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Protein

PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC component

Gene

mngA

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:14645248, PubMed:9063979). This system is involved in mannosyl-D-glycerate transport (PubMed:14645248). Also involved in thermoinduction of ompC (PubMed:9063979).2 Publications

Catalytic activityi

[Protein]-N(pi)-phospho-L-histidine + 2-O-alpha-mannosyl-D-glycerate (Side 1) = [protein]-L-histidine + 2-O-(6-phospho-alpha-D-mannosyl)-D-glycerate (Side 2).1 Publication

Kineticsi

  1. KM=10 µM for mannosyl-D-glycerate1 Publication
  1. Vmax=0.65 nmol/min/mg enzyme for mannosyl-D-glycerate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei87 – 871Tele-phosphohistidine intermediate; for EIIA activityPROSITE-ProRule annotation1 Publication
Active sitei192 – 1921Phosphocysteine intermediate; for EIIB activity1 Publication

GO - Molecular functioni

GO - Biological processi

  • mannosylglycerate 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:HRSA-MONOMER.
ECOL316407:JW0720-MONOMER.
MetaCyc:HRSA-MONOMER.

Protein family/group databases

TCDBi4.A.2.1.3. the pts fructose-mannitol (fru) family.

Names & Taxonomyi

Protein namesi
Recommended name:
PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC component1 Publication
Alternative name(s):
2-O-alpha-mannosyl-D-glycerate-specific phosphotransferase enzyme MngA1 Publication
Protein-Npi-phosphohistidine--2-O-alpha-mannosyl-D-glycerate phosphotransferase1 Publication
Including the following 3 domains:
2-O-alpha-mannosyl-D-glycerate-specific phosphotransferase enzyme IIA component1 Publication (EC:2.7.1.1951 Publication)
Alternative name(s):
PTS system EIIA component1 Publication
2-O-alpha-mannosyl-D-glycerate-specific phosphotransferase enzyme IIB component1 Publication (EC:2.7.1.1951 Publication)
Alternative name(s):
PTS system EIIB component1 Publication
2-O-alpha-mannosyl-D-glycerate-specific permease IIC component1 Publication
Alternative name(s):
PTS system EIIC component1 Publication
Gene namesi
Name:mngA1 Publication
Synonyms:hrsA1 Publication
Ordered Locus Names:b0731, JW0720
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13235. hrsA.

Subcellular locationi

  • Cell inner membrane PROSITE-ProRule annotation1 Publication; Multi-pass membrane protein PROSITE-ProRule annotation1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 313313PeriplasmicSequence analysisAdd
BLAST
Transmembranei314 – 33421HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini335 – 35824CytoplasmicSequence analysisAdd
BLAST
Transmembranei359 – 37921HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini380 – 38910PeriplasmicSequence analysis
Transmembranei390 – 41021HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini411 – 43323CytoplasmicSequence analysisAdd
BLAST
Transmembranei434 – 45421HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini455 – 47420PeriplasmicSequence analysisAdd
BLAST
Transmembranei475 – 49521HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini496 – 5005CytoplasmicSequence analysis
Transmembranei501 – 52121HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini522 – 55130PeriplasmicSequence analysisAdd
BLAST
Transmembranei552 – 57221HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini573 – 5731CytoplasmicSequence analysis
Transmembranei574 – 59421HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini595 – 62026PeriplasmicSequence analysisAdd
BLAST
Transmembranei621 – 64121HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini642 – 65817CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are unable to transport mannosyl-D-glycerate.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 658658PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC componentPRO_0000186699Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei87 – 871Phosphohistidine; by HPrCurated
Modified residuei192 – 1921Phosphocysteine; by EIIAPROSITE-ProRule annotationCurated

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP54745.
PRIDEiP54745.

Expressioni

Inductioni

Induced by mannosyl-D-glycerate. Repressed by MngR.1 Publication

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
sspAP0ACA34EBI-558542,EBI-558482

Protein-protein interaction databases

BioGridi4263541. 9 interactions.
DIPiDIP-9939N.
IntActiP54745. 1 interaction.
MINTiMINT-1249398.
STRINGi511145.b0731.

Structurei

3D structure databases

ProteinModelPortaliP54745.
SMRiP54745. Positions 34-168, 186-281.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 171147PTS EIIA type-2PROSITE-ProRule annotationAdd
BLAST
Domaini186 – 28297PTS EIIB type-2PROSITE-ProRule annotationAdd
BLAST
Domaini306 – 641336PTS EIIC type-2PROSITE-ProRule annotationAdd
BLAST

Domaini

The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain.PROSITE-ProRule annotation
The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-2 domain.PROSITE-ProRule annotation
The EIIC type-2 domain forms the PTS system translocation channel and contains the specific substrate-binding site.PROSITE-ProRule annotation

Sequence similaritiesi

Contains 1 PTS EIIA type-2 domain.PROSITE-ProRule annotation
Contains 1 PTS EIIB type-2 domain.PROSITE-ProRule annotation
Contains 1 PTS EIIC type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105DM4. Bacteria.
COG1299. LUCA.
COG1445. LUCA.
COG1762. LUCA.
HOGENOMiHOG000227678.
KOiK11198.
K11199.
K11200.
OMAiNNALTAW.
PhylomeDBiP54745.

Family and domain databases

CDDicd05569. PTS_IIB_fructose. 1 hit.
Gene3Di3.40.930.10. 1 hit.
InterProiIPR016152. PTrfase/Anion_transptr.
IPR002178. PTS_EIIA_type-2_dom.
IPR013011. PTS_EIIB_2.
IPR003501. PTS_EIIB_2/3.
IPR003352. PTS_EIIC.
IPR013014. PTS_EIIC_2.
IPR004715. PTS_IIA_fruc.
IPR003353. PTS_IIB_fruc.
IPR006327. PTS_IIC_fruc.
[Graphical view]
PfamiPF00359. PTS_EIIA_2. 1 hit.
PF02378. PTS_EIIC. 1 hit.
PF02302. PTS_IIB. 1 hit.
[Graphical view]
SUPFAMiSSF52794. SSF52794. 1 hit.
SSF55804. SSF55804. 1 hit.
TIGRFAMsiTIGR00829. FRU. 1 hit.
TIGR00848. fruA. 1 hit.
TIGR01427. PTS_IIC_fructo. 1 hit.
PROSITEiPS51094. PTS_EIIA_TYPE_2. 1 hit.
PS00372. PTS_EIIA_TYPE_2_HIS. 1 hit.
PS51099. PTS_EIIB_TYPE_2. 1 hit.
PS51104. PTS_EIIC_TYPE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P54745-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLFYRAHWR DYKNDQVRIM MNLTTLTHRD ALCLNARFTS REEAIHALTQ
60 70 80 90 100
RLAALGKISS TEQFLEEVYR RESLGPTALG EGLAVPHGKT AAVKEAAFAV
110 120 130 140 150
ATLSEPLQWE GVDGPEAVDL VVLLAIPPNE AGTTHMQLLT ALTTRLADDE
160 170 180 190 200
IRARIQSATT PDELLSALDD KGGTQPSASF SNAPTIVCVT ACPAGIAHTY
210 220 230 240 250
MAAEYLEKAG RKLGVNVYVE KQGANGIEGR LTADQLNSAT ACIFAAEVAI
260 270 280 290 300
KESERFNGIP ALSVPVAEPI RHAEALIQQA LTLKRSDETR TVQQDTQPVK
310 320 330 340 350
SVKTELKQAL LSGISFAVPL IVAGGTVLAV AVLLSQIFGL QDLFNEENSW
360 370 380 390 400
LWMYRKLGGG LLGILMVPVL AAYTAYSLAD KPALAPGFAA GLAANMIGSG
410 420 430 440 450
FLGAVVGGLI AGYLMRWVKN HLRLSSKFNG FLTFYLYPVL GTLGAGSLML
460 470 480 490 500
FVVGEPVAWI NNSLTAWLNG LSGSNALLLG AILGFMCSFD LGGPVNKAAY
510 520 530 540 550
AFCLGAMANG VYGPYAIFAS VKMVSAFTVT ASTMLAPRLF KEFEIETGKS
560 570 580 590 600
TWLLGLAGIT EGAIPMAIED PLRVIGSFVL GSMVTGAIVG AMNIGLSTPG
610 620 630 640 650
AGIFSLFLLH DNGAGGVMAA IGWFGAALVG AAISTAILLM WRRHAVKHGN

YLTDGVMP
Length:658
Mass (Da):69,668
Last modified:October 1, 1996 - v1
Checksum:iC1F0999A1C48C5C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D64014 Genomic DNA. Translation: BAA10893.1.
U00096 Genomic DNA. Translation: AAC73825.1.
AP009048 Genomic DNA. Translation: BAA35397.2.
PIRiJC4598.
RefSeqiNP_415259.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC73825; AAC73825; b0731.
BAA35397; BAA35397; BAA35397.
GeneIDi945355.
KEGGiecj:JW0720.
eco:b0731.
PATRICi32116657. VBIEscCol129921_0761.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D64014 Genomic DNA. Translation: BAA10893.1.
U00096 Genomic DNA. Translation: AAC73825.1.
AP009048 Genomic DNA. Translation: BAA35397.2.
PIRiJC4598.
RefSeqiNP_415259.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP54745.
SMRiP54745. Positions 34-168, 186-281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263541. 9 interactions.
DIPiDIP-9939N.
IntActiP54745. 1 interaction.
MINTiMINT-1249398.
STRINGi511145.b0731.

Protein family/group databases

TCDBi4.A.2.1.3. the pts fructose-mannitol (fru) family.

Proteomic databases

PaxDbiP54745.
PRIDEiP54745.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73825; AAC73825; b0731.
BAA35397; BAA35397; BAA35397.
GeneIDi945355.
KEGGiecj:JW0720.
eco:b0731.
PATRICi32116657. VBIEscCol129921_0761.

Organism-specific databases

EchoBASEiEB3024.
EcoGeneiEG13235. hrsA.

Phylogenomic databases

eggNOGiENOG4105DM4. Bacteria.
COG1299. LUCA.
COG1445. LUCA.
COG1762. LUCA.
HOGENOMiHOG000227678.
KOiK11198.
K11199.
K11200.
OMAiNNALTAW.
PhylomeDBiP54745.

Enzyme and pathway databases

BioCyciEcoCyc:HRSA-MONOMER.
ECOL316407:JW0720-MONOMER.
MetaCyc:HRSA-MONOMER.

Miscellaneous databases

PROiP54745.

Family and domain databases

CDDicd05569. PTS_IIB_fructose. 1 hit.
Gene3Di3.40.930.10. 1 hit.
InterProiIPR016152. PTrfase/Anion_transptr.
IPR002178. PTS_EIIA_type-2_dom.
IPR013011. PTS_EIIB_2.
IPR003501. PTS_EIIB_2/3.
IPR003352. PTS_EIIC.
IPR013014. PTS_EIIC_2.
IPR004715. PTS_IIA_fruc.
IPR003353. PTS_IIB_fruc.
IPR006327. PTS_IIC_fruc.
[Graphical view]
PfamiPF00359. PTS_EIIA_2. 1 hit.
PF02378. PTS_EIIC. 1 hit.
PF02302. PTS_IIB. 1 hit.
[Graphical view]
SUPFAMiSSF52794. SSF52794. 1 hit.
SSF55804. SSF55804. 1 hit.
TIGRFAMsiTIGR00829. FRU. 1 hit.
TIGR00848. fruA. 1 hit.
TIGR01427. PTS_IIC_fructo. 1 hit.
PROSITEiPS51094. PTS_EIIA_TYPE_2. 1 hit.
PS00372. PTS_EIIA_TYPE_2_HIS. 1 hit.
PS51099. PTS_EIIB_TYPE_2. 1 hit.
PS51104. PTS_EIIC_TYPE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMNGA_ECOLI
AccessioniPrimary (citable) accession number: P54745
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 7, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.