TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*2.A.64.1.1









TatABCE translocase. Early contacts between substrate proteins and TatA have been demonstrated (Fröbel et al., 2011). TatC helix 5 and the TatB transmembrane helix interact (Kneuper et al., 2012).  TatC functions as an obligate oligomer (Cleon et al. 2015). TatA is the most abundant component of the complex and facilitates assembly of this complex.It exhibits a uniform distribution throughout the inner membrane, but forms linear clusters upon increased expression of TatBC (Smith et al. 2017).  TatA and TatB both have the capacity to bind at two TatC sites, one in TMS5 and one in TMS6 (Habersetzer et al. 2017). However in vivo this is regulated according to the activation state of the complex. In the resting-state system, TatB binds the polar cluster site in TMS 5 with TatA occupying the site in TMS 6. However, when the system is activated by overproduction of a substrate, TatA and TatB switch binding sites. Habersetzer et al. 2017 proposed that this substrate-triggered positional exchange is a key step in the assembly of an active Tat translocase. A  highly conserved glutamate residue in the transmembrane region of E. coli TatC, which, when modified by DCCD, interferes with the deep insertion of a Tat signal peptide into the TatBC receptor complex (Blümmel et al. 2017).

Bacteria
Proteobacteria
TatABCE of E. coli
*2.A.64.1.2









Twin arginine targeting protein translocase, TatABC (Kimura et al. 2006).

Bacteria
Proteobacteria
TatABC (MXAN_2960, MXAN5905-4) of Myxococcus xanthus.
*2.A.64.1.3









TatABCE.  The twin-arginine translocation (Tat) system transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides (Eimer et al. 2015; Kuzniatsova et al. 2016; Cléon et al. 2015).

Bacteria
Proteobacteria
TatABCE of Bdellovibrio bacteriovorus
*2.A.64.2.1









The chloroplast Tat translocase (cpTatC/Hcf106/Tha4) (Gérard and Cline, 2007).  The precursor mature domain of the substrate protein interacts directly with Tha4 (Pal et al. 2012).  Hcf106 is predicted to contain a single amino terminal transmembrane domain followed by a Pro-Gly hinge, a predicted amphipathic alpha-helix (APH), and a loosely structured carboxy terminus.  The amphipathic α-helix interacts with the bilayer (Zhang et al., 2013a; Zhang et al. 2013b)

Eukaryota
Viridiplantae
cpTatC/Hcf106/Tha4 of Arabidopsis thaliana
cpTatC (TatC or MttB family; APG2; albino and pale green 2; 340 aas) (Q9SJV5)
Hcf106 (TatA or MttA family; 260 aas) (Q9XH75)
Tha4 (TatA or MttA family; 147 aas) (Q9LKU2)
*2.A.64.2.2









Sec-independent protein translocase, TatABC (Widdick et al. 2006).

Bacteria
Actinobacteria
Sec-independent protein translocase protein TatACB of Streptomyces coelicolor

TatA (Q9RJ68)
TatB (Q9FBK8)
TatC (Q9RJ69)
*2.A.64.3.1









TatAd/Bd translocase (Jongbloed et al., 2004)
Bacteria
Firmicutes
TatAd/Cd of Bacillus subtilis
TatAd (70 aas; O31467)
TatCd (245 aas; P42252)
*2.A.64.3.2









TatAy/Cy translocase (Jongbloed et al., 2004)
Bacteria
Firmicutes
TatAy/Cy of Bacillus subtilis
TatAy (57 aas; O05522)
TatCy (254 aas; O05523)
*2.A.64.4.1









Twin arginine (TatA0/TatC0) protein translocase (Dilks et al. 2005; Giménez et al. 2007; Szabo and Pohlschroder 2012).

Archaea
Euryarchaeota
Twin arginine translocase, TatAC0 of Haloferax volcanii
TatA0 (D4GVK4)
TatC0 (D4GZD0) 
*2.A.64.5.1









Twin Arginine (TatAt/TatCt) protein translocase (Dilks et al. 2005; Giménez et al. 2007; Szabo and Pohlschroder 2012).

Archaea
Euryarchaeota
Tat system, TatACt of Haloferax volcanii
TatAt (91aas) (D4GWC8)
TatCt (718aas; duplicated with 8+6=14 putative TMSs) (D4GWC9) 
*2.A.64.6.1









A Tat system, TatC of 365 aas and 6 TMSs, and a potential TatB of 71 aas and 1 TMS.

Bacteria
Candidatus Saccharibacteria
Tat (TatBC) system of Candidatus Saccharibacteria bacterium  
*2.A.64.6.2









Tat (TatCB) system consisting of TatC (238 aas and 5 or 6 TMSs) and TatB (73 aas and 1 TMS).

Bacteria
Candidatus Saccharibacteria
TatBC of Candidatus Saccharibacteria bacterium
*2.A.64.6.3









Tat system consisting of TatC (355 aas and 5 or 6 TMSs) and putative TatB (62 aas and 1 TMS). The tat genes are flanked by a sortase gene (WP_104944876) and a groL chaparone protein-encoding gene (WP_104944880).

Bacteria
Candidatus Saccharibacteria
TatBC of Candidatus Saccharibacteria bacterium