NC_020519.1|WP_003855829.1|319038_319338_+|flp-pilus-assembly-TadE/G-like-family-protein |
gnl|CDD|274799 |
TIGR03816, tadE_like_DECH, helicase/secretion neighborhood TadE-like protein. Members of this small, highly hydrophobic protein family occur in a pilus/secretion-like region that usually is next to an uncharacterized DEAH-box helicase, in Actinobacteria. Members show sequence similarity to the TadE-like family described by pfam07811. The function is unknown. [Unknown function, General].
|
9.82352e-08 |
NC_020519.1|WP_011013542.1|310131_311328_+|MarP-family-serine-protease |
gnl|CDD|367140 |
pfam02674, Colicin_V, Colicin V production protein. Colicin V production protein is required in E. Coli for colicin V production from plasmid pColV-K30. This protein is coded for in the purF operon.
|
1.69959e-18 |
NC_020519.1|WP_011013540.1|308744_309305_+|TlpA-family-protein-disulfide-reductase |
gnl|CDD|239264 |
cd02966, TlpA_like_family, TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.
|
4.94736e-22 |
NC_020519.1|WP_011013541.1|309297_310041_+|CoA-pyrophosphatase |
gnl|CDD|239518 |
cd03426, CoAse, Coenzyme A pyrophosphatase (CoAse), a member of the Nudix hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative stress. CoAse has a conserved Nudix fold and requires a single divalent cation for catalysis. In addition to a signature Nudix motif G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val, CoAse contains an additional motif upstream called the NuCoA motif (LLTXT(SA)X3RX3GX3FPGG) which is postulated to be involved in CoA recognition. CoA plays a central role in lipid metabolism. It is involved in the initial steps of fatty acid sythesis in the cytosol, in the oxidation of fatty acids and the citric acid cycle in the mitochondria, and in the oxidation of long-chain fatty acids in peroxisomes. CoA has the important role of activating fatty acids for further modification into key biological signalling molecules.
|
6.21532e-53 |
NC_020519.1|WP_003855827.1|318491_318692_+|DUF4244-domain-containing-protein |
gnl|CDD|379429 |
pfam14029, DUF4244, Protein of unknown function (DUF4244). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 66 and 95 amino acids in length. There is a conserved EYA sequence motif.
|
1.21917e-15 |
NC_020519.1|WP_011013547.1|316001_317135_+|TadA-family-conjugal-transfer-associated-ATPase |
gnl|CDD|200328 |
TIGR03819, heli_sec_ATPase, helicase/secretion neighborhood ATPase. Members of this protein family comprise a distinct clade of putative ATPase associated with an integral membrane complex likely to act in pilus formation, secretion, or conjugal transfer. The association of most members with a nearby gene for a DEAH-box helicase suggests a role in conjugal transfer.
|
2.31214e-154 |
NC_020519.1|WP_011013536.1|304069_305266_+|acyl-CoA-dehydrogenase |
gnl|CDD|173840 |
cd01151, GCD, Glutaryl-CoA dehydrogenase. Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
|
6.49897e-107 |
NC_020519.1|WP_011013549.1|317892_318468_+|type-II-secretion-system-F-family-protein |
gnl|CDD|224975 |
COG2064, TadC, Flp pilus assembly protein TadC [Cell motility and secretion / Intracellular trafficking and secretion].
|
1.403e-14 |
NC_020519.1|WP_003863309.1|305287_305761_+|MaoC-family-dehydratase |
gnl|CDD|239534 |
cd03450, NodN, NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. Rhizobium and related species form nodules on the roots of their legume hosts, a symbiotic process that requires production of Nod factors, which are signal molecules involved in root hair deformation and meristematic cell division. The nodulation gene products, including NodN, are involved in producing the Nod factors, however the role played by NodN is unclear.
|
1.47997e-80 |
NC_020519.1|WP_011013545.1|313621_314464_-|HAD-family-hydrolase |
gnl|CDD|319796 |
cd02612, HAD_PGPPase, phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C. This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.
|
2.04883e-74 |
NC_020519.1|WP_011013548.1|317119_317896_+|type-II-secretion-system-F-family-protein |
gnl|CDD|227300 |
COG4965, TadB, Flp pilus assembly protein TadB [Intracellular trafficking and secretion].
|
4.49256e-67 |
NC_020519.1|WP_011013544.1|312905_313457_-|phage-holin-family-protein |
gnl|CDD|377816 |
pfam07332, Phage_holin_3_6, Putative Actinobacterial Holin-X, holin superfamily III. Phage_holin_3_6 is a family of small hydrophobic proteins with two or three transmembrane domains of the Hol-X family. Holin proteins are produced by double-stranded DNA bacteriophages that use an endolysin-holin strategy to achieve lysis of their hosts. The endolysins are peptidoglycan-degrading enzymes that are usually accumulated in the cytosol until access to the cell wall substrate is provided by the holin membrane lesion.
|
6.93881e-32 |
NC_020519.1|WP_020948499.1|305875_306703_+|MBL-fold-metallo-hydrolase |
gnl|CDD|293836 |
cd16278, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.
|
5.85899e-64 |
NC_020519.1|WP_011013535.1|303132_304077_+|4-hydroxyphenyl-beta-ketoacyl-CoA-hydrolase |
gnl|CDD|225070 |
COG2159, COG2159, Predicted metal-dependent hydrolase of the TIM-barrel fold [General function prediction only].
|
2.74268e-86 |
NC_020519.1|WP_011013539.1|307954_308737_+|endonuclease-III |
gnl|CDD|223255 |
COG0177, Nth, Predicted EndoIII-related endonuclease [DNA replication, recombination, and repair].
|
3.20732e-106 |
NC_020519.1|WP_003855810.1|306778_307462_-|Crp/Fnr-family-transcriptional-regulator |
gnl|CDD|223736 |
COG0664, Crp, cAMP-binding proteins - catabolite gene activator and regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms].
|
1.34158e-55 |
NC_020519.1|WP_011013546.1|314943_316005_+|hypothetical-protein |
gnl|CDD|274798 |
TIGR03815, CpaE_hom_Actino, helicase/secretion neighborhood CpaE-like protein. Members of this protein family belong to the MinD/ParA family of P-loop NTPases, and in particular show homology to the CpaE family of pilus assembly proteins (see ). Nearly all members are found, not only in a gene context consistent with pilus biogenesis or a pilus-like secretion apparatus, but also near a DEAD/DEAH-box helicase, suggesting an involvement in DNA transfer activity. The model describes a clade restricted to the Actinobacteria.
|
2.11979e-92 |
NC_020519.1|WP_015439409.1|311895_312891_-|alpha/beta-hydrolase |
gnl|CDD|223669 |
COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].
|
1.26176e-21 |