ULAA_ECOLI
ID ULAA_ECOLI Reviewed; 465 AA.
AC P39301; Q2M6B2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Ascorbate-specific PTS system EIIC component {ECO:0000303|PubMed:12644495};
DE AltName: Full=Ascorbate-specific permease IIC component UlaA {ECO:0000303|PubMed:12644495};
GN Name=ulaA {ECO:0000303|PubMed:11741871}; Synonyms=sgaT, yjfS;
GN OrderedLocusNames=b4193, JW5744;
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, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, AND
RP 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).
RN [9]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH ASCORBATE, AND
RP SUBUNIT.
RX PubMed=25686089; DOI=10.1038/nsmb.2975;
RA Luo P., Yu X., Wang W., Fan S., Li X., Wang J.;
RT "Crystal structure of a phosphorylation-coupled vitamin C transporter.";
RL Nat. Struct. Mol. Biol. 22:238-241(2015).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 uM for L-ascorbate {ECO:0000269|PubMed:12644495};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25686089}.
CC -!- INTERACTION:
CC P39301; P39301: ulaA; NbExp=2; IntAct=EBI-556234, EBI-556234;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
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: In classical PTS systems, the PTS EIIC type-2 domain forms the
CC translocation channel and contains the specific substrate-binding site.
CC UlaA does not exhibit the topological features of any recognized enzyme
CC IIC. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to use L-
CC ascorbate. {ECO:0000269|PubMed:12644495}.
CC -!- SIMILARITY: Belongs to the UlaA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97089.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97089.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77150.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78194.1; -; Genomic_DNA.
DR PIR; D65230; D65230.
DR RefSeq; NP_418614.4; NC_000913.3.
DR RefSeq; WP_001350568.1; NZ_LN832404.1.
DR PDB; 4RP8; X-ray; 2.36 A; A/C=1-465.
DR PDB; 4RP9; X-ray; 1.65 A; A=1-465.
DR PDBsum; 4RP8; -.
DR PDBsum; 4RP9; -.
DR AlphaFoldDB; P39301; -.
DR SMR; P39301; -.
DR BioGRID; 4262713; 11.
DR ComplexPortal; CPX-5967; L-ascorbate-specific enzyme II complex.
DR DIP; DIP-10870N; -.
DR IntAct; P39301; 1.
DR STRING; 511145.b4193; -.
DR TCDB; 4.A.7.1.1; the pts l-ascorbate (l-asc) family.
DR PaxDb; P39301; -.
DR PRIDE; P39301; -.
DR EnsemblBacteria; AAC77150; AAC77150; b4193.
DR EnsemblBacteria; BAE78194; BAE78194; BAE78194.
DR GeneID; 948717; -.
DR KEGG; ecj:JW5744; -.
DR KEGG; eco:b4193; -.
DR PATRIC; fig|1411691.4.peg.2508; -.
DR EchoBASE; EB2386; -.
DR eggNOG; COG3037; Bacteria.
DR HOGENOM; CLU_031784_1_0_6; -.
DR InParanoid; P39301; -.
DR OMA; IAHQQMF; -.
DR PhylomeDB; P39301; -.
DR BioCyc; EcoCyc:SGAT-MON; -.
DR BioCyc; MetaCyc:SGAT-MON; -.
DR BRENDA; 2.7.1.194; 2026.
DR PRO; PR:P39301; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0090585; F:protein-phosphocysteine-L-ascorbate-phosphotransferase system transporter activity; IDA: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 InterPro; IPR004703; PTS_sugar-sp_permease.
DR Pfam; PF03611; EIIC-GAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..465
FT /note="Ascorbate-specific PTS system EIIC component"
FT /id="PRO_0000097714"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:25686089"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:25686089"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:25686089"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:25686089"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:25686089"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:25686089"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:25686089"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:25686089"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:25686089"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:25686089"
FT BINDING 86..87
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:25686089"
FT BINDING 135..139
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:25686089"
FT BINDING 194..195
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:25686089"
FT BINDING 314
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:25686089"
FT CONFLICT 451..465
FT /note="RAEEDAEKQLAEQSA -> AQKKMQKNNWQNSLLNKEF (in Ref. 1;
FT AAA97089)"
FT /evidence="ECO:0000305"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:4RP9"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 38..76
FT /evidence="ECO:0007829|PDB:4RP9"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 102..120
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:4RP9"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 134..150
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 155..185
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:4RP9"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 232..249
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 253..260
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 265..304
FT /evidence="ECO:0007829|PDB:4RP9"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 315..321
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 323..346
FT /evidence="ECO:0007829|PDB:4RP9"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 357..402
FT /evidence="ECO:0007829|PDB:4RP9"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 417..427
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:4RP9"
FT HELIX 431..455
FT /evidence="ECO:0007829|PDB:4RP9"
SQ SEQUENCE 465 AA; 50737 MW; CCFF1C776FEA4716 CRC64;
MEILYNIFTV FFNQVMTNAP LLLGIVTCLG YILLRKSVSV IIKGTIKTII GFMLLQAGSG
ILTSTFKPVV AKMSEVYGIN GAISDTYASM MATIDRMGDA YSWVGYAVLL ALALNICYVL
LRRITGIRTI MLTGHIMFQQ AGLIAVTLFI FGYSMWTTII CTAILVSLYW GITSNMMYKP
TQEVTDGCGF SIGHQQQFAS WIAYKVAPFL GKKEESVEDL KLPGWLNIFH DNIVSTAIVM
TIFFGAILLS FGIDTVQAMA GKVHWTVYIL QTGFSFAVAI FIITQGVRMF VAELSEAFNG
ISQRLIPGAV LAIDCAAIYS FAPNAVVWGF MWGTIGQLIA VGILVACGSS ILIIPGFIPM
FFSNATIGVF ANHFGGWRAA LKICLVMGMI EIFGCVWAVK LTGMSAWMGM ADWSILAPPM
MQGFFSIGIA FMAVIIVIAL AYMFFAGRAL RAEEDAEKQL AEQSA
