Translocase binding subunit (ATPase); Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family.

Protein-export membrane protein; Required for efficient translocation of secretory pre- proteins under conditions of hypersecretion but is not required for the release of mature proteins from the membrane. In the N-terminal section; belongs to the SecD/SecF family. SecD subfamily.

Translocase binding subunit (ATPase); Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family.

Preprotein translocase subunit; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.

Translocase binding subunit (ATPase); Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family.

Preprotein translocase subunit; Involved in protein export. Participates in an early event of protein translocation (By similarity).

Translocase binding subunit (ATPase); Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family.

Preprotein translocase subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.

Protein-export membrane protein; Required for efficient translocation of secretory pre- proteins under conditions of hypersecretion but is not required for the release of mature proteins from the membrane. In the N-terminal section; belongs to the SecD/SecF family. SecD subfamily.

Translocase binding subunit (ATPase); Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family.

Protein-export membrane protein; Required for efficient translocation of secretory pre- proteins under conditions of hypersecretion but is not required for the release of mature proteins from the membrane. In the N-terminal section; belongs to the SecD/SecF family. SecD subfamily.

Preprotein translocase subunit; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.

Protein-export membrane protein; Required for efficient translocation of secretory pre- proteins under conditions of hypersecretion but is not required for the release of mature proteins from the membrane. In the N-terminal section; belongs to the SecD/SecF family. SecD subfamily.

Preprotein translocase subunit; Involved in protein export. Participates in an early event of protein translocation (By similarity).

Protein-export membrane protein; Required for efficient translocation of secretory pre- proteins under conditions of hypersecretion but is not required for the release of mature proteins from the membrane. In the N-terminal section; belongs to the SecD/SecF family. SecD subfamily.

Preprotein translocase subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.

Protein-export membrane protein; Required for efficient translocation of secretory pre- proteins under conditions of hypersecretion but is not required for the release of mature proteins from the membrane. In the N-terminal section; belongs to the SecD/SecF family. SecD subfamily.

Component of the twin-arginine pre-protein translocation pathway; 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. Required for PhoD secretion. TatCd promotes membrane localization of TatAd via domain specific interactions. TatCd is required for stabile production of TatAd as well as for its maintenance; Belongs to the TatC family.

Protein-export membrane protein; Required for efficient translocation of secretory pre- proteins under conditions of hypersecretion but is not required for the release of mature proteins from the membrane. In the N-terminal section; belongs to the SecD/SecF family. SecD subfamily.

Component of the twin-arginine pre-protein translocation pathway; 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. Required for YwbN secretion; Belongs to the TatC family.

Preprotein translocase subunit; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.

Translocase binding subunit (ATPase); Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family.

Preprotein translocase subunit; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.

Protein-export membrane protein; Required for efficient translocation of secretory pre- proteins under conditions of hypersecretion but is not required for the release of mature proteins from the membrane. In the N-terminal section; belongs to the SecD/SecF family. SecD subfamily.

Preprotein translocase subunit; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.

Preprotein translocase subunit; Involved in protein export. Participates in an early event of protein translocation (By similarity).

Preprotein translocase subunit; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.

Preprotein translocase subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.

Preprotein translocase subunit; Involved in protein export. Participates in an early event of protein translocation (By similarity).

Translocase binding subunit (ATPase); Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family.

Preprotein translocase subunit; Involved in protein export. Participates in an early event of protein translocation (By similarity).

Protein-export membrane protein; Required for efficient translocation of secretory pre- proteins under conditions of hypersecretion but is not required for the release of mature proteins from the membrane. In the N-terminal section; belongs to the SecD/SecF family. SecD subfamily.

Preprotein translocase subunit; Involved in protein export. Participates in an early event of protein translocation (By similarity).

Preprotein translocase subunit; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.

Preprotein translocase subunit; Involved in protein export. Participates in an early event of protein translocation (By similarity).

Preprotein translocase subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.

Preprotein translocase subunit; Involved in protein export. Participates in an early event of protein translocation (By similarity).

Component of the twin-arginine pre-protein translocation pathway; 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. Required for PhoD secretion. TatCd promotes membrane localization of TatAd via domain specific interactions. TatCd is required for stabile production of TatAd as well as for its maintenance; Belongs to the TatC family.

Preprotein translocase subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.

Translocase binding subunit (ATPase); Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family.