ULAB_SALTI
ID ULAB_SALTI Reviewed; 101 AA.
AC Q8Z171; Q83SS3;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Ascorbate-specific PTS system EIIB component {ECO:0000250|UniProtKB:P69822};
DE EC=2.7.1.194 {ECO:0000250|UniProtKB:P69822};
DE AltName: Full=Ascorbate-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P69822};
GN Name=ulaB; OrderedLocusNames=STY4740, t4435;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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:P69822}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ascorbate(out) + N(pros)-phospho-L-histidyl-[protein] = L-
CC ascorbate 6-phosphate(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:42436, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:38290, ChEBI:CHEBI:61698,
CC ChEBI:CHEBI:64837; EC=2.7.1.194;
CC Evidence={ECO:0000250|UniProtKB:P69822};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by L-ascorbate. Repressed by UlaR.
CC {ECO:0000250|UniProtKB:P69822}.
CC -!- DOMAIN: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on
CC a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00422}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO71882.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL513382; CAD06861.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO71882.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; NP_458818.1; NC_003198.1.
DR RefSeq; WP_000218360.1; NZ_QXGZ01000019.1.
DR AlphaFoldDB; Q8Z171; -.
DR SMR; Q8Z171; -.
DR STRING; 220341.16505509; -.
DR EnsemblBacteria; AAO71882; AAO71882; t4435.
DR GeneID; 58391105; -.
DR KEGG; stt:t4435; -.
DR KEGG; sty:STY4740; -.
DR PATRIC; fig|220341.7.peg.4841; -.
DR eggNOG; COG3414; Bacteria.
DR HOGENOM; CLU_1509537_0_0_6; -.
DR OMA; QSKGMTN; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR013011; PTS_EIIB_2.
DR InterPro; IPR003501; PTS_EIIB_2/3.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 1.
DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system; Transferase;
KW Transport.
FT CHAIN 1..101
FT /note="Ascorbate-specific PTS system EIIB component"
FT /id="PRO_0000230325"
FT DOMAIN 3..96
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT ACT_SITE 9
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00550, ECO:0000305"
FT MOD_RES 9
FT /note="Phosphocysteine"
FT /evidence="ECO:0000250|UniProtKB:P00550, ECO:0000305"
SQ SEQUENCE 101 AA; 10838 MW; 30CFB6B17250D47B CRC64;
MTVRILAVCG NGQGSSMIMK MKVDQFLTQS NIDHTVNSCA VGEYKSELSG ADIIIASTHI
AGEITVTGNK YVVGVRNMLS PADFGPKLLE VIKAHFPQDV K
