ID   PTHB_ERWAM              Reviewed;         333 AA.
AC   O32522;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=PTS system glucitol/sorbitol-specific EIIB component {ECO:0000303|PubMed:9435786};
DE            EC=2.7.1.198 {ECO:0000250|UniProtKB:P56580};
DE   AltName: Full=EII-Gut {ECO:0000303|PubMed:9435786};
DE   AltName: Full=Enzyme II-Gut {ECO:0000303|PubMed:9435786};
DE   AltName: Full=Glucitol/sorbitol-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:9435786};
GN   Name=srlE;
OS   Erwinia amylovora (Fire blight bacteria).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=552;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=EA7/74;
RX   PubMed=9435786; DOI=10.1007/s004380050609;
RA   Aldridge P., Metzger M., Geider K.;
RT   "Genetics of sorbitol metabolism in Erwinia amylovora and its influence on
RT   bacterial virulence.";
RL   Mol. Gen. Genet. 256:611-619(1997).
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. {ECO:0000305|PubMed:9435786}.
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:0000250|UniProtKB:P56580};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Activated by sorbitol and repressed by glucose.
CC       {ECO:0000269|PubMed:9435786}.
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; Y14603; CAA74942.1; -; Genomic_DNA.
DR   RefSeq; WP_004159990.1; NZ_RQKG01000018.1.
DR   AlphaFoldDB; O32522; -.
DR   GeneID; 8914015; -.
DR   OMA; HKFIYIT; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; ISS:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Cell inner membrane; Cell membrane; Kinase; Membrane; Phosphoprotein;
KW   Phosphotransferase system; Sugar transport; Transferase; Transmembrane;
KW   Transmembrane helix; Transport; Virulence.
FT   CHAIN           1..333
FT                   /note="PTS system glucitol/sorbitol-specific EIIB
FT                   component"
FT                   /id="PRO_0000186563"
FT   TRANSMEM        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1..192
FT                   /note="PTS EIIB type-5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00425"
FT   ACT_SITE        72
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         72
FT                   /note="Phosphocysteine; by EIIA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00425"
SQ   SEQUENCE   333 AA;  34292 MW;  6181206F04A61CAB CRC64;
     MANTIEIRKG ESGWGGPLSI NVTAGKKIVY ITAGTKPAIV DHLVALTGWE AVDGFKQGEP
     PAEEIGVAVI DCGGTLRCGL YPKRRIPTIN IHATGKSGPL AQFITEDIYV SGVRVADIRV
     ANDAEAAPPE VAVADVAVNA GKGTGRDYDT SKKITEQSDG LLAKVGMGMG SAVAILFQSG
     RETIDTVLKT ILPFMAFVSA LIGIIMASGL GDFIAHGLTP LANSPVGLVT LALICSFPLL
     SPFLGPGAVI AQVIGVLVGV QIGQGTIPPH LALPALFAIN AQAACDFIPV GLSLANARQE
     TVRVGVPAVL VGRFITGAPT VLLAWAASSF IYH