ULAA_SALTY
ID ULAA_SALTY Reviewed; 465 AA.
AC Q8ZK90;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Ascorbate-specific PTS system EIIC component {ECO:0000250|UniProtKB:P39301};
DE AltName: Full=Ascorbate-specific permease IIC component UlaA {ECO:0000250|UniProtKB:P39301};
GN Name=ulaA; OrderedLocusNames=STM4383;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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:P39301}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P39301}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P39301}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P39301}.
CC -!- INDUCTION: Induced by L-ascorbate. Repressed by UlaR.
CC {ECO:0000250|UniProtKB:P39301}.
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:0000250|UniProtKB:P39301}.
CC -!- SIMILARITY: Belongs to the UlaA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL23203.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE006468; AAL23203.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_463244.3; NC_003197.2.
DR AlphaFoldDB; Q8ZK90; -.
DR SMR; Q8ZK90; -.
DR STRING; 99287.STM4383; -.
DR PaxDb; Q8ZK90; -.
DR EnsemblBacteria; AAL23203; AAL23203; STM4383.
DR GeneID; 1255909; -.
DR KEGG; stm:STM4383; -.
DR PATRIC; fig|99287.12.peg.4608; -.
DR HOGENOM; CLU_031784_1_0_6; -.
DR OMA; IAHQQMF; -.
DR PhylomeDB; Q8ZK90; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR InterPro; IPR004703; PTS_sugar-sp_permease.
DR Pfam; PF03611; EIIC-GAT; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..465
FT /note="Ascorbate-specific PTS system EIIC component"
FT /id="PRO_0000230660"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39301"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39301"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39301"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39301"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39301"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39301"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39301"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39301"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39301"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39301"
FT BINDING 86..87
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:P39301"
FT BINDING 135..139
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:P39301"
FT BINDING 194..195
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:P39301"
FT BINDING 314
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:P39301"
SQ SEQUENCE 465 AA; 50818 MW; 869E1B7550481F64 CRC64;
MEILYNIFTI FFNQVMTNAP LLLGIVTCLG YILLRKSVSV IIKGTIKTII GFMLLQAGSG
ILTSTFKPVV AKMSEVYGIN GAISDTYASM MATIERMGDA YSWVGYAVLL ALALNICYVL
LRRITGIRTI MLTGHIMFQQ AGLIAVSFYI FGYSMWTTII CTAILVSLYW GITSNMMYKP
TQEVTDGCGF SIGHQQQFAS WIAYKVAPFL GKKEESVEDL KLPGWLNIFH DNIVSTAIVM
TIFFGAILLS FGIDTVQAMA GKTHWTIYIL QTGFSFAVAI FIITQGVRMF VAELSEAFNG
ISQRLIPGAV LAIDCAAIYS FAPNAVVWGF MWGTIGQLIA VGILVACGSS ILIIPGFIPM
FFSNATIGVF ANHFGGWRAA LKICLVMGMI EIFGCVWAVK LTGMSAWMGM ADWSILAPPM
MQGFFSLGIA FMAVIIVIAL AYMFFAGRAL RAEEDAEKQL AEQSA
