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Protein

PTS system glucose-specific EIIA component

Gene

crr

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:3129430, PubMed:17158705). The enzyme II complex composed of PtsG and Crr is involved in glucose transport (PubMed:2657735). The non-phosphorylated EIII-Glc is an inhibitor for uptake of certain sugars such as maltose, melibiose, lactose, and glycerol. Phosphorylated EIII-Glc, however, may be an activator for adenylate cyclase. It is an important regulatory protein for cell metabolism (PubMed:789369).1 Publication3 Publications

Catalytic activityi

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

Cofactori

Zn2+2 PublicationsNote: Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi76 – 761Zinc; shared with glycerol kinase1 Publication3 Publications
Sitei76 – 761Important for phospho-donor activity1 Publication
Active sitei91 – 911Tele-phosphohistidine intermediate; for EIIA activityPROSITE-ProRule annotation2 Publications2 Publications
Metal bindingi91 – 911Zinc; shared with glycerol kinase1 Publication3 Publications

GO - Molecular functioni

GO - Biological processi

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:CRR-MONOMER.
ECOL316407:JW2410-MONOMER.
MetaCyc:CRR-MONOMER.

Protein family/group databases

TCDBi4.A.1.1.1. the pts glucose-glucoside (glc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
PTS system glucose-specific EIIA component1 Publication
Alternative name(s):
EIIA-Glc1 Publication
EIII-Glc1 Publication
Glucose-specific phosphotransferase enzyme IIA component1 Publication (EC:2.7.1.1991 Publication)
Gene namesi
Name:crr1 Publication
Synonyms:gsr, iex, tgs, treD
Ordered Locus Names:b2417, JW2410
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10165. crr.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • extrinsic component of cytoplasmic side of plasma membrane Source: EcoCyc
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

In mutants defective in enzyme I and histidine-containing phosphate carrier protein (HPr), cells lacking this gene are able to grow on the non-PTS compounds such as glycerol, maltose, melibiose, mannose 6-phosphate, and alpha-glycerol phosphate.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi4 – 41F → W: Same activity as the wild-type. 1 Publication
Mutagenesisi76 – 761H → Q: Unable to transfer phosphoryl group. 1 Publication
Mutagenesisi91 – 911H → Q: Unable to be phosphorylated by Hpr. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved3 Publications
Chaini2 – 169168PTS system glucose-specific EIIA componentPRO_0000186532Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei91 – 911Phosphohistidine; by HPr1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP69783.
PaxDbiP69783.
PRIDEiP69783.

2D gel databases

SWISS-2DPAGEP69783.

Interactioni

Subunit structurei

Heterodimer with glycerol kinase (glpk).1 Publication2 Publications

Protein-protein interaction databases

BioGridi4260572. 21 interactions.
DIPiDIP-31863N.
IntActiP69783. 4 interactions.
STRINGi511145.b2417.

Structurei

Secondary structure

1
169
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Beta strandi21 – 244Combined sources
Beta strandi29 – 335Combined sources
Helixi34 – 363Combined sources
Beta strandi37 – 393Combined sources
Helixi40 – 434Combined sources
Beta strandi45 – 473Combined sources
Beta strandi49 – 557Combined sources
Beta strandi57 – 615Combined sources
Beta strandi63 – 719Combined sources
Beta strandi75 – 828Combined sources
Turni83 – 853Combined sources
Beta strandi87 – 915Combined sources
Beta strandi93 – 953Combined sources
Helixi96 – 994Combined sources
Turni100 – 1034Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi119 – 1235Combined sources
Helixi125 – 1317Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi137 – 1426Combined sources
Helixi144 – 1463Combined sources
Beta strandi148 – 1525Combined sources
Beta strandi155 – 1573Combined sources
Turni159 – 1613Combined sources
Beta strandi162 – 1687Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F3GX-ray2.10A9-169[»]
1F3ZX-ray1.98A9-169[»]
1GGRNMR-A2-169[»]
1GLAX-ray2.60F2-169[»]
1GLBX-ray2.60F2-169[»]
1GLCX-ray2.65F2-169[»]
1GLDX-ray2.93F2-169[»]
1GLEX-ray2.94F2-169[»]
1O2FNMR-A2-169[»]
2F3GX-ray2.13A/B2-169[»]
2MP0NMR-B2-169[»]
4JBWX-ray3.91M/N/O/P1-169[»]
ProteinModelPortaliP69783.
SMRiP69783. Positions 20-169.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69783.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 143105PTS EIIA type-1PROSITE-ProRule annotationAdd
BLAST

Domaini

The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.PROSITE-ProRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C5Y. Bacteria.
COG2190. LUCA.
HOGENOMiHOG000224567.
InParanoidiP69783.
KOiK02777.
OMAiEGQEVKM.
PhylomeDBiP69783.

Family and domain databases

InterProiIPR011055. Dup_hybrid_motif.
IPR001127. PTS_EIIA_1_perm.
[Graphical view]
PfamiPF00358. PTS_EIIA_1. 1 hit.
[Graphical view]
SUPFAMiSSF51261. SSF51261. 1 hit.
TIGRFAMsiTIGR00830. PTBA. 1 hit.
PROSITEiPS51093. PTS_EIIA_TYPE_1. 1 hit.
PS00371. PTS_EIIA_TYPE_1_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P69783-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLFDKLKSL VSDDKKDTGT IEIIAPLSGE IVNIEDVPDV VFAEKIVGDG
60 70 80 90 100
IAIKPTGNKM VAPVDGTIGK IFETNHAFSI ESDSGVELFV HFGIDTVELK
110 120 130 140 150
GEGFKRIAEE GQRVKVGDTV IEFDLPLLEE KAKSTLTPVV ISNMDEIKEL
160
IKLSGSVTVG ETPVIRIKK
Length:169
Mass (Da):18,251
Last modified:January 23, 2007 - v2
Checksum:iEA18020745531215
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 319Missing in AAC44167 (PubMed:8764513).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02796 Genomic DNA. Translation: AAA24442.1.
M21994 Genomic DNA. Translation: AAA24386.1.
M93578 Genomic DNA. Translation: AAA23602.1.
M93579 Genomic DNA. Translation: AAA23605.1.
M93580 Genomic DNA. Translation: AAA23603.1.
M93581 Genomic DNA. Translation: AAA23606.1.
M93582 Genomic DNA. Translation: AAA23604.1.
M93584 Genomic DNA. Translation: AAA23610.1.
M93587 Genomic DNA. Translation: AAA23612.1.
M93594 Genomic DNA. Translation: AAA23607.1.
M93595 Genomic DNA. Translation: AAA23608.1.
M93596 Genomic DNA. Translation: AAA23611.1.
M93597 Genomic DNA. Translation: AAA23609.1.
M93598 Genomic DNA. Translation: AAA23613.1.
U53700 Genomic DNA. Translation: AAC44167.1.
U00096 Genomic DNA. Translation: AAC75470.1.
AP009048 Genomic DNA. Translation: BAA16291.1.
PIRiC29785. WQECP3.
RefSeqiNP_416912.1. NC_000913.3.
WP_000522247.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75470; AAC75470; b2417.
BAA16291; BAA16291; BAA16291.
GeneIDi946880.
KEGGiecj:JW2410.
eco:b2417.
PATRICi32120217. VBIEscCol129921_2511.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02796 Genomic DNA. Translation: AAA24442.1.
M21994 Genomic DNA. Translation: AAA24386.1.
M93578 Genomic DNA. Translation: AAA23602.1.
M93579 Genomic DNA. Translation: AAA23605.1.
M93580 Genomic DNA. Translation: AAA23603.1.
M93581 Genomic DNA. Translation: AAA23606.1.
M93582 Genomic DNA. Translation: AAA23604.1.
M93584 Genomic DNA. Translation: AAA23610.1.
M93587 Genomic DNA. Translation: AAA23612.1.
M93594 Genomic DNA. Translation: AAA23607.1.
M93595 Genomic DNA. Translation: AAA23608.1.
M93596 Genomic DNA. Translation: AAA23611.1.
M93597 Genomic DNA. Translation: AAA23609.1.
M93598 Genomic DNA. Translation: AAA23613.1.
U53700 Genomic DNA. Translation: AAC44167.1.
U00096 Genomic DNA. Translation: AAC75470.1.
AP009048 Genomic DNA. Translation: BAA16291.1.
PIRiC29785. WQECP3.
RefSeqiNP_416912.1. NC_000913.3.
WP_000522247.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F3GX-ray2.10A9-169[»]
1F3ZX-ray1.98A9-169[»]
1GGRNMR-A2-169[»]
1GLAX-ray2.60F2-169[»]
1GLBX-ray2.60F2-169[»]
1GLCX-ray2.65F2-169[»]
1GLDX-ray2.93F2-169[»]
1GLEX-ray2.94F2-169[»]
1O2FNMR-A2-169[»]
2F3GX-ray2.13A/B2-169[»]
2MP0NMR-B2-169[»]
4JBWX-ray3.91M/N/O/P1-169[»]
ProteinModelPortaliP69783.
SMRiP69783. Positions 20-169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260572. 21 interactions.
DIPiDIP-31863N.
IntActiP69783. 4 interactions.
STRINGi511145.b2417.

Protein family/group databases

TCDBi4.A.1.1.1. the pts glucose-glucoside (glc) family.

2D gel databases

SWISS-2DPAGEP69783.

Proteomic databases

EPDiP69783.
PaxDbiP69783.
PRIDEiP69783.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75470; AAC75470; b2417.
BAA16291; BAA16291; BAA16291.
GeneIDi946880.
KEGGiecj:JW2410.
eco:b2417.
PATRICi32120217. VBIEscCol129921_2511.

Organism-specific databases

EchoBASEiEB0163.
EcoGeneiEG10165. crr.

Phylogenomic databases

eggNOGiENOG4105C5Y. Bacteria.
COG2190. LUCA.
HOGENOMiHOG000224567.
InParanoidiP69783.
KOiK02777.
OMAiEGQEVKM.
PhylomeDBiP69783.

Enzyme and pathway databases

BioCyciEcoCyc:CRR-MONOMER.
ECOL316407:JW2410-MONOMER.
MetaCyc:CRR-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP69783.
PROiP69783.

Family and domain databases

InterProiIPR011055. Dup_hybrid_motif.
IPR001127. PTS_EIIA_1_perm.
[Graphical view]
PfamiPF00358. PTS_EIIA_1. 1 hit.
[Graphical view]
SUPFAMiSSF51261. SSF51261. 1 hit.
TIGRFAMsiTIGR00830. PTBA. 1 hit.
PROSITEiPS51093. PTS_EIIA_TYPE_1. 1 hit.
PS00371. PTS_EIIA_TYPE_1_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPTGA_ECOLI
AccessioniPrimary (citable) accession number: P69783
Secondary accession number(s): P08837, Q47703
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 108 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.