Reviewed, UniProtKB/Swiss-Prot P56580 (PTHB_ECOLI)

Names and origin

Protein names

Recommended name:
    Glucitol/sorbitol-specific phosphotransferase enzyme IIB component
    EC=2.7.1.69
Alternative name(s):
    PTS system glucitol/sorbitol-specific EIIB component
    EII-Gut

Gene names

Name:	srlE
Synonyms:	gutE
Ordered Locus Names:	b2703, JW5430

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 glucitol/sorbitol transport.
Catalytic activity	Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.
Subcellular location	Cell inner membrane; Multi-pass membrane protein.
Domain	The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.
Sequence similarities	Contains 1 PTS EIIB type-5 domain.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein-N(PI)-phosphohistidine-sugar phosphotransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 319	319	Glucitol/sorbitol-specific phosphotransferase enzyme IIB component		PRO_0000186562
Regions
	Topological domain	1 – 176	176	Cytoplasmic Potential
	Transmembrane	177 – 197	21	Potential
	Topological domain	198 – 199	2	Periplasmic Potential
	Transmembrane	200 – 220	21	Potential
	Topological domain	221 – 228	8	Cytoplasmic Potential
	Transmembrane	229 – 249	21	Potential
	Topological domain	250 – 256	7	Periplasmic Potential
	Transmembrane	257 – 277	21	Potential
	Topological domain	278 – 296	19	Cytoplasmic Potential
	Transmembrane	297 – 317	21	Potential
	Topological domain	318 – 319	2	Periplasmic Potential
	Domain	1 – 178	178	PTS EIIB type-5
	Region	179 – 319	141	Unknown
Sites
	Active site	71	1	Phosphocysteine intermediate; for EIIB activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	P56580-1 [UniParc]. Last modified December 15, 1998. Version 1. Checksum: 3680B56EB625499F	FASTA	319	33,332
	10 20 30 40 50 60 MTHIRIEKGT GGWGGPLELK ATPGKKIVYI TAGTRPAIVD KLAQLTGWQA IDGFKEGEPA 70 80 90 100 110 120 EAEIGVAVID CGGTLRCGIY PKRRIPTINI HSTGKSGPLA QYIVEDIYVS GVKEENITVV 130 140 150 160 170 180 GDATPQPSSV GRDYDTSKKI TEQSDGLLAK VGMGMGSTVA VLFQSGRDTI DTVLKTILPF 190 200 210 220 230 240 MAFVSALIGI IMASGLGDWI AHGLAPLASH PLGLVMLALI CSFPLLSPFL GPGAVIAQVI 250 260 270 280 290 300 GVLIGVQIGL GNIPPHLALP ALFAINAQAA CDFIPVGLSL AEARQDTVRV GVPSVLVSRF 310 LTGAPTVLIA WFVSGFIYQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Glucitol-specific enzymes of the phosphotransferase system in Escherichia coli. Nucleotide sequence of the gut operon." Yamada M., Saier M.H. Jr. J. Biol. Chem. 262:5455-5463(1987) [PubMed: 3553176] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The glucitol permease of Escherichia coli: a tripartite permease of the phosphotransferase system." Reizer J., Reizer A., Yamada M., Saier M.H. Jr. Microbiology 144:1463-1464(1998) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
[3]	"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.
[4]	"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.
[5]	"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005." Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., Thomson N.R., Wishart D., Wanner B.L. Nucleic Acids Res. 34:1-9(2006) [PubMed: 16397293] [Abstract] Cited for: SEQUENCE REVISION TO 128 AND 230.
[6]	"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.
[7]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed: 15919996] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J02708 Genomic DNA. Translation: AAC13416.1. U00096 Genomic DNA. Translation: AAT48149.1. AP009048 Genomic DNA. Translation: BAA16564.2.
PIR	WQEC2S. A26725.
RefSeq	AP_003270.1. YP_026181.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P56580.
Protein family/group databases
TCDB	4.A.4.1.1. PTS glucitol (Gut) family.
Genome annotation databases
GeneID	948933.
GenomeReviews	Gene locus JW5430 in contig AP009048_GR. Gene locus b2703 in contig U00096_GR.
KEGG	ecj:JW5430. eco:b2703.
Organism-specific databases
EchoBASE	EB4116.
EcoGene	EG14373. srlE.
CMR	Search...
Phylogenomic databases
HOGENOM	P56580.
OMA	YPKKGIP.
Enzyme and pathway databases
BioCyc	EcoCyc:GUTA-MON.
Gene expression databases
Genevestigator	P56580.
Family and domain databases
InterPro	IPR011638. PTS_EIIBC_GUT_C. IPR011618. PTS_EIIBC_GUT_N. IPR004702. PTS_sorb_EIIBC. [Graphical view]
Pfam	PF07663. EIIBC-GUT_C. 1 hit. PF03612. EIIBC-GUT_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR00825. EIIBC-GUT. 1 hit.
PROSITE	PS51102. PTS_EIIB_TYPE_5. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PTHB_ECOLI

Accession

Primary (citable) accession number: P56580
Secondary accession number(s): P05705, P78103, P78215

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	December 15, 1998
Last modified:	November 3, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)