{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"B2RLK9","uniProtkbId":"BAMH_PORG3","entryAudit":{"firstPublicDate":"2026-06-10","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2008-07-01","entryVersion":58,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)","taxonId":431947,"lineage":["Bacteria","Pseudomonadati","Bacteroidota","Bacteroidia","Bacteroidales","Porphyromonadaceae","Porphyromonas"]},"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":"BAG34254.1"}],"value":"PGN_1735"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41034344"},{"evidenceCode":"ECO:0000305","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 (Probable)"}],"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 pronounced extracellular dome-like structure (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:0000269","source":"PubMed","id":"41034344"}],"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":"Glycosylated"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41034344"}],"value":"Deletion of the gene disrupts the main surface lipoproteins-barrel complexes (PubMed:41034344). The level of 146 proteins is significantly decreased, including 17 lipoproteins, 9 TonB-dependent transporters (TBDTs) and 9 other beta-barrels (PubMed:41034344). BamH is the most depleted protein, but the levels of other components of PgBAM remain unchanged, except for BamK, which is the most enriched protein in the analysis (PubMed:41034344). Deletion of the gene leads to slightly reduced growth in rich medium, and to a drastic growth reduction in minimal medium containing 1% bovine serum albumin (BSA) as carbon and nitrogen source (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":18,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Chain","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":455,"modifier":"EXACT"}},"description":"Outer membrane protein assembly factor BamH","featureId":"PRO_5030165534"},{"type":"Lipidation","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":19,"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":"18524787","citationType":"journal article","authors":["Naito M.","Hirakawa H.","Yamashita A.","Ohara N.","Shoji M.","Yukitake H.","Nakayama K.","Toh H.","Yoshimura F.","Kuhara S.","Hattori M.","Hayashi T.","Nakayama K."],"citationCrossReferences":[{"database":"PubMed","id":"18524787"},{"database":"DOI","id":"10.1093/dnares/dsn013"}],"title":"Determination of the genome sequence of Porphyromonas gingivalis strain ATCC 33277 and genomic comparison with strain W83 revealed extensive genome rearrangements in P. gingivalis.","publicationDate":"2008","journal":"DNA Res.","firstPage":"215","lastPage":"225","volume":"15"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"BAG34254.1"}]},{"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 (3.24 ANGSTROMS) OF BAMADGHIJK COMPLEX","FUNCTION","SUBUNIT","SUBCELLULAR LOCATION","GLYCOSYLATION","DISRUPTION PHENOTYPE"],"referenceComments":[{"value":"ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP009380","properties":[{"key":"ProteinId","value":"BAG34254.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_012458494.1","properties":[{"key":"NucleotideSequenceId","value":"NC_010729.1"}]},{"database":"PDB","id":"9HJM","properties":[{"key":"Method","value":"EM"},{"key":"Resolution","value":"3.24 A"},{"key":"Chains","value":"G=1-455"}]},{"database":"PDBsum","id":"9HJM","properties":[{"key":"Description","value":"-"}]},{"database":"AlphaFoldDB","id":"B2RLK9","properties":[{"key":"Description","value":"-"}]},{"database":"EMDB","id":"EMD-52218","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"B2RLK9","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"29256896","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pgn:PGN_1735","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"ENOG502ZCA6","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"HOGENOM","id":"CLU_041004_0_0_10","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"1110209at2","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"PGIN431947:G1G2V-1946-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000008842","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":"MKRYLLLVFSLMALLTVACDDDLSPIGGSIQPPSDPVSARVDTLEFSVKTIPMGDIYNRTNYTLLGDLTDPEYGDLKADYIMQFKSPRNFKFKYPPKDGKIDSVKLSINYDSWAGDSTSIMKVSIYKINKAIPPSYYSTQELASLLDETQIIASQTFKAGNDSAFHRVRIPLPNEIGQKIYDLSVNNPSVFDTQESFYNNVLGGLYVTTTTGTGVVLSVYNTQMAIFYSYKVAADSTATASETFVNTSESYQVNHIKNSQISHLLQENDSLSCVKSPAGVMTQLTISKEQFTDAFTSNLSSSLAWQIGEAQFNISASKPSEGLMLSPPSYLLLLPQDSVRNFFEQEQTELMQPRTAFLSTIYNIKKREYRFSNISRLLMEHIKNNTEKTPEGKPYITKDLVLVLLPVKRQVAGASNSLYTSQLNNFMFPSGVKLQLGKKNKTARIGVYSMTYTDN","length":455,"molWeight":50836,"crc64":"F2AF2932799F4478","md5":"6A3CF1CC9457FCF93FA7FB48B8FA8007"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"PTM":1,"DISRUPTION PHENOTYPE":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1,"Lipidation":2},"uniParcId":"UPI000174FD04"}}