PTEB_GEOSE
ID PTEB_GEOSE Reviewed; 100 AA.
AC Q45399;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=PTS system cellobiose-specific EIIB component {ECO:0000303|PubMed:8407820};
DE AltName: Full=Cellobiose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:8407820};
DE EC=2.7.1.205 {ECO:0000255|PROSITE-ProRule:PRU00423, ECO:0000305|PubMed:8407820};
DE AltName: Full=EIIB-Cel {ECO:0000303|PubMed:8407820};
GN Name=celA {ECO:0000303|PubMed:8407820};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=XL-65-6;
RX PubMed=8407820; DOI=10.1128/jb.175.20.6441-6450.1993;
RA Lai X., Ingram L.O.;
RT "Cloning and sequencing of a cellobiose phosphotransferase system operon
RT from Bacillus stearothermophilus XL-65-6 and functional expression in
RT Escherichia coli.";
RL J. Bacteriol. 175:6441-6450(1993).
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 CelABD PTS system is involved in cellobiose transport.
CC {ECO:0000305|PubMed:8407820}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-cellobiose(out) + N(pros)-phospho-L-histidyl-[protein] = 6-
CC phospho-beta-D-glucosyl-(1->4)-D-glucose(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:49292, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:17057, ChEBI:CHEBI:29979, ChEBI:CHEBI:58312,
CC ChEBI:CHEBI:64837; EC=2.7.1.205; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00423, ECO:0000305|PubMed:8407820};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The PTS EIIB type-3 domain is phosphorylated by phospho-EIIA on
CC a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-3 domain. {ECO:0000255|PROSITE-ProRule:PRU00423}.
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DR EMBL; U07818; AAA17389.1; -; Unassigned_DNA.
DR PIR; B49898; B49898.
DR AlphaFoldDB; Q45399; -.
DR SMR; Q45399; -.
DR GO; GO:0005737; C:cytoplasm; 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:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR003501; PTS_EIIB_2/3.
DR InterPro; IPR013012; PTS_EIIB_3.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 1.
DR TIGRFAMs; TIGR00853; pts-lac; 1.
DR PROSITE; PS51100; PTS_EIIB_TYPE_3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Sugar transport; Transferase; Transport.
FT CHAIN 1..100
FT /note="PTS system cellobiose-specific EIIB component"
FT /id="PRO_0000186486"
FT DOMAIN 1..100
FT /note="PTS EIIB type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00423"
FT ACT_SITE 7
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000305"
FT MOD_RES 7
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00423"
SQ SEQUENCE 100 AA; 10737 MW; 7CCD2F32C72F1747 CRC64;
MNILLICAAG MSTSLLVTKM KEAAKQKGIE ANIWAVSADE AKSHLDQADV VLIGPQIRYK
LAAFKKEGEA RGIPVDVINP ADYGRVNGAG VLDFALRLKK
