{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q8A1D9","uniProtkbId":"BAMI_BACTN","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2003-06-01","entryVersion":94,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)","taxonId":226186,"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Bacteroidia","Bacteroidales","Bacteroidaceae","Bacteroides"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Outer membrane protein assembly factor BamI"}},"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"41034344"}],"value":"bamI"},"orderedLocusNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAO78832.1"}],"value":"BT_3727"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41034344"}],"value":"Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41034344"}],"value":"The Bacteroidota beta-barrel assembly machinery (BAM) complex is composed of seven components: the canonical outer membrane protein assembly factors BamA and BamD, the integral beta-barrel protein BamG and four surface-exposed lipoproteins, BamH, BamI, BamJ and BamK (PubMed:41034344). BamG-K form a striking, half dome-shaped structure in the extracellular space, with its apex almost exactly above the lateral opening of BamA (PubMed:41034344). BamI interacts with BamJ and BamH (PubMed:41034344)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41034344"}],"value":"Cell outer membrane","id":"SL-0040"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}],"value":"Lipid-anchor","id":"SL-9901"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41034344"}],"value":"Extracellular side","id":"SL-9911"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41034344"}],"value":"The small N-terminal domain is conserved and interacts with BamJ (PubMed:41034344). The less-conserved C-terminal domain contacts BamH and adopts a six-bladed beta-propeller fold, with each blade consisting of three to four beta-strands (PubMed:41034344)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41034344"}],"value":"O-glycosylated (PubMed:41034344). It is unclear whether glycosylation has any functional relevance (PubMed:41034344)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the BamI family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Chain","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":493,"modifier":"EXACT"}},"description":"Outer membrane protein assembly factor BamI","featureId":"PRO_5004306347"},{"type":"Lipidation","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"S-diacylglycerol cysteine","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0998","category":"Cellular component","name":"Cell outer membrane"},{"id":"KW-0449","category":"PTM","name":"Lipoprotein"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0564","category":"PTM","name":"Palmitate"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"12663928","citationType":"journal article","authors":["Xu J.","Bjursell M.K.","Himrod J.","Deng S.","Carmichael L.K.","Chiang H.C.","Hooper L.V.","Gordon J.I."],"citationCrossReferences":[{"database":"PubMed","id":"12663928"},{"database":"DOI","id":"10.1126/science.1080029"}],"title":"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.","publicationDate":"2003","journal":"Science","firstPage":"2074","lastPage":"2076","volume":"299"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAO78832.1"}]},{"referenceNumber":2,"citation":{"id":"41034344","citationType":"journal article","authors":["Silale A.","Madej M.","Mikruta K.","Frey A.M.","Hart A.J.","Basle A.","Scavenius C.","Enghild J.J.","Trost M.","Hirt R.P.","van den Berg B."],"citationCrossReferences":[{"database":"PubMed","id":"41034344"},{"database":"DOI","id":"10.1038/s41564-025-02132-2"}],"title":"Structure of a distinct beta-barrel assembly machinery complex in the Bacteroidota.","publicationDate":"2025","journal":"Nat. 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