ULAB_ECOLI
ID ULAB_ECOLI Reviewed; 101 AA.
AC P69822; P39302; Q2M6B1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Ascorbate-specific PTS system EIIB component {ECO:0000303|PubMed:12644495};
DE EC=2.7.1.194 {ECO:0000269|PubMed:12644495};
DE AltName: Full=Ascorbate-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:12644495};
GN Name=ulaB {ECO:0000303|PubMed:11741871}; Synonyms=sgaB, yjfT;
GN OrderedLocusNames=b4194, JW4152;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP DISCUSSION OF SEQUENCE.
RA Reizer J., Charbit A., Reizer A., Saier M.H. Jr.;
RT "Novel phosphotransferases system genes revealed by bacterial genome
RT analysis: operons encoding homologues of sugar-specific permease domains of
RT the phosphotransferase system and pentose catabolic enzymes.";
RL Genome Sci. Technol. 1:53-75(1996).
RN [5]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=12374842; DOI=10.1128/jb.184.21.6065-6068.2002;
RA Campos E., Aguilar J., Baldoma L., Badia J.;
RT "The gene yjfQ encodes the repressor of the yjfR-X regulon (ula), which is
RT involved in L-ascorbate metabolism in Escherichia coli.";
RL J. Bacteriol. 184:6065-6068(2002).
RN [6]
RP FUNCTION, AND GENE NAME.
RX PubMed=11741871; DOI=10.1128/jb.184.1.302-306.2002;
RA Yew W.S., Gerlt J.A.;
RT "Utilization of L-ascorbate by Escherichia coli K-12: assignments of
RT functions to products of the yjf-sga and yia-sgb operons.";
RL J. Bacteriol. 184:302-306(2002).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, AND INDUCTION.
RX PubMed=12644495; DOI=10.1128/jb.185.7.2243-2250.2003;
RA Zhang Z., Aboulwafa M., Smith M.H., Saier M.H. Jr.;
RT "The ascorbate transporter of Escherichia coli.";
RL J. Bacteriol. 185:2243-2250(2003).
RN [8]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=14996803; DOI=10.1128/jb.186.6.1720-1728.2004;
RA Campos E., Baldoma L., Aguilar J., Badia J.;
RT "Regulation of expression of the divergent ulaG and ulaABCDEF operons
RT involved in L-ascorbate dissimilation in Escherichia coli.";
RL J. Bacteriol. 186:1720-1728(2004).
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:0000269|PubMed:12644495, ECO:0000305|PubMed:11741871}.
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:0000269|PubMed:12644495};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 uM for L-ascorbate {ECO:0000269|PubMed:12644495};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by L-ascorbate. Repressed by UlaR.
CC {ECO:0000269|PubMed:12374842, ECO:0000269|PubMed:12644495,
CC ECO:0000269|PubMed:14996803}.
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}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to use L-
CC ascorbate. {ECO:0000269|PubMed:12644495}.
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DR EMBL; U14003; AAA97090.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77151.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78195.1; -; Genomic_DNA.
DR PIR; S56419; S56419.
DR RefSeq; NP_418615.1; NC_000913.3.
DR RefSeq; WP_000218362.1; NZ_STEB01000013.1.
DR AlphaFoldDB; P69822; -.
DR SMR; P69822; -.
DR BioGRID; 4262714; 8.
DR ComplexPortal; CPX-5967; L-ascorbate-specific enzyme II complex.
DR IntAct; P69822; 5.
DR STRING; 511145.b4194; -.
DR TCDB; 4.A.7.1.1; the pts l-ascorbate (l-asc) family.
DR PaxDb; P69822; -.
DR PRIDE; P69822; -.
DR EnsemblBacteria; AAC77151; AAC77151; b4194.
DR EnsemblBacteria; BAE78195; BAE78195; BAE78195.
DR GeneID; 60903012; -.
DR GeneID; 66671893; -.
DR GeneID; 948716; -.
DR KEGG; ecj:JW4152; -.
DR KEGG; eco:b4194; -.
DR PATRIC; fig|1411691.4.peg.2507; -.
DR EchoBASE; EB2387; -.
DR eggNOG; COG3414; Bacteria.
DR HOGENOM; CLU_159248_0_0_6; -.
DR OMA; QSKGMTN; -.
DR PhylomeDB; P69822; -.
DR BioCyc; EcoCyc:YJFT-MON; -.
DR BioCyc; MetaCyc:YJFT-MON; -.
DR PRO; PR:P69822; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
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:0090585; F:protein-phosphocysteine-L-ascorbate-phosphotransferase system transporter activity; IMP:EcoCyc.
DR GO; GO:0015882; P:L-ascorbic acid transmembrane transport; IMP:EcoCyc.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:EcoCyc.
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 1: Evidence at protein level;
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_0000186686"
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
