ULAC_ECO57
ID ULAC_ECO57 Reviewed; 154 AA.
AC P69821; P39303;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
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; Synonyms=sgaA; OrderedLocusNames=Z5804, ECs5171;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG59391.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38594.1; -; Genomic_DNA.
DR PIR; C86116; C86116.
DR PIR; C91275; C91275.
DR RefSeq; NP_313198.1; NC_002695.1.
DR RefSeq; WP_000776517.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P69821; -.
DR SMR; P69821; -.
DR STRING; 155864.EDL933_5540; -.
DR EnsemblBacteria; AAG59391; AAG59391; Z5804.
DR EnsemblBacteria; BAB38594; BAB38594; ECs_5171.
DR GeneID; 914001; -.
DR KEGG; ece:Z5804; -.
DR KEGG; ecs:ECs_5171; -.
DR PATRIC; fig|386585.9.peg.5405; -.
DR eggNOG; COG1762; Bacteria.
DR HOGENOM; CLU_072531_2_0_6; -.
DR OMA; MGPYIIL; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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;
KW Reference proteome; Transferase; Transport.
FT CHAIN 1..154
FT /note="Ascorbate-specific PTS system EIIA component"
FT /id="PRO_0000186684"
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; 17238 MW; BE83931C5A98DB79 CRC64;
MKLRDSLAEN KSIRLQAEAE TWQEAVKIGV DLLVAADVVE PRYYQAILDG VEQFGPYFVI
APGLAMPHGR PEEGVKKTGF SLVTLKKPLE FNHDDNDPVD ILITMAAVDA NTHQEVGIMQ
IVNLFEDEEN FDRLRACRTE QEVLDLIDRT NAAA
