{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9HVU5","uniProtkbId":"YHDP_PSEAE","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2001-03-01","entryVersion":103,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","taxonId":208964,"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAG07864.1"},{"evidenceCode":"ECO:0000312","source":"Proteomes","id":"UP000002438"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Intermembrane phospholipid transporter YhdP"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"38305166"}],"value":"AsmA-like protein YhdP"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Phospholipid transport protein YhdP"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"38305166"}],"value":"yhdP"},"orderedLocusNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAG07864.1"}],"value":"PA4476"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P46474"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38305166"}],"value":"Involved in outer membrane lipid homeostasis (PubMed:38305166). Likely transports phospholipids between the inner membrane and the outer membrane (By similarity). It would provide a bridge-like structure that protects phospholipids as they travel across the periplasm (By similarity). 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 (By similarity). Important for proper cell morphology and integrity of the outer membrane (PubMed:38305166)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38305166"}],"value":"EpaF, TamB, YdbH and YhdP are redundant, but not equivalent, in performing an essential function for growth and maintaining lipid homeostasis in the outer membrane. Any of these four proteins is sufficient for growth"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P46474"}],"value":"Forms a periplasm spanning bridge. A periplasmic localization is essential for function and stability, while the N-terminal transmembrane region is required for YhdP to be fully functional"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P46474"}],"value":"Cell inner membrane","id":"SL-0037"},"topology":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P46474"}],"value":"Single-pass type II membrane protein","id":"SL-9906"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P46474"}],"value":"Periplasmic side","id":"SL-9916"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38305166"}],"value":"The single mutant does not exhibit growth defects or cellular morphology alterations, but it shows a 20-fold increase in outer membrane (OM) permeability to fluorescent probe 1-N-phenylnaphthylamine (NPN), indicating that the permeability barrier of the OM is significantly compromised. Deletion of the gene leads to increased sensitivity to vancomycin. The tamB-yhdP double mutant shows slightly impaired growth (smaller colonies on Mueller-Hinton (MH) agar), hugely increased vancomycin sensitivity, and slightly increased sensitivity to colistin. The tamB-yhdP double mutant cells are smaller (reduced cell area) and rounder (lower length/width ratio) than wild-type cells. Both ydbH-yhdP and epaF-yhdP double mutant cells show further increase in OM permeability to NPN. The defects in the OM permeability are partially rescued by lowering the synthesis or transport of lipopolysaccharide (LPS). The tamB-ydbH-yhdP triple mutant is strongly growth-defective on MH agar and more sensitive to the membrane-destabilizing agents SDS and EDTA. The tamB-ydbH-yhdP triple mutant has drastically reduced growth rate and yield in a planktonic growth assay performed in MH broth. In the planktonic assay, a slight decrease in growth yields is seen for the tamB-yhdP double mutant and, to a greater extent, for the tamB-epaF-yhdP triple mutant. The cells of both the tamB-ydbH-yhdP and tamB-epaF-yhdP triple mutants are smaller and rounder than wild-type. Z-ring assembly or localization is not affected in any of the double or triple mutants. Simultaneous deletion of epaF, tamB, ydbH, yhdP is lethal"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the YhdP family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1276,"modifier":"EXACT"}},"description":"Intermembrane phospholipid transporter YhdP","featureId":"PRO_0000463943"},{"type":"Topological domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Transmembrane","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"Helical; Signal-anchor for type II membrane protein","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Topological domain","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":1276,"modifier":"EXACT"}},"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Region","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"P-helix","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P46474"}]},{"type":"Region","location":{"start":{"value":1133,"modifier":"EXACT"},"end":{"value":1156,"modifier":"EXACT"}},"description":"C-helix_2","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P46474"}]},{"type":"Region","location":{"start":{"value":1216,"modifier":"EXACT"},"end":{"value":1250,"modifier":"EXACT"}},"description":"C-helix_1","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P46474"}]}],"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":"10984043","citationType":"journal article","authors":["Stover C.K.","Pham X.-Q.T.","Erwin A.L.","Mizoguchi S.D.","Warrener P.","Hickey M.J.","Brinkman F.S.L.","Hufnagle W.O.","Kowalik D.J.","Lagrou M.","Garber R.L.","Goltry L.","Tolentino E.","Westbrock-Wadman S.","Yuan Y.","Brody L.L.","Coulter S.N.","Folger K.R.","Kas A.","Larbig K.","Lim R.M.","Smith K.A.","Spencer D.H.","Wong G.K.-S.","Wu Z.","Paulsen I.T.","Reizer J.","Saier M.H. 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