{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P76264","secondaryAccessions":["O07974"],"uniProtkbId":"MNTP_ECOLI","entryAudit":{"firstPublicDate":"1998-07-15","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2004-09-27","entryVersion":161,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01521"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29440394"}],"value":"Manganese exporter MntP"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"36190429"}],"value":"Manganese efflux protein MntP"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01521"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21908668"}],"value":"mntP"},"synonyms":[{"value":"yebN"}],"orderedLocusNames":[{"value":"b1821"},{"value":"JW5830"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21908668"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25774656"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29440394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38869303"}],"value":"Functions as a manganese exporter (PubMed:29440394, PubMed:38869303). Involved in manganese homeostasis (PubMed:21908668, PubMed:25774656, PubMed:29440394). Important for reducing the concentration of manganese in the cell when manganese levels are high, thus reducing its toxicity (PubMed:25774656). Transport of Mn(2+) by MntP is unlikely to be accompanied by an H(+) antiport (PubMed:38869303). Alters cellular resistance to reactive oxygen species (ROS) (PubMed:29440394)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Mn(2+)(in) = Mn(2+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28699"},{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01521"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29440394"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21908668"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:28700"},"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01521"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29440394"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21908668"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25774656"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38104967"}],"value":"When manganese levels drop, MntP export activity is inhibited by MntS (PubMed:25774656, PubMed:38104967). MntS acts by binding directly to MntP (PubMed:38104967). Inhibition of MntP by MntS could modestly increase the intracellular manganese pool and thereby enhance manganese entry into proteins (PubMed:25774656)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38104967"}],"value":"Interacts with the small protein MntS"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15919996"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29440394"}],"value":"Cell inner membrane","id":"SL-0037"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21908668"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25794618"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36190429"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38869303"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39510182"}],"value":"Expression is regulated by manganese at both the transcriptional and post-transcriptional levels (PubMed:25794618). Transcription is up-regulated by Fur and MntR in response to Mn(2+) (PubMed:21908668, PubMed:25794618). The Fur and MntR repressors activate mntP transcription by counteracting the repressive effects of the histone-like H-NS protein (PubMed:25794618). Translation is then regulated by the Mn(2+)-responsive mntP riboswitch, a member of the yybP-ykoY riboswitch family, which is located in the 5' untranslated region (5'-UTR) of mntP (PubMed:25794618). When intracellular manganese levels are high, the riboswitch directly binds Mn(2+), resulting in a conformation that liberates the ribosome-binding site, leading to increased mntP translation and increased Mn(2+) export (PubMed:25794618). The riboswitch is also responsive to alkaline pH, which favors the interaction between manganese and the riboswitch, resulting in increased mntP translation (PubMed:36190429). Manganese and alkaline pH are both necessary for maximal mntP riboswitch activation to mitigate the manganese toxicity (PubMed:36190429). Alkaline pH alone has no impact on mntP expression (PubMed:38869303). The mntP riboswitch also serves as a platform for the Rho-dependent transcription termination to down-regulate mntP expression (PubMed:39510182). Rho-dependent termination acts to moderate MntP levels and protects the cell from excessive MntP expression, which causes membrane protein toxicity (PubMed:39510182)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21908668"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29440394"}],"value":"Deletion causes manganese sensitivity and leads to increased intracellular manganese levels (PubMed:21908668, PubMed:29440394). The deletion mutant can only tolerate up to 0.1 mM supplemental MnCl(2), whereas the wild-type strain can grow in the presence of up to 5 mM MnCl(2) (PubMed:29440394)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25774656"}],"value":"E.coli may control manganese levels by balancing the actions of MntH, MntP and MntS against one another"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01521"},{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the MntP (TC 9.B.29) family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"Manganese exporter MntP","featureId":"PRO_0000155649"},{"type":"Topological domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":6,"modifier":"EXACT"}},"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Transmembrane","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Topological domain","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Transmembrane","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Topological domain","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Transmembrane","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Topological domain","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Transmembrane","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Topological domain","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Transmembrane","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Topological domain","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Transmembrane","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Topological domain","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15919996"}]},{"type":"Mutagenesis","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"Loss of activity, cannot complement a deletion mutant.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29440394"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"Does not affect manganese export.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29440394"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"Decrease in activity. 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