ID   PTKA_ECOL6              Reviewed;         150 AA.
AC   P69813; P37187; P76413;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=PTS system galactitol-specific EIIA component {ECO:0000250|UniProtKB:P69828};
DE   AltName: Full=EIIB-Gat {ECO:0000250|UniProtKB:P69828};
DE   AltName: Full=Galactitol-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P69828};
GN   Name=gatA; OrderedLocusNames=c2619;
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 GatA, GatB and GatC is involved in
CC       galactitol transport. {ECO:0000250|UniProtKB:P69828}.
CC   -!- SUBUNIT: Forms a complex with one each of subunit of GatA, GatB and 2
CC       subunits of GatC. {ECO:0000250|UniProtKB:P69828}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Constitutively expressed. {ECO:0000250|UniProtKB:P69828}.
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:PRU00417}.
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DR   EMBL; AE014075; AAN81075.1; -; Genomic_DNA.
DR   RefSeq; WP_000182899.1; NC_004431.1.
DR   AlphaFoldDB; P69813; -.
DR   SMR; P69813; -.
DR   STRING; 199310.c2619; -.
DR   PRIDE; P69813; -.
DR   EnsemblBacteria; AAN81075; AAN81075; c2619.
DR   GeneID; 66674010; -.
DR   KEGG; ecc:c2619; -.
DR   eggNOG; COG1762; Bacteria.
DR   HOGENOM; CLU_072531_6_2_6; -.
DR   OMA; FADYHEA; -.
DR   BioCyc; ECOL199310:C2619-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:0019402; P:galactitol metabolic process; 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; cd00211; PTS_IIA_fru; 1.
DR   Gene3D; 3.40.930.10; -; 1.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   SUPFAM; SSF55804; SSF55804; 1.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Galactitol metabolism; Kinase; Phosphoprotein;
KW   Phosphotransferase system; Sugar transport; Transferase; Transport.
FT   CHAIN           1..150
FT                   /note="PTS system galactitol-specific EIIA component"
FT                   /id="PRO_0000186577"
FT   DOMAIN          1..144
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT   ACT_SITE        62
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT   MOD_RES         62
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   150 AA;  16907 MW;  1A760676BE5FB61D CRC64;
     MTNLFVRSGI SFVDRSEVLT HIGNEMLAKG VVHDTWPQAL IAREAEFPTG IMLEQHAIAI
     PHCEAIHAKS SAIYLLRPTN KVHFQQADDD NDVAVSLVIA LIVENPQQQL KLLRCLFGKL
     QQPDIVETLI TLPETQLKEY FTKYVLDSDE