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PTS system glucitol/sorbitol-specific EIIB component (EC 2.7.1.198) (EII-Gut) (Enzyme II-Gut) (Glucitol/sorbitol-specific phosphotransferase enzyme IIB component)

 PTHB_ECOLI              Reviewed;         319 AA.
P56580; P05705; P78103; P78215;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 1.
28-MAR-2018, entry version 141.
RecName: Full=PTS system glucitol/sorbitol-specific EIIB component {ECO:0000303|PubMed:3553176};
EC=2.7.1.198 {ECO:0000269|PubMed:1100608};
AltName: Full=EII-Gut {ECO:0000303|PubMed:3553176};
AltName: Full=Enzyme II-Gut {ECO:0000303|PubMed:3553176};
AltName: Full=Glucitol/sorbitol-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:3553176};
Name=srlE; Synonyms=gutA {ECO:0000303|PubMed:3553176}, gutE;
OrderedLocusNames=b2703, JW5430;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
PubMed=3553176;
Yamada M., Saier M.H. Jr.;
"Glucitol-specific enzymes of the phosphotransferase system in
Escherichia coli. Nucleotide sequence of the gut operon.";
J. Biol. Chem. 262:5455-5463(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
Reizer J., Reizer A., Yamada M., Saier M.H. Jr.;
"The glucitol permease of Escherichia coli: a tripartite permease of
the phosphotransferase system.";
Microbiology 144:1463-1464(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9205837; DOI=10.1093/dnares/4.2.91;
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.;
"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.";
DNA Res. 4:91-113(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
SEQUENCE REVISION TO 128 AND 230.
PubMed=16397293; DOI=10.1093/nar/gkj405;
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.;
"Escherichia coli K-12: a cooperatively developed annotation snapshot
-- 2005.";
Nucleic Acids Res. 34:1-9(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[7]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBSTRATE SPECIFICITY.
PubMed=1100608;
Lengeler J.;
"Nature and properties of hexitol transport systems in Escherichia
coli.";
J. Bacteriol. 124:39-47(1975).
[8]
INDUCTION.
PubMed=3062173; DOI=10.1016/0022-2836(88)90193-3;
Yamada M., Saier M.H. Jr.;
"Positive and negative regulators for glucitol (gut) operon expression
in Escherichia coli.";
J. Mol. Biol. 203:569-583(1988).
[9]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
-!- 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. The enzyme II complex composed of SrlA, SrlB and SrlE is
involved in glucitol/sorbitol transport. It can also use D-
mannitol. {ECO:0000269|PubMed:1100608}.
-!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + D-
sorbitol(Side 1) = [protein]-L-histidine + D-sorbitol 6-
phosphate(Side 2). {ECO:0000269|PubMed:1100608}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=44 uM for D-glucitol {ECO:0000269|PubMed:1100608};
KM=60 uM for D-mannitol {ECO:0000269|PubMed:1100608};
Vmax=7.2 nmol/min/mg enzyme with D-mannitol as substrate
{ECO:0000269|PubMed:1100608};
Vmax=0.83 nmol/min/mg enzyme with D-glucitol as substrate
{ECO:0000269|PubMed:1100608};
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000305|PubMed:3553176}; Multi-pass membrane protein
{ECO:0000255, ECO:0000305|PubMed:3553176}.
-!- INDUCTION: Regulated by an unusual system which consists of the
activator GutM and the repressor GutR in addition to the cAMP-CRP
complex. {ECO:0000269|PubMed:3062173}.
-!- 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.
{ECO:0000255|PROSITE-ProRule:PRU00425}.
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EMBL; J02708; AAC13416.1; -; Genomic_DNA.
EMBL; U00096; AAT48149.1; -; Genomic_DNA.
EMBL; AP009048; BAA16564.2; -; Genomic_DNA.
PIR; A26725; WQEC2S.
RefSeq; WP_000148878.1; NZ_LN832404.1.
RefSeq; YP_026181.1; NC_000913.3.
ProteinModelPortal; P56580; -.
SMR; P56580; -.
BioGrid; 4262075; 19.
STRING; 316385.ECDH10B_2871; -.
TCDB; 4.A.4.1.1; the pts glucitol (gut) family.
PaxDb; P56580; -.
PRIDE; P56580; -.
EnsemblBacteria; AAT48149; AAT48149; b2703.
EnsemblBacteria; BAA16564; BAA16564; BAA16564.
GeneID; 948933; -.
KEGG; ecj:JW5430; -.
KEGG; eco:b2703; -.
PATRIC; fig|1411691.4.peg.4039; -.
EchoBASE; EB4116; -.
EcoGene; EG14373; srlE.
eggNOG; ENOG4105DZY; Bacteria.
eggNOG; COG3732; LUCA.
HOGENOM; HOG000242653; -.
InParanoid; P56580; -.
KO; K02782; -.
KO; K02783; -.
OMA; HKFIYIT; -.
PhylomeDB; P56580; -.
BioCyc; EcoCyc:GUTA-MONOMER; -.
BioCyc; MetaCyc:GUTA-MONOMER; -.
PRO; PR:P56580; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IDA:UniProtKB.
GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:UniProtKB.
InterPro; IPR011638; PTS_EIIBC_GUT_C.
InterPro; IPR011618; PTS_EIIBC_GUT_N.
InterPro; IPR004702; PTS_sorb_EIIBC.
PANTHER; PTHR39427; PTHR39427; 1.
Pfam; PF07663; EIIBC-GUT_C; 1.
Pfam; PF03612; EIIBC-GUT_N; 1.
TIGRFAMs; TIGR00825; EIIBC-GUT; 1.
PROSITE; PS51102; PTS_EIIB_TYPE_5; 1.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Complete proteome; Kinase;
Membrane; Phosphoprotein; Phosphotransferase system;
Reference proteome; Sugar transport; Transferase; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 319 PTS system glucitol/sorbitol-specific
EIIB component.
/FTId=PRO_0000186562.
TOPO_DOM 1 176 Cytoplasmic. {ECO:0000255}.
TRANSMEM 177 197 Helical. {ECO:0000255}.
TOPO_DOM 198 199 Periplasmic. {ECO:0000255}.
TRANSMEM 200 220 Helical. {ECO:0000255}.
TOPO_DOM 221 228 Cytoplasmic. {ECO:0000255}.
TRANSMEM 229 249 Helical. {ECO:0000255}.
TOPO_DOM 250 256 Periplasmic. {ECO:0000255}.
TRANSMEM 257 277 Helical. {ECO:0000255}.
TOPO_DOM 278 296 Cytoplasmic. {ECO:0000255}.
TRANSMEM 297 317 Helical. {ECO:0000255}.
TOPO_DOM 318 319 Periplasmic. {ECO:0000255}.
DOMAIN 1 178 PTS EIIB type-5. {ECO:0000255|PROSITE-
ProRule:PRU00425}.
ACT_SITE 71 71 Phosphocysteine intermediate; for EIIB
activity. {ECO:0000305}.
MOD_RES 71 71 Phosphocysteine; by EIIA.
{ECO:0000255|PROSITE-ProRule:PRU00425}.
SEQUENCE 319 AA; 33332 MW; 3680B56EB625499F CRC64;
MTHIRIEKGT GGWGGPLELK ATPGKKIVYI TAGTRPAIVD KLAQLTGWQA IDGFKEGEPA
EAEIGVAVID CGGTLRCGIY PKRRIPTINI HSTGKSGPLA QYIVEDIYVS GVKEENITVV
GDATPQPSSV GRDYDTSKKI TEQSDGLLAK VGMGMGSTVA VLFQSGRDTI DTVLKTILPF
MAFVSALIGI IMASGLGDWI AHGLAPLASH PLGLVMLALI CSFPLLSPFL GPGAVIAQVI
GVLIGVQIGL GNIPPHLALP ALFAINAQAA CDFIPVGLSL AEARQDTVRV GVPSVLVSRF
LTGAPTVLIA WFVSGFIYQ


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