ULAC_SALTI
ID ULAC_SALTI Reviewed; 154 AA.
AC Q8Z170; Q7C545;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Ascorbate-specific PTS system EIIA component {ECO:0000250|UniProtKB:P69820};
DE AltName: Full=Ascorbate-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P69820};
GN Name=ulaC; OrderedLocusNames=STY4741, t4436;
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:P69820}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by L-ascorbate. Repressed by UlaR.
CC {ECO:0000250|UniProtKB:P69820}.
CC -!- DOMAIN: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on
CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC EIIB type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00417}.
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DR EMBL; AL513382; CAD06862.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO71883.1; -; Genomic_DNA.
DR RefSeq; NP_458819.1; NC_003198.1.
DR RefSeq; WP_000776536.1; NZ_WSUR01000012.1.
DR AlphaFoldDB; Q8Z170; -.
DR SMR; Q8Z170; -.
DR STRING; 220341.16505510; -.
DR EnsemblBacteria; AAO71883; AAO71883; t4436.
DR KEGG; stt:t4436; -.
DR KEGG; sty:STY4741; -.
DR PATRIC; fig|220341.7.peg.4842; -.
DR eggNOG; COG1762; Bacteria.
DR HOGENOM; CLU_072531_2_0_6; -.
DR OMA; MGPYIIL; -.
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:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00211; PTS_IIA_fru; 1.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR SUPFAM; SSF55804; SSF55804; 1.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system; Transferase;
KW Transport.
FT CHAIN 1..154
FT /note="Ascorbate-specific PTS system EIIA component"
FT /id="PRO_0000230316"
FT DOMAIN 6..150
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 68
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT MOD_RES 68
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250|UniProtKB:P69820"
SQ SEQUENCE 154 AA; 17134 MW; 302502FE231F780E CRC64;
MKLRDSLAEN NSIRLQAEAN TWQEAVKIGV DLLVAADVVE PRYYQAILDG VEQFGPYFVI
APGLVMPHGR PEEGVKKTGF SLVTLKKPLE FNHEDNDPVD ILITMAAVDA NTHQEVGIMQ
IVNLFEDEAN FDRLRACRTA QEVLDLIDRT NAAA
