NC_008086.1|WP_000003589.1|918319_919048_-|hydrogenase-nickel-incorporation-protein-HypB |
gnl|CDD|272891 |
TIGR00073, nickel_incorporation_protein_HypB, hydrogenase accessory protein HypB. A GTP hydrolase for assembly of nickel metallocenter of hydrogenase. A similar protein, ureG, is an accessory protein for urease, which also uses nickel. hits scoring 75 and above are safe as orthologs. [SS 1/05/04 I changed the role_ID and process GO from protein folding to to protein modification, since a protein folding role has not been established, but HypB is implicated in insertion of nickel into the large subunit of NiFe hydrogenases.] [Protein fate, Protein modification and repair].
|
1.32809e-108 |
NC_008086.1|WP_000109782.1|916953_918066_-|hydrogenase-formation-protein-HypD |
gnl|CDD|272892 |
TIGR00075, Hydrogenase_isoenzymes_formation_protein_HypD, hydrogenase expression/formation protein HypD. HypD is involved in the hyp operon which is needed for the activity of the three hydrogenase isoenzymes in Escherichia coli. HypD is one of the genes needed for formation of these enzymes. This protein has been found in gram-negative and gram-positive bacteria and Archaea. [Protein fate, Protein modification and repair].
|
0 |
NC_008086.1|WP_000716293.1|913626_915861_-|Hop-family-adhesin-BabA |
gnl|CDD|375731 |
pfam18304, SabA_adhesion, SabA N-terminal extracellular adhesion domain. This is the N-terminal extracellular adhesion domain of Sialic acid binding adhesin (SabA) present in Helicobacter pylori. The N-terminal domain of SabA functions as a sugar-binding adhesion domain with conserved disulfide bonds. Notably, these amino acid residues are not only conserved among SabA orthologs but also between SabA and BabA.
|
6.12238e-72 |
NC_008086.1|WP_001135623.1|912042_912567_+|acyl-CoA-thioesterase |
gnl|CDD|224523 |
COG1607, COG1607, Acyl-CoA hydrolase [Lipid metabolism].
|
3.69539e-64 |
NC_008086.1|WP_001000248.1|925087_926905_+|flagellar-hook-protein-FlgE |
gnl|CDD|235620 |
PRK05841, flgE, flagellar hook protein FlgE; Validated.
|
0 |
NC_008086.1|WP_000242349.1|909308_910076_-|ABC-transporter-ATP-binding-protein |
gnl|CDD|224045 |
COG1120, FepC, ABC-type cobalamin/Fe3+-siderophores transport systems, ATPase components [Inorganic ion transport and metabolism / Coenzyme metabolism].
|
9.28427e-100 |
NC_008086.1|WP_000335461.1|918083_918320_-|HypC/HybG/HupF-family-hydrogenase-formation-chaperone |
gnl|CDD|223375 |
COG0298, HypC, Hydrogenase maturation factor [Posttranslational modification, protein turnover, chaperones].
|
1.92061e-31 |
NC_008086.1|WP_000471388.1|902487_903885_+|cysteine--tRNA-ligase |
gnl|CDD|234705 |
PRK00260, cysS, cysteinyl-tRNA synthetase; Validated.
|
0 |
NC_008086.1|WP_000921465.1|910075_911056_-|iron-ABC-transporter-permease |
gnl|CDD|376439 |
pfam01032, FecCD, FecCD transport family. This is a sub-family of bacterial binding protein-dependent transport systems family. This Pfam entry contains the inner components of this multicomponent transport system.
|
1.29891e-66 |
NC_008086.1|WP_000405540.1|904114_908005_+|autotransporter-outer-membrane-beta-barrel-domain-containing-protein |
gnl|CDD|111576 |
pfam02691, VacA, Vacuolating cyotoxin. This family consists of Vacuolating cyotoxin proteins form Proteobacteria. These proteins are an important virulence determinate in H. pylori and induce cytoplasmic vacuolation in a variety of mammalian cell lines.
|
0 |
NC_008086.1|WP_187145837.1|908124_909198_-|glycosyltransferase-family-8-protein |
gnl|CDD|224359 |
COG1442, RfaJ, Lipopolysaccharide biosynthesis proteins, LPS:glycosyltransferases [Cell envelope biogenesis, outer membrane].
|
9.07031e-94 |
NC_008086.1|WP_001139877.1|922482_924057_+|flagellar-hook-length-control-protein-FliK |
gnl|CDD|376734 |
pfam02120, Flg_hook, Flagellar hook-length control protein FliK. This is the C terminal domain of FliK. FliK controls the length of the flagellar hook by directly measuring the hook length as a molecular ruler. This family also includes YscP of the Yersinia type III secretion system, and equivalent proteins in other pathogenic bacterial type III secretion systems.
|
6.02449e-12 |
NC_008086.1|WP_000913546.1|901026_902487_+|murein-biosynthesis-integral-membrane-protein-MurJ |
gnl|CDD|367301 |
pfam03023, MVIN, MviN-like protein. Deletion of the mviN virulence gene in Salmonella enterica serovar. Typhimurium greatly reduces virulence in a mouse model of typhoid-like disease. Open reading frames encoding homologs of MviN have since been identified in a variety of bacteria, including pathogens and non-pathogens and plant-symbionts. In the nitrogen-fixing symbiont Rhizobium tropici, mviN is required for motility. The MviM protein is predicted to be membrane-associated.
|
1.01831e-117 |
NC_008086.1|WP_000963291.1|924107_925091_+|flagellar-hook-assembly-protein-FlgD |
gnl|CDD|235621 |
PRK05842, flgD, flagellar hook assembly protein FlgD.
|
5.68952e-171 |
NC_008086.1|WP_000454245.1|919290_919590_-|cupin-domain-containing-protein |
gnl|CDD|380358 |
cd02230, cupin_HP0902-like, Helicobacter pylori HP0902 and related proteins, cupin domain. This family includes prokaryotic and archaeal proteins homologous to HP0902, a functionally uncharacterized protein from Helicobacter pylori and Spy1581, a protein of unknown function from Streptococcus pyogenes. These proteins demonstrate all-beta cupin folds that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins, and thus may have a putative role in H. pylori pathogenicity.
|
1.18738e-20 |
NC_008086.1|WP_000538083.1|911048_911903_-|SDR-family-oxidoreductase |
gnl|CDD|187632 |
cd05374, 17beta-HSD-like_SDR_c, 17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs. 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
|
3.22198e-92 |
NC_008086.1|WP_148194192.1|920024_920204_-|acetate-kinase |
gnl|CDD|234680 |
PRK00180, PRK00180, acetate kinase A/propionate kinase 2; Reviewed.
|
1.87693e-30 |
NC_008086.1|WP_011550059.1|912672_912939_-|type-II-toxin-antitoxin-system-mRNA-interferase-toxin,-RelE/StbE-family |
gnl|CDD|379750 |
pfam15738, YafQ_toxin, Bacterial toxin of type II toxin-antitoxin system, YafQ. YafQ is a family of bacterial toxin ribonucleases of type II toxin-antitoxin systems. The E.coli gene is expressed from the dinB operon. The cognate antitoxin for the E. coli protein is DinJ, in family RelB_antitoxin, pfam02604.
|
1.23543e-33 |