TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.B.33.1.1









Omp85 outer membrane OMP translocase.  The high resolution 3-d structure of the N. gonorrhoea orthologue has been solved (Noinaj et al. 2013).

Bacteria
Proteobacteria
Omp85 of Neisseria meningitidis
*1.B.33.1.2









Protective surface antigen D15 precursor.  The high resolution 3-d structure of the H. ducreyi orthologue has been solved (Noinaj et al. 2013).

Bacteria
Proteobacteria
D15 of Haemophilus influenzae
*1.B.33.1.3









Outer membrane biogenesis complex (Wu et al., 2005). YaeT (BamA) may serve as an outer membrane "receptor" for the CdiA/CdiB 2-partner secretion system that mediates direct cell-cell contact-dependent growth inhibition (Aoki et al., 2008). High-resolution structures of crystal forms of BamA POTRA4-5 from E. coli has been reported (Zhang et al., 2011; Sinnige et al. 2014). Solid-state NMR on BamA, a large multidomain integral membrane protein, revealed dynamic conformational states (Renault et al., 2011).  The NMR structure of SmpA (OmlA) is also known (Vanini et al. 2006).  The periplasmic region of BamA is firmly attached to the beta-barrel and does not experience fast global motion around the angle between POTRA 2 and 3, but the barrel is flexible (Sinnige et al. 2014).  It appears that the BAM complex does not catalyzed insertion and assembly of all out membrane (α- and β-)porins (Dunstan et al. 2015).  YfgL shows significant sequence similarity (e-9) with YxaL/K of Bacillus subtilis

Bacteria
Proteobacteria
OM biogenesis complex of E. coli
YaeT/YfiO/NlpB/YfgL
YaeT precursor (810 aas) (P0A943)
YfiO precursor (245 aas; lipoprotein) (P0AC02)
NlpB (lipoprotein-38; 344 aas) (P0A903)
YfgL (392 aas) (P77774)
SmpA (Small membrane lipoprotein A) (P0A937)
*1.B.33.1.4









The BAM complex required for outer membrane integrity and correct assembly of outer membrane β-barrel proteins, including one or more substrates required for the initiation of stalk biogenesis (Ryan et al., 2010).

Bacteria
Proteobacteria
The BamABDE complex of Caulobacter crescentus
BamA (182aas) (Q9A7T5)
BamB (476aas) (Q9A7R7)
BamD (305aas) (Q9A6U9)
BamE (161aas) (Q9A8I8)
*1.B.33.2.1









The chloroplast import-associated channel porin, IAP75 or Toc75 that functions with two receptor GTPases, Toc34 and Toc159 (see 3.A.9, the CEPT family).  It contains a polyglycine sequence (residues 91 - 110) that acts as a "rejection signal" at the outer envelope for protein transport into the chloroplast (Endow et al. 2016).

Eukaryota
Viridiplantae
IAP75 of chloroplasts in Pisum sativum
*1.B.33.2.2









Chloroplast Outer Envelope Protein, 80 KD (OEP80) (One of two; Toc75 (TC #) and OEP80). OEP80 is essential for viability (Patel et al., 2008).
Eukaryota
Viridiplantae
OEP80 of Arabidopsis thaliana (Q9C5J8)
*1.B.33.2.3









Omp85 family member

Bacteria
Firmicutes
Omp85 homologue of Selenomonas sputigena
*1.B.33.2.4









TamA (YftM) of 577 aas; has a 16 transmembrane β-stranded β-barrel with 3 PORTRA domains.  The 2.3 Å crystal structure is known revealing that the barrel is closed by a lid-loop (Gruss et al. 2013).  The C-terminal β-strand of the barrel forms an unusual inward kink, which weakens the lateral barrel wall and creates a gate for substrate access to the lipid bilayer.  TamA is an Omp85 homologue that may function in autotransporter biogenesis together with TamB (TC# 1.B.22.1.2) and OMP85 (Selkrig et al. 2012). The TAM complex likely evolved from an original combination of BamA and TamB, with a later gene duplication event of BamA, giving rise to an additional Omp85 sequence that evolved to be TamA in Proteobacteria and TamL in Bacteroidetes/Chlorobi (Heinz et al. 2015). Possibly TamB nucleates folding of the passenger domain while TamA/B-BamA interact to catalyze β-domain membrane insertion and pore enlargement to facmilitate translocation of partially folded autotransporters (M. Babu et al., unpublished hypothesis).

Bacteria
Proteobacteria
TamA of E. coli
*1.B.33.2.5









TamA of 604 aas; surface antigen D15; involved in autotransporter protein insertion in the outer membrane together with TamB (TC# 9.B.22.1.5).

Bacteria
Proteobacteria
TamA of Sagittula stellata
*1.B.33.3.1









The mitochondrial Sorting and Assembly Machinery (SAM) includes Tom37 (Mas37; Sam37) and Tom13 (Mim1), see 3.A.8 (Paschen et al., 2005). Can assemble C-terminal α-helical anchor proteins as well as β-barrel proteins in the outer mitochondrial membrane (Stojanovski et al., 2007). Mim1 is required for the biogenesis of the beta-barrel protein Tom40 and also for membrane insertion and assembly of signal-anchored Tom receptors (Becker et al., 2008; 2011). Tom7 regulates Mdm10-mediated assembly of the mitochondrial import channel protein Tom40 (Yamano et al., 2010).

Eukaryota
Fungi
SAM of Saccharomyces cerevisiae:
SAM50 or TOB55 (β-barrel protein, homologous to Omp85) (P53969)
SAM35 or TOB38 (essential peripheral OM protein) (NP_011951)
MAS37 or TOM37 or TOB37 (nonessential component of the SAM complex) (P50110)
Mdm10 integral outer membrane protein; controls mitochondrial morphology and inheritance (493 aas) (P18409)
Mim1 (Tom13) (Q08176)
*1.B.33.3.2









Sam50 of 475 aas

Eukaryota
Fungi
Sam50 of Schizosaccharomyces pombe
*1.B.33.3.3









Sam50 of 521 aas

Eukaryota
Fungi
Sam50 of Neurospora crassa
*1.B.33.3.4









Sam50 of 469 aas

Eukaryota
Metazoa
Sam50 of Homo sapiens
*1.B.33.3.5









Sam50 of 443 aas

Eukaryota
Metazoa
Sam 50 of Drosophila melanogaster
*1.B.33.3.6









Sam50 of 453 aas

Eukaryota
Bangiophyceae
Sam50 of Galdieria sulphuraria
*1.B.33.3.7









Sam50-like protein, Gop-3 of 434 aas

Eukaryota
Metazoa
Gop-3 of Caenorhabditis elegans
*1.B.33.3.8









Sam50 of 521 aas

Eukaryota
Viridiplantae
Sam50 of Ostreococcus tauri
*1.B.33.3.9









Sam50 of 672 aas

Eukaryota
Bacillariophyta
Sam50 of Thalassiosira pseudonana (Marine diatom) (Cyclotella nana)
*1.B.33.4.1









Omp85 homologue of 527 aas

Bacteria
Spirochaetes
Omp85 of Leptospira interrogans
*1.B.33.5.1









Omp85 homologue of 1,107 aas

Bacteria
Planctomycetes
Omp85 of Planctomyces limnophilus
*1.B.33.6.1









Omp85 homologue of 446 aas

Bacteria
Nitrospirae
Omp85 of Leptospirillum ferriphilum