ATP-binding cassette (ABC) transporters form a large family of proteins responsible for translocation of a variety of compounds across biological membranes. They are composed of two transmembrane domains responsible for binding and transport and two nucleotide-binding domains responsible for coupling the energy of ATP hydrolysis to conformational changes in the TMDs. Similar to TREMBL:Q88H94 (52% identity); TREMBL:Q9RXZ1 (29% identity); SWISSPROT:Q9WYC4 (25% identity). Pfam (PF00664): ABC transporter transmembrane region. Pfam (PF00005): ABC transporter. TMHMM reporting six transmembra [...]

Hypothetical secreted protein. No significant homology to the data bank. no domains pedicted. signal peptide. TMH in signal peptide.

Putative transmembrane sensor protein, no similarity to other bacterial proteins. Best hits to mus musculus and homo sapiens. Domains (LCCL_dom and TIR) are found in proteins (animal and plants) involved in protection against bacterial infection. InterPro: IPR004043 LCCL_dom. IPR000157 TIR. TMHMM reporting 1 transmembrane helices.

Conserved hypothetical secreted protein. Homology to rsc1270 of R. solanacearum of 44% (trembl|Q8XQF7(SRS)). no domains predicted .signal peptide present. no TMHs; Conserved hypothetical protein.

Conserved hypothetical protein; Similar to TREMBL:Q7NTT5 (32% identity).

Conserved hypothetical secreted protein. Homology to ebA651 of Azoarcus sp. EbN1 of 37% (gnl|keqq|eba:ebA651(KEGG)). InterproterPro (IPR000694): Proline-rich region. SignalP reporting signal peptide. no TMHs.

Probable quinohemoprotein amine dehydrogenase,gamma subunit. Homology to qhnDH of P. putida of 54% (sprot|QADG_PSEPK(SRS). Quinoproteins are a class of amine-oxidising enzymes that catalyse the oxidation of biological amines, using quinone as a redox cofactor to store reducing equivalents. Quinohemoprotein amine dehydrogenase (QH-AmDH) from bacteria represents a new class of quinoproteins that contains both quinone and one or two hemes as redox active groups. The presence of extra redox active groups allows for intramolecular electron transfer. QH-AmDH is a heterotrimeric enzyme contai [...]

Probable quinohemoprotein amine dehydrogenase,alpha subunit. Homology to qhpA of P.putida of 50% (gi|18655859|pdb|1JMZ|A(PDB (RCSB))). Quinoproteins are a class of amine-oxidising enzymes that catalyse the oxidation of biological amines, using quinone as a redox cofactor to store reducing equivalents. Quinohemoprotein amine dehydrogenase (QH-AmDH) from bacteria represents a new class of quinoproteins that contains both quinone and one or two hemes as redox active groups. The presence of extra redox active groups allows for intramolecular electron transfer. QH-AmDH is a heterotrimeric e [...]

Preprotein translocase SecY 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.