PTHB_ECOLI
ID PTHB_ECOLI Reviewed; 319 AA.
AC P56580; P05705; P78103; P78215;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=PTS system glucitol/sorbitol-specific EIIB component {ECO:0000303|PubMed:3553176};
DE EC=2.7.1.198 {ECO:0000269|PubMed:1100608};
DE AltName: Full=EII-Gut {ECO:0000303|PubMed:3553176};
DE AltName: Full=Enzyme II-Gut {ECO:0000303|PubMed:3553176};
DE AltName: Full=Glucitol/sorbitol-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:3553176};
GN Name=srlE; Synonyms=gutA {ECO:0000303|PubMed:3553176}, gutE;
GN OrderedLocusNames=b2703, JW5430;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=3553176; DOI=10.1016/s0021-9258(18)45594-9;
RA Yamada M., Saier M.H. Jr.;
RT "Glucitol-specific enzymes of the phosphotransferase system in Escherichia
RT coli. Nucleotide sequence of the gut operon.";
RL J. Biol. Chem. 262:5455-5463(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RA Reizer J., Reizer A., Yamada M., Saier M.H. Jr.;
RT "The glucitol permease of Escherichia coli: a tripartite permease of the
RT phosphotransferase system.";
RL Microbiology 144:1463-1464(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
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 [5]
RP SEQUENCE REVISION TO 128 AND 230.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=1100608; DOI=10.1128/jb.124.1.39-47.1975;
RA Lengeler J.;
RT "Nature and properties of hexitol transport systems in Escherichia coli.";
RL J. Bacteriol. 124:39-47(1975).
RN [8]
RP INDUCTION.
RX PubMed=3062173; DOI=10.1016/0022-2836(88)90193-3;
RA Yamada M., Saier M.H. Jr.;
RT "Positive and negative regulators for glucitol (gut) operon expression in
RT Escherichia coli.";
RL J. Mol. Biol. 203:569-583(1988).
RN [9]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
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).
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 SrlA, SrlB and SrlE is involved in
CC glucitol/sorbitol transport. It can also use D-mannitol.
CC {ECO:0000269|PubMed:1100608}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-sorbitol(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC sorbitol 6-phosphate(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:42484, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:17924, ChEBI:CHEBI:29979, ChEBI:CHEBI:60084,
CC ChEBI:CHEBI:64837; EC=2.7.1.198;
CC Evidence={ECO:0000269|PubMed:1100608};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=44 uM for D-glucitol {ECO:0000269|PubMed:1100608};
CC KM=60 uM for D-mannitol {ECO:0000269|PubMed:1100608};
CC Vmax=7.2 nmol/min/mg enzyme with D-mannitol as substrate
CC {ECO:0000269|PubMed:1100608};
CC Vmax=0.83 nmol/min/mg enzyme with D-glucitol as substrate
CC {ECO:0000269|PubMed:1100608};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:3553176};
CC Multi-pass membrane protein {ECO:0000255, ECO:0000305|PubMed:3553176}.
CC -!- INDUCTION: Regulated by an unusual system which consists of the
CC activator GutM and the repressor GutR in addition to the cAMP-CRP
CC complex. {ECO:0000269|PubMed:3062173}.
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:PRU00425}.
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DR EMBL; J02708; AAC13416.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48149.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16564.2; -; Genomic_DNA.
DR PIR; A26725; WQEC2S.
DR RefSeq; WP_000148878.1; NZ_LN832404.1.
DR RefSeq; YP_026181.1; NC_000913.3.
DR AlphaFoldDB; P56580; -.
DR BioGRID; 4262075; 19.
DR ComplexPortal; CPX-5969; Glucitol/sorbitol enzyme II complex.
DR STRING; 511145.b2703; -.
DR TCDB; 4.A.4.1.1; the pts glucitol (gut) family.
DR jPOST; P56580; -.
DR PaxDb; P56580; -.
DR PRIDE; P56580; -.
DR EnsemblBacteria; AAT48149; AAT48149; b2703.
DR EnsemblBacteria; BAA16564; BAA16564; BAA16564.
DR GeneID; 948933; -.
DR KEGG; ecj:JW5430; -.
DR KEGG; eco:b2703; -.
DR PATRIC; fig|1411691.4.peg.4039; -.
DR EchoBASE; EB4116; -.
DR eggNOG; COG3732; Bacteria.
DR HOGENOM; CLU_054195_0_0_6; -.
DR InParanoid; P56580; -.
DR OMA; HKFIYIT; -.
DR PhylomeDB; P56580; -.
DR BioCyc; EcoCyc:GUTA-MON; -.
DR BioCyc; MetaCyc:GUTA-MON; -.
DR PRO; PR:P56580; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
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:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IDA:UniProtKB.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0015795; P:sorbitol transmembrane transport; IC:ComplexPortal.
DR InterPro; IPR011638; PTS_EIIBC_GUT_C.
DR InterPro; IPR011618; PTS_EIIBC_GUT_N.
DR InterPro; IPR004702; PTS_sorb_EIIBC.
DR PANTHER; PTHR39427; PTHR39427; 1.
DR Pfam; PF07663; EIIBC-GUT_C; 1.
DR Pfam; PF03612; EIIBC-GUT_N; 1.
DR TIGRFAMs; TIGR00825; EIIBC-GUT; 1.
DR PROSITE; PS51102; PTS_EIIB_TYPE_5; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Kinase; Membrane; Phosphoprotein;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..319
FT /note="PTS system glucitol/sorbitol-specific EIIB
FT component"
FT /id="PRO_0000186562"
FT TOPO_DOM 1..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..199
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..256
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..319
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..178
FT /note="PTS EIIB type-5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00425"
FT ACT_SITE 71
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000305"
FT MOD_RES 71
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00425"
SQ 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
