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Protein

PTS system mannose-specific EIIAB component

Gene

manX

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

[Protein]-N(pi)-phospho-L-histidine + D-mannose(Side 1) = [protein]-L-histidine + D-mannose 6-phosphate(Side 2).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101Tele-phosphohistidine intermediate; for EIIA activityPROSITE-ProRule annotation
Active sitei175 – 1751Pros-phosphohistidine intermediate; for EIIB activityBy similarity

GO - Molecular functioni

  • kinase activity Source: EcoCyc
  • protein-N(PI)-phosphohistidine-mannose phosphotransferase system transporter activity Source: EcoCyc

GO - Biological processi

  • glucose import into cell Source: EcoCyc
  • mannose transport Source: EcoCyc
  • phosphoenolpyruvate-dependent sugar phosphotransferase system Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Phosphotransferase system, Sugar transport, Transport

Enzyme and pathway databases

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

Protein family/group databases

TCDBi4.A.6.1.1. the pts mannose-fructose-sorbose (man) family.

Names & Taxonomyi

Protein namesi
Recommended name:
PTS system mannose-specific EIIAB component
Alternative name(s):
EIIAB-Man
Including the following 2 domains:
Mannose-specific phosphotransferase enzyme IIA component
Alternative name(s):
EIII-Man
PTS system mannose-specific EIIA component
Mannose-specific phosphotransferase enzyme IIB component (EC:2.7.1.191)
Alternative name(s):
PTS system mannose-specific EIIB component
Gene namesi
Name:manX
Synonyms:gptB, ptsL
Ordered Locus Names:b1817, JW1806
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10567. manX.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoCyc
  • cytosol Source: UniProtKB
  • integral component of plasma membrane Source: EcoCyc
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 323322PTS system mannose-specific EIIAB componentPRO_0000186653Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551N6-acetyllysine1 Publication
Modified residuei234 – 2341N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP69797.
PaxDbiP69797.
PRIDEiP69797.

2D gel databases

SWISS-2DPAGEP69797.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
cytRP0ACN72EBI-554089,EBI-1125696

Protein-protein interaction databases

BioGridi4259144. 308 interactions.
DIPiDIP-35846N.
IntActiP69797. 14 interactions.
MINTiMINT-1228428.
STRINGi511145.b1817.

Structurei

Secondary structure

1
323
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Helixi13 – 2513Combined sources
Beta strandi29 – 346Combined sources
Helixi42 – 5312Combined sources
Beta strandi62 – 687Combined sources
Helixi72 – 8110Combined sources
Beta strandi87 – 926Combined sources
Helixi95 – 10511Combined sources
Helixi111 – 12414Combined sources
Beta strandi163 – 1708Combined sources
Helixi178 – 1858Combined sources
Beta strandi189 – 1946Combined sources
Helixi196 – 1994Combined sources
Helixi202 – 2109Combined sources
Beta strandi217 – 2215Combined sources
Helixi223 – 2308Combined sources
Helixi233 – 2353Combined sources
Beta strandi239 – 2468Combined sources
Helixi247 – 2559Combined sources
Beta strandi261 – 2677Combined sources
Beta strandi274 – 2763Combined sources
Beta strandi278 – 2803Combined sources
Helixi285 – 29612Combined sources
Beta strandi300 – 3034Combined sources
Helixi314 – 3196Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PDOX-ray1.70A2-133[»]
1VRCNMR-A/B1-133[»]
1VSQNMR-A/B2-134[»]
C159-323[»]
2JZHNMR-A154-323[»]
2JZNNMR-A/B2-134[»]
C159-323[»]
2JZONMR-A/B2-134[»]
D159-323[»]
ProteinModelPortaliP69797.
SMRiP69797. Positions 2-130, 159-323.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69797.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 124123PTS EIIA type-4PROSITE-ProRule annotationAdd
BLAST
Domaini157 – 320164PTS EIIB type-4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni137 – 15519HingeAdd
BLAST

Domaini

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 similaritiesi

Contains 1 PTS EIIA type-4 domain.PROSITE-ProRule annotation
Contains 1 PTS EIIB type-4 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105DAS. Bacteria.
COG2893. LUCA.
COG3444. LUCA.
HOGENOMiHOG000140047.
InParanoidiP69797.
KOiK02793.
K02794.
OMAiWTKESRV.
OrthoDBiEOG6FJNGT.
PhylomeDBiP69797.

Family and domain databases

Gene3Di3.40.35.10. 1 hit.
3.40.50.510. 1 hit.
InterProiIPR013789. PTS_EIIA_man.
IPR004701. PTS_EIIA_man-typ.
IPR004720. PTS_IIB_sorbose-sp.
IPR018455. PTS_IIB_sorbose-sp_subgr.
[Graphical view]
PfamiPF03610. EIIA-man. 1 hit.
PF03830. PTSIIB_sorb. 1 hit.
[Graphical view]
SUPFAMiSSF52728. SSF52728. 1 hit.
SSF53062. SSF53062. 1 hit.
TIGRFAMsiTIGR00824. EIIA-man. 1 hit.
TIGR00854. pts-sorbose. 1 hit.
PROSITEiPS51096. PTS_EIIA_TYPE_4. 1 hit.
PS51101. PTS_EIIB_TYPE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P69797-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIAIVIGTH GWAAEQLLKT AEMLLGEQEN VGWIDFVPGE NAETLIEKYN
60 70 80 90 100
AQLAKLDTTK GVLFLVDTWG GSPFNAASRI VVDKEHYEVI AGVNIPMLVE
110 120 130 140 150
TLMARDDDPS FDELVALAVE TGREGVKALK AKPVEKAAPA PAAAAPKAAP
160 170 180 190 200
TPAKPMGPND YMVIGLARID DRLIHGQVAT RWTKETNVSR IIVVSDEVAA
210 220 230 240 250
DTVRKTLLTQ VAPPGVTAHV VDVAKMIRVY NNPKYAGERV MLLFTNPTDV
260 270 280 290 300
ERLVEGGVKI TSVNVGGMAF RQGKTQVNNA VSVDEKDIEA FKKLNARGIE
310 320
LEVRKVSTDP KLKMMDLISK IDK
Length:323
Mass (Da):35,048
Last modified:January 23, 2007 - v2
Checksum:iA446B79421B8C040
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 2322TIAIV…KTAEM → GWGCRAGCLKRQKW in AAA24110 (Ref. 1) CuratedAdd
BLAST
Sequence conflicti35 – 351D → N in AAA24110 (Ref. 1) Curated
Sequence conflicti101 – 1011T → R in AAA24110 (Ref. 1) Curated
Sequence conflicti142 – 1421A → G in AAA24110 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36404 Genomic DNA. Translation: AAA24110.1.
J02699 Genomic DNA. Translation: AAA24443.1.
U00096 Genomic DNA. Translation: AAC74887.1.
AP009048 Genomic DNA. Translation: BAA15624.1.
PIRiA30286. WQECM3.
RefSeqiNP_416331.1. NC_000913.3.
WP_000150543.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74887; AAC74887; b1817.
BAA15624; BAA15624; BAA15624.
GeneIDi946334.
KEGGiecj:JW1806.
eco:b1817.
PATRICi32118953. VBIEscCol129921_1894.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36404 Genomic DNA. Translation: AAA24110.1.
J02699 Genomic DNA. Translation: AAA24443.1.
U00096 Genomic DNA. Translation: AAC74887.1.
AP009048 Genomic DNA. Translation: BAA15624.1.
PIRiA30286. WQECM3.
RefSeqiNP_416331.1. NC_000913.3.
WP_000150543.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PDOX-ray1.70A2-133[»]
1VRCNMR-A/B1-133[»]
1VSQNMR-A/B2-134[»]
C159-323[»]
2JZHNMR-A154-323[»]
2JZNNMR-A/B2-134[»]
C159-323[»]
2JZONMR-A/B2-134[»]
D159-323[»]
ProteinModelPortaliP69797.
SMRiP69797. Positions 2-130, 159-323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259144. 308 interactions.
DIPiDIP-35846N.
IntActiP69797. 14 interactions.
MINTiMINT-1228428.
STRINGi511145.b1817.

Protein family/group databases

TCDBi4.A.6.1.1. the pts mannose-fructose-sorbose (man) family.

2D gel databases

SWISS-2DPAGEP69797.

Proteomic databases

EPDiP69797.
PaxDbiP69797.
PRIDEiP69797.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74887; AAC74887; b1817.
BAA15624; BAA15624; BAA15624.
GeneIDi946334.
KEGGiecj:JW1806.
eco:b1817.
PATRICi32118953. VBIEscCol129921_1894.

Organism-specific databases

EchoBASEiEB0562.
EcoGeneiEG10567. manX.

Phylogenomic databases

eggNOGiENOG4105DAS. Bacteria.
COG2893. LUCA.
COG3444. LUCA.
HOGENOMiHOG000140047.
InParanoidiP69797.
KOiK02793.
K02794.
OMAiWTKESRV.
OrthoDBiEOG6FJNGT.
PhylomeDBiP69797.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP69797.
PROiP69797.

Family and domain databases

Gene3Di3.40.35.10. 1 hit.
3.40.50.510. 1 hit.
InterProiIPR013789. PTS_EIIA_man.
IPR004701. PTS_EIIA_man-typ.
IPR004720. PTS_IIB_sorbose-sp.
IPR018455. PTS_IIB_sorbose-sp_subgr.
[Graphical view]
PfamiPF03610. EIIA-man. 1 hit.
PF03830. PTSIIB_sorb. 1 hit.
[Graphical view]
SUPFAMiSSF52728. SSF52728. 1 hit.
SSF53062. SSF53062. 1 hit.
TIGRFAMsiTIGR00824. EIIA-man. 1 hit.
TIGR00854. pts-sorbose. 1 hit.
PROSITEiPS51096. PTS_EIIA_TYPE_4. 1 hit.
PS51101. PTS_EIIB_TYPE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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], FUNCTION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. 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. 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, IDENTIFICATION BY 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.

Entry informationi

Entry nameiPTNAB_ECOLI
AccessioniPrimary (citable) accession number: P69797
Secondary accession number(s): P08186, Q47350
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.