Putative acyl-CoA thioesterase. Homology to tesA of E. coli of 32% (sprot|TESA_ECOLI) Hydrolyzes long chain acyl thioesters (c12-c18): 2-lysophosphatidylcholine + h(2)o = glycerophosphocholine + a fatty acid anion. InterPro: GDSL lipolytic enzyme (IPR001087) Pfam: Lipase/Acylhydrolase GDSL-like motif signal peptide no TMH; Family membership.

GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.

Flagellar basal-body rod protein flgG (Distal rod protein). The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity.

Conserved hypothetical secreted protein. Homology to RS04458 of Ralstonia solanacearum of 31% (tremble:Q8Y292). No domains predicted .Signal peptide reported. NO TMH present; Conserved hypothetical protein.

Conserved hypothetical peptidase. Homology to rsc0445 of R. solanacearum of 50% (trembl|Q8Y291). Pfam: Peptidas_C39. Lantibiotic and non-lantibiotic bacteriocins are synthesised as precursor peptides containing N-terminal extensions (leader peptides) which are cleaved off during maturation. Most non-lantibiotics and also some lantibiotics have leader peptides of the so-called double-glycine type. These leader peptides share consensus sequences and also a common processing site with two conserved glycine residues in positions -1 and -2. The double- glycine-type leader peptides are unrel [...]

Hypothetical secreted protein. No good homology over the entire length in DB. No domains predicted. Signal Peptide present. No TMH present.

Subtilisin Savinase precursor, 36% identity to SwissProt; P29600. Has PF00082, Subtilase family;IPR000209, Pept_S8_S53;Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see Trypsin). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567. PROSITE;) PS00136; SUBTILASE_ASP; 1. PS00137; SUBTILASE_HIS; 1. PS00138; SUBTILASE_SER; 1.

Putative Autotransporter,30% identity to TrEMBL;Q87UU2. Weak homology with hits in the DB. Signal Peptide present. No TMH reported present. Has PF03797;Autotransporter beta-domain;The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the proteins secreted in this way are called autotransporters. This family corresponds to the presumed integral membrane beta-barrel domain that transports the protein. This domain is found at the C terminus of the proteins it occurs in. The N terminus contains the variable passenger [...]

Bifunctional chorismate mutase/prephenate dehydratase P-protein, pheA,; High confidence in function and specificity.