ID   ULAA_SHIBS              Reviewed;         456 AA.
AC   Q31TC4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 67.
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=SBO_4262;
OS   Shigella boydii serotype 4 (strain Sb227).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb227;
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   -!- SEQUENCE CAUTION:
CC       Sequence=ABB68684.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000036; ABB68684.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q31TC4; -.
DR   SMR; Q31TC4; -.
DR   EnsemblBacteria; ABB68684; ABB68684; SBO_4262.
DR   KEGG; sbo:SBO_4262; -.
DR   HOGENOM; CLU_031784_1_0_6; -.
DR   Proteomes; UP000007067; 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   Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..456
FT                   /note="Ascorbate-specific PTS system EIIC component"
FT                   /id="PRO_0000230661"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P39301"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P39301"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P39301"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P39301"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P39301"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P39301"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P39301"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P39301"
FT   TRANSMEM        370..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P39301"
FT   TRANSMEM        418..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P39301"
FT   BINDING         77..78
FT                   /ligand="L-ascorbate"
FT                   /ligand_id="ChEBI:CHEBI:38290"
FT                   /evidence="ECO:0000250|UniProtKB:P39301"
FT   BINDING         126..130
FT                   /ligand="L-ascorbate"
FT                   /ligand_id="ChEBI:CHEBI:38290"
FT                   /evidence="ECO:0000250|UniProtKB:P39301"
FT   BINDING         185..186
FT                   /ligand="L-ascorbate"
FT                   /ligand_id="ChEBI:CHEBI:38290"
FT                   /evidence="ECO:0000250|UniProtKB:P39301"
FT   BINDING         305
FT                   /ligand="L-ascorbate"
FT                   /ligand_id="ChEBI:CHEBI:38290"
FT                   /evidence="ECO:0000250|UniProtKB:P39301"
SQ   SEQUENCE   456 AA;  49621 MW;  586EC682640696FE CRC64;
     MFFNQVMTNA PLLLGIVTCL GYILLRKSVS VIIKGTIKTI IGFMLLQAGS GILTSTFKPV
     VAKMSEVYGI NGAISDTYAS MMATIDRMGD AYSWVGYAVL LALALNICYV LLRRITGIRT
     IMLTGHIMFQ QAGLIAVTLF IFGYSMWTTI ICTAILVSLY WGITSNMMYK PTQEVTDGCG
     FSIGHQQQFA SWIAYKVAPF LGKKEESVED LKLPGWLNIF HDNIVSTAIV MTIFFGAILL
     SFGIDTVQAM AGKVNWTVYI LQTGFSFAVA IFIITQGVRM FVAELSEAFN GISQRLIPGA
     VLAIDCAAIY SFAPNAVVWG FMWGTIGQLI AVGILVACGS SILIIPGFIP MFFSNATIGV
     FANHFGGWRA ALKICLVMGM IEIFGCVWAV KLTGMSAWMG MADWSILAPP MMQGFFSIGI
     AFMAVIIVIA LAYMFFAGRA LRAEEDAEKQ LAEQSA