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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: -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)DescriptionActionsGraphical viewLength
Active sitei87Tele-phosphohistidine intermediate; for EIIA activityPROSITE-ProRule annotation1 Publication1
Active sitei192Phosphocysteine intermediate; for EIIB activity1 Publication1

GO - Molecular functioni

GO - Biological processi

  • mannosylglycerate transport Source: EcoCyc
  • phosphoenolpyruvate-dependent sugar phosphotransferase system Source: EcoCyc

Keywordsi

Molecular functionKinase, Transferase
Biological processPhosphotransferase system, Sugar transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:HRSA-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
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Topological domaini1 – 313PeriplasmicSequence analysisAdd BLAST313
Transmembranei314 – 334HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini335 – 358CytoplasmicSequence analysisAdd BLAST24
Transmembranei359 – 379HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini380 – 389PeriplasmicSequence analysis10
Transmembranei390 – 410HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini411 – 433CytoplasmicSequence analysisAdd BLAST23
Transmembranei434 – 454HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini455 – 474PeriplasmicSequence analysisAdd BLAST20
Transmembranei475 – 495HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini496 – 500CytoplasmicSequence analysis5
Transmembranei501 – 521HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini522 – 551PeriplasmicSequence analysisAdd BLAST30
Transmembranei552 – 572HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini573CytoplasmicSequence analysis1
Transmembranei574 – 594HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini595 – 620PeriplasmicSequence analysisAdd BLAST26
Transmembranei621 – 641HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini642 – 658CytoplasmicSequence analysisAdd BLAST17

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001866991 – 658PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC componentAdd BLAST658

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei87Phosphohistidine; by HPrCurated1
Modified residuei192Phosphocysteine; by EIIAPROSITE-ProRule annotationCurated1

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
sspAP0ACA35EBI-558542,EBI-558482

Protein-protein interaction databases

BioGridi4263541, 15 interactors
DIPiDIP-9939N
IntActiP54745, 1 interactor
STRINGi316385.ECDH10B_0797

Structurei

3D structure databases

ProteinModelPortaliP54745
SMRiP54745
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 171PTS EIIA type-2PROSITE-ProRule annotationAdd BLAST147
Domaini186 – 282PTS EIIB type-2PROSITE-ProRule annotationAdd BLAST97
Domaini306 – 641PTS EIIC type-2PROSITE-ProRule annotationAdd BLAST336

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105DM4 Bacteria
COG1299 LUCA
COG1445 LUCA
COG1762 LUCA
HOGENOMiHOG000227678
KOiK11198
K11199
K11200
OMAiQENSWLW
PhylomeDBiP54745

Family and domain databases

CDDicd05569 PTS_IIB_fructose, 1 hit
Gene3Di3.40.930.10, 1 hit
InterProiView protein in InterPro
IPR016152 PTrfase/Anion_transptr
IPR002178 PTS_EIIA_type-2_dom
IPR036095 PTS_EIIB-like_sf
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
PfamiView protein in Pfam
PF00359 PTS_EIIA_2, 1 hit
PF02378 PTS_EIIC, 1 hit
PF02302 PTS_IIB, 1 hit
SUPFAMiSSF52794 SSF52794, 1 hit
SSF55804 SSF55804, 1 hit
TIGRFAMsiTIGR00829 FRU, 1 hit
TIGR00848 fruA, 1 hit
TIGR01427 PTS_IIC_fructo, 1 hit
PROSITEiView protein in PROSITE
PS51094 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

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
WP_000242633.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73825; AAC73825; b0731
BAA35397; BAA35397; BAA35397
GeneIDi945355
KEGGiecj:JW0720
eco:b0731
PATRICifig|511145.12.peg.761

Similar proteinsi

Entry informationi

Entry nameiMNGA_ECOLI
AccessioniPrimary (citable) accession number: P54745
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 25, 2018
This is version 152 of the entry and version 1 of the sequence. See 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

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