ULAC_ECOL6
ID ULAC_ECOL6 Reviewed; 154 AA.
AC Q8FAJ0;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Ascorbate-specific PTS system EIIA component {ECO:0000250|UniProtKB:P69820};
DE AltName: Full=Ascorbate-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P69820};
GN Name=ulaC; OrderedLocusNames=c5284;
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 UlaABC PTS system is involved in ascorbate transport.
CC {ECO:0000250|UniProtKB:P69820}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by L-ascorbate. Repressed by UlaR.
CC {ECO:0000250|UniProtKB:P69820}.
CC -!- DOMAIN: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on
CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC EIIB type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00417}.
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DR EMBL; AE014075; AAN83705.1; -; Genomic_DNA.
DR RefSeq; WP_000776521.1; NC_004431.1.
DR AlphaFoldDB; Q8FAJ0; -.
DR SMR; Q8FAJ0; -.
DR STRING; 199310.c5284; -.
DR EnsemblBacteria; AAN83705; AAN83705; c5284.
DR KEGG; ecc:c5284; -.
DR eggNOG; COG1762; Bacteria.
DR HOGENOM; CLU_072531_2_0_6; -.
DR OMA; MGPYIIL; -.
DR BioCyc; ECOL199310:C5284-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: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.
DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system; Transferase;
KW Transport.
FT CHAIN 1..154
FT /note="Ascorbate-specific PTS system EIIA component"
FT /id="PRO_0000230313"
FT DOMAIN 6..150
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 68
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT MOD_RES 68
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250|UniProtKB:P69820"
SQ SEQUENCE 154 AA; 17237 MW; B6D4931C527EDDCF CRC64;
MKLRDSLAEN KSIRLQAEAN TWQEAVKIGV DLLVAADVVE PRYYQAILDG VEQFGPYFVI
APGLAMPHGR PEEGVKKTGF SLVTLKKPLE FNHEDNDPVD ILITMAAVDA NTHQEVGIMQ
IVNLFEDEEN FDRLRACRTE QEVLDLIDRT NAAA
