P39321 · TAMB_ECOLI
- ProteinTranslocation and assembly module subunit TamB
- GenetamB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1259 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane (PubMed:22466966).
In reconstituted TAM this subunit (Ag43, AC P39180) is not necessary for substrate penetration in the outer membrane. Substrate binding to TamA moves its POTRA domains about 30 Angstroms into the periplasm, which would deform either the outer membrane or TamB and may provide force to reset TAM (PubMed:25341963).
In reconstituted TAM this subunit (Ag43, AC P39180) is not necessary for substrate penetration in the outer membrane. Substrate binding to TamA moves its POTRA domains about 30 Angstroms into the periplasm, which would deform either the outer membrane or TamB and may provide force to reset TAM (PubMed:25341963).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell outer membrane | |
Cellular Component | plasma membrane | |
Cellular Component | TAM protein secretion complex | |
Biological Process | protein localization to outer membrane | |
Biological Process | protein secretion |
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameTranslocation and assembly module subunit TamB
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP39321
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Single-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Topological domain | 1-6 | Cytoplasmic | |||
Transmembrane | 7-27 | Helical; Signal-anchor for type II membrane protein | |||
Topological domain | 28-1259 | Periplasmic | |||
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Loss of localization of an exogenous protein, P1121 (ROD_p1121 of Citrobacter rodentium), to outer membranes, loss of cell aggregation when adhesins are over-expressed in a double tamA-tamB deletion mutant.
Interaction
Subunit
Interacts with TamA to form the translocation and assembly module (TAM).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | IntAct | |
---|---|---|---|---|---|
BINARY | P39321 | tamA P0ADE4 | 3 | EBI-1117885, EBI-1114298 |
Complex viewer
Protein-protein interaction databases
Structure
Family & Domains
Domain
The periplasmic domain is elongated (up to 160 Angstroms long) and forms contacts with the N-terminal POTRA domains of TamA (PubMed:25341963).
Sequence similarities
Belongs to the TamB family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,259
- Mass (Da)136,780
- Last updated1997-11-01 v2
- MD5 ChecksumAB9F35FF31EA84B1CC7329DC6B7A0D73
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U14003 EMBL· GenBank· DDBJ | AAA97117.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
U14003 EMBL· GenBank· DDBJ | AAA97118.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
U00096 EMBL· GenBank· DDBJ | AAC77178.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE78222.1 EMBL· GenBank· DDBJ | Genomic DNA |