{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P46474","secondaryAccessions":["P46475","P46476","P76676","Q2M8W8","Q6BF41"],"uniProtkbId":"YHDP_ECOLI","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2004-11-23","entryVersion":153,"sequenceVersion":4},"annotationScore":4.0,"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:0000303","source":"PubMed","id":"38913742"}],"value":"Intermembrane phospholipid transporter YhdP"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Phospholipid transport protein YhdP"}}]},"genes":[{"geneName":{"value":"yhdP"},"synonyms":[{"value":"yhdQ"},{"value":"yhdR"}],"orderedLocusNames":[{"value":"b4472"},{"value":"JW5542"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30087168"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33046656"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34781743"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35226662"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38913742"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39638236"}],"value":"Involved in outer membrane lipid homeostasis (PubMed:33046656, PubMed:34781743, PubMed:35226662, PubMed:38913742, PubMed:39638236). Likely transports phospholipids between the inner membrane and the outer membrane (PubMed:33046656, PubMed:34781743, PubMed:35226662, PubMed:38913742, PubMed:39638236). It would provide a bridge-like structure that protects phospholipids as they travel across the periplasm (PubMed:34781743, PubMed:39638236). The phosphate-containing molecules are captured along the length of a hydrophobic groove that is continuous along all but the extreme N-terminus of the protein (PubMed:39638236). It also appears to control, directly or indirectly, levels of cyclic enterobacterial common antigen (cyclic ECA), a soluble cyclic ECA molecule present in the periplasm (PubMed:30087168)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34781743"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38913742"}],"value":"TamB, YdbH and YhdP are redundant, but not equivalent, in performing an essential function for growth and maintaining lipid homeostasis in the outer membrane (PubMed:34781743). The transport functions of TamB and YhdP could be differentiated according to the fatty acid saturation state of the phospholipids, with TamB transporting more unsaturated phospholipids and YhdP more saturated phospholipids (PubMed:38913742). Any of these three proteins is sufficient for growth (PubMed:34781743)"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39638236"}],"value":"Forms a periplasm spanning bridge (PubMed:39638236). A periplasmic localization is essential for function and stability, while the N-terminal transmembrane region is required for YhdP to be fully functional (PubMed:39638236)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39638236"}],"value":"Cell inner membrane","id":"SL-0037"},"topology":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"39638236"}],"value":"Single-pass type II membrane protein","id":"SL-9906"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39638236"}],"value":"Periplasmic side","id":"SL-9916"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39638236"}],"value":"Forms long, thin, rod-type structures predicted to consist of stacked beta strands (PubMed:39638236). Contains essential helical regions at the N-and C-termini, which may embed into the inner and outer membranes respectively, reinforcing the envelope spanning nature of YhdP (PubMed:39638236). The inner membrane-interacting regions, particularly the P-helix, are required for YhdP stability (PubMed:39638236). The C-terminal helices, particularly C-helix_1, are required for function, potentially in anchoring the protein to the outer membrane (PubMed:39638236)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30087168"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33046656"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34781743"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35226662"}],"value":"The single mutant does not exhibit growth defects but it shows a slight increase in outer membrane permeability (PubMed:34781743). Deletion of the gene leads to increased sensitivity to detergents and antibiotics such as sodium dodecyl sulfate (SDS) and vancomycin (PubMed:30087168). The deletion decreases cyclic enterobacterial common antigen (cyclic ECA) levels, causing changes in outer membrane permeability (PubMed:30087168). Deletion of the gene in the mlaA* mutant (which carries a dominant negative mutation that reverses the normal function of the MlaA protein) delays cell death by slowing the flow of phospholipids to the outer membrane (PubMed:33046656). The tamB-yhdP double mutant shows defects in outer membrane lipid homeostasis and sensitivity to bile salts and various antibiotics such as vancomycin (PubMed:34781743, PubMed:35226662). The loss of tamB and yhdP severely compromises the integrity of the cell envelope, and causes lysis and alterations to cellular morphology (PubMed:34781743, PubMed:35226662). The double mutant results in a more visible rounding of the cell leading to increased cell width, decreased cell length, and a significant decrease in cell surface area (PubMed:35226662). The absence of tamB and yhdP also leads to excess amounts of outer membrane vesicles (OMVs) that are rich in lipopolysaccharides, presumably to compensate for the lack of proper phospholipid transport to the outer membrane and to maintain outer membrane integrity (PubMed:35226662). Deletion of tamB, ydbH and yhdP is lethal (PubMed:34781743, PubMed:35226662)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the YhdP family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"AAA58047.1","note":"Produces three separate ORFs (yhdP, yhdQ and yhdR).","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"AAA58048.1","note":"Produces three separate ORFs (yhdP, yhdQ and yhdR).","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"AAA58049.1","note":"Produces three separate ORFs (yhdP, yhdQ and yhdR).","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1266,"modifier":"EXACT"}},"description":"Intermembrane phospholipid transporter YhdP","featureId":"PRO_0000013923"},{"type":"Topological domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":5,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"34781743"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"39638236"}]},{"type":"Transmembrane","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"Helical; Signal-anchor for type II membrane protein","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Topological domain","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":1266,"modifier":"EXACT"}},"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39638236"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"34781743"}]},{"type":"Region","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"P-helix","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"39638236"}]},{"type":"Region","location":{"start":{"value":1121,"modifier":"EXACT"},"end":{"value":1144,"modifier":"EXACT"}},"description":"C-helix_2","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"39638236"}]},{"type":"Region","location":{"start":{"value":1203,"modifier":"EXACT"},"end":{"value":1237,"modifier":"EXACT"}},"description":"C-helix_1","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"39638236"}]},{"type":"Sequence conflict","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":351,"modifier":"EXACT"}},"description":"in Ref. 1; AAA58048","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"G","alternativeSequences":["A"]}},{"type":"Sequence conflict","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"in Ref. 1; AAA58048","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"P","alternativeSequences":["R"]}}],"keywords":[{"id":"KW-0997","category":"Cellular component","name":"Cell inner membrane"},{"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"id":"KW-0445","category":"Biological process","name":"Lipid transport"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0735","category":"Domain","name":"Signal-anchor"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"9278503","citationType":"journal article","authors":["Blattner F.R.","Plunkett G. 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