ID   PTGA_ECOL6              Reviewed;         169 AA.
AC   P69784; P08837; Q47703;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=PTS system glucose-specific EIIA component {ECO:0000250|UniProtKB:P69783};
DE   AltName: Full=EIIA-Glc {ECO:0000250|UniProtKB:P69783};
DE   AltName: Full=EIII-Glc {ECO:0000250|UniProtKB:P69783};
DE   AltName: Full=Glucose-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P69783};
GN   Name=crr; OrderedLocusNames=c2952;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 PtsG and Crr is involved in glucose
CC       transport. {ECO:0000250|UniProtKB:P69783}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P69783};
CC       Note=Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion
CC       is important for dimerization. {ECO:0000250|UniProtKB:P69783};
CC   -!- SUBUNIT: Heterodimer with glycerol kinase (glpk).
CC       {ECO:0000250|UniProtKB:P69783}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a histidyl
CC       residue. Then, it transfers the phosphoryl group to the EIIB domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00416}.
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DR   EMBL; AE014075; AAN81402.1; -; Genomic_DNA.
DR   RefSeq; WP_000522247.1; NC_004431.1.
DR   AlphaFoldDB; P69784; -.
DR   BMRB; P69784; -.
DR   SMR; P69784; -.
DR   MINT; P69784; -.
DR   STRING; 199310.c2952; -.
DR   EnsemblBacteria; AAN81402; AAN81402; c2952.
DR   GeneID; 67416817; -.
DR   KEGG; ecc:c2952; -.
DR   eggNOG; COG2190; Bacteria.
DR   HOGENOM; CLU_012312_5_1_6; -.
DR   OMA; HTKHAVG; -.
DR   BioCyc; ECOL199310:C2952-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; 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   Gene3D; 2.70.70.10; -; 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR001127; PTS_EIIA_1_perm.
DR   Pfam; PF00358; PTS_EIIA_1; 1.
DR   SUPFAM; SSF51261; SSF51261; 1.
DR   TIGRFAMs; TIGR00830; PTBA; 1.
DR   PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
DR   PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Kinase; Metal-binding; Phosphoprotein;
KW   Phosphotransferase system; Sugar transport; Transferase; Transport; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P69783"
FT   CHAIN           2..169
FT                   /note="PTS system glucose-specific EIIA component"
FT                   /id="PRO_0000186533"
FT   DOMAIN          39..143
FT                   /note="PTS EIIA type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT   ACT_SITE        91
FT                   /note="Tele-phosphohistidine intermediate; for EIIA
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P69783,
FT                   ECO:0000255|PROSITE-ProRule:PRU00416"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared with glycerol kinase"
FT                   /evidence="ECO:0000250|UniProtKB:P69783"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared with glycerol kinase"
FT                   /evidence="ECO:0000250|UniProtKB:P69783"
FT   SITE            76
FT                   /note="Important for phospho-donor activity"
FT                   /evidence="ECO:0000250|UniProtKB:P69783"
FT   MOD_RES         91
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000250|UniProtKB:P69783"
SQ   SEQUENCE   169 AA;  18251 MW;  EA18020745531215 CRC64;
     MGLFDKLKSL VSDDKKDTGT IEIIAPLSGE IVNIEDVPDV VFAEKIVGDG IAIKPTGNKM
     VAPVDGTIGK IFETNHAFSI ESDSGVELFV HFGIDTVELK GEGFKRIAEE GQRVKVGDTV
     IEFDLPLLEE KAKSTLTPVV ISNMDEIKEL IKLSGSVTVG ETPVIRIKK