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Protein

Glucose-specific phosphotransferase enzyme IIA 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. This system is involved in glucose transport.

Catalytic activityi

Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine.PROSITE-ProRule annotation

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi76 – 761Zinc; shared with glycerol kinase
Sitei76 – 761Important for phospho-donor activity
Active sitei91 – 911Tele-phosphohistidine intermediate
Metal bindingi91 – 911Zinc; shared with glycerol kinase

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:
Glucose-specific phosphotransferase enzyme IIA component (EC:2.7.1.-)
Alternative name(s):
EIIA-Glc
EIII-Glc
PTS system glucose-specific EIIA component
Gene namesi
Name:crr
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved3 Publications
Chaini2 – 169168Glucose-specific phosphotransferase enzyme IIA componentPRO_0000186532Add
BLAST

Proteomic databases

EPDiP69783.
PaxDbiP69783.
PRIDEiP69783.

2D gel databases

SWISS-2DPAGEP69783.

Interactioni

Subunit structurei

Heterodimer with glycerol kinase (glpk).1 Publication

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.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C5Y. Bacteria.
COG2190. LUCA.
HOGENOMiHOG000224567.
InParanoidiP69783.
KOiK02777.
OMAiEGQEVKM.
OrthoDBiEOG6ND0GQ.
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 (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.
OrthoDBiEOG6ND0GQ.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The ptsH, ptsI, and crr genes of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: a complex operon with several modes of transcription."
    de Reuse H., Danchin A.
    J. Bacteriol. 170:3827-3837(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsI, and crr genes."
    Saffen D.W., Presper K.A., Doering T.L., Roseman S.
    J. Biol. Chem. 262:16241-16253(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Identification of the pdxK gene that encodes pyridoxine (vitamin B6) kinase in Escherichia coli K-12."
    Yang Y., Zhao G., Winkler M.E.
    FEMS Microbiol. Lett. 141:89-95(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Molecular population genetics of Escherichia coli: DNA sequence diversity at the celC, crr, and gutB loci of natural isolates."
    Hall B.G., Sharp P.M.
    Mol. Biol. Evol. 9:654-665(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Various ECOR strains.
  5. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21.
    Strain: K12 / EMG2.
  9. Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  10. Cited for: PROTEIN SEQUENCE OF 2-5.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  11. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  12. "Three-dimensional structure of the Escherichia coli phosphocarrier protein IIIglc."
    Worthylake D., Meadow N.D., Roseman S., Liao D.-I., Herzberg O., Remington S.J.
    Proc. Natl. Acad. Sci. U.S.A. 88:10382-10386(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  13. "Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase."
    Hurley J.H., Faber H.R., Worthylake D., Meadow N.D., Roseman S., Pettigrew D.W., Remington S.J.
    Science 259:673-677(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH GLYCEROL KINASE.
  14. "Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation."
    Feese M., Pettigrew D.W., Meadow N.D., Roseman S., Remington S.J.
    Proc. Natl. Acad. Sci. U.S.A. 91:3544-3548(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
  15. "Structural studies of the Escherichia coli signal transducing protein IIAGlc: implications for target recognition."
    Feese M.D., Comolli L., Meadow N.D., Roseman S., Remington S.J.
    Biochemistry 36:16087-16096(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 20-169.
  16. "1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniques."
    Pelton J.G., Torchia D.A., Meadow N.D., Wong C.Y., Roseman S.
    Biochemistry 30:10043-10057(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  17. "Secondary structure of the phosphocarrier protein IIIGlc, a signal-transducing protein from Escherichia coli, determined by heteronuclear three-dimensional NMR spectroscopy."
    Pelton J.G., Torchia D.A., Meadow N.D., Wong C.-Y., Roseman S.
    Proc. Natl. Acad. Sci. U.S.A. 88:3479-3483(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  18. "Structural comparison of phosphorylated and unphosphorylated forms of IIIGlc, a signal-transducing protein from Escherichia coli, using three-dimensional NMR techniques."
    Pelton J.G., Torchia D.A., Meadow N.D., Roseman S.
    Biochemistry 31:5215-5224(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

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: March 16, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The non-phosphorylated factor III is an inhibitor for uptake of certain sugars such as maltose, melibiose, lactose, and glycerol. Phosphorylated factor III, however, may be an activator for adenylate cyclase. It is an important regulatory protein for cell metabolism.

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.