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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 (PubMed:2951378, PubMed:2999119, PubMed:2681202, PubMed:8262947). The enzyme II ManXYZ PTS system is involved in mannose transport (PubMed:2951378, PubMed:2999119, PubMed:2681202, PubMed:8262947). Also functions as a receptor for bacterial chemotaxis and is required for infection of the cell by bacteriophage lambda where it most likely functions as a pore for penetration of lambda DNA (PubMed:4604906, PubMed:353494).6 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101Tele-phosphohistidine intermediate; for EIIA activityPROSITE-ProRule annotation4 Publications
Sitei89 – 891Involved in the phosphoryl transfer between H-10 and H-1751 Publication
Active sitei175 – 1751Pros-phosphohistidine intermediate; for EIIB activity2 Publications

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 component1 Publication (EC:2.7.1.1912 Publications)
Alternative name(s):
EIIAB-Man1 Publication
EIII-Man1 Publication
Including the following 2 domains:
Mannose-specific phosphotransferase enzyme IIA component1 Publication
Alternative name(s):
PTS system mannose-specific EIIA component1 Publication
Mannose-specific phosphotransferase enzyme IIB component1 Publication
Alternative name(s):
PTS system mannose-specific EIIB component1 Publication
Gene namesi
Name:manX1 Publication
Synonyms:gptB, ptsL1 Publication
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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101H → C: Loss of phosphotransferase activity. Unable to dimerize. 1 Publication
Mutagenesisi10 – 101H → E: Results in the formation of a single complex corresponding to the productive phosphoryl transfer complex. 1 Publication
Mutagenesisi12 – 121W → F: Slight phosphotransferase activity. Unable to dimerize. 1 Publication
Mutagenesisi48 – 481K → C: Retains more than 50% of phosphotransferase activity. 1 Publication
Mutagenesisi72 – 721S → C: Slight phosphotransferase activity. Unable to dimerize. 1 Publication
Mutagenesisi86 – 861H → N: Loss of phosphotransferase activity. 1 Publication
Mutagenesisi110 – 1101S → C: Retains more than 50% of phosphotransferase activity. 1 Publication
Mutagenesisi175 – 1751H → C: Loss of phosphotransferase activity. 1 Publication
Mutagenesisi219 – 2191H → Q: Slight phosphotransferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication1 Publication
Chaini2 – 323322PTS system mannose-specific EIIAB componentPRO_0000186653Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101Phosphohistidine; by HPr2 Publications
Modified residuei55 – 551N6-acetyllysine1 Publication
Modified residuei175 – 1751Phosphohistidine; by EIIAPROSITE-ProRule annotation1 Publication
Modified residuei234 – 2341N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP69797.
PaxDbiP69797.
PRIDEiP69797.

2D gel databases

SWISS-2DPAGEP69797.

Interactioni

Subunit structurei

Homodimer.1 Publication4 Publications

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 annotation2 PublicationsAdd
BLAST
Domaini157 – 320164PTS EIIB type-4PROSITE-ProRule annotation1 PublicationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni137 – 15519Hinge1 PublicationAdd
BLAST

Domaini

The PTS EIIA type-4 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-4 domain.2 Publications
The PTS EIIB type-4 domain is phosphorylated by phospho-EIIA on a histidyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-4 domain.PROSITE-ProRule annotation1 Publication

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.
OMAiEMIFGKQ.
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.
OMAiEMIFGKQ.
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...

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: September 7, 2016
This is version 117 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.