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P69797 (PTNAB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PTS system mannose-specific EIIAB component
Alternative name(s):
EIIAB-Man

Including the following 2 domains:

  1. Mannose-specific phosphotransferase enzyme IIA component
    EC=2.7.1.-
    Alternative name(s):
    EIII-Man
    PTS system mannose-specific EIIA component
  2. Mannose-specific phosphotransferase enzyme IIB component
    EC=2.7.1.69
    Alternative name(s):
    PTS system mannose-specific EIIB component
Gene names
Name:manX
Synonyms:gptB, ptsL
Ordered Locus Names:b1817, JW1806
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 mannose transport.

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

Cytoplasm. Cell inner membrane; Peripheral membrane protein Ref.7.

Domain

The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB 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.

Sequence similarities

Contains 1 PTS EIIA type-4 domain.

Contains 1 PTS EIIB type-4 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

cytRP0ACN72EBI-554089,EBI-1125696

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 323322PTS system mannose-specific EIIAB component
PRO_0000186653

Regions

Domain2 – 124123PTS EIIA type-4
Domain157 – 320164PTS EIIB type-4
Region137 – 15519Hinge

Sites

Active site101Tele-phosphohistidine intermediate; for EIIA activity By similarity
Active site1751Pros-phosphohistidine intermediate; for EIIB activity By similarity

Amino acid modifications

Modified residue551N6-acetyllysine Ref.8
Modified residue2341N6-acetyllysine Ref.8

Experimental info

Sequence conflict2 – 2322TIAIV…KTAEM → GWGCRAGCLKRQKW in AAA24110. Ref.1
Sequence conflict351D → N in AAA24110. Ref.1
Sequence conflict1011T → R in AAA24110. Ref.1
Sequence conflict1421A → G in AAA24110. Ref.1

Secondary structure

1 .................................................. 323
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P69797 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A446B79421B8C040

FASTA32335,048
        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

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of manX(ptsL) encoding the enzyme III(Man) (II-A(Man)) function in the phosphotransferase system of Escherichia coli K-12."
Saris P.E.J., Liljestroem P., Palva E.T.
FEMS Microbiol. Lett. 49:69-73(1988)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"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."
Erni B., Zanolari B., Kocher H.P.
J. Biol. Chem. 262:5238-5247(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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."
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. expand/collapse author list , 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.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13.
Strain: K12 / EMG2.
[7]"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: BL21-DE3.
[8]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55 AND LYS-234, MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[9]"Structure of the IIA domain of the mannose transporter from Escherichia coli at 1.7-A resolution."
Nunn R.S., Markovic-Housley Z., Genovesio-Taverne J.-C., Fluekiger K., Rizkallah P.J., Jansonius J.N., Schirmer T., Erni B.
J. Mol. Biol. 259:502-511(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-134.
[10]"Predicted topology of the N-terminal domain of the hydrophilic subunit of the mannose transporter of Escherichia coli."
Markovic-Housley Z., Balbach J., Stolz B., Genovesio-Taverne J.-C.
FEBS Lett. 340:202-206(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-121.
[11]"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."
Gschwind R.M., Gemmecker G., Leutner M., Kessler H., Gutknecht R., Lanz R., Fluekiger K., Erni B.
FEBS Lett. 404:45-50(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 156-323.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M36404 Genomic DNA. Translation: AAA24110.1.
J02699 Genomic DNA. Translation: AAA24443.1.
U00096 Genomic DNA. Translation: AAC74887.1.
AP009048 Genomic DNA. Translation: BAA15624.1.
PIRWQECM3. A30286.
RefSeqNP_416331.1. NC_000913.2.
YP_490078.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PDOX-ray1.70A2-133[»]
1VRCNMR-A/B2-132[»]
1VSQNMR-A/B2-134[»]
C159-323[»]
2JZHNMR-A154-323[»]
2JZNNMR-A/B2-134[»]
C159-323[»]
2JZONMR-A/B2-134[»]
D159-323[»]
ProteinModelPortalP69797.
SMRP69797. Positions 2-130, 159-323.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-35846N.
IntActP69797. 12 interactions.
MINTMINT-1228428.
STRING511145.b1817.

Protein family/group databases

TCDB4.A.6.1.1. PTS mannose-fructose-sorbose (Man) family.

PTM databases

PhosSiteP0809410.

2D gel databases

SWISS-2DPAGEP69797.

Proteomic databases

PaxDbP69797.
PRIDEP69797.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74887; AAC74887; b1817.
BAA15624; BAA15624; BAA15624.
GeneID12930150.
946334.
KEGGecj:Y75_p1792.
eco:b1817.
PATRIC32118953. VBIEscCol129921_1894.

Organism-specific databases

EchoBASEEB0562.
EcoGeneEG10567. manX.

Phylogenomic databases

eggNOGCOG3444.
HOGENOMHOG000140047.
KOK02793.
K02794.
OMATTEMLIG.
ProtClustDBPRK15088.

Enzyme and pathway databases

BioCycEcoCyc:MANX-MONOMER.
ECOL316407:JW1806-MONOMER.
MetaCyc:MANX-MONOMER.

Gene expression databases

GenevestigatorP69797.

Family and domain databases

Gene3D3.40.35.10. 1 hit.
3.40.50.510. 1 hit.
InterProIPR004701. PTS_EIIA_fruc.
IPR013789. PTS_EIIA_fruc_subgr.
IPR004720. PTS_IIB_sorbose-sp.
IPR018455. PTS_IIB_sorbose-sp_subgr.
[Graphical view]
PfamPF03610. EIIA-man. 1 hit.
PF03830. PTSIIB_sorb. 1 hit.
[Graphical view]
SUPFAMSSF53062. PTS_EIIA_fruc. 1 hit.
SSF52728. PTS_IIB_sorb. 1 hit.
TIGRFAMsTIGR00824. EIIA-man. 1 hit.
TIGR00854. pts-sorbose. 1 hit.
PROSITEPS51096. PTS_EIIA_TYPE_4. 1 hit.
PS51101. PTS_EIIB_TYPE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP69797.

Entry information

Entry namePTNAB_ECOLI
AccessionPrimary (citable) accession number: P69797
Secondary accession number(s): P08186, Q47350
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents