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HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Also phosphorylates/dephosphorylates the HPr-like catabolite repression protein crh on a specific serine residue. Therefore, by controlling the phosphorylation state of HPr and crh, HPrK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-serine + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46600"},{"database":"Rhea","id":"RHEA-COMP:11602"},{"database":"Rhea","id":"RHEA-COMP:11603"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001120"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01249"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[HPr protein]-O-phospho-L-serine + phosphate + H(+) = [HPr protein]-L-serine + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46604"},{"database":"Rhea","id":"RHEA-COMP:11602"},{"database":"Rhea","id":"RHEA-COMP:11603"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:83421"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047657"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01249"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01249"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011643"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01249"}],"value":"Homohexamer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01249"}],"value":"The Walker A ATP-binding motif also binds Pi and PPi"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01249"}],"value":"Both phosphorylation and phosphorolysis are carried out by the same active site and suggest a common mechanism for both reactions"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006883"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01249"}],"value":"Belongs to the HPrK/P family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MEV4913422.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"HPr(Ser) kinase/phosphorylase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02603"}]},{"type":"Domain","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"HPr kinase/phosphorylase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF07475"}]},{"type":"Region","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"Important for the catalytic mechanism of both phosphorylation and dephosphorylation","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01249"}]},{"type":"Region","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"Important for the catalytic mechanism of dephosphorylation","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01249"}]},{"type":"Active site","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01249"}]},{"type":"Active site","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01249"}]},{"type":"Active site","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"Proton acceptor; for phosphorylation activity. 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