ULAC_SALPA
ID ULAC_SALPA Reviewed; 154 AA.
AC Q5PJ64;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=SPA4202;
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: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; CP000026; AAV79939.1; -; Genomic_DNA.
DR RefSeq; WP_000776534.1; NC_006511.1.
DR AlphaFoldDB; Q5PJ64; -.
DR SMR; Q5PJ64; -.
DR EnsemblBacteria; AAV79939; AAV79939; SPA4202.
DR KEGG; spt:SPA4202; -.
DR HOGENOM; CLU_072531_2_0_6; -.
DR OMA; MGPYIIL; -.
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: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.
DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 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_0000230315"
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; 17083 MW; 303482762C786E69 CRC64;
MKLRDSLAEN NSIRLQAEAN TWQEAVKIGV DLLVAADVVE PRYYQAILDG VEQFGPYFVI
APGLAMPHGR PEEGVKKTGF SLVTLKKPLE FNHEDNDPVD ILITMAAVDA NTNQEVGIMQ
IVNLFEDEAN FDRLRACRTA QEVLDLIDRT NAAA
