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ULAB_SHIFL
ID   ULAB_SHIFL              Reviewed;         101 AA.
AC   Q83P29; Q7UAK7;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 4.
DT   03-AUG-2022, entry version 115.
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=SF4349, S4619;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(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}.
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DR   EMBL; AE005674; AAN45766.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP19548.1; -; Genomic_DNA.
DR   RefSeq; NP_710059.2; NC_004337.2.
DR   RefSeq; WP_000218360.1; NZ_WPGW01000113.1.
DR   AlphaFoldDB; Q83P29; -.
DR   SMR; Q83P29; -.
DR   STRING; 198214.SF4349; -.
DR   EnsemblBacteria; AAN45766; AAN45766; SF4349.
DR   EnsemblBacteria; AAP19548; AAP19548; S4619.
DR   GeneID; 1025912; -.
DR   GeneID; 58391105; -.
DR   KEGG; sfl:SF4349; -.
DR   KEGG; sfx:S4619; -.
DR   PATRIC; fig|198214.7.peg.5128; -.
DR   HOGENOM; CLU_159248_0_0_6; -.
DR   OMA; QSKGMTN; -.
DR   OrthoDB; 1884107at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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;
KW   Reference proteome; Transferase; Transport.
FT   CHAIN           1..101
FT                   /note="Ascorbate-specific PTS system EIIB component"
FT                   /id="PRO_0000230329"
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
 
 
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