PTHB_CLOB8
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 03-AUG-2022, entry version 123.
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; Eubacteriales; 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; DOI=10.1128/aem.64.5.1612-1619.1998;
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., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA Blaschek H., 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 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:9572925}.
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 membrane {ECO:0000305}; Multi-pass membrane
CC 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}.
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DR EMBL; AJ002527; CAA05514.1; -; Genomic_DNA.
DR EMBL; CP000721; ABR32525.1; -; Genomic_DNA.
DR RefSeq; WP_011967686.1; NC_009617.1.
DR AlphaFoldDB; O32333; -.
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 eggNOG; COG3732; Bacteria.
DR HOGENOM; CLU_054195_0_0_9; -.
DR OMA; HKFIYIT; -.
DR OrthoDB; 635898at2; -.
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 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 membrane; Kinase; Membrane; Phosphoprotein; Phosphotransferase system;
KW Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..336
FT /note="PTS system glucitol/sorbitol-specific EIIB
FT component"
FT /id="PRO_0000186564"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 3..195
FT /note="PTS EIIB type-5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00425"
FT ACT_SITE 75
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000305"
FT MOD_RES 75
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00425"
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
