ULAB_ECO57
ID ULAB_ECO57 Reviewed; 101 AA.
AC P69823; P39302;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Ascorbate-specific PTS system EIIB component {ECO:0000250|UniProtKB:P69822};
DE EC=2.7.1.194 {ECO:0000250|UniProtKB:P69822};
DE AltName: Full=Ascorbate-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P69822};
GN Name=ulaB; Synonyms=sgaB; OrderedLocusNames=Z5803, ECs5170;
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:P69822}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ascorbate(out) + N(pros)-phospho-L-histidyl-[protein] = L-
CC ascorbate 6-phosphate(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:42436, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:38290, ChEBI:CHEBI:61698,
CC ChEBI:CHEBI:64837; EC=2.7.1.194;
CC Evidence={ECO:0000250|UniProtKB:P69822};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by L-ascorbate. Repressed by UlaR.
CC {ECO:0000250|UniProtKB:P69822}.
CC -!- DOMAIN: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on
CC a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00422}.
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DR EMBL; AE005174; AAG59390.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38593.1; -; Genomic_DNA.
DR PIR; B86116; B86116.
DR PIR; B91275; B91275.
DR RefSeq; NP_313197.1; NC_002695.1.
DR RefSeq; WP_000218362.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P69823; -.
DR SMR; P69823; -.
DR STRING; 155864.EDL933_5539; -.
DR EnsemblBacteria; AAG59390; AAG59390; Z5803.
DR EnsemblBacteria; BAB38593; BAB38593; ECs_5170.
DR GeneID; 60903012; -.
DR GeneID; 66671893; -.
DR GeneID; 914003; -.
DR KEGG; ece:Z5803; -.
DR KEGG; ecs:ECs_5170; -.
DR PATRIC; fig|386585.9.peg.5404; -.
DR eggNOG; COG3414; Bacteria.
DR HOGENOM; CLU_159248_0_0_6; -.
DR OMA; QSKGMTN; -.
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:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR013011; PTS_EIIB_2.
DR InterPro; IPR003501; PTS_EIIB_2/3.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 1.
DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Transferase; Transport.
FT CHAIN 1..101
FT /note="Ascorbate-specific PTS system EIIB component"
FT /id="PRO_0000186687"
FT DOMAIN 1..100
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT ACT_SITE 9
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00550, ECO:0000305"
FT MOD_RES 9
FT /note="Phosphocysteine"
FT /evidence="ECO:0000250|UniProtKB:P00550, ECO:0000305"
SQ SEQUENCE 101 AA; 10896 MW; 84CFB6B17250D47D CRC64;
MTVRILAVCG NGQGSSMIMK MKVDQFLTQS NIDHTVNSCA VGEYKSELSG ADIIIASTHI
AGEITVTGNK YVVGVRNMLS PADFGPKLLE VIKEHFPQDV K
