| NC_017360.1|WP_000364710.1|568866_570570_+|flagellar-basal-body-M-ring-protein-FliF |
gnl|CDD|129310 |
TIGR00206, Flagellar_M-ring_protein, flagellar basal-body M-ring protein/flagellar hook-basal body protein (fliF). Component of the M (cytoplasmic associated) ring, one of four rings (L,P,S,M) which make up the flagellar hook-basal body which is a major portion of the flagellar organelle. Although the basic structure of the flagella appears to be similar for all bacteria, additional rings and structures surrounding the basal body have been observed for some bacteria (eg Vibrio cholerae and Treponema pallidum). [Cellular processes, Chemotaxis and motility].
|
0 |
| NC_017360.1|WP_000840090.1|557922_558723_+|DNA-protecting-protein-DprA |
gnl|CDD|273238 |
TIGR00732, Protein_smf, DNA protecting protein DprA. Disruption of this gene in both Haemophilus influenzae and Helicobacter pylori drastically reduces the efficiency of transformation with exogenous DNA, but with different levels of effect on chromosomal (linear) and plasmid (circular) DNA. This difference suggests the DprA is not active in recombination, and it has been shown not to affect DNA binding, leaving the intermediate step in natural transformation, DNA processing. In Strep. pneumoniae, inactivation of dprA had no effect on the uptake of DNA. All of these data indicated that DprA is required at a later stage in transformation. Subsequently DprA and RecA were both shown in S. pneumoniae to be required to protect incoming ssDNA from immediate degradation. Role of DprA in non-transformable species is not known. The gene symbol smf was assigned in E. coli, but without assignment of function. [Cellular processes, DNA transformation].
|
3.1427e-94 |
| NC_017360.1|WP_147588954.1|559235_559466_+|tetratricopeptide-repeat-protein |
gnl|CDD|276807 |
sd00010, SLR, Sel1-like repeat. Sel1-like repeats (SLRs) share similar alpha-helical conformations with Tetratricopeptide repeats (TPRs), but with different consensus sequence lengths and superhelical topologies. SLRs contain 36 to 44 amino acids and are present in bacteria and eukaryotes but not in archaea. SLR proteins are involved in a variety of functions, and many serve as adaptor proteins for the assembly of macromolecular complexes. The SLR family was named after the Caenorhabditis elegans Sel1 protein which is predicted to fold into 11 SLRs, a transmembrane domain, and an N-terminal signal sequence. The human Sel1L protein contains an additional fibronectin type-II domain and an N-terminal PEST sequence. Its downregulation is associated with the development of breast and pancreatic carcinomas.
|
3.35461e-13 |
| NC_017360.1|WP_000051412.1|557677_557911_+|cell-division-topological-specificity-factor-MinE |
gnl|CDD|188120 |
TIGR01215, Cell_division_topological_specificity_factor, cell division topological specificity factor MinE. This protein is involved in the process of cell division. This protein prevents the proteins MinC and MinD to inhibit cell division at internal sites, but allows inhibiton at polar sites. This allows for correct cell division at the proper sites. [Cellular processes, Cell division].
|
1.39865e-25 |
| NC_017360.1|WP_000599161.1|558719_559124_+|Holliday-junction-resolvase-RuvX |
gnl|CDD|234639 |
PRK00109, PRK00109, Holliday junction resolvase RuvX.
|
3.49744e-37 |
| NC_017360.1|WP_001207776.1|555863_556856_+|ketol-acid-reductoisomerase |
gnl|CDD|235491 |
PRK05479, PRK05479, ketol-acid reductoisomerase; Provisional.
|
1.23077e-179 |
| NC_017360.1|WP_000742742.1|553423_553966_+|UDP-4-amino-4,-6-dideoxy-N-acetyl-beta-L-altrosamine-N-acetyltransferase |
gnl|CDD|274661 |
TIGR03585, PseH, UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase. Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.
|
2.55592e-58 |
| NC_017360.1|WP_000201843.1|570588_571620_+|flagellar-motor-switch-protein-FliG |
gnl|CDD|272961 |
TIGR00207, Flagellar_motor_switch_protein_FliG, flagellar motor switch protein FliG. The fliG protein along with fliM and fliN interact to form the switch complex of the bacterial flagellar motor located at the base of the basal body. This complex interacts with chemotaxis proteins (eg CHEY). In addition the complex interacts with other components of the motor that determine the direction of flagellar rotation. The model contains putative members of the fliG family at scores of less than 100 from Agrobacterium radiobacter and Sinorhizobium meliloti as well as fliG-like genes from treponema pallidum and Borrelia burgdorferi. That is why the suggested cutoff is set at 20 but was set at 100 to construct the family. [Cellular processes, Chemotaxis and motility].
|
2.78332e-164 |
| NC_017360.1|WP_001117099.1|563839_564721_-|RluA-family-pseudouridine-synthase |
gnl|CDD|223638 |
COG0564, RluA, Pseudouridylate synthases, 23S RNA-specific [Translation, ribosomal structure and biogenesis].
|
2.64249e-66 |
| NC_017360.1|WP_000810717.1|564720_566271_-|single-stranded-DNA-specific-exonuclease-RecJ |
gnl|CDD|273193 |
TIGR00644, recJ, single-stranded-DNA-specific exonuclease RecJ. All proteins in this family are 5'-3' single-strand DNA exonucleases. These proteins are used in some aspects of mismatch repair, recombination, and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair].
|
0 |
| NC_017360.1|WP_000833960.1|553898_554837_-|tetraacyldisaccharide-4'-kinase |
gnl|CDD|224577 |
COG1663, LpxK, Tetraacyldisaccharide-1-P 4'-kinase [Cell envelope biogenesis, outer membrane].
|
5.5846e-90 |
| NC_017360.1|WP_001168214.1|554833_555616_-|NAD+-synthase |
gnl|CDD|184435 |
PRK13980, PRK13980, NAD synthetase; Provisional.
|
1.09139e-124 |
| NC_017360.1|WP_000373231.1|566279_567896_-|CTP-synthase-(glutamine-hydrolyzing) |
gnl|CDD|235437 |
PRK05380, pyrG, CTP synthetase; Validated.
|
0 |
| NC_017360.1|WP_001019098.1|556874_557681_+|septum-site-determining-protein-MinD |
gnl|CDD|225447 |
COG2894, MinD, Septum formation inhibitor-activating ATPase [Cell division and chromosome partitioning].
|
4.58495e-151 |
| NC_017360.1|WP_000829871.1|568160_568823_+|hypothetical-protein |
gnl|CDD|239486 |
cd03392, PAP2_like_2, PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.
|
4.44374e-13 |
| NC_017360.1|WP_000397545.1|561546_561933_+|DUF1294-domain-containing-protein |
gnl|CDD|225863 |
COG3326, COG3326, Predicted membrane protein [Function unknown].
|
2.22695e-28 |
