ID   ULAA_SHISS              Reviewed;         465 AA.
AC   P0C184;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 46.
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=SSON_4375;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CP000038; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CP000038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0C184; -.
DR   SMR; P0C184; -.
DR   Proteomes; UP000002529; 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   5: Uncertain;
KW   Cell inner membrane; Cell membrane; Membrane; Phosphotransferase system;
KW   Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..465
FT                   /note="Ascorbate-specific PTS system EIIC component"
FT                   /id="PRO_0000230664"
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;  50699 MW;  1E3217BF916C9C7F CRC64;
     MEILYNIFTV FFNQVMTNAP LLLGIVTCLG YILLRKSVSV IIKGTIKTII GFMLLQAGSG
     ILTSTFKPVV AKMSEVYGIN GAISDTYASM MATIDRMGDA YSWVGYAVLL ALALNICYVL
     LRRITGIRTI MLTGHIMFQQ AGLIAVTLFI FGYSMWTTII CTAILVSLYW GITSNMMYKP
     TQEVTDGCGF SIGHQQQFAS WTAYKVAPFL GKKEESVEDL KLPGWLNIFH DNIVSTAIVM
     TIFFGAILLS FGIDTVQAMA GKVHWTVYIL QTGFSFAVAI FIITQGVRMF VAELSEAFNG
     ISQRLIPGAV LAIDCAAIYS FAPNAVVWGF MWGTIGQLIA VGILVACGSS SLIIPGFIPM
     FFSNATIGVF ANHFGGWRAA LKICLVMGMI EIFGCVWAVK LTGMSAWMGM ADWSILAPPM
     MQGFFSIGIA FMAVIIVIAL AYMFFAGRAL RAEEDAEKQL AEQSA