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Protein

PTS system N-acetylglucosamine-specific EIICBA component

Gene

nagE

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:4919472). This system is involved in N-acetylglucosamine transport (PubMed:4919472). It can also transport and phosphorylate the antibiotic streptozotocin (PubMed:161156). Could play a significant role in the recycling of peptidoglycan (PubMed:19617367).1 Publication3 Publications

Catalytic activityi

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

Cofactori

Zn2+By similarity

Enzyme regulationi

P-chloromercuribenzoate inhibits the accumulation of both N-acetyl-D-glucosamine and antibiotic streptozotocin (2-deoxy-2-(3-methyl-3-nitrosoureido)-D-glucopyranose). N-acetyl-D-glucosamine is a competitive inhibitor for the uptake of streptozotocin.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei412 – 4121Phosphocysteine intermediate; for EIIB activityPROSITE-ProRule annotation
Metal bindingi554 – 5541ZincBy similarity
Sitei554 – 5541Important for phospho-donor activityBy similarity
Active sitei569 – 5691Tele-phosphohistidine intermediate; for EIIA activityPROSITE-ProRule annotation1 Publication
Metal bindingi569 – 5691ZincBy similarity

GO - Molecular functioni

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • N-acetylglucosamine 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

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:NAGE-MONOMER.
ECOL316407:JW0665-MONOMER.
MetaCyc:NAGE-MONOMER.

Protein family/group databases

TCDBi4.A.1.1.2. the pts glucose-glucoside (glc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
PTS system N-acetylglucosamine-specific EIICBA component1 Publication
Alternative name(s):
EIICBA-Nag1 Publication
Short name:
EII-Nag1 Publication
Including the following 3 domains:
N-acetylglucosamine permease IIC component1 Publication
Alternative name(s):
PTS system N-acetylglucosamine-specific EIIC component1 Publication
N-acetylglucosamine-specific phosphotransferase enzyme IIB component1 Publication (EC:2.7.1.1931 Publication)
Alternative name(s):
PTS system N-acetylglucosamine-specific EIIB component1 Publication
N-acetylglucosamine-specific phosphotransferase enzyme IIA component1 Publication (EC:2.7.1.1931 Publication)
Alternative name(s):
PTS system N-acetylglucosamine-specific EIIA component1 Publication
Gene namesi
Name:nagE1 Publication
Synonyms:pstN
Ordered Locus Names:b0679, JW0665
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10635. nagE.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei16 – 3621HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei38 – 5821HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei70 – 9021HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei92 – 11221HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei132 – 15221HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei159 – 17921HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei192 – 21221HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei232 – 25221HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei260 – 28021HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei282 – 30221HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei303 – 32321HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei339 – 35921HelicalPROSITE-ProRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Cells lacking nagE and nagA reduce by 50% the amount of GlcNAc6P. Together with the mutations of the genes of the peptidoglycan recycling pathway (ampG, anmK, murQ, nagK and nagZ), the accumulation of GlcNAc6P is eliminated.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 648648PTS system N-acetylglucosamine-specific EIICBA componentPRO_0000186475Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei412 – 4121Phosphocysteine; by EIIABy similarityCurated
Modified residuei569 – 5691Phosphohistidine; by HPrBy similarityCurated

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP09323.
PaxDbiP09323.
PRIDEiP09323.

Expressioni

Inductioni

Induced by N-acetylglucosamine-6-phosphate and repressed by NagC.2 Publications

Interactioni

Protein-protein interaction databases

BioGridi4261209. 4 interactions.
STRINGi511145.b0679.

Structurei

3D structure databases

ProteinModelPortaliP09323.
SMRiP09323. Positions 392-466, 500-648.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 371371PTS EIIC type-1PROSITE-ProRule annotationAdd
BLAST
Domaini390 – 47283PTS EIIB type-1PROSITE-ProRule annotationAdd
BLAST
Domaini517 – 621105PTS EIIA type-1PROSITE-ProRule annotationAdd
BLAST

Domaini

The PTS EIIC type-1 domain forms the PTS system translocation channel and contains the specific substrate-binding site.PROSITE-ProRule annotation
The PTS EIIB type-1 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-1 domain.PROSITE-ProRule annotation
The PTS EIIA type-1 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-1 domain.PROSITE-ProRule annotation

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CI1. Bacteria.
COG1263. LUCA.
COG1264. LUCA.
COG2190. LUCA.
HOGENOMiHOG000250993.
InParanoidiP09323.
KOiK02802.
K02803.
K02804.
OMAiACLAMYR.
PhylomeDBiP09323.

Family and domain databases

CDDicd00212. PTS_IIB_glc. 1 hit.
Gene3Di3.30.1360.60. 1 hit.
InterProiIPR011055. Dup_hybrid_motif.
IPR018113. PTrfase_EIIB_Cys.
IPR001127. PTS_EIIA_1_perm.
IPR003352. PTS_EIIC.
IPR013013. PTS_EIIC_1.
IPR001996. PTS_IIB_1.
IPR010974. PTS_IIBC_nag.
[Graphical view]
PfamiPF00358. PTS_EIIA_1. 1 hit.
PF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
SUPFAMiSSF51261. SSF51261. 1 hit.
SSF55604. SSF55604. 1 hit.
TIGRFAMsiTIGR00826. EIIB_glc. 1 hit.
TIGR00830. PTBA. 1 hit.
TIGR01998. PTS-II-BC-nag. 1 hit.
PROSITEiPS51093. PTS_EIIA_TYPE_1. 1 hit.
PS00371. PTS_EIIA_TYPE_1_HIS. 1 hit.
PS51098. PTS_EIIB_TYPE_1. 1 hit.
PS01035. PTS_EIIB_TYPE_1_CYS. 1 hit.
PS51103. PTS_EIIC_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09323-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNILGFFQRL GRALQLPIAV LPVAALLLRF GQPDLLNVAF IAQAGGAIFD
60 70 80 90 100
NLALIFAIGV ASSWSKDSAG AAALAGAVGY FVLTKAMVTI NPEINMGVLA
110 120 130 140 150
GIITGLVGGA AYNRWSDIKL PDFLSFFGGK RFVPIATGFF CLVLAAIFGY
160 170 180 190 200
VWPPVQHAIH AGGEWIVSAG ALGSGIFGFI NRLLIPTGLH QVLNTIAWFQ
210 220 230 240 250
IGEFTNAAGT VFHGDINRFY AGDGTAGMFM SGFFPIMMFG LPGAALAMYF
260 270 280 290 300
AAPKERRPMV GGMLLSVAVT AFLTGVTEPL EFLFMFLAPL LYLLHALLTG
310 320 330 340 350
ISLFVATLLG IHAGFSFSAG AIDYALMYNL PAASQNVWML LVMGVIFFAI
360 370 380 390 400
YFVVFSLVIR MFNLKTPGRE DKEDEIVTEE ANSNTEEGLT QLATNYIAAV
410 420 430 440 450
GGTDNLKAID ACITRLRLTV ADSARVNDTM CKRLGASGVV KLNKQTIQVI
460 470 480 490 500
VGAKAESIGD AMKKVVARGP VAAASAEATP ATAAPVAKPQ AVPNAVSIAE
510 520 530 540 550
LVSPITGDVV ALDQVPDEAF ASKAVGDGVA VKPTDKIVVS PAAGTIVKIF
560 570 580 590 600
NTNHAFCLET EKGAEIVVHM GIDTVALEGK GFKRLVEEGA QVSAGQPILE
610 620 630 640
MDLDYLNANA RSMISPVVCS NIDDFSGLII KAQGHIVAGQ TPLYEIKK
Length:648
Mass (Da):68,347
Last modified:July 1, 1989 - v1
Checksum:i1E24C97CFCBBAA59
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19284 Genomic DNA. Translation: AAA24192.1.
U00096 Genomic DNA. Translation: AAC73773.1.
AP009048 Genomic DNA. Translation: BAA35327.1.
PIRiB29895. WQEC2N.
RefSeqiNP_415205.1. NC_000913.3.
WP_001023093.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73773; AAC73773; b0679.
BAA35327; BAA35327; BAA35327.
GeneIDi945292.
KEGGiecj:JW0665.
eco:b0679.
PATRICi32116545. VBIEscCol129921_0705.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19284 Genomic DNA. Translation: AAA24192.1.
U00096 Genomic DNA. Translation: AAC73773.1.
AP009048 Genomic DNA. Translation: BAA35327.1.
PIRiB29895. WQEC2N.
RefSeqiNP_415205.1. NC_000913.3.
WP_001023093.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP09323.
SMRiP09323. Positions 392-466, 500-648.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261209. 4 interactions.
STRINGi511145.b0679.

Protein family/group databases

TCDBi4.A.1.1.2. the pts glucose-glucoside (glc) family.

Proteomic databases

EPDiP09323.
PaxDbiP09323.
PRIDEiP09323.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73773; AAC73773; b0679.
BAA35327; BAA35327; BAA35327.
GeneIDi945292.
KEGGiecj:JW0665.
eco:b0679.
PATRICi32116545. VBIEscCol129921_0705.

Organism-specific databases

EchoBASEiEB0629.
EcoGeneiEG10635. nagE.

Phylogenomic databases

eggNOGiENOG4105CI1. Bacteria.
COG1263. LUCA.
COG1264. LUCA.
COG2190. LUCA.
HOGENOMiHOG000250993.
InParanoidiP09323.
KOiK02802.
K02803.
K02804.
OMAiACLAMYR.
PhylomeDBiP09323.

Enzyme and pathway databases

BioCyciEcoCyc:NAGE-MONOMER.
ECOL316407:JW0665-MONOMER.
MetaCyc:NAGE-MONOMER.

Miscellaneous databases

PROiP09323.

Family and domain databases

CDDicd00212. PTS_IIB_glc. 1 hit.
Gene3Di3.30.1360.60. 1 hit.
InterProiIPR011055. Dup_hybrid_motif.
IPR018113. PTrfase_EIIB_Cys.
IPR001127. PTS_EIIA_1_perm.
IPR003352. PTS_EIIC.
IPR013013. PTS_EIIC_1.
IPR001996. PTS_IIB_1.
IPR010974. PTS_IIBC_nag.
[Graphical view]
PfamiPF00358. PTS_EIIA_1. 1 hit.
PF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
SUPFAMiSSF51261. SSF51261. 1 hit.
SSF55604. SSF55604. 1 hit.
TIGRFAMsiTIGR00826. EIIB_glc. 1 hit.
TIGR00830. PTBA. 1 hit.
TIGR01998. PTS-II-BC-nag. 1 hit.
PROSITEiPS51093. PTS_EIIA_TYPE_1. 1 hit.
PS00371. PTS_EIIA_TYPE_1_HIS. 1 hit.
PS51098. PTS_EIIB_TYPE_1. 1 hit.
PS01035. PTS_EIIB_TYPE_1_CYS. 1 hit.
PS51103. PTS_EIIC_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPTW3C_ECOLI
AccessioniPrimary (citable) accession number: P09323
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 7, 2016
This is version 153 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.