YADI_ECOLI
ID YADI_ECOLI Reviewed; 146 AA.
AC P36881; P75658;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Putative phosphotransferase enzyme IIA component YadI;
DE AltName: Full=Putative PTS system EIIA component;
GN Name=yadI; OrderedLocusNames=b0129, JW0125;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
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.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a histidyl
CC residue. Then, it transfers the phosphoryl group to the EIIB domain.
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DR EMBL; U00096; AAC73240.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96706.2; -; Genomic_DNA.
DR PIR; A64736; A64736.
DR RefSeq; NP_414671.1; NC_000913.3.
DR RefSeq; WP_000901987.1; NZ_STEB01000010.1.
DR AlphaFoldDB; P36881; -.
DR SMR; P36881; -.
DR STRING; 511145.b0129; -.
DR PaxDb; P36881; -.
DR PRIDE; P36881; -.
DR DNASU; 947397; -.
DR EnsemblBacteria; AAC73240; AAC73240; b0129.
DR EnsemblBacteria; BAB96706; BAB96706; BAB96706.
DR GeneID; 947397; -.
DR KEGG; ecj:JW0125; -.
DR KEGG; eco:b0129; -.
DR PATRIC; fig|1411691.4.peg.2153; -.
DR EchoBASE; EB2227; -.
DR eggNOG; COG2893; Bacteria.
DR HOGENOM; CLU_123235_1_0_6; -.
DR InParanoid; P36881; -.
DR OMA; GWVIACH; -.
DR PhylomeDB; P36881; -.
DR BioCyc; EcoCyc:AGAX-MON; -.
DR BioCyc; MetaCyc:AGAX-MON; -.
DR PRO; PR:P36881; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
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; cd00006; PTS_IIA_man; 1.
DR Gene3D; 3.40.50.510; -; 1.
DR InterPro; IPR004701; PTS_EIIA_man-typ.
DR InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR InterPro; IPR033887; PTS_IIA_man.
DR Pfam; PF03610; EIIA-man; 1.
DR SUPFAM; SSF53062; SSF53062; 1.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Kinase; Phosphotransferase system; Reference proteome;
KW Sugar transport; Transferase; Transport.
FT CHAIN 1..146
FT /note="Putative phosphotransferase enzyme IIA component
FT YadI"
FT /id="PRO_0000186708"
FT DOMAIN 1..124
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
SQ SEQUENCE 146 AA; 16540 MW; 9534A95A41130CE5 CRC64;
MLGWVITCHD DRAQEILDAL EKKHGALLQC RAVNFWRGLS SNMLSRMMCD ALHEADSGEG
VIFLTDIAGA PPYRVASLLS HKHSRCEVIS GVTLPLIEQM MACRETMTSS EFRERIVELG
APEVSSLWHQ QQKNPPFVLK HNLYEY