| NC_017285.1|WP_014517670.1|286172_287438_+|tRNA-(N(6)-L-threonylcarbamoyladenosine(37)-C(2))--methylthiotransferase-MtaB |
gnl|CDD|273704 |
TIGR01579, MiaB-like-C, MiaB-like tRNA modifying enzyme. This clade of sequences is closely related to MiaB, a modifier of isopentenylated adenosine-37 of certain eukaryotic and bacterial tRNAs (see TIGR01574). Sequence alignments suggest that this equivalog performs the same chemical transformation as MiaB, perhaps on a different (or differently modified) tRNA base substrate. This clade is a member of a subfamily (TIGR00089) and spans low GC Gram positive bacteria, alpha and epsilon proteobacteria, Campylobacter, Porphyromonas, Aquifex, Thermotoga, Chlamydia, Treponema and Fusobacterium. [Protein synthesis, tRNA and rRNA base modification].
|
0 |
| NC_017285.1|WP_157857985.1|296770_297640_-|autotransporter-domain-containing-protein |
gnl|CDD|214872 |
smart00869, Autotransporter, Autotransporter beta-domain. Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type IV pathway was first described for the IgA1 protease. 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 domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different peptidase is used and in some cases no cleavage occurs.
|
3.14711e-35 |
| NC_017285.1|WP_035416646.1|310281_311451_+|DUF562-domain-containing-protein |
gnl|CDD|368104 |
pfam04763, DUF562, Protein of unknown function (DUF562). Family of uncharacterized proteins.
|
1.34216e-55 |
| NC_017285.1|WP_014517664.1|280541_281321_+|transporter-substrate-binding-domain-containing-protein |
gnl|CDD|270220 |
cd00999, PBP2_ArtJ, The solute binding domain of ArtJ protein, a member of the type 2 periplasmic binding fold protein superfamily. An arginine-binding protein found in Chlamydiae trachomatis (CT-ArtJ) and pneumoniae (CPn-ArtJ) and its closely related proteins. CT- and CPn-ArtJ are shown to have different immunogenic properties despite a high sequence similarity. The ArtJ proteins display the type 2 periplasmic binding fold organized in two alpha-beta domains with arginine-binding region at their interface.
|
2.44569e-119 |
| NC_017285.1|WP_014517679.1|306112_308935_-|autotransporter-domain-containing-protein |
gnl|CDD|214872 |
smart00869, Autotransporter, Autotransporter beta-domain. Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type IV pathway was first described for the IgA1 protease. 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 domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different peptidase is used and in some cases no cleavage occurs.
|
6.40948e-29 |
| NC_017285.1|WP_014517668.1|283853_284666_+|MBL-fold-metallo-hydrolase |
gnl|CDD|293837 |
cd16279, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo. 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. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B).
|
2.80134e-69 |
| NC_017285.1|WP_014517677.1|300120_302970_-|autotransporter-domain-containing-protein |
gnl|CDD|214872 |
smart00869, Autotransporter, Autotransporter beta-domain. Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type IV pathway was first described for the IgA1 protease. 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 domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different peptidase is used and in some cases no cleavage occurs.
|
1.88096e-31 |
| NC_017285.1|WP_041466856.1|277256_280424_-|hypothetical-protein |
gnl|CDD|223880 |
COG0810, TonB, Periplasmic protein TonB, links inner and outer membranes [Cell envelope biogenesis, outer membrane].
|
4.51359e-11 |
| NC_017285.1|WP_014517675.1|294259_296587_+|FlxA-like-family-protein |
gnl|CDD|223039 |
PHA03307, PHA03307, transcriptional regulator ICP4; Provisional.
|
0.00902018 |
| NC_017285.1|WP_014517666.1|282975_283632_+|hypothetical-protein |
gnl|CDD|274763 |
TIGR03750, hypothetical_protein, conjugative transfer region protein, TIGR03750 family. Members of this protein family are found occasionally on plasmids. Usually, however, they are found on the bacterial main chromosome in regions flanked by markers of conjugative transfer and/or transposition. [Mobile and extrachromosomal element functions, Plasmid functions].
|
0.00183712 |
| NC_017285.1|WP_014517688.1|321120_323193_+|DUF562-domain-containing-protein |
gnl|CDD|368104 |
pfam04763, DUF562, Protein of unknown function (DUF562). Family of uncharacterized proteins.
|
1.36296e-68 |
| NC_017285.1|WP_049755959.1|303215_306020_-|autotransporter-domain-containing-protein |
gnl|CDD|214872 |
smart00869, Autotransporter, Autotransporter beta-domain. Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type IV pathway was first described for the IgA1 protease. 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 domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different peptidase is used and in some cases no cleavage occurs.
|
6.311e-37 |
| NC_017285.1|WP_014517689.1|323532_326469_-|autotransporter-domain-containing-protein |
gnl|CDD|214872 |
smart00869, Autotransporter, Autotransporter beta-domain. Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type IV pathway was first described for the IgA1 protease. 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 domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different peptidase is used and in some cases no cleavage occurs.
|
4.2237e-26 |
| NC_017285.1|WP_080511711.1|297548_299708_-|hypothetical-protein |
gnl|CDD|311484 |
pfam07548, ChlamPMP_M, Chlamydia polymorphic membrane protein middle domain. This family contains several Chlamydia polymorphic membrane proteins. Chlamydia pneumoniae is an obligate intracellular bacterium and a common human pathogen causing infection of the upper and lower respiratory tract. This domain is found between the beta-helical repeats (pfam02415) and the C-terminal pfam03797. This domain is excised subsequent to secretion.
|
7.79861e-16 |
| NC_017285.1|WP_014517669.1|284653_286072_+|GTPase-HflX |
gnl|CDD|225171 |
COG2262, HflX, GTPases [General function prediction only].
|
8.01415e-179 |
| NC_017285.1|WP_014517672.1|288434_290597_+|1,4-alpha-glucan-branching-protein-GlgB |
gnl|CDD|235445 |
PRK05402, PRK05402, 1,4-alpha-glucan branching protein GlgB.
|
0 |
