEGGVKI TSVNVGGMAF RQGKTQVNNA VSVDEKDIEA FKKLNARGIE 

       310        320 
LEVRKVSTDP KLKMMDLISK IDK 

P69797 in FASTA format

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