Entry sw:PTHB_ERWAM

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   02-NOV-2016, entry version 81.
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
RT   influence on bacterial virulence.";
RL   Mol. Gen. Genet. 256:611-619(1997).
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.
CC       {ECO:0000305|PubMed:9435786}.
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:0000250|UniProtKB:P56580}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-
CC       pass 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}.
CC   -!- SIMILARITY: Contains 1 PTS EIIB type-5 domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00425}.
DR   EMBL; Y14603; CAA74942.1; -; Genomic_DNA.
DR   STRING; 665029.EAMY_3075; -.
DR   GeneID; 8914015; -.
DR   eggNOG; ENOG4105DZY; Bacteria.
DR   eggNOG; COG3732; LUCA.
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:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; ISS:UniProtKB.
DR   InterPro; IPR011638; PTS_EIIBC_GUT_C.
DR   InterPro; IPR011618; PTS_EIIBC_GUT_N.
DR   InterPro; IPR004702; PTS_sorb_EIIBC.
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;
KW   Transmembrane; Transmembrane helix; Transport; Virulence.
FT   CHAIN         1    333       PTS system glucitol/sorbitol-specific
FT                                EIIB component.
FT                                /FTId=PRO_0000186563.
FT   TRANSMEM    191    211       Helical. {ECO:0000255}.
FT   TRANSMEM    220    240       Helical. {ECO:0000255}.
FT   TRANSMEM    243    263       Helical. {ECO:0000255}.
FT   TRANSMEM    271    291       Helical. {ECO:0000255}.
FT   TRANSMEM    304    324       Helical. {ECO:0000255}.
FT   DOMAIN        1    192       PTS EIIB type-5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00425}.
FT   ACT_SITE     72     72       Phosphocysteine intermediate; for EIIB
FT                                activity. {ECO:0000305}.
FT   MOD_RES      72     72       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    192       iprf:PTS_EIIB_TYPE_5 [T]
FT   MYHIT         5    185       ipfam:EIIBC-GUT_N [T]
FT   MYHIT       240    332       ipfam:EIIBC-GUT_C [T]
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
//