Entry bact: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   15-MAR-2017, entry version 136.
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;
RA   Yamada M., Saier M.H. Jr.;
RT   "Glucitol-specific enzymes of the phosphotransferase system in
RT   Escherichia 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
RT   the 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.,
RA   Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA   Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA   Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA   Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA   Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT   K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT   analysis of 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.,
RA   Mau B., 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.,
RA   Thomas G.H., 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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBSTRATE SPECIFICITY.
RX   PubMed=1100608;
RA   Lengeler J.;
RT   "Nature and properties of hexitol transport systems in Escherichia
RT   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
RT   in 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
CC       phosphotransferase system (sugar PTS), a major carbohydrate active
CC       transport system, catalyzes the phosphorylation of incoming sugar
CC       substrates concomitantly with their translocation across the cell
CC       membrane. The enzyme II complex composed of SrlA, SrlB and SrlE is
CC       involved in glucitol/sorbitol transport. It can also use D-
CC       mannitol. {ECO:0000269|PubMed:1100608}.
CC   -!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + D-
CC       sorbitol(Side 1) = [protein]-L-histidine + D-sorbitol 6-
CC       phosphate(Side 2). {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
CC       {ECO:0000305|PubMed:3553176}; Multi-pass membrane protein
CC       {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   ProteinModelPortal; P56580; -.
DR   BioGrid; 4262075; 19.
DR   STRING; 511145.b2703; -.
DR   TCDB; 4.A.4.1.1; the pts glucitol (gut) family.
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; 32120804; VBIEscCol129921_2794.
DR   EchoBASE; EB4116; -.
DR   EcoGene; EG14373; srlE.
DR   eggNOG; ENOG4105DZY; Bacteria.
DR   eggNOG; COG3732; LUCA.
DR   HOGENOM; HOG000242653; -.
DR   InParanoid; P56580; -.
DR   KO; K02782; -.
DR   KO; K02783; -.
DR   OMA; ALAIVDC; -.
DR   PhylomeDB; P56580; -.
DR   BioCyc; EcoCyc:GUTA-MONOMER; -.
DR   BioCyc; MetaCyc:GUTA-MONOMER; -.
DR   PRO; PR:P56580; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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   InterPro; IPR011638; PTS_EIIBC_GUT_C.
DR   InterPro; IPR011618; PTS_EIIBC_GUT_N.
DR   InterPro; IPR004702; PTS_sorb_EIIBC.
DR   PANTHER; PTHR39427:SF2; PTHR39427:SF2; 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; Complete proteome; Kinase;
KW   Membrane; Phosphoprotein; Phosphotransferase system;
KW   Reference proteome; Sugar transport; Transferase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    319       PTS system glucitol/sorbitol-specific
FT                                EIIB component.
FT                                /FTId=PRO_0000186562.
FT   TOPO_DOM      1    176       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    177    197       Helical. {ECO:0000255}.
FT   TOPO_DOM    198    199       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    200    220       Helical. {ECO:0000255}.
FT   TOPO_DOM    221    228       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    229    249       Helical. {ECO:0000255}.
FT   TOPO_DOM    250    256       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    257    277       Helical. {ECO:0000255}.
FT   TOPO_DOM    278    296       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    297    317       Helical. {ECO:0000255}.
FT   TOPO_DOM    318    319       Periplasmic. {ECO:0000255}.
FT   DOMAIN        1    178       PTS EIIB type-5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00425}.
FT   ACT_SITE     71     71       Phosphocysteine intermediate; for EIIB
FT                                activity. {ECO:0000305}.
FT   MOD_RES      71     71       Phosphocysteine; by EIIA.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00425}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         1    178       iprf:PTS_EIIB_TYPE_5 [T]
FT   MYHIT       226    318       ipfam:EIIBC-GUT_C [T]
FT   MYHIT         4    171       ipfam:EIIBC-GUT_N [T]
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
//