MULTISPECIES: ethanolamine utilization protein EutJ [Bacteria][Archaea]
Protein Classification
ethanolamine utilization protein EutJ( domain architecture ID 11487625)
ethanolamine utilization protein EutJ
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PRK15080 | PRK15080 | ethanolamine utilization protein EutJ; Provisional |
8-269 | 8.60e-155 | |||||
ethanolamine utilization protein EutJ; Provisional : Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 431.95 E-value: 8.60e-155
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| Name | Accession | Description | Interval | E-value | |||||
| PRK15080 | PRK15080 | ethanolamine utilization protein EutJ; Provisional |
8-269 | 8.60e-155 | |||||
ethanolamine utilization protein EutJ; Provisional Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 431.95 E-value: 8.60e-155
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| EutJ | COG4820 | Ethanolamine utilization protein EutJ, possible chaperonin [Amino acid transport and ... |
11-274 | 1.36e-152 | |||||
Ethanolamine utilization protein EutJ, possible chaperonin [Amino acid transport and metabolism]; Pssm-ID: 443848 [Multi-domain] Cd Length: 270 Bit Score: 426.53 E-value: 1.36e-152
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| ASKHA_NBD_EutJ | cd24047 | nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
31-267 | 2.89e-145 | |||||
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; 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. Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 407.04 E-value: 2.89e-145
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| EutJ | TIGR02529 | ethanolamine utilization protein EutJ family protein; |
34-268 | 5.32e-136 | |||||
ethanolamine utilization protein EutJ family protein; Pssm-ID: 274180 [Multi-domain] Cd Length: 239 Bit Score: 383.72 E-value: 5.32e-136
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| PilM_2 | pfam11104 | Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for ... |
106-245 | 2.43e-09 | |||||
Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for competency and pilus biogenesis. It binds to PilN and ATP. Pssm-ID: 431656 [Multi-domain] Cd Length: 340 Bit Score: 57.30 E-value: 2.43e-09
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| Name | Accession | Description | Interval | E-value | |||||
| PRK15080 | PRK15080 | ethanolamine utilization protein EutJ; Provisional |
8-269 | 8.60e-155 | |||||
ethanolamine utilization protein EutJ; Provisional Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 431.95 E-value: 8.60e-155
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| EutJ | COG4820 | Ethanolamine utilization protein EutJ, possible chaperonin [Amino acid transport and ... |
11-274 | 1.36e-152 | |||||
Ethanolamine utilization protein EutJ, possible chaperonin [Amino acid transport and metabolism]; Pssm-ID: 443848 [Multi-domain] Cd Length: 270 Bit Score: 426.53 E-value: 1.36e-152
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| ASKHA_NBD_EutJ | cd24047 | nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
31-267 | 2.89e-145 | |||||
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; 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. Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 407.04 E-value: 2.89e-145
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| EutJ | TIGR02529 | ethanolamine utilization protein EutJ family protein; |
34-268 | 5.32e-136 | |||||
ethanolamine utilization protein EutJ family protein; Pssm-ID: 274180 [Multi-domain] Cd Length: 239 Bit Score: 383.72 E-value: 5.32e-136
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| ASKHA_NBD_PilM-like | cd24004 | nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
33-267 | 2.00e-28 | |||||
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: 109.69 E-value: 2.00e-28
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| ASKHA_NBD_PilM | cd24049 | nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
111-246 | 1.02e-17 | |||||
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: 81.56 E-value: 1.02e-17
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| FtsA | COG0849 | Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
111-253 | 1.34e-16 | |||||
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 78.64 E-value: 1.34e-16
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| ASKHA_NBD_FtsA | cd24048 | nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
111-253 | 1.02e-13 | |||||
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: 70.25 E-value: 1.02e-13
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| PilM_2 | pfam11104 | Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for ... |
106-245 | 2.43e-09 | |||||
Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for competency and pilus biogenesis. It binds to PilN and ATP. Pssm-ID: 431656 [Multi-domain] Cd Length: 340 Bit Score: 57.30 E-value: 2.43e-09
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| ftsA | TIGR01174 | cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
115-256 | 2.52e-09 | |||||
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: 57.26 E-value: 2.52e-09
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| FtsA | pfam14450 | Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
142-193 | 2.12e-07 | |||||
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: 49.64 E-value: 2.12e-07
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| DnaK | COG0443 | Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
117-172 | 4.56e-06 | |||||
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 47.51 E-value: 4.56e-06
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| ASKHA_NBD_ParM_pCBH-like | cd24025 | nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and ... |
84-252 | 1.02e-05 | |||||
nucleotide-binding domain (NBD) of Clostridium botulinum plasmid segregation protein ParM and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Clostridium botulinum pCBH plasmid segregation protein ParM, an actin-like polymerizing motor. pCBH ParM filament structure is far more complex in comparison to the known filament structures of actin, MreB, and other ParMs. It is bipolar and stiff and like microtubules. The 15 polymerizing strands are likely to exert greater combined force relative to typical two-stranded actin-like filaments. Pssm-ID: 466875 [Multi-domain] Cd Length: 326 Bit Score: 46.12 E-value: 1.02e-05
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| ASKHA_NBD_MreB-like | cd10225 | nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
111-258 | 1.78e-05 | |||||
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like 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: 466824 [Multi-domain] Cd Length: 317 Bit Score: 45.16 E-value: 1.78e-05
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| mreB | TIGR00904 | cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also ... |
33-170 | 1.96e-05 | |||||
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also called envB) and the paralogous pair MreB and Mrl of Bacillus subtilis have all been shown to help determine cell shape. This protein is present in a wide variety of bacteria, including spirochetes, but is missing from the Mycoplasmas and from Gram-positive cocci. Most completed bacterial genomes have a single member of this family. In some species it is an essential gene. A close homolog is found in the Archaeon Methanobacterium thermoautotrophicum, and a more distant homolog in Archaeoglobus fulgidus. The family is related to cell division protein FtsA and heat shock protein DnaK. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan] Pssm-ID: 129982 [Multi-domain] Cd Length: 333 Bit Score: 45.09 E-value: 1.96e-05
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| pilM | TIGR01175 | type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV ... |
111-245 | 2.80e-05 | |||||
type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV fimbria in Pseudomonas aeruginosa responsible for twitching motility, and for a similar pilus-like structure in Synechocystis. It is also found in species such as Deinococcus described as having natural transformation (for which a type IV pilus-like structure is proposed) but not fimbria. Pssm-ID: 273484 [Multi-domain] Cd Length: 348 Bit Score: 44.78 E-value: 2.80e-05
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| ASKHA_NBD_MamK | cd24009 | nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
63-181 | 2.87e-05 | |||||
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK 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: 466859 [Multi-domain] Cd Length: 328 Bit Score: 44.89 E-value: 2.87e-05
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| PRK13929 | PRK13929 | rod-share determining protein MreBH; Provisional |
64-170 | 7.15e-05 | |||||
rod-share determining protein MreBH; Provisional Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 43.74 E-value: 7.15e-05
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| ASKHA_NBD_HSP70_HSPA13 | cd10237 | nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
87-183 | 1.71e-04 | |||||
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; HSPA13, also called 70-kDa heat shock protein 13, STCH, microsomal stress-70 protein ATPase core, or stress-70 protein chaperone microsome-associated 60 kDa protein, has peptide-independent ATPase activity. It belongs 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). HSPA13 contains an NBD but lacks an SBD. It may function to regulate cell proliferation and survival and modulate the TRAIL-mediated cell death pathway. The HSPA13 gene is a candidate stomach cancer susceptibility gene; a mutation in the NBD coding region of HSPA13 has been identified in stomach cancer cells. The NBD of HSPA13 interacts with the ubiquitin-like proteins Chap1 and Chap2, implicating HSPA13 in regulating cell cycle and cell death events. HSPA13 is induced by the Ca2+ ionophore A23187. Pssm-ID: 466835 [Multi-domain] Cd Length: 409 Bit Score: 42.71 E-value: 1.71e-04
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| HSP70 | pfam00012 | Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
84-155 | 3.32e-04 | |||||
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region. Pssm-ID: 394970 [Multi-domain] Cd Length: 598 Bit Score: 41.86 E-value: 3.32e-04
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| ASKHA_NBD_HSP70 | cd10170 | nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
33-257 | 4.30e-04 | |||||
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: 41.32 E-value: 4.30e-04
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| ASKHA_NBD_HSP70_Ssc1_3 | cd11734 | nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
117-173 | 6.70e-04 | |||||
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein Ssc1p and Ssc3p and similar proteins; This subgroup 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 sc3p (also called extracellular mutant protein 10/Ecm10). Ssc1p is an essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. It constitutes the ATP-driven core of the motor and binds the precursor preprotein. It is required for the import of the processed frataxin homolog YFH1 into the mitochondrion. Ssc1p also acts as a non-catalytic component of endonuclease SceI (endo.SceI), which cleaves specifically at multiple sites on mitochondrial DNA and produces double-stranded breaks. Ssc1p confers broader sequence specificity, greater stability, and higher activity on the catalytic subunit. Ssc3p plays a role in facilitating the assembly of some protein complexes inside the mitochondria. It may initiate the events that lead to refolding of imported precursors in the matrix space. Pssm-ID: 466840 [Multi-domain] Cd Length: 378 Bit Score: 40.51 E-value: 6.70e-04
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| PRK13410 | PRK13410 | molecular chaperone DnaK; Provisional |
117-170 | 6.74e-04 | |||||
molecular chaperone DnaK; Provisional Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 40.77 E-value: 6.74e-04
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| ASKHA_NBD_HSP70_HSPA9 | cd11733 | nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
117-160 | 7.07e-04 | |||||
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and similar proteins; This subgroup includes human mitochondrial HSPA9 (also known as mitochondrial stress-70 protein; mortalin; 75 kDa glucose-regulated protein/GRP-75; HSPA9B; MOT; peptide-binding protein 74/PBP74). It acts as a chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. It interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. HSPA9 regulates erythropoiesis via stabilization of ISC assembly. It may play a role in the control of cell proliferation and cellular aging. Members in this subgroup 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). Pssm-ID: 466839 [Multi-domain] Cd Length: 377 Bit Score: 40.71 E-value: 7.07e-04
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| EutA | pfam06277 | Ethanolamine utilization protein EutA; This family consists of several bacterial EutA ... |
143-226 | 1.22e-03 | |||||
Ethanolamine utilization protein EutA; This family consists of several bacterial EutA ethanolamine utilization proteins. The EutA protein is thought to protect the lyase (EutBC) from inhibition by CNB12. Pssm-ID: 377642 Cd Length: 475 Bit Score: 39.92 E-value: 1.22e-03
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| ASKHA_NBD_HSP70_HscA | cd10236 | nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
117-171 | 1.90e-03 | |||||
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar proteins; 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. Members in this subfamily 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). HscA's partner J-domain protein is HscB; it does not appear to require a NEF and has been shown to be induced by cold-shock. The HscA-HscB chaperone/co-chaperone pair is involved in [Fe-S] cluster assembly. Pssm-ID: 466834 [Multi-domain] Cd Length: 367 Bit Score: 39.12 E-value: 1.90e-03
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| hscA | PRK05183 | chaperone protein HscA; Provisional |
117-171 | 2.55e-03 | |||||
chaperone protein HscA; Provisional Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 39.00 E-value: 2.55e-03
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| PRK13411 | PRK13411 | molecular chaperone DnaK; Provisional |
117-173 | 2.63e-03 | |||||
molecular chaperone DnaK; Provisional Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 38.97 E-value: 2.63e-03
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| hscA | PRK01433 | chaperone protein HscA; Provisional |
87-246 | 2.74e-03 | |||||
chaperone protein HscA; Provisional Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 39.07 E-value: 2.74e-03
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| ASKHA_NBD_HSP70_DnaK_HscA_HscC | cd24029 | nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
115-248 | 3.63e-03 | |||||
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: 38.33 E-value: 3.63e-03
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| EutA | COG4819 | Ethanolamine utilization protein EutA, possible chaperonin [Amino acid transport and ... |
143-226 | 3.70e-03 | |||||
Ethanolamine utilization protein EutA, possible chaperonin [Amino acid transport and metabolism]; Pssm-ID: 443847 Cd Length: 477 Bit Score: 38.63 E-value: 3.70e-03
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| MreB_Mbl | pfam06723 | MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
111-173 | 3.73e-03 | |||||
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl. Pssm-ID: 399596 [Multi-domain] Cd Length: 327 Bit Score: 38.31 E-value: 3.73e-03
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| ASKHA_NBD_PPX_GppA | cd24006 | nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate ... |
119-163 | 3.93e-03 | |||||
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GppA) domain family; Members of the PPX/GppA family are involved in bacterial survival and metabolism. They may play distinct biochemical roles involved in polyphosphate and (p)ppGpp metabolic pathways. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). Some bacteria, such as Escherichia coli, possesses two homologs, EcGppA and EcPPX. Some others, such as Helicobacter pylori and Aquifex aeolicus, encode only one PPX/GppA homolog, which may play important roles in the homeostasis of both (p)ppGpp and PolyP. The PPX/GppA family belongs 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: 466856 [Multi-domain] Cd Length: 294 Bit Score: 37.90 E-value: 3.93e-03
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| eutA | PRK10719 | ethanolamine ammonia-lyase reactivating factor EutA; |
143-221 | 4.56e-03 | |||||
ethanolamine ammonia-lyase reactivating factor EutA; Pssm-ID: 236743 [Multi-domain] Cd Length: 475 Bit Score: 38.31 E-value: 4.56e-03
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| PTZ00400 | PTZ00400 | DnaK-type molecular chaperone; Provisional |
117-156 | 5.15e-03 | |||||
DnaK-type molecular chaperone; Provisional Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 38.27 E-value: 5.15e-03
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| ASKHA_NBD_HSP70_HSPA1-like | cd24028 | nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
117-155 | 6.53e-03 | |||||
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The HSPA1-like family includes human HSPA1A (70-kDa heat shock protein 1A, also known as HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A), HSPA1B (70-kDa heat shock protein 1B, also known as HSPA1A; HSP70-2; HSP70-1B), and HSPA1L (70-kDa heat shock protein 1-like, also known as HSP70T; hum70t; HSP70-1L; HSP70-HOM), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B), HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10), HSPA13 (also known as 70-kDa heat shock protein 13; STCH; microsomal stress-70 protein ATPase core; stress-70 protein chaperone microsome-associated 60 kDa protein), as well as Saccharmoyces cerevisiae Hsp70 chaperone Ssb1-2 and heat shock protein Ssa1-4. HSPA1A/1B, HSPA1L, HSPA2 and HSPA6-8 are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). HSPA13 has peptide-independent ATPase activity. All family members 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). Pssm-ID: 466878 [Multi-domain] Cd Length: 376 Bit Score: 37.49 E-value: 6.53e-03
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| PRK13930 | PRK13930 | rod shape-determining protein MreB; Provisional |
111-163 | 7.67e-03 | |||||
rod shape-determining protein MreB; Provisional Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 37.42 E-value: 7.67e-03
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| dnaK | PRK00290 | molecular chaperone DnaK; Provisional |
117-149 | 8.94e-03 | |||||
molecular chaperone DnaK; Provisional Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 37.39 E-value: 8.94e-03
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| ASKHA_NBD_HSP70_BiP | cd10241 | nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
117-149 | 9.46e-03 | |||||
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; This subfamily includes human BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), Sacchaormyces cerevisiae BiP (also known as Grp78p), Arabidopsis thaliana BiP1-3 (also known as luminal-binding protein 1-3) and related proteins. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). BiP may function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. It appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. BiP may also play a role in apoptosis and cell proliferation. Plant BiP may be required for pollen development and pollen tube growth. This subfamily belongs 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). Pssm-ID: 466837 [Multi-domain] Cd Length: 376 Bit Score: 37.19 E-value: 9.46e-03
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