{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P39321","secondaryAccessions":["P39322","P76802","Q2M684"],"uniProtkbId":"TAMB_ECOLI","entryAudit":{"firstPublicDate":"1995-02-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1997-11-01","entryVersion":146,"sequenceVersion":2},"annotationScore":5.0,"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":"22466966"}],"value":"Translocation and assembly module subunit TamB"}},"alternativeNames":[{"fullName":{"value":"Autotransporter assembly factor TamB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"38913742"}],"value":"Intermembrane phospholipid transporter TamB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Phospholipid transport protein TamB"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"22466966"}],"value":"tamB"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAC77178.1"}],"value":"ytfN"},{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAC77178.1"}],"value":"ytfO"}],"orderedLocusNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAC77178.1"}],"value":"b4221"},{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"BAE78222.1"}],"value":"JW4180"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22466966"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25341963"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26243377"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29129383"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39174534"}],"value":"Component of the translocation and assembly module (TAM), which facilitates the insertion and assembly of specific beta-barrel proteins into the outer membrane (PubMed:22466966, PubMed:25341963, PubMed:29129383, PubMed:39174534). Promotes the assembly and secretion across the outer membrane of a subset of autotransporters, such as Ag43 (PubMed:22466966, PubMed:25341963). Involved in the assembly of the outer membrane usher protein FimD (PubMed:29129383). In vitro, when TAM is reconstituted into preformed liposomes, it can promote the assembly of several outer membrane proteins, including OmpA, EspP, Ag43 and FadL (PubMed:39174534). TamA is sufficient to catalyze a low level of outer membrane protein (OMP) assembly, but both TamA and TamB are required for efficient OMP assembly (PubMed:39174534). TamB may regulate TamA activity (PubMed:25341963). It could regulate conformational changes in TamA to drive its function in OMP assembly (PubMed:26243377). It could also act as a chaperone that facilitate the transport of nascent membrane proteins across the periplasm to TamA in the outer membrane (PubMed:29129383)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"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":"39174534"}],"value":"In addition, is involved in outer membrane lipid homeostasis (PubMed:34781743, PubMed:35226662, PubMed:38913742). Likely transports phospholipids between the inner membrane and the outer membrane (PubMed:34781743, PubMed:35226662, PubMed:38913742). It would provide a bridge-like structure that protects phospholipids as they travel across the periplasm (PubMed:34781743). One possible explanation for the apparent dual function of TAM is that TamB is a somewhat generic transporter of hydrophobic molecules (PubMed:39174534)"}],"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"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22466966"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25341963"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26243377"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39174534"}],"value":"Interacts with TamA to form the translocation and assembly module (TAM)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P39321","intActId":"EBI-1117885"},"interactantTwo":{"uniProtKBAccession":"P0ADE4","geneName":"tamA","intActId":"EBI-1114298"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22466966"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25341963"}],"value":"Cell inner membrane","id":"SL-0037"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22466966"}],"value":"Single-pass type II membrane protein","id":"SL-9906"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25341963"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22466966"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"29129383"}],"value":"Periplasmic side","id":"SL-9916"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25341963"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25994932"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29129383"}],"value":"The periplasmic domain is elongated (up to 160 Angstroms long) and forms contacts with the N-terminal POTRA domains of TamA (PubMed:25341963). The C-terminal region mimics outer membrane protein beta strands (PubMed:25994932). This region (residues 963-1138) consists of a concave, taco-shaped beta sheet with a hydrophobic interior, which can accommodate and shield the hydrophobic side of an amphipathic beta strand, potentially allowing TamB to chaperone nascent membrane proteins across the periplasm to TamA in the outer membrane (PubMed:29129383)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22466966"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34781743"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35226662"}],"value":"Loss of cell aggregation when adhesins are over-expressed in a double tamA-tamB deletion mutant (PubMed:22466966). The single mutant does not exhibit growth defects but it shows a slight increase in outer membrane permeability (PubMed:34781743). 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:0000269","source":"PubMed","id":"25994932"}],"value":"TamB is widely distributed across the majority of Gram-negative bacterial lineages and is far more widely distributed than its partner TamA"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the TamB family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"AAA97118.1","note":"Produces two separate ORFs.","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1259,"modifier":"EXACT"}},"description":"Translocation and assembly module subunit TamB","featureId":"PRO_0000169830"},{"type":"Topological domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":6,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Transmembrane","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"Helical; Signal-anchor for type II membrane protein","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Topological domain","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":1259,"modifier":"EXACT"}},"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25341963"}]},{"type":"Modified residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"N-formylmethionine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22466966"}]},{"type":"Mutagenesis","location":{"start":{"value":1049,"modifier":"EXACT"},"end":{"value":1049,"modifier":"EXACT"}},"description":"Can complement a tamB null-phenotype. 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