twin-arginine translocase subunit TatC is part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes
Twin arginine targeting (Tat) protein translocase TatC, Archaeal clade; This model represents ...
7-240
2.59e-60
Twin arginine targeting (Tat) protein translocase TatC, Archaeal clade; This model represents the TatC translocase component of the Sec-independent protein translocation system. This system is responsible for translocation of folded proteins, often with bound cofactors across the periplasmic membrane. A related model (TIGR00945) represents the bacterial clade of this family. TatC is often found (in bacteria) in a gene cluster with the two other components of the system, TatA/E (TIGR01411) and TatB (TIGR01410). A model also exists for the Twin-arginine signal sequence (TIGR01409).
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Pssm-ID: 162597 Cd Length: 237 Bit Score: 190.30 E-value: 2.59e-60
Twin arginine targeting (Tat) protein translocase TatC, Archaeal clade; This model represents ...
7-240
2.59e-60
Twin arginine targeting (Tat) protein translocase TatC, Archaeal clade; This model represents the TatC translocase component of the Sec-independent protein translocation system. This system is responsible for translocation of folded proteins, often with bound cofactors across the periplasmic membrane. A related model (TIGR00945) represents the bacterial clade of this family. TatC is often found (in bacteria) in a gene cluster with the two other components of the system, TatA/E (TIGR01411) and TatB (TIGR01410). A model also exists for the Twin-arginine signal sequence (TIGR01409).
Pssm-ID: 162597 Cd Length: 237 Bit Score: 190.30 E-value: 2.59e-60
Sec-independent protein translocase protein (TatC); The bacterial Tat system has a remarkable ...
11-223
6.49e-45
Sec-independent protein translocase protein (TatC); The bacterial Tat system has a remarkable ability to transport folded proteins even enzyme complexes across the cytoplasmic membrane. It is structurally and mechanistically similar to the Delta pH-driven thylakoidal protein import pathway. A functional Tat system or Delta pH-dependent pathway requires three integral membrane proteins: TatA/Tha4, TatB/Hcf106 and TatC/cpTatC. The TatC protein is essential for the function of both pathways. It might be involved in twin-arginine signal peptide recognition, protein translocation and proton translocation. Sequence analysis predicts that TatC contains six transmembrane helices (TMHs), and experimental data confirmed that N- and C-termini of TatC or cpTatC are exposed to the cytoplasmic or stromal face of the membrane. The cytoplasmic N-terminus and the first cytoplasmic loop region of the Escherichia coli TatC protein are essential for protein export. At least two TatC molecules co-exist within each Tat translocon.
Pssm-ID: 459989 Cd Length: 210 Bit Score: 149.89 E-value: 6.49e-45
Twin arginine targeting (Tat) protein translocase TatC, Archaeal clade; This model represents ...
7-240
2.59e-60
Twin arginine targeting (Tat) protein translocase TatC, Archaeal clade; This model represents the TatC translocase component of the Sec-independent protein translocation system. This system is responsible for translocation of folded proteins, often with bound cofactors across the periplasmic membrane. A related model (TIGR00945) represents the bacterial clade of this family. TatC is often found (in bacteria) in a gene cluster with the two other components of the system, TatA/E (TIGR01411) and TatB (TIGR01410). A model also exists for the Twin-arginine signal sequence (TIGR01409).
Pssm-ID: 162597 Cd Length: 237 Bit Score: 190.30 E-value: 2.59e-60
Sec-independent protein translocase protein (TatC); The bacterial Tat system has a remarkable ...
11-223
6.49e-45
Sec-independent protein translocase protein (TatC); The bacterial Tat system has a remarkable ability to transport folded proteins even enzyme complexes across the cytoplasmic membrane. It is structurally and mechanistically similar to the Delta pH-driven thylakoidal protein import pathway. A functional Tat system or Delta pH-dependent pathway requires three integral membrane proteins: TatA/Tha4, TatB/Hcf106 and TatC/cpTatC. The TatC protein is essential for the function of both pathways. It might be involved in twin-arginine signal peptide recognition, protein translocation and proton translocation. Sequence analysis predicts that TatC contains six transmembrane helices (TMHs), and experimental data confirmed that N- and C-termini of TatC or cpTatC are exposed to the cytoplasmic or stromal face of the membrane. The cytoplasmic N-terminus and the first cytoplasmic loop region of the Escherichia coli TatC protein are essential for protein export. At least two TatC molecules co-exist within each Tat translocon.
Pssm-ID: 459989 Cd Length: 210 Bit Score: 149.89 E-value: 6.49e-45
Twin arginine targeting (Tat) protein translocase TatC; This model represents the TatC ...
8-228
4.57e-29
Twin arginine targeting (Tat) protein translocase TatC; This model represents the TatC translocase component of the Sec-independent protein translocation system. This system is responsible for translocation of folded proteins, often with bound cofactors across the periplasmic membrane. A related model (TIGR01912) represents the archaeal clade of this family. TatC is often found in a gene cluster with the two other components of the system, TatA/E (TIGR01411) and TatB (TIGR01410). A model also exists for the Twin-arginine signal sequence (TIGR01409). [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273355 Cd Length: 215 Bit Score: 109.23 E-value: 4.57e-29
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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