cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ...
4-374
9.32e-170
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the bacterial homolog of tubulin. It is an ATP-binding protein and shows structural similarities to actin and heat shock cognate protein 70. [Cellular processes, Cell division]
:
Pssm-ID: 273483 [Multi-domain] Cd Length: 371 Bit Score: 481.75 E-value: 9.32e-170
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ...
4-374
9.32e-170
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the bacterial homolog of tubulin. It is an ATP-binding protein and shows structural similarities to actin and heat shock cognate protein 70. [Cellular processes, Cell division]
Pssm-ID: 273483 [Multi-domain] Cd Length: 371 Bit Score: 481.75 E-value: 9.32e-170
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ...
5-374
1.73e-126
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.
Pssm-ID: 466898 [Multi-domain] Cd Length: 372 Bit Score: 371.86 E-value: 1.73e-126
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
5-191
8.48e-72
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains.
Pssm-ID: 214850 Cd Length: 187 Bit Score: 225.05 E-value: 8.48e-72
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
202-370
5.04e-31
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.
Pssm-ID: 464177 [Multi-domain] Cd Length: 167 Bit Score: 117.43 E-value: 5.04e-31
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ...
4-374
9.32e-170
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the bacterial homolog of tubulin. It is an ATP-binding protein and shows structural similarities to actin and heat shock cognate protein 70. [Cellular processes, Cell division]
Pssm-ID: 273483 [Multi-domain] Cd Length: 371 Bit Score: 481.75 E-value: 9.32e-170
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ...
5-374
1.73e-126
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.
Pssm-ID: 466898 [Multi-domain] Cd Length: 372 Bit Score: 371.86 E-value: 1.73e-126
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
5-191
8.48e-72
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains.
Pssm-ID: 214850 Cd Length: 187 Bit Score: 225.05 E-value: 8.48e-72
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
202-370
5.04e-31
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.
Pssm-ID: 464177 [Multi-domain] Cd Length: 167 Bit Score: 117.43 E-value: 5.04e-31
SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes ...
84-157
2.02e-22
SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. The SHS2 domain is inserted in to the RNAseH fold of FtsA, and is involved in protein-protein interaction.
Pssm-ID: 460571 [Multi-domain] Cd Length: 73 Bit Score: 90.63 E-value: 2.02e-22
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ...
6-373
3.17e-16
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 78.87 E-value: 3.17e-16
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ...
6-332
1.41e-15
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 77.70 E-value: 1.41e-15
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ...
164-376
2.83e-05
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and similar proteins; Escherichia coli DnaK, also called heat shock 70 kDa protein/HSP70, plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Moreover, DnaK participates actively in the response to hyperosmotic shock. Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. The family also includes Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.
Pssm-ID: 466879 [Multi-domain] Cd Length: 351 Bit Score: 46.03 E-value: 2.83e-05
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ...
5-88
1.24e-03
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) family; The eukaryotic-type NAGK-like family includes a group of proteins similar to eukaryotic N-acetyl-D-glucosamine kinases, such as Vibrio cholerae glucosamine kinase GspK, Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK), Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK) and Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK). NAGK (EC 2.7.1.59), also called GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. GspK (EC 2.7.1.8), also called GlcN kinase, acts as ATP-dependent kinase, which is specific for glucosamine. StHK is a novel hexokinase that can phosphorylate not only glucose but also GlcNAc, glucosamine, and mannose. KdgK (EC 2.7.1.45), also called 2-keto-3-deoxy-D-gluconate kinase, or KDG kinase, catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). It is specific for KDG. MurK (EC 2.7.1.-/EC 2.7.1.59), also known MurNAc/GlcNAc kinase, or murein sugar kinase, catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. The eukaryotic-type N-acetylglucosamine kinase (NAGK) family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466857 [Multi-domain] Cd Length: 295 Bit Score: 40.75 E-value: 1.24e-03
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
135-326
2.58e-03
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466811 [Multi-domain] Cd Length: 329 Bit Score: 39.78 E-value: 2.58e-03
nucleotide-binding domain (NBD) of Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase ...
5-80
4.68e-03
nucleotide-binding domain (NBD) of Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK) and similar proteins; The family includes a group of uncharacterized proteins similar to Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK; EC 2.7.1.45), also called 2-keto-3-deoxy-D-gluconate kinase, or KDG kinase. It catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). It is specific for KDG.
Pssm-ID: 466933 [Multi-domain] Cd Length: 284 Bit Score: 38.91 E-value: 4.68e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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