PTGCB_ECOLI
ID PTGCB_ECOLI Reviewed; 477 AA.
AC P69786; P05053;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=PTS system glucose-specific EIICB component {ECO:0000303|PubMed:3023349};
DE AltName: Full=EIICB-Glc {ECO:0000303|PubMed:3023349};
DE Short=EII-Glc {ECO:0000303|PubMed:3023349};
DE Includes:
DE RecName: Full=Glucose permease IIC component {ECO:0000303|PubMed:3023349};
DE AltName: Full=PTS system glucose-specific EIIC component {ECO:0000303|PubMed:3023349};
DE Includes:
DE RecName: Full=Glucose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:3129430};
DE EC=2.7.1.199 {ECO:0000269|PubMed:3129430};
DE AltName: Full=PTS system glucose-specific EIIB component {ECO:0000303|PubMed:3129430};
GN Name=ptsG; Synonyms=glcA, umg; OrderedLocusNames=b1101, JW1087;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-16, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=3023349; DOI=10.1016/s0021-9258(18)66579-2;
RA Erni B., Zanolari B.;
RT "Glucose permease of the bacterial phosphotransferase system. Gene cloning,
RT overproduction, and amino acid sequence of enzyme IIGlc.";
RL J. Biol. Chem. 261:16398-16403(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-204; CYS-326 AND CYS-421,
RP SUBCELLULAR LOCATION, AND ACTIVE SITE.
RX PubMed=3129430; DOI=10.1016/s0021-9258(18)68691-0;
RA Nuoffer C., Zanolari B., Erni B.;
RT "Glucose permease of Escherichia coli. The effect of cysteine to serine
RT mutations on the function, stability, and regulation of transport and
RT phosphorylation.";
RL J. Biol. Chem. 263:6647-6655(1988).
RN [6]
RP PHOSPHORYLATION AT CYS-421.
RX PubMed=8505292; DOI=10.1016/s0021-9258(19)50244-7;
RA Meins M., Jenoe P., Mueller D., Richter W.J., Rosenbusch J.P., Erni B.;
RT "Cysteine phosphorylation of the glucose transporter of Escherichia coli.";
RL J. Biol. Chem. 268:11604-11609(1993).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=10562420; DOI=10.1006/abbi.1999.1458;
RA Zhuang J., Gutknecht R., Fluekiger K., Hasler L., Erni B., Engel A.;
RT "Purification and electron microscopic characterization of the membrane
RT subunit (IICB(Glc)) of the Escherichia coli glucose transporter.";
RL Arch. Biochem. Biophys. 372:89-96(1999).
RN [9]
RP INDUCTION BY POST-TRANSCRIPTIONAL RNA REGULATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15522088; DOI=10.1111/j.1365-2958.2004.04348.x;
RA Vanderpool C.K., Gottesman S.;
RT "Involvement of a novel transcriptional activator and small RNA in post-
RT transcriptional regulation of the glucose phosphoenolpyruvate
RT phosphotransferase system.";
RL Mol. Microbiol. 54:1076-1089(2004).
RN [10]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [11]
RP ACTIVITY REGULATION, AND INDUCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16549791; DOI=10.1073/pnas.0509638103;
RA Morita T., Mochizuki Y., Aiba H.;
RT "Translational repression is sufficient for gene silencing by bacterial
RT small noncoding RNAs in the absence of mRNA destruction.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:4858-4863(2006).
RN [12]
RP RECEPTOR FOR CDI TOXIN ENTRY INTO TARGET CELL CYTOPLASM (MICROBIAL
RP INFECTION), DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-421.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=26305955; DOI=10.1073/pnas.1512124112;
RA Willett J.L., Gucinski G.C., Fatherree J.P., Low D.A., Hayes C.S.;
RT "Contact-dependent growth inhibition toxins exploit multiple independent
RT cell-entry pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11341-11346(2015).
RN [13]
RP RECEPTOR FOR CDI TOXIN ENTRY INTO TARGET CELL CYTOPLASM (MICROBIAL
RP INFECTION), AND DISRUPTION PHENOTYPE.
RC STRAIN=EPI100;
RX PubMed=28351921; DOI=10.1128/mbio.00290-17;
RA Ruhe Z.C., Nguyen J.Y., Xiong J., Koskiniemi S., Beck C.M., Perkins B.R.,
RA Low D.A., Hayes C.S.;
RT "CdiA effectors use modular receptor-binding domains to recognize target
RT bacteria.";
RL MBio 8:0-0(2017).
RN [14]
RP STRUCTURE BY NMR OF 391-476.
RX PubMed=8112346; DOI=10.1111/j.1432-1033.1994.tb18576.x;
RA Golic Grdadolnik S., Eberstadt M., Gemmecker G., Kessler H., Buhr A.,
RA Erni B.;
RT "The glucose transporter of Escherichia coli. Assignment of the 1H, 13C and
RT 15N resonances and identification of the secondary structure of the soluble
RT IIB domain.";
RL Eur. J. Biochem. 219:945-952(1994).
RN [15]
RP STRUCTURE BY NMR OF 386-477.
RX PubMed=8784182; DOI=10.1021/bi960492l;
RA Eberstadt M., Golic Grdadolnik S., Gemmecker G., Kessler H., Buhr A.,
RA Erni B.;
RT "Solution structure of the IIB domain of the glucose transporter of
RT Escherichia coli.";
RL Biochemistry 35:11286-11292(1996).
RN [16]
RP STRUCTURE BY NMR OF 386-477.
RX PubMed=9200688; DOI=10.1021/bi963053v;
RA Gemmecker G., Eberstadt M., Buhr A., Lanz R., Golic Grdadolnik S.,
RA Kessler H., Erni B.;
RT "Glucose transporter of Escherichia coli: NMR characterization of the
RT phosphocysteine form of the IIB(Glc) domain and its binding interface with
RT the IIA(Glc) subunit.";
RL Biochemistry 36:7408-7417(1997).
RN [17]
RP STRUCTURE BY NMR OF 387-476, ACTIVE SITE, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=12716891; DOI=10.1074/jbc.m302677200;
RA Cai M., Williams D.C. Jr., Wang G., Lee B.R., Peterkofsky A., Clore G.M.;
RT "Solution structure of the phosphoryl transfer complex between the signal-
RT transducing protein IIAGlucose and the cytoplasmic domain of the glucose
RT transporter IICBGlucose of the Escherichia coli glucose phosphotransferase
RT system.";
RL J. Biol. Chem. 278:25191-25206(2003).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 396-477 IN COMPLEX WITH MLC,
RP FUNCTION, MUTAGENESIS OF VAL-449; ALA-451 AND GLN-456, ACTIVE SITE, AND
RP SUBUNIT.
RX PubMed=18319344; DOI=10.1073/pnas.0709295105;
RA Nam T.W., Jung H.I., An Y.J., Park Y.H., Lee S.H., Seok Y.J., Cha S.S.;
RT "Analyses of Mlc-IIBGlc interaction and a plausible molecular mechanism of
RT Mlc inactivation by membrane sequestration.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3751-3756(2008).
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (sugar PTS), a major carbohydrate active transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane. The
CC enzyme II complex composed of PtsG and Crr is involved in glucose
CC transport (PubMed:3129430, PubMed:10562420). Also functions as a
CC chemoreceptor monitoring the environment for changes in sugar
CC concentration and an effector modulating the activity of the
CC transcriptional repressor Mlc (PubMed:18319344).
CC {ECO:0000269|PubMed:10562420, ECO:0000269|PubMed:18319344,
CC ECO:0000269|PubMed:3129430}.
CC -!- FUNCTION: (Microbial infection) Probably transports the toxic C-
CC terminal region of CdiA from E.coli strains NC101 and 3006 across the
CC inner membrane to the cytoplasm, where CdiA degrades specific tRNAs.
CC Toxin transport is strain-specific, mutations in this gene do not
CC confer resistance to several other tested CdiA toxins
CC (PubMed:26305955). Probably also serves as the inner membrane receptor
CC for CdiA-STECO31 from E.coli strain STEC_O31 (Probable).
CC {ECO:0000269|PubMed:26305955, ECO:0000305|PubMed:28351921}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC glucose 6-phosphate(in) + L-histidyl-[protein]; Xref=Rhea:RHEA:33367,
CC Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:61548, ChEBI:CHEBI:64837;
CC EC=2.7.1.199; Evidence={ECO:0000269|PubMed:3129430};
CC -!- ACTIVITY REGULATION: Transporter activity may be inhibited by SgrT.
CC {ECO:0000269|PubMed:16549791}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10562420,
CC ECO:0000269|PubMed:12716891, ECO:0000269|PubMed:18319344,
CC ECO:0000305|PubMed:3023349}.
CC -!- INTERACTION:
CC P69786; P50456: mlc; NbExp=3; IntAct=EBI-903497, EBI-1116104;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426, ECO:0000269|PubMed:15919996,
CC ECO:0000305|PubMed:3129430}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00426, ECO:0000305|PubMed:15919996}.
CC -!- INDUCTION: The ptsG transcript is degraded under conditions of glucose-
CC phosphate stress (due to intracellular accumulation of glucose-6-
CC phosphate caused by disruption of glycolytic flux), or in the presence
CC of (toxic) non-metabolizable glucose phosphate analogs due to
CC hybridization with the small RNA sgrS (originally known as ryaA). This
CC hybridization is sufficient to repress mRNA translation
CC (PubMed:16549791). The hybrid is subsequently degraded by RNase E. This
CC reduces the quantity of transporter and relieves glucose phosphate
CC stress. {ECO:0000269|PubMed:15522088, ECO:0000269|PubMed:16549791}.
CC -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC cysteinyl or histidyl residue, depending on the transported sugar.
CC Then, it transfers the phosphoryl group to the sugar substrate
CC concomitantly with the sugar uptake processed by the EIIC domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00421}.
CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site. {ECO:0000255|PROSITE-
CC ProRule:PRU00426}.
CC -!- DISRUPTION PHENOTYPE: Disruption confers resistance to cellular
CC contact-dependent growth inhibition (CDI) CdiA of E.coli strains NC101
CC and 3006, but not to several other tested CdiA toxins
CC (PubMed:26305955). Disruption confers resistance to cellular contact-
CC dependent growth inhibition (CDI) CdiA-STECO31 of E.coli strain
CC STEC_O31 (PubMed:28351921). {ECO:0000269|PubMed:26305955,
CC ECO:0000269|PubMed:28351921}.
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DR EMBL; J02618; AAA24437.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74185.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35908.1; -; Genomic_DNA.
DR PIR; A25336; WQEC2G.
DR RefSeq; NP_415619.1; NC_000913.3.
DR RefSeq; WP_000475719.1; NZ_STEB01000016.1.
DR PDB; 1IBA; NMR; -; A=391-476.
DR PDB; 1O2F; NMR; -; B=387-476.
DR PDB; 3BP3; X-ray; 1.65 A; A/B=396-477.
DR PDB; 3BP8; X-ray; 2.85 A; C/D=401-475.
DR PDBsum; 1IBA; -.
DR PDBsum; 1O2F; -.
DR PDBsum; 3BP3; -.
DR PDBsum; 3BP8; -.
DR AlphaFoldDB; P69786; -.
DR SMR; P69786; -.
DR BioGRID; 4260940; 16.
DR ComplexPortal; CPX-2242; mlc-EIIB transcriptional regulator complex.
DR ComplexPortal; CPX-5943; Glucose-specific enzyme II complex.
DR DIP; DIP-29833N; -.
DR IntAct; P69786; 3.
DR STRING; 511145.b1101; -.
DR MoonProt; P69786; -.
DR TCDB; 4.A.1.1.1; the pts glucose-glucoside (glc) family.
DR iPTMnet; P69786; -.
DR jPOST; P69786; -.
DR PaxDb; P69786; -.
DR PRIDE; P69786; -.
DR EnsemblBacteria; AAC74185; AAC74185; b1101.
DR EnsemblBacteria; BAA35908; BAA35908; BAA35908.
DR GeneID; 66670633; -.
DR GeneID; 945651; -.
DR KEGG; ecj:JW1087; -.
DR KEGG; eco:b1101; -.
DR PATRIC; fig|1411691.4.peg.1167; -.
DR EchoBASE; EB0780; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_1_0_6; -.
DR OMA; AWAFNRF; -.
DR PhylomeDB; P69786; -.
DR BioCyc; EcoCyc:PTSG-MON; -.
DR BioCyc; MetaCyc:PTSG-MON; -.
DR BRENDA; 2.7.1.199; 2026.
DR EvolutionaryTrace; P69786; -.
DR PRO; PR:P69786; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:1902495; C:transmembrane transporter complex; IPI:ComplexPortal.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0090564; F:protein-phosphocysteine-glucose phosphotransferase system transporter activity; IMP:EcoCyc.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:1904659; P:glucose transmembrane transport; IMP:CACAO.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:ComplexPortal.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:ComplexPortal.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR CDD; cd00212; PTS_IIB_glc; 1.
DR Gene3D; 3.30.1360.60; -; 1.
DR InterPro; IPR036878; Glu_permease_IIB.
DR InterPro; IPR018113; PTrfase_EIIB_Cys.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR001996; PTS_IIB_1.
DR InterPro; IPR011299; PTS_IIBC_glc.
DR InterPro; IPR004719; PTS_maltose/Glc_sub_IIC.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF55604; SSF55604; 1.
DR TIGRFAMs; TIGR00826; EIIB_glc; 1.
DR TIGRFAMs; TIGR00852; pts-Glc; 1.
DR TIGRFAMs; TIGR02002; PTS-II-BC-glcB; 1.
DR PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Kinase; Membrane; Phosphoprotein;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..477
FT /note="PTS system glucose-specific EIICB component"
FT /id="PRO_0000186528"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 36..50
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 72..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 101..111
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 133..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 173..190
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 212..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 271..279
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 301..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 331..355
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 377..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 1..388
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 399..477
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 421
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421,
FT ECO:0000305|PubMed:12716891, ECO:0000305|PubMed:18319344,
FT ECO:0000305|PubMed:3129430"
FT MOD_RES 421
FT /note="Phosphocysteine"
FT /evidence="ECO:0000269|PubMed:8505292"
FT MUTAGEN 204
FT /note="C->S: Destabilizes the protein structure; when
FT associated with S-326."
FT /evidence="ECO:0000269|PubMed:3129430"
FT MUTAGEN 326
FT /note="C->S: Destabilizes the protein structure; when
FT associated with S-204."
FT /evidence="ECO:0000269|PubMed:3129430"
FT MUTAGEN 421
FT /note="C->S: Unable to be phosphorylated and to catalyze
FT the phosphoryl exchange between glucose and glucose 6-
FT phosphate at equilibrium. Remains susceptible to CdiA toxin
FT from E.coli strain 3006."
FT /evidence="ECO:0000269|PubMed:26305955,
FT ECO:0000269|PubMed:3129430"
FT MUTAGEN 449
FT /note="V->Q: Interaction with Mlc is hardly detectable."
FT /evidence="ECO:0000269|PubMed:18319344"
FT MUTAGEN 451
FT /note="A->F: The complex with mlc shows much weaker
FT association than the wild-type."
FT /evidence="ECO:0000269|PubMed:18319344"
FT MUTAGEN 456
FT /note="Q->A: Interaction with Mlc is hardly detectable."
FT /evidence="ECO:0000269|PubMed:18319344"
FT HELIX 401..408
FT /evidence="ECO:0007829|PDB:3BP3"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:3BP3"
FT STRAND 415..420
FT /evidence="ECO:0007829|PDB:3BP3"
FT STRAND 422..430
FT /evidence="ECO:0007829|PDB:3BP3"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:3BP3"
FT HELIX 437..442
FT /evidence="ECO:0007829|PDB:3BP3"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:3BP3"
FT STRAND 454..458
FT /evidence="ECO:0007829|PDB:3BP3"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:3BP3"
FT HELIX 463..475
FT /evidence="ECO:0007829|PDB:3BP3"
SQ 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
