ULAC_ECOLI
ID ULAC_ECOLI Reviewed; 154 AA.
AC P69820; P39303; Q2M6B0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ascorbate-specific PTS system EIIA component {ECO:0000303|PubMed:12644495};
DE AltName: Full=Ascorbate-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:12644495};
GN Name=ulaC {ECO:0000303|PubMed:11741871}; Synonyms=ptxA, sgaA, yjfU;
GN OrderedLocusNames=b4195, JW4153;
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], AND SEQUENCE REVISION TO
RP C-TERMINUS.
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, DISRUPTION 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 -!- 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 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}.
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; AAA97091.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77152.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78196.1; -; Genomic_DNA.
DR PIR; F65230; F65230.
DR RefSeq; NP_418616.1; NC_000913.3.
DR RefSeq; WP_000776517.1; NZ_LN832404.1.
DR AlphaFoldDB; P69820; -.
DR SMR; P69820; -.
DR BioGRID; 4262708; 9.
DR ComplexPortal; CPX-5967; L-ascorbate-specific enzyme II complex.
DR IntAct; P69820; 1.
DR STRING; 511145.b4195; -.
DR TCDB; 4.A.7.1.1; the pts l-ascorbate (l-asc) family.
DR PaxDb; P69820; -.
DR PRIDE; P69820; -.
DR EnsemblBacteria; AAC77152; AAC77152; b4195.
DR EnsemblBacteria; BAE78196; BAE78196; BAE78196.
DR GeneID; 948715; -.
DR KEGG; ecj:JW4153; -.
DR KEGG; eco:b4195; -.
DR PATRIC; fig|1411691.4.peg.2506; -.
DR EchoBASE; EB2388; -.
DR eggNOG; COG1762; Bacteria.
DR HOGENOM; CLU_072531_2_0_6; -.
DR InParanoid; P69820; -.
DR OMA; MGPYIIL; -.
DR PhylomeDB; P69820; -.
DR BioCyc; EcoCyc:YJFU-MON; -.
DR BioCyc; MetaCyc:YJFU-MON; -.
DR PRO; PR:P69820; -.
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: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 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 1: Evidence at protein level;
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_0000186683"
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:0000305"
FT CONFLICT 153..154
FT /note="AA -> GSLRRN (in Ref. 1; AAA97091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 154 AA; 17238 MW; BE83931C5A98DB79 CRC64;
MKLRDSLAEN KSIRLQAEAE TWQEAVKIGV DLLVAADVVE PRYYQAILDG VEQFGPYFVI
APGLAMPHGR PEEGVKKTGF SLVTLKKPLE FNHDDNDPVD ILITMAAVDA NTHQEVGIMQ
IVNLFEDEEN FDRLRACRTE QEVLDLIDRT NAAA
