{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q89ZS0","uniProtkbId":"BAMH_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 BamH"}},"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"41034344"}],"value":"bamH"},"orderedLocusNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAO79411.1"}],"value":"BT_4306"}]}],"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 (PubMed:41034344). BamH probably functions as a scaffold (PubMed:41034344)"}],"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). BamH interacts with BamI and BamJ on one side and with BamK on the other (PubMed:41034344). The highly conserved N-terminus of BamH is wedged between two strands of the BamG barrel and interacts with the conserved BamG N-terminus (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":"O-glycosylated (PubMed:41034344). It is unclear whether glycosylation has any functional relevance (PubMed:41034344)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41034344"}],"value":"Deletion of the gene affects cell surface structure biogenesis (PubMed:41034344). A total of 131 proteins are less abundant in the mutant strain compared with wild-type strain (PubMed:41034344). Pulldown experiments show that deletion of the gene leads to the loss of all surface components from the BtBAM complex (BamH-K) while the levels of the BamADG core remain similar, but the total membrane proteomics show that only the BamH and BamK levels are lower in the mutant, while BamI and BamJ are not affected (PubMed:41034344). However, it does not result in global depletion of outer membrane beta-barrels and surface lipoproteins, and it does not drastically affect the normal BtBAM beta-barrel insertase function in vitro (PubMed:41034344). The mutant shows growth defects in rich medium and minimal medium with both monosaccharides and polysaccharides as carbon sources (PubMed:41034344). The mutant also shows a severe decrease in outer membrane stress tolerance when cultured in the presence of the outer membrane stressors SDS and sodium deoxycholate (PubMed:41034344)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the BamH family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Chain","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":542,"modifier":"EXACT"}},"description":"Outer membrane protein assembly factor BamH","featureId":"PRO_0000463737"},{"type":"Lipidation","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":18,"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":"AAO79411.1"}]},{"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. Microbiol.","firstPage":"2845","lastPage":"2859","volume":"10"},"referencePositions":["STRUCTURE BY ELECTRON MICROSCOPY (3.28 ANGSTROMS) OF BAMHIJK AND BAMADGHIJK COMPLEXES","FUNCTION","SUBUNIT","SUBCELLULAR LOCATION","GLYCOSYLATION","DISRUPTION PHENOTYPE"],"referenceComments":[{"value":"ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"9HIS"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"9HJ3"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AE015928","properties":[{"key":"ProteinId","value":"AAO79411.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_008764494.1","properties":[{"key":"NucleotideSequenceId","value":"NC_004663.1"}]},{"database":"PDB","id":"9HIS","properties":[{"key":"Method","value":"EM"},{"key":"Resolution","value":"3.28 A"},{"key":"Chains","value":"G=18-542"}]},{"database":"PDB","id":"9HJ3","properties":[{"key":"Method","value":"EM"},{"key":"Resolution","value":"3.46 A"},{"key":"Chains","value":"G=18-542"}]},{"database":"PDBsum","id":"9HIS","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"9HJ3","properties":[{"key":"Description","value":"-"}]},{"database":"AlphaFoldDB","id":"Q89ZS0","properties":[{"key":"Description","value":"-"}]},{"database":"EMDB","id":"EMD-52200","properties":[{"key":"Description","value":"-"}]},{"database":"EMDB","id":"EMD-52209","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q89ZS0","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"226186.BT_4306","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"226186-BT_4306","properties":[{"key":"Description","value":"-"}]},{"database":"DNASU","id":"1074038","properties":[{"key":"Description","value":"-"}]},{"database":"EnsemblBacteria","id":"AAO79411","properties":[{"key":"ProteinId","value":"AAO79411"},{"key":"GeneId","value":"BT_4306"}]},{"database":"GeneID","id":"60925484","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"bth:BT_4306","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|226186.12.peg.4381","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"ENOG502ZBIE","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"HOGENOM","id":"CLU_041004_0_0_10","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"Q89ZS0","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"1110209at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000001414","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0009279","properties":[{"key":"GoTerm","value":"C:cell outer membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"InterPro","id":"IPR025366","properties":[{"key":"EntryName","value":"DUF4270"}]},{"database":"Pfam","id":"PF14092","properties":[{"key":"EntryName","value":"BamH"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKAKYALIALLAITFFGCDDNTGGLGLGMFPGNDQNIKGKLSTFDVTTESVKTGDIYAKTNIGYIGKFTDETFGTYQAGFLAQLNCPDGLTFPEPYKEVTDASGNVISATGRMVVDDKDPENKDVTFIKDGNQIIGNIRAVELYLWYDSYFGDSLTACRLSVYELGGNGKETLNLDNAYYTDINPEDFYDSQNILGTKAYTAVDLSVKDSIRNLSTYVPSVHIAFKEDIATRVGGNILTAARKAKNADKEFNSQLFREAFQGIYVKSDYGDGTVLYIDQPQMNVVYKCYATDSITGKKLQKKDGSGKDSTYYSYRVFATTREVIQANQLKNDPERIDALIKEDKNTYLKSPAGIFTEATLPISDIQNELTGDTLNAVKLTFTNYNQTGDKKFGMAIPSTVMLVRKKFQDSFFKDNKLSDGVSSYLTSHTSSTNQYVFSNITKLVNACIAEKEEAKKNAGSSWDETKWLQENPDWNKVVLIPVLVTYDSSNTTTGQANIIRIQHDLKPGYVRLKGGSLGKTNPDYKLKLEVISTDFGLTTKSN","length":542,"molWeight":60056,"crc64":"E1C31EFE67BC9F05","md5":"9E91888622B6AE880101E8C7737EF1C4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"PTM":1,"DISRUPTION PHENOTYPE":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1,"Lipidation":2},"uniParcId":"UPI000005BAA5"}}