ID B7MMZ8_ECO45 Unreviewed; 104 AA. AC B7MMZ8; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAR-2024, entry version 71. DE SubName: Full=Phosphotransferase system PTS, lactose/cellobiose-specific IIA subunit {ECO:0000313|EMBL:CAR02926.1}; GN OrderedLocusNames=ECS88_1611 {ECO:0000313|EMBL:CAR02926.1}; OS Escherichia coli O45:K1 (strain S88 / ExPEC). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR02926.1, ECO:0000313|Proteomes:UP000000747}; RN [1] {ECO:0000313|Proteomes:UP000000747} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747}; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E., RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR000699-2}; CC Note=Binds 1 Mg(2+) ion per trimer. {ECO:0000256|PIRSR:PIRSR000699-2}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU928161; CAR02926.1; -; Genomic_DNA. DR AlphaFoldDB; B7MMZ8; -. DR SMR; B7MMZ8; -. DR KEGG; ecz:ECS88_1611; -. DR HOGENOM; CLU_152490_1_0_6; -. DR Proteomes; UP000000747; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro. DR CDD; cd00215; PTS_IIA_lac; 1. DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1. DR InterPro; IPR003188; PTS_IIA_lac/cel. DR InterPro; IPR036542; PTS_IIA_lac/cel_sf. DR PANTHER; PTHR34382; PTS SYSTEM N,N'-DIACETYLCHITOBIOSE-SPECIFIC EIIA COMPONENT; 1. DR PANTHER; PTHR34382:SF7; PTS SYSTEM N,N'-DIACETYLCHITOBIOSE-SPECIFIC EIIA COMPONENT; 1. DR Pfam; PF02255; PTS_IIA; 1. DR PIRSF; PIRSF000699; PTS_IILac_III; 1. DR SUPFAM; SSF46973; Enzyme IIa from lactose specific PTS, IIa-lac; 1. DR PROSITE; PS51095; PTS_EIIA_TYPE_3; 1. PE 4: Predicted; KW Magnesium {ECO:0000256|PIRSR:PIRSR000699-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000699-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000747}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transport {ECO:0000256|ARBA:ARBA00022448}. FT ACT_SITE 77 FT /note="Tele-phosphohistidine intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR000699-1" FT BINDING 80 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared between all trimeric partners" FT /evidence="ECO:0000256|PIRSR:PIRSR000699-2" FT MOD_RES 77 FT /note="Phosphohistidine; by HPr" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00418" SQ SEQUENCE 104 AA; 11462 MW; 1F5051ACE8C7EB11 CRC64; MMFADEELVM ELLINAGQAR SDAMEAIRCA GQKDWQGATK LMASSESACL QAHKIQTALI SQDEGCGKIE VNLILIHAQD HLMNAILCQD LAREIISLRK ELHA //