ULAA_MYCPN
ID ULAA_MYCPN Reviewed; 660 AA.
AC P75291;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 96.
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; Synonyms=sgaT; OrderedLocusNames=MPN_496; ORFNames=MP347;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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 membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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}.
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DR EMBL; U00089; AAB95995.1; -; Genomic_DNA.
DR PIR; S73673; S73673.
DR RefSeq; NP_110184.1; NC_000912.1.
DR RefSeq; WP_010874852.1; NC_000912.1.
DR AlphaFoldDB; P75291; -.
DR SMR; P75291; -.
DR STRING; 272634.MPN_496; -.
DR EnsemblBacteria; AAB95995; AAB95995; MPN_496.
DR GeneID; 66608832; -.
DR KEGG; mpn:MPN_496; -.
DR PATRIC; fig|272634.6.peg.536; -.
DR HOGENOM; CLU_031784_1_2_14; -.
DR OMA; IAHQQMF; -.
DR BioCyc; MPNE272634:G1GJ3-813-MON; -.
DR Proteomes; UP000000808; 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 membrane; Membrane; Phosphotransferase system; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..660
FT /note="Ascorbate-specific PTS system EIIC component"
FT /id="PRO_0000097715"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 592..612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 141..142
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:P39301"
FT BINDING 196..200
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:P39301"
FT BINDING 268..269
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:P39301"
FT BINDING 409
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:P39301"
SQ SEQUENCE 660 AA; 70859 MW; AA45EC672921BAA8 CRC64;
MLNKIKLQQK RKLIIGWSVF ALINLVVILL TVLLRAGLPN LVSKGVTPFS AQAFGDAFIF
LITRVYLDNF LRQPALLLGV ITLIGYLALG RGGVQSVVGA LKTVIGFILL SIGSGVLVST
ARPVFDTIKG LGGTGVVLLD PYFSLASAND FFTNSFLNND YVSLIAFSLL VGFIVNIIFV
GLKRWTNTNS IMVTGHVMLQ QAAVVTTLFY IVLFRQIPLL GTGIAYGAQA GLVIISGIFL
GVYWSTASTG TYLVTNKVTN NAGFSIGHQQ MLGIMTVAKL GKYFGDKNDS AEHKKLPKAL
KIFEDNIFTQ TIIILSLFVV LFIVILASYK GDKPLLINWD KFGAINGLEI WNTTFGGANF
TLNIIGGALK MVASLIAIMT GVRMFITELQ QAFQGISEKV VPGAVVAVDI AAVYGFSINS
VTFGFLSGVI GQFLAVAIMA GISYIPGNQF SFVAIPLFIT LFFNSGAFGV YANAEGGWKA
ALLLPGIIGF LEIIVISFAL RTVSNAYQAS ALLDAKQSFD LKALMGNSLD NNNGSALKTA
VEKVVNATGV NRITEAQSFV KSDSFNSLKA VNSTLAQAIE WISKSASPVD NGFIGMADWN
LYFGLLVWIG AYNVIGGWIL VILATVGLIL LAQIIDNGKQ TKVTKLQQLL KINPQLDLNN
