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PTS system glucose-specific EIICB component (EIICB-Glc) (EII-Glc) [Includes: Glucose permease IIC component (PTS system glucose-specific EIIC component); Glucose-specific phosphotransferase enzyme IIB component (EC 2.7.1.199) (PTS system glucose-specific EIIB component)]

 PTGCB_ECOLI             Reviewed;         477 AA.
P69786; P05053;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
25-OCT-2017, entry version 115.
RecName: Full=PTS system glucose-specific EIICB component {ECO:0000303|PubMed:3023349};
AltName: Full=EIICB-Glc {ECO:0000303|PubMed:3023349};
Short=EII-Glc {ECO:0000303|PubMed:3023349};
Includes:
RecName: Full=Glucose permease IIC component {ECO:0000303|PubMed:3023349};
AltName: Full=PTS system glucose-specific EIIC component {ECO:0000303|PubMed:3023349};
Includes:
RecName: Full=Glucose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:3129430};
EC=2.7.1.199 {ECO:0000269|PubMed:3129430};
AltName: Full=PTS system glucose-specific EIIB component {ECO:0000303|PubMed:3129430};
Name=ptsG; Synonyms=glcA, umg; OrderedLocusNames=b1101, JW1087;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-16, AND
SUBUNIT.
STRAIN=K12;
PubMed=3023349;
Erni B., Zanolari B.;
"Glucose permease of the bacterial phosphotransferase system. Gene
cloning, overproduction, and amino acid sequence of enzyme IIGlc.";
J. Biol. Chem. 261:16398-16403(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[3]
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).
[4]
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).
[5]
FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-204; CYS-326 AND
CYS-421, SUBCELLULAR LOCATION, AND ACTIVE SITE.
PubMed=3129430;
Nuoffer C., Zanolari B., Erni B.;
"Glucose permease of Escherichia coli. The effect of cysteine to
serine mutations on the function, stability, and regulation of
transport and phosphorylation.";
J. Biol. Chem. 263:6647-6655(1988).
[6]
PHOSPHORYLATION AT CYS-421.
PubMed=8505292;
Meins M., Jenoe P., Mueller D., Richter W.J., Rosenbusch J.P.,
Erni B.;
"Cysteine phosphorylation of the glucose transporter of Escherichia
coli.";
J. Biol. Chem. 268:11604-11609(1993).
[7]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[8]
FUNCTION, AND SUBUNIT.
PubMed=10562420; DOI=10.1006/abbi.1999.1458;
Zhuang J., Gutknecht R., Fluekiger K., Hasler L., Erni B., Engel A.;
"Purification and electron microscopic characterization of the
membrane subunit (IICB(Glc)) of the Escherichia coli glucose
transporter.";
Arch. Biochem. Biophys. 372:89-96(1999).
[9]
INDUCTION BY POST-TRANSCRIPTIONAL RNA REGULATION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15522088; DOI=10.1111/j.1365-2958.2004.04348.x;
Vanderpool C.K., Gottesman S.;
"Involvement of a novel transcriptional activator and small RNA in
post-transcriptional regulation of the glucose phosphoenolpyruvate
phosphotransferase system.";
Mol. Microbiol. 54:1076-1089(2004).
[10]
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).
[11]
ENZYME REGULATION, AND INDUCTION.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16549791; DOI=10.1073/pnas.0509638103;
Morita T., Mochizuki Y., Aiba H.;
"Translational repression is sufficient for gene silencing by
bacterial small noncoding RNAs in the absence of mRNA destruction.";
Proc. Natl. Acad. Sci. U.S.A. 103:4858-4863(2006).
[12]
STRUCTURE BY NMR OF 391-476.
PubMed=8112346; DOI=10.1111/j.1432-1033.1994.tb18576.x;
Golic Grdadolnik S., Eberstadt M., Gemmecker G., Kessler H., Buhr A.,
Erni B.;
"The glucose transporter of Escherichia coli. Assignment of the 1H,
13C and 15N resonances and identification of the secondary structure
of the soluble IIB domain.";
Eur. J. Biochem. 219:945-952(1994).
[13]
STRUCTURE BY NMR OF 386-477.
PubMed=8784182; DOI=10.1021/bi960492l;
Eberstadt M., Golic Grdadolnik S., Gemmecker G., Kessler H., Buhr A.,
Erni B.;
"Solution structure of the IIB domain of the glucose transporter of
Escherichia coli.";
Biochemistry 35:11286-11292(1996).
[14]
STRUCTURE BY NMR OF 386-477.
PubMed=9200688; DOI=10.1021/bi963053v;
Gemmecker G., Eberstadt M., Buhr A., Lanz R., Golic Grdadolnik S.,
Kessler H., Erni B.;
"Glucose transporter of Escherichia coli: NMR characterization of the
phosphocysteine form of the IIB(Glc) domain and its binding interface
with the IIA(Glc) subunit.";
Biochemistry 36:7408-7417(1997).
[15]
STRUCTURE BY NMR OF 387-476, ACTIVE SITE, SUBUNIT, AND REACTION
MECHANISM.
PubMed=12716891; DOI=10.1074/jbc.M302677200;
Cai M., Williams D.C. Jr., Wang G., Lee B.R., Peterkofsky A.,
Clore G.M.;
"Solution structure of the phosphoryl transfer complex between the
signal-transducing protein IIAGlucose and the cytoplasmic domain of
the glucose transporter IICBGlucose of the Escherichia coli glucose
phosphotransferase system.";
J. Biol. Chem. 278:25191-25206(2003).
[16]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 396-477 IN COMPLEX WITH MLC,
FUNCTION, MUTAGENESIS OF VAL-449; ALA-451 AND GLN-456, ACTIVE SITE,
AND SUBUNIT.
PubMed=18319344; DOI=10.1073/pnas.0709295105;
Nam T.W., Jung H.I., An Y.J., Park Y.H., Lee S.H., Seok Y.J.,
Cha S.S.;
"Analyses of Mlc-IIBGlc interaction and a plausible molecular
mechanism of Mlc inactivation by membrane sequestration.";
Proc. Natl. Acad. Sci. U.S.A. 105:3751-3756(2008).
-!- 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 PtsG and Crr is
involved in glucose transport (PubMed:3129430, PubMed:10562420).
Also functions as a chemoreceptor monitoring the environment for
changes in sugar concentration and an effector modulating the
activity of the transcriptional repressor Mlc (PubMed:18319344).
{ECO:0000269|PubMed:10562420, ECO:0000269|PubMed:18319344,
ECO:0000269|PubMed:3129430}.
-!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + D-
glucose(Side 1) = [protein]-L-histidine + D-glucose 6-
phosphate(Side 2). {ECO:0000269|PubMed:3129430}.
-!- ENZYME REGULATION: Transporter activity may be inhibited by SgrT.
{ECO:0000269|PubMed:16549791}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10562420,
ECO:0000269|PubMed:12716891, ECO:0000269|PubMed:18319344,
ECO:0000305|PubMed:3023349}.
-!- INTERACTION:
P50456:mlc; NbExp=3; IntAct=EBI-903497, EBI-1116104;
-!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
ProRule:PRU00426, ECO:0000305|PubMed:3129430}; Multi-pass membrane
protein {ECO:0000255|PROSITE-ProRule:PRU00426}.
-!- INDUCTION: The ptsG transcript is degraded under conditions of
glucose-phosphate stress (due to intracellular accumulation of
glucose-6-phosphate caused by disruption of glycolytic flux), or
in the presence of (toxic) non-metabolizable glucose phosphate
analogs due to hybridization with the small RNA sgrS (originally
known as ryaA). This hybridization is sufficient to repress mRNA
translation (PubMed:16549791). The hybrid is subsequently degraded
by RNase E. This reduces the quantity of transporter and relieves
glucose phosphate stress. {ECO:0000269|PubMed:15522088,
ECO:0000269|PubMed:16549791}.
-!- 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:PRU00421}.
-!- DOMAIN: The EIIC domain forms the PTS system translocation channel
and contains the specific substrate-binding site.
{ECO:0000255|PROSITE-ProRule:PRU00426}.
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EMBL; J02618; AAA24437.1; -; Genomic_DNA.
EMBL; U00096; AAC74185.1; -; Genomic_DNA.
EMBL; AP009048; BAA35908.1; -; Genomic_DNA.
PIR; A25336; WQEC2G.
RefSeq; NP_415619.1; NC_000913.3.
RefSeq; WP_000475719.1; NZ_LN832404.1.
PDB; 1IBA; NMR; -; A=391-476.
PDB; 1O2F; NMR; -; B=387-476.
PDB; 3BP3; X-ray; 1.65 A; A/B=396-477.
PDB; 3BP8; X-ray; 2.85 A; C/D=401-475.
PDBsum; 1IBA; -.
PDBsum; 1O2F; -.
PDBsum; 3BP3; -.
PDBsum; 3BP8; -.
ProteinModelPortal; P69786; -.
SMR; P69786; -.
BioGrid; 4260940; 8.
DIP; DIP-29833N; -.
IntAct; P69786; 3.
STRING; 316385.ECDH10B_1173; -.
MoonProt; P69786; -.
TCDB; 4.A.1.1.1; the pts glucose-glucoside (glc) family.
iPTMnet; P69786; -.
PaxDb; P69786; -.
PRIDE; P69786; -.
EnsemblBacteria; AAC74185; AAC74185; b1101.
EnsemblBacteria; BAA35908; BAA35908; BAA35908.
GeneID; 945651; -.
KEGG; ecj:JW1087; -.
KEGG; eco:b1101; -.
PATRIC; fig|1411691.4.peg.1167; -.
EchoBASE; EB0780; -.
EcoGene; EG10787; ptsG.
eggNOG; ENOG4105CI1; Bacteria.
eggNOG; COG1263; LUCA.
eggNOG; COG1264; LUCA.
HOGENOM; HOG000250993; -.
KO; K02778; -.
KO; K02779; -.
PhylomeDB; P69786; -.
BioCyc; EcoCyc:PTSG-MONOMER; -.
BioCyc; MetaCyc:PTSG-MONOMER; -.
EvolutionaryTrace; P69786; -.
PRO; PR:P69786; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0005355; F:glucose transmembrane transporter activity; IEA:InterPro.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
GO; GO:0090564; F:protein-phosphocysteine-glucose phosphotransferase system transporter activity; IMP:EcoCyc.
GO; GO:0015758; P:glucose transport; IMP:CACAO.
GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:EcoCyc.
CDD; cd00212; PTS_IIB_glc; 1.
Gene3D; 3.30.1360.60; -; 1.
InterPro; IPR036878; Glu_permease_IIB.
InterPro; IPR018113; PTrfase_EIIB_Cys.
InterPro; IPR003352; PTS_EIIC.
InterPro; IPR013013; PTS_EIIC_1.
InterPro; IPR001996; PTS_IIB_1.
InterPro; IPR011299; PTS_IIBC_glc.
InterPro; IPR004719; PTS_maltose/Glc_sub_IIC.
Pfam; PF00367; PTS_EIIB; 1.
Pfam; PF02378; PTS_EIIC; 1.
SUPFAM; SSF55604; SSF55604; 1.
TIGRFAMs; TIGR00826; EIIB_glc; 1.
TIGRFAMs; TIGR00852; pts-Glc; 1.
TIGRFAMs; TIGR02002; PTS-II-BC-glcB; 1.
PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Complete proteome;
Direct protein sequencing; Kinase; Membrane; Phosphoprotein;
Phosphotransferase system; Reference proteome; Sugar transport;
Transferase; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 477 PTS system glucose-specific EIICB
component.
/FTId=PRO_0000186528.
TOPO_DOM 1 14 Cytoplasmic. {ECO:0000255}.
TRANSMEM 15 35 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 36 50 Periplasmic. {ECO:0000255}.
TRANSMEM 51 71 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 72 79 Cytoplasmic. {ECO:0000255}.
TRANSMEM 80 100 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 101 111 Periplasmic. {ECO:0000255}.
TRANSMEM 112 132 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 133 151 Cytoplasmic. {ECO:0000255}.
TRANSMEM 152 172 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 173 190 Periplasmic. {ECO:0000255}.
TRANSMEM 191 211 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 212 249 Cytoplasmic. {ECO:0000255}.
TRANSMEM 250 270 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 271 279 Periplasmic. {ECO:0000255}.
TRANSMEM 280 300 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 301 309 Cytoplasmic. {ECO:0000255}.
TRANSMEM 310 330 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 331 355 Periplasmic. {ECO:0000255}.
TRANSMEM 356 376 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 377 477 Cytoplasmic. {ECO:0000255}.
DOMAIN 1 388 PTS EIIC type-1. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
DOMAIN 399 477 PTS EIIB type-1. {ECO:0000255|PROSITE-
ProRule:PRU00421}.
ACT_SITE 421 421 Phosphocysteine intermediate; for EIIB
activity. {ECO:0000255|PROSITE-
ProRule:PRU00421,
ECO:0000305|PubMed:12716891,
ECO:0000305|PubMed:18319344,
ECO:0000305|PubMed:3129430}.
MOD_RES 421 421 Phosphocysteine.
{ECO:0000269|PubMed:8505292}.
MUTAGEN 204 204 C->S: Destabilizes the protein structure;
when associated with S-326.
{ECO:0000269|PubMed:3129430}.
MUTAGEN 326 326 C->S: Destabilizes the protein structure;
when associated with S-204.
{ECO:0000269|PubMed:3129430}.
MUTAGEN 421 421 C->S: Unable to be phosphorylated and to
catalyze the phosphoryl exchange between
glucose and glucose 6-phosphate at
equilibrium.
{ECO:0000269|PubMed:3129430}.
MUTAGEN 449 449 V->Q: Interaction with Mlc is hardly
detectable.
{ECO:0000269|PubMed:18319344}.
MUTAGEN 451 451 A->F: The complex with mlc shows much
weaker association than the wild-type.
{ECO:0000269|PubMed:18319344}.
MUTAGEN 456 456 Q->A: Interaction with Mlc is hardly
detectable.
{ECO:0000269|PubMed:18319344}.
HELIX 401 408 {ECO:0000244|PDB:3BP3}.
HELIX 412 414 {ECO:0000244|PDB:3BP3}.
STRAND 415 420 {ECO:0000244|PDB:3BP3}.
STRAND 422 430 {ECO:0000244|PDB:3BP3}.
HELIX 432 434 {ECO:0000244|PDB:3BP3}.
HELIX 437 442 {ECO:0000244|PDB:3BP3}.
STRAND 446 451 {ECO:0000244|PDB:3BP3}.
STRAND 454 458 {ECO:0000244|PDB:3BP3}.
HELIX 460 462 {ECO:0000244|PDB:3BP3}.
HELIX 463 475 {ECO:0000244|PDB:3BP3}.
SEQUENCE 477 AA; 50677 MW; D97A80FD64B74F73 CRC64;
MFKNAFANLQ KVGKSLMLPV SVLPIAGILL GVGSANFSWL PAVVSHVMAE AGGSVFANMP
LIFAIGVALG FTNNDGVSAL AAVVAYGIMV KTMAVVAPLV LHLPAEEIAS KHLADTGVLG
GIISGAIAAY MFNRFYRIKL PEYLGFFAGK RFVPIISGLA AIFTGVVLSF IWPPIGSAIQ
TFSQWAAYQN PVVAFGIYGF IERCLVPFGL HHIWNVPFQM QIGEYTNAAG QVFHGDIPRY
MAGDPTAGKL SGGFLFKMYG LPAAAIAIWH SAKPENRAKV GGIMISAALT SFLTGITEPI
EFSFMFVAPI LYIIHAILAG LAFPICILLG MRDGTSFSHG LIDFIVLSGN SSKLWLFPIV
GIGYAIVYYT IFRVLIKALD LKTPGREDAT EDAKATGTSE MAPALVAAFG GKENITNLDA
CITRLRVSVA DVSKVDQAGL KKLGAAGVVV AGSGVQAIFG TKSDNLKTEM DEYIRNH


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