UniProt functional annotation for P69797



	UniProt functional annotation for P69797

UniProt code: P69797.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II ManXYZ PTS system is involved in mannose transport. {ECO:0000269|PubMed:2681202, ECO:0000269|PubMed:2951378, ECO:0000269|PubMed:2999119, ECO:0000269|PubMed:8262947}.

Function: Also functions as a receptor for bacterial chemotaxis and is required for infection of the cell by bacteriophage lambda where it most likely functions as a pore for penetration of lambda DNA. {ECO:0000269|PubMed:353494, ECO:0000269|PubMed:4604906}.

Catalytic activity: Reaction=D-mannose(out) + N(pros)-phospho-L-histidyl-[protein] = D- mannose 6-phosphate(in) + L-histidyl-[protein]; Xref=Rhea:RHEA:49232, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:4208, ChEBI:CHEBI:29979, ChEBI:CHEBI:58735, ChEBI:CHEBI:64837; EC=2.7.1.191; Evidence={ECO:0000269|PubMed:2681202, ECO:0000269|PubMed:8262947};

Subunit: Homodimer. {ECO:0000269|PubMed:15788390, ECO:0000269|PubMed:2681202, ECO:0000269|PubMed:2951378, ECO:0000269|PubMed:2999119, ECO:0000305|PubMed:8262947}.

Subcellular location: Cytoplasm {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:2951378, ECO:0000269|PubMed:2999119}. Cell inner membrane {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:2999119}; Peripheral membrane protein {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:2999119}.

Induction: Transcriptionally regulated by the Mlc transcriptional repressor and by the cAMP-CRP complex. Also weakly repressed by NagC. {ECO:0000269|PubMed:11361067}.

Domain: The PTS EIIA type-4 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-4 domain. {ECO:0000255|PROSITE-ProRule:PRU00419, ECO:0000305|PubMed:18270202, ECO:0000305|PubMed:8676384}.

Domain: The PTS EIIB type-4 domain is phosphorylated by phospho-EIIA on a histidyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-4 domain. {ECO:0000255|PROSITE-ProRule:PRU00424, ECO:0000305|PubMed:18270202}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II ManXYZ PTS system is involved in mannose transport. {ECO:0000269\|PubMed:2681202, ECO:0000269\|PubMed:2951378, ECO:0000269\|PubMed:2999119, ECO:0000269\|PubMed:8262947}.



Function:		Also functions as a receptor for bacterial chemotaxis and is required for infection of the cell by bacteriophage lambda where it most likely functions as a pore for penetration of lambda DNA. {ECO:0000269\|PubMed:353494, ECO:0000269\|PubMed:4604906}.


Catalytic activity:		Reaction=D-mannose(out) + N(pros)-phospho-L-histidyl-[protein] = D- mannose 6-phosphate(in) + L-histidyl-[protein]; Xref=Rhea:RHEA:49232, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:4208, ChEBI:CHEBI:29979, ChEBI:CHEBI:58735, ChEBI:CHEBI:64837; EC=2.7.1.191; Evidence={ECO:0000269\|PubMed:2681202, ECO:0000269\|PubMed:8262947};
Subunit:		Homodimer. {ECO:0000269\|PubMed:15788390, ECO:0000269\|PubMed:2681202, ECO:0000269\|PubMed:2951378, ECO:0000269\|PubMed:2999119, ECO:0000305\|PubMed:8262947}.
Subcellular location:		Cytoplasm {ECO:0000269\|PubMed:16079137, ECO:0000269\|PubMed:2951378, ECO:0000269\|PubMed:2999119}. Cell inner membrane {ECO:0000269\|PubMed:16079137, ECO:0000269\|PubMed:2999119}; Peripheral membrane protein {ECO:0000269\|PubMed:16079137, ECO:0000269\|PubMed:2999119}.
Induction:		Transcriptionally regulated by the Mlc transcriptional repressor and by the cAMP-CRP complex. Also weakly repressed by NagC. {ECO:0000269\|PubMed:11361067}.
Domain:		The PTS EIIA type-4 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-4 domain. {ECO:0000255\|PROSITE-ProRule:PRU00419, ECO:0000305\|PubMed:18270202, ECO:0000305\|PubMed:8676384}.
Domain:		The PTS EIIB type-4 domain is phosphorylated by phospho-EIIA on a histidyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-4 domain. {ECO:0000255\|PROSITE-ProRule:PRU00424, ECO:0000305\|PubMed:18270202}.