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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=PTS system glucitol/sorbitol-specific EIIB component {ECO:0000250|UniProtKB:P56580}; EC=2.7.1.198 {ECO:0000250|UniProtKB:P56580}; AltName: Full=EII-Gut {ECO:0000250|UniProtKB:P56580}; AltName: Full=Enzyme II-Gut {ECO:0000250|UniProtKB:P56580}; AltName: Full=Glucitol/sorbitol-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P56580};
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MyHits synonymsPTHB_CLOB8 , O32333 , A6LQ95 , D766D0501EA10694
match map segment
iprf:PTS_EIIB_TYPE_5 ipfam:EIIBC-GUT_N ipfam:EIIBC-GUT_C  
Legends: 1, ACT_SITE Phosphocysteine intermediate; for EIIB activity. {ECO:0000305}; 2, Phosphocysteine; by EIIA. {ECO:0000255|PROSITE-ProRule:PRU00425}; 3, TRANSMEM Helical. {ECO:0000255}.
ID   PTHB_CLOB8              Reviewed;         336 AA.
AC   O32333; A6LQ95;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   02-NOV-2016, entry version 103.
DE   RecName: Full=PTS system glucitol/sorbitol-specific EIIB component {ECO:0000250|UniProtKB:P56580};
DE            EC=2.7.1.198 {ECO:0000250|UniProtKB:P56580};
DE   AltName: Full=EII-Gut {ECO:0000250|UniProtKB:P56580};
DE   AltName: Full=Enzyme II-Gut {ECO:0000250|UniProtKB:P56580};
DE   AltName: Full=Glucitol/sorbitol-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P56580};
GN   Name=srlE; Synonyms=gutA2; OrderedLocusNames=Cbei_0337;
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=ATCC 51743 / NCIMB 8052;
RX   PubMed=9572925;
RA   Tangney M., Brehm J.K., Minton N.P., Mitchell W.J.;
RT   "A gene system for glucitol transport and metabolism in Clostridium
RT   beijerinckii NCIMB 8052.";
RL   Appl. Environ. Microbiol. 64:1612-1619(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Tapia R., Brainard J.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bennet G., Cann I., Chen J.-S., Contreras A.L.,
RA   Jones D., Kashket E., Mitchell W., Stoddard S., Schwarz W.,
RA   Qureshi N., Young M., Shi Z., Ezeji T., White B., Blaschek H.,
RA   Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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:9572925}.
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 membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Activated by sorbitol and repressed by glucose.
CC       {ECO:0000269|PubMed:9572925}.
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; AJ002527; CAA05514.1; -; Genomic_DNA.
DR   EMBL; CP000721; ABR32525.1; -; Genomic_DNA.
DR   RefSeq; WP_011967686.1; NC_009617.1.
DR   STRING; 290402.Cbei_0337; -.
DR   TCDB; 4.A.4.1.2; the pts glucitol (gut) family.
DR   EnsemblBacteria; ABR32525; ABR32525; Cbei_0337.
DR   KEGG; cbe:Cbei_0337; -.
DR   PATRIC; 19344528; VBICloBei69853_0347.
DR   eggNOG; ENOG4105DZY; Bacteria.
DR   eggNOG; COG3732; LUCA.
DR   HOGENOM; HOG000242653; -.
DR   KO; K02782; -.
DR   KO; K02783; -.
DR   OMA; ALAIVDC; -.
DR   OrthoDB; POG091H0RIL; -.
DR   Proteomes; UP000000565; Chromosome.
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   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 membrane; Complete proteome; Kinase; Membrane; Phosphoprotein;
KW   Phosphotransferase system; Reference proteome; Sugar transport;
KW   Transferase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    336       PTS system glucitol/sorbitol-specific
FT                                EIIB component.
FT                                /FTId=PRO_0000186564.
FT   TRANSMEM    194    214       Helical. {ECO:0000255}.
FT   TRANSMEM    228    248       Helical. {ECO:0000255}.
FT   TRANSMEM    250    270       Helical. {ECO:0000255}.
FT   TRANSMEM    278    298       Helical. {ECO:0000255}.
FT   TRANSMEM    312    332       Helical. {ECO:0000255}.
FT   DOMAIN        3    195       PTS EIIB type-5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00425}.
FT   ACT_SITE     75     75       Phosphocysteine intermediate; for EIIB
FT                                activity. {ECO:0000305}.
FT   MOD_RES      75     75       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         3    195       iprf:PTS_EIIB_TYPE_5 [T]
FT   MYHIT         6    188       ipfam:EIIBC-GUT_N [T]
FT   MYHIT       243    335       ipfam:EIIBC-GUT_C [T]
SQ   SEQUENCE   336 AA;  35174 MW;  D766D0501EA10694 CRC64;
     MEKYNAIKIV KGSGGFGGPL TVKPEEGKDT LLYITGGGAE PEIVEKIVNL TGCKAVNGFK
     TSVPEEQIFL VIIDCGGTLR CGIYPQKRIP TINVMPVGKS GPLAKFITED IYVSAVGLNQ
     ISLADSSAEP IKSTKVPEEG KREFKYSADK KVSQSLAENS KSSIVQKIGM GAGKVVNTLY
     QAGRDAVQSM ITTILPFMAF VAMLIGIIQG SGFGNWFAKI LVPLAGNGIG LMILGFICSI
     PLLSALLGPG AVIAQIVGTL IGVEIGKGTI PPSLALPALF AINTQCACDF IPVGLGLAEA
     EPETVEVGVP SVLYSRFMIG VPRVAVAWVA SIGLYQ
//