ID   ULAB_SALPA              Reviewed;         101 AA.
AC   Q5PJ47;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=SPA4201;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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}.
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DR   EMBL; CP000026; AAV79938.1; -; Genomic_DNA.
DR   RefSeq; WP_000218360.1; NC_006511.1.
DR   AlphaFoldDB; Q5PJ47; -.
DR   SMR; Q5PJ47; -.
DR   EnsemblBacteria; AAV79938; AAV79938; SPA4201.
DR   GeneID; 58391105; -.
DR   KEGG; spt:SPA4201; -.
DR   HOGENOM; CLU_159248_0_0_6; -.
DR   OMA; QSKGMTN; -.
DR   Proteomes; UP000008185; 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_0000230324"
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