P39321 · TAMB_ECOLI

  • Protein
    Translocation and assembly module subunit TamB
  • Gene
    tamB
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell outer membrane
Cellular Componentplasma membrane
Cellular ComponentTAM protein secretion complex
Biological Processprotein localization to outer membrane
Biological Processprotein secretion

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Translocation and assembly module subunit TamB
  • Alternative names
    • Autotransporter assembly factor TamB

Gene names

    • Name
      tamB
    • Synonyms
      ytfN, ytfO
    • Ordered locus names
      b4221, JW4180

Organism names

  • Taxonomic identifier
  • Strains
    • K12 / MG1655 / ATCC 47076
    • K12 / W3110 / ATCC 27325 / DSM 5911
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P39321
  • Secondary accessions
    • P39322
    • P76802
    • Q2M684

Proteomes

Subcellular Location

Features

Showing features for topological domain, transmembrane.

Type
IDPosition(s)Description
Topological domain1-6Cytoplasmic
Transmembrane7-27Helical; Signal-anchor for type II membrane protein
Topological domain28-1259Periplasmic

Keywords

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.

PTM/Processing

Features

Showing features for modified residue, chain.

Type
IDPosition(s)Description
Modified residue1N-formylmethionine
ChainPRO_00001698301-1259Translocation and assembly module subunit TamB

Keywords

Proteomic databases

Interaction

Subunit

Interacts with TamA to form the translocation and assembly module (TAM).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY P39321tamA P0ADE43EBI-1117885, EBI-1114298

Complex viewer

View interactors in UniProtKB
View CPX-5890 in Complex Portal

Protein-protein interaction databases

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,259
  • Mass (Da)
    136,780
  • Last updated
    1997-11-01 v2
  • MD5 Checksum
    AB9F35FF31EA84B1CC7329DC6B7A0D73
MSLWKKISLGVVIVILLLLGSVAFLVGTTSGLHLVFKAADRWVPGLDIGKVTGGWRDLTLSDVRYEQPGVAVKAGNLHLAVGLECLWNSSVCINDLALKDIQVNIDSKKMPPSEQVEEEEDSGPLDLSTPYPITLTRVALDNVNIKIDDTTVSVMDFTSGLNWQEKTLTLKPTSLKGLLIALPKVAEVAQEEVVEPKIENPQPDEKPLGETLKDLFSRPVLPEMTDVHLPLNLNIEEFKGEQLRVTGDTDITVSTMLLKVSSIDGNTKLDALDIDSSQGIVNASGTAQLSDNWPVDITLNSTLNVEPLKGEKVKLKMGGALREQLEIGVNLSGPVDMDLRAQTRLAEAGLPLNVEVNSKQLYWPFTGEKQYQADDLKLKLTGKMTDYTLSMRTAVKGQEIPPATITLDAKGNEQQVNLDKLTVAALEGKTELKALLDWQQAISWRGELTLNGINTAKEFPDWPSKLNGLIKTRGSLYGGTWQMDVPELKLTGNVKQNKVNVDGTLKGNSYMQWMIPGLHLELGPNSAEVKGELGVKDLNLDATINAPGLDNALPGLGGTAKGLVKVRGTVEAPQLLADITARGLRWQELSVAQVRVEGDIKSTDQIAGKLDVRVEQISQPDVNINLVTLNAKGSEKQHELQLRIQGEPVSGQLNLAGSFDRKEERWKGTLSNTRFQTPVGPWSLTRDIALDYRNKEQKISIGPHCWLNPNAELCVPQTIDAGAEGRAVVNLNRFDLAMLKPFMPETTQASGIFTGKADVAWDTTKEGLPQGSITLSGRNVQVTQTVNDAALPVAFQTLNLTAELRNNRAELGWTIRLTNNGQFDGQVQVTDPQGRRNLGGNVNIRNFNLAMINPIFTRGEKAAGMVSANLRLGGDVQSPQLFGQLQVTGVDIDGNFMPFDMQPSQLAVNFNGMRSTLAGTVRTQQGEIYLNGDADWSQIENWRARVTAKGSKVRITVPPMVRMDVSPDVVFEATPNLFTLDGRVDVPWARIVVHDLPESAVGVSSDVVMLNDNLQPEEPKTASIPINSNLIVHVGNNVRIDAFGLKARLTGDLNVVQDKQGLGLNGQINIPEGRFHAYGQDLIVRKGELLFSGPPDQPYLNIEAIRNPDATEDDVIAGVRVTGLADEPKAEIFSDPAMSQQAALSYLLRGQGLESDQSDSAAMTSMLIGLGVAQSGQIVGKIGETFGVSNLALDTQGVGDSSQVVVSGYVLPGLQVKYGVGIFDSIATLTLRYRLMPKLYLEAVSGVDQALDLLYQFEF

Sequence caution

The sequence AAA97118.1 differs from that shown. Reason: Frameshift Produces two separate ORFs.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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