ID   PTEB_AERHY              Reviewed;          88 AA.
AC   P55901;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=PTS system cellobiose-specific EIIB component {ECO:0000250|UniProtKB:Q45399};
DE   AltName: Full=Cellobiose-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:Q45399};
DE            EC=2.7.1.205 {ECO:0000250|UniProtKB:Q45399, ECO:0000255|PROSITE-ProRule:PRU00423};
DE   AltName: Full=EIIB-Cel {ECO:0000250|UniProtKB:Q45399};
DE   Flags: Fragment;
GN   Name=celA {ECO:0000250|UniProtKB:Q45399};
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ah65;
RX   PubMed=8407845; DOI=10.1128/jb.175.20.6695-6703.1993;
RA   Howard S.P., Critch J., Bedi A.;
RT   "Isolation and analysis of eight exe genes and their involvement in
RT   extracellular protein secretion and outer membrane assembly in Aeromonas
RT   hydrophila.";
RL   J. Bacteriol. 175:6695-6703(1993).
RN   [2]
RP   IDENTIFICATION.
RA   Reizer J., Charbit A., Reizer A., Saier M.H. Jr.;
RT   "Novel phosphotransferases system genes revealed by bacterial genome
RT   analysis: operons encoding homologues of sugar-specific permease domains of
RT   the phosphotransferase system and pentose catabolic enzymes.";
RL   Genome Sci. Technol. 1:53-75(1996).
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:0000250|UniProtKB:Q45399}.
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;
CC         Evidence={ECO:0000250|UniProtKB:Q45399, ECO:0000255|PROSITE-
CC         ProRule:PRU00423};
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; X66504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; H49905; H49905.
DR   AlphaFoldDB; P55901; -.
DR   SMR; P55901; -.
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   3: Inferred from homology;
KW   Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW   Sugar transport; Transferase; Transport.
FT   CHAIN           1..>88
FT                   /note="PTS system cellobiose-specific EIIB component"
FT                   /id="PRO_0000186488"
FT   DOMAIN          3..>88
FT                   /note="PTS EIIB type-3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00423"
FT   ACT_SITE        10
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         10
FT                   /note="Phosphocysteine; by EIIA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00423"
FT   NON_TER         88
SQ   SEQUENCE   88 AA;  9716 MW;  2EA61F78BD1F30DF CRC64;
     MEKKRIYLFC SAGMSTSLLV SKMKAQAEKY DVPVLIDAYP ETLAGEKGQD ADLVLLGPQI
     AYMLPEIQQQ LPGKPVEVID TLLYGKVD