P69783 (PTGA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	crr
Synonyms:	gsr, iex, tgs, treD
Ordered Locus Names:	b2417, JW2410

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	169 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine.
Cofactor	Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization.
Subunit structure	Heterodimer with glycerol kinase (glpk).
Subcellular location	Cytoplasm.
Domain	The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.
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.
Sequence similarities	Contains 1 PTS EIIA type-1 domain.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB membrane Inferred from direct assay. Source: UniProtKB
Molecular function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW sugar:hydrogen symporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8 Ref.9 Ref.10

Chain

2 – 169

168

Glucose-specific phosphotransferase enzyme IIA component

PRO_0000186532

Regions

Domain

39 – 143

105

PTS EIIA type-1

Sites

Active site

91

1

Tele-phosphohistidine intermediate

Metal binding

76

1

Zinc; shared with glycerol kinase

Metal binding

91

1

Zinc; shared with glycerol kinase

Site

76

1

Important for phospho-donor activity

Experimental info

Sequence conflict

23 – 31

9

Missing Ref.3

Secondary structure

1

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169

Helix Strand Turn

Details...

Beta strand

21 – 24

4

Beta strand

29 – 33

5

Helix

34 – 36

3

Helix

40 – 43

4

Beta strand

49 – 55

7

Beta strand

57 – 61

5

Beta strand

63 – 71

9

Beta strand

75 – 82

8

Beta strand

87 – 91

5

Beta strand

93 – 95

3

Helix

96 – 99

4

Turn

100 – 103

4

Beta strand

104 – 106

3

Beta strand

119 – 123

5

Helix

125 – 131

7

Beta strand

132 – 134

3

Beta strand

137 – 141

5

Helix

144 – 146

3

Beta strand

148 – 152

5

Beta strand

155 – 157

3

Turn

159 – 161

3

Beta strand

162 – 168

7

Sequences

	Sequence		Length	Mass (Da)
	P69783 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: EA18020745531215	FASTA	169	18,251
	10 20 30 40 50 60 MGLFDKLKSL VSDDKKDTGT IEIIAPLSGE IVNIEDVPDV VFAEKIVGDG IAIKPTGNKM 70 80 90 100 110 120 VAPVDGTIGK IFETNHAFSI ESDSGVELFV HFGIDTVELK GEGFKRIAEE GQRVKVGDTV 130 140 150 160 IEFDLPLLEE KAKSTLTPVV ISNMDEIKEL IKLSGSVTVG ETPVIRIKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2457575] [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: 2960675] [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: 8764513] [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: 1630305] [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: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21. Strain: K12 / EMG2.
[9]	Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F. Submitted (SEP-1994) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[10]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed: 9600841] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[11]	"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: 1961703] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[12]	"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: 8430315] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH GLYCEROL KINASE.
[13]	"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: 8170944] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
[14]	"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: 9405042] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 20-169.
[15]	"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: 1911770] [Abstract] Cited for: STRUCTURE BY NMR.
[16]	"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: 2014267] [Abstract] Cited for: STRUCTURE BY NMR.
[17]	"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: 1606145] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

WQECP3. C29785.

RefSeq

NP_416912.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F3G	X-ray	2.10	A	9-169	[»]
1F3Z	X-ray	1.98	A	9-169	[»]
1GGR	NMR	-	A	2-168	[»]
1GLA	X-ray	2.60	F	2-169	[»]
1GLB	X-ray	2.60	F	2-169	[»]
1GLC	X-ray	2.65	F	2-169	[»]
1GLD	X-ray	2.93	F	2-169	[»]
1GLE	X-ray	2.94	F	2-169	[»]
1O2F	NMR	-	A	2-168	[»]
2F3G	X-ray	2.13	A/B	2-169	[»]

ProteinModelPortal

P69783.

SMR

P69783. Positions 20-169.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31863N.

IntAct

P69783. 6 interactions.

Protein family/group databases

TCDB

4.A.1.1.1. PTS glucose-glucoside (Glc) family.

PTM databases

PhosSite

P69783.

2D gel databases

SWISS-2DPAGE

P69783.

2DBase-Ecoli

P69783.

ECO2DBASE

B018.7. 6TH EDITION.

Proteomic databases

PRIDE

P69783.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001185; EBESCP00000001185; EBESCG00000000980.
EBESCT00000001186; EBESCP00000001186; EBESCG00000000980.
EBESCT00000001187; EBESCP00000001187; EBESCG00000000980.
EBESCT00000001188; EBESCP00000001188; EBESCG00000000980.
EBESCT00000001189; EBESCP00000001189; EBESCG00000000980.
EBESCT00000001190; EBESCP00000001190; EBESCG00000000980.
EBESCT00000001191; EBESCP00000001191; EBESCG00000000980.
EBESCT00000018235; EBESCP00000017526; EBESCG00000017290.

GeneID

946880.

GenomeReviews

Gene locus JW2410 in contig AP009048_GR.
Gene locus b2417 in contig U00096_GR.

KEGG

ecj:JW2410.
eco:b2417.

PATRIC

32120217. VBIEscCol129921_2511.

Organism-specific databases

EchoBASE

EB0163.

EcoGene

EG10165. crr.

Phylogenomic databases

eggNOG

COG2190.

GeneTree

EBGT00050000009158.

HOGENOM

HBG517865.

OMA

RRLISGQ.

PhylomeDB

P69783.

ProtClustDB

PRK09439.

Enzyme and pathway databases

BioCyc

EcoCyc:CRR-MONOMER.
MetaCyc:CRR-MONOMER.

Gene expression databases

Genevestigator

P69783.

Family and domain databases

InterPro

IPR011055. Dup_hybrid_motif.
IPR001127. PTS_EIIA_1_perm.
[Graphical view]

KO

K02777.

Pfam

PF00358. PTS_EIIA_1. 1 hit.
[Graphical view]

SUPFAM

SSF51261. Dup_hybrid_motif. 1 hit.

TIGRFAMs

TIGR00830. PTBA. 1 hit.

PROSITE

PS51093. PTS_EIIA_TYPE_1. 1 hit.
PS00371. PTS_EIIA_TYPE_1_HIS. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PTGA_ECOLI

Accession

Primary (citable) accession number: P69783
Secondary accession number(s): P08837, Q47703

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program