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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)DescriptionActionsGraphical viewLength
Active sitei10Tele-phosphohistidine intermediate; for EIIA activityPROSITE-ProRule annotation4 Publications1
Sitei89Involved in the phosphoryl transfer between H-10 and H-1751 Publication1
Active sitei175Pros-phosphohistidine intermediate; for EIIB activity2 Publications1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi10H → C: Loss of phosphotransferase activity. Unable to dimerize. 1 Publication1
Mutagenesisi10H → E: Results in the formation of a single complex corresponding to the productive phosphoryl transfer complex. 1 Publication1
Mutagenesisi12W → F: Slight phosphotransferase activity. Unable to dimerize. 1 Publication1
Mutagenesisi48K → C: Retains more than 50% of phosphotransferase activity. 1 Publication1
Mutagenesisi72S → C: Slight phosphotransferase activity. Unable to dimerize. 1 Publication1
Mutagenesisi86H → N: Loss of phosphotransferase activity. 1 Publication1
Mutagenesisi110S → C: Retains more than 50% of phosphotransferase activity. 1 Publication1
Mutagenesisi175H → C: Loss of phosphotransferase activity. 1 Publication1
Mutagenesisi219H → Q: Slight phosphotransferase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication1 Publication
ChainiPRO_00001866532 – 323PTS system mannose-specific EIIAB componentAdd BLAST322

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei10Phosphohistidine; by HPr2 Publications1
Modified residuei55N6-acetyllysine1 Publication1
Modified residuei175Phosphohistidine; by EIIAPROSITE-ProRule annotation1 Publication1
Modified residuei234N6-acetyllysine1 Publication1

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 interactors.
DIPiDIP-35846N.
IntActiP69797. 14 interactors.
MINTiMINT-1228428.
STRINGi511145.b1817.

Structurei

Secondary structure

1323
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Helixi13 – 25Combined sources13
Beta strandi29 – 34Combined sources6
Helixi42 – 53Combined sources12
Beta strandi62 – 68Combined sources7
Helixi72 – 81Combined sources10
Beta strandi87 – 92Combined sources6
Helixi95 – 105Combined sources11
Helixi111 – 124Combined sources14
Beta strandi163 – 170Combined sources8
Helixi178 – 185Combined sources8
Beta strandi189 – 194Combined sources6
Helixi196 – 199Combined sources4
Helixi202 – 210Combined sources9
Beta strandi217 – 221Combined sources5
Helixi223 – 230Combined sources8
Helixi233 – 235Combined sources3
Beta strandi239 – 246Combined sources8
Helixi247 – 255Combined sources9
Beta strandi261 – 267Combined sources7
Beta strandi274 – 276Combined sources3
Beta strandi278 – 280Combined sources3
Helixi285 – 296Combined sources12
Beta strandi300 – 303Combined sources4
Helixi314 – 319Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69797.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 124PTS EIIA type-4PROSITE-ProRule annotation2 PublicationsAdd BLAST123
Domaini157 – 320PTS EIIB type-4PROSITE-ProRule annotation1 PublicationAdd BLAST164

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni137 – 155Hinge1 PublicationAdd BLAST19

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

CDDicd00006. PTS_IIA_man. 1 hit.
cd00001. PTS_IIB_man. 1 hit.
Gene3Di3.40.35.10. 1 hit.
3.40.50.510. 1 hit.
InterProiIPR013789. PTS_EIIA_man.
IPR004701. PTS_EIIA_man-typ.
IPR033887. PTS_IIA_man.
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)DescriptionActionsGraphical viewLength
Sequence conflicti2 – 23TIAIV…KTAEM → GWGCRAGCLKRQKW in AAA24110 (Ref. 1) CuratedAdd BLAST22
Sequence conflicti35D → N in AAA24110 (Ref. 1) Curated1
Sequence conflicti101T → R in AAA24110 (Ref. 1) Curated1
Sequence conflicti142A → G in AAA24110 (Ref. 1) Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259144. 308 interactors.
DIPiDIP-35846N.
IntActiP69797. 14 interactors.
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

CDDicd00006. PTS_IIA_man. 1 hit.
cd00001. PTS_IIB_man. 1 hit.
Gene3Di3.40.35.10. 1 hit.
3.40.50.510. 1 hit.
InterProiIPR013789. PTS_EIIA_man.
IPR004701. PTS_EIIA_man-typ.
IPR033887. PTS_IIA_man.
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: November 30, 2016
This is version 120 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.