| NC_018496.1|WP_014894314.1|489281_490154_-|GTPase-Era |
gnl|CDD|129528 |
TIGR00436, GTPase_Era, GTP-binding protein Era. Era is an essential GTPase in Escherichia coli and many other bacteria. It plays a role in ribosome biogenesis. Few bacteria lack this protein. [Protein synthesis, Other].
|
1.59875e-117 |
| NC_018496.1|WP_009885939.1|474025_474340_-|DUF3217-domain-containing-protein |
gnl|CDD|371569 |
pfam11506, DUF3217, Protein of unknown function (DUF3217). This family of proteins with unknown function appears to be restricted to Mycoplasma. Some members in this family of proteins are annotated as MG376 however this cannot be confirmed.
|
7.09205e-52 |
| NC_018496.1|WP_014894315.1|490976_492959_-|peptidase-domain-containing-ABC-transporter |
gnl|CDD|225183 |
COG2274, SunT, ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms].
|
0 |
| NC_018496.1|WP_009885634.1|490141_490606_-|rRNA-maturation-RNase-YbeY |
gnl|CDD|223396 |
COG0319, COG0319, Predicted metal-dependent hydrolase [General function prediction only].
|
3.43138e-37 |
| NC_018496.1|WP_014894060.1|493066_494410_-|leucyl-aminopeptidase |
gnl|CDD|223338 |
COG0260, PepB, Leucyl aminopeptidase [Amino acid transport and metabolism].
|
2.37097e-168 |
| NC_018496.1|WP_009885945.1|481513_482815_-|GTPase-ObgE |
gnl|CDD|237046 |
PRK12297, obgE, GTPase CgtA; Reviewed.
|
0 |
| NC_018496.1|WP_009885944.1|480774_481521_-|NAD(+)-synthase |
gnl|CDD|273132 |
TIGR00552, Probable_NH3-dependent_NAD+_synthetase, NAD+ synthetase. NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides].
|
7.58551e-129 |
| NC_018496.1|WP_010869457.1|472331_474026_-|threonine--tRNA-ligase |
gnl|CDD|273068 |
TIGR00418, Threonine--tRNA_ligase, threonyl-tRNA synthetase. This model represents the threonyl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. Note that B. subtilis has closely related isozymes thrS and thrZ. The N-terminal regions are quite dissimilar between archaeal and eubacterial forms, while some eukaryotic forms are missing sequence there altogether. . [Protein synthesis, tRNA aminoacylation].
|
0 |
| NC_018496.1|WP_014894312.1|483433_484144_-|hypothetical-protein |
gnl|CDD|223657 |
COG0584, UgpQ, Glycerophosphoryl diester phosphodiesterase [Energy production and conversion].
|
4.85938e-36 |
| NC_018496.1|WP_009885942.1|478445_479024_+|16S-rRNA-(guanine(527)-N(7))-methyltransferase-RsmG |
gnl|CDD|223434 |
COG0357, GidB, Predicted S-adenosylmethionine-dependent methyltransferase involved in bacterial cell division [Cell envelope biogenesis, outer membrane].
|
1.47946e-48 |
| NC_018496.1|WP_009885631.1|494426_496058_-|chaperonin-GroEL |
gnl|CDD|234573 |
PRK00013, groEL, chaperonin GroEL; Reviewed.
|
0 |
| NC_018496.1|WP_014894316.1|496528_497749_-|serine-hydroxymethyltransferase |
gnl|CDD|234571 |
PRK00011, glyA, serine hydroxymethyltransferase; Reviewed.
|
0 |
| NC_018496.1|WP_009885941.1|474973_476587_-|arginine--tRNA-ligase |
gnl|CDD|273085 |
TIGR00456, Arginine--tRNA_ligase, arginyl-tRNA synthetase. This model recognizes arginyl-tRNA synthetase in every completed genome to date. An interesting feature of the alignment of all arginyl-tRNA synthetases is a fairly deep split between two families. One family includes archaeal, eukaryotic and organellar, spirochete, E. coli, and Synechocystis sp. The second, sharing a deletion of about 25 residues in the central region relative to the first, includes Bacillus subtilis, Aquifex aeolicus, the Mycoplasmas and Mycobacteria, and the Gram-negative bacterium Helicobacter pylori. [Protein synthesis, tRNA aminoacylation].
|
0 |
| NC_018496.1|WP_050982313.1|497758_499330_-|DUF31-family-protein |
gnl|CDD|366776 |
pfam01732, DUF31, Putative peptidase (DUF31). This domain has no known function. It is found in various hypothetical proteins and putative lipoproteins from mycoplasmas. It appears to be related to the superfamily of trypsin peptidases and so may have a peptidase function.
|
3.58019e-55 |
| NC_018496.1|WP_010869464.1|496070_496403_-|co-chaperone-GroES |
gnl|CDD|223312 |
COG0234, GroS, Co-chaperonin GroES (HSP10) [Posttranslational modification, protein turnover, chaperones].
|
3.0581e-28 |
| NC_018496.1|WP_009885626.1|499701_500160_-|ribose-5-phosphate-isomerase-B |
gnl|CDD|129772 |
TIGR00689, Probable_ribose-5-phosphate_isomerase_B, sugar-phosphate isomerase, RpiB/LacA/LacB family. Proteins of known function in this family act as sugar (pentose and/or hexose)-phosphate isomerases, including the LacA and LacB subunits of galactose-6-phosphate isomerases from Gram-positive bacteria and RpiB. RpiB is the second ribose phosphate isomerase of E. coli. It lacks homology to RpiA, its inducer is unknown (but is not ribose), and it can be replaced by the homologous galactose-6-phosphate isomerase of Streptococcus mutans, all of which suggests that the ribose phosphate isomerase activity of RpiB is a secondary function. On the other hand, there appear to be a significant number of species which contain rpiB, lack rpiA and seem to require rpi activity in order to complete the pentose phosphate pathway.
|
5.01198e-83 |
