ID   PTEA_GEOSE              Reviewed;         108 AA.
AC   Q45402;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=PTS system cellobiose-specific EIIA component {ECO:0000303|PubMed:8407820};
DE   AltName: Full=Cellobiose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:8407820};
DE   AltName: Full=EIIA-Cel {ECO:0000303|PubMed:8407820};
DE   AltName: Full=EIII-Cel {ECO:0000303|PubMed:8407820};
GN   Name=celD {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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The PTS EIIA type-3 domain is phosphorylated by phospho-HPr on
CC       a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC       EIIB type-3 domain. {ECO:0000255|PROSITE-ProRule:PRU00418}.
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DR   EMBL; U07818; AAA17392.1; -; Unassigned_DNA.
DR   PIR; E49898; E49898.
DR   AlphaFoldDB; Q45402; -.
DR   SMR; Q45402; -.
DR   BRENDA; 2.7.1.205; 623.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00215; PTS_IIA_lac; 1.
DR   InterPro; IPR003188; PTS_IIA_lac/cel.
DR   InterPro; IPR036542; PTS_IIA_lac/cel_sf.
DR   PANTHER; PTHR34382; PTHR34382; 1.
DR   Pfam; PF02255; PTS_IIA; 1.
DR   PIRSF; PIRSF000699; PTS_IILac_III; 1.
DR   SUPFAM; SSF46973; SSF46973; 1.
DR   TIGRFAMs; TIGR00823; EIIA-LAC; 1.
DR   PROSITE; PS51095; PTS_EIIA_TYPE_3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW   Sugar transport; Transferase; Transport.
FT   CHAIN           1..108
FT                   /note="PTS system cellobiose-specific EIIA component"
FT                   /id="PRO_0000186492"
FT   DOMAIN          2..100
FT                   /note="PTS EIIA type-3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00418"
FT   ACT_SITE        76
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         76
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00418"
SQ   SEQUENCE   108 AA;  11785 MW;  406966C7AB122327 CRC64;
     MQTYEQTVFQ LILHGGNGRS YAMEAITAAK KGEFAEARRL LEQAGAELQA AHGLQTALLQ
     QEASGGQPVV TLLMVHAQDH LMTAITVKDL AAEFVELYEA LKRQTTES