universal stress protein [Pseudarthrobacter humi]
universal stress protein( domain architecture ID 10001747)
universal stress protein (USP) enhances the rate of cell survival during prolonged exposure to stress agents
List of domain hits
Name | Accession | Description | Interval | E-value | |||
UspA | COG0589 | Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms]; |
6-139 | 2.90e-29 | |||
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms]; : Pssm-ID: 440354 Cd Length: 136 Bit Score: 103.85 E-value: 2.90e-29
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Name | Accession | Description | Interval | E-value | |||
UspA | COG0589 | Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms]; |
6-139 | 2.90e-29 | |||
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms]; Pssm-ID: 440354 Cd Length: 136 Bit Score: 103.85 E-value: 2.90e-29
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Usp | pfam00582 | Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ... |
8-140 | 1.00e-25 | |||
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. UspA enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae UspA reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, though UspA lacks ATP-binding activity. Pssm-ID: 425765 [Multi-domain] Cd Length: 137 Bit Score: 94.78 E-value: 1.00e-25
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USP_Rv2623_repeat1 | cd23944 | universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis ... |
8-140 | 5.96e-24 | |||
universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis universal stress protein Rv2623 regulates mycobacterial growth in vitro and in vivo and is required for the entry of the tubercle bacillus into the chronic phase of infection in the host. In addition Rv2623 binds ATP and the growth-regulatory attribute of this USP is dependent on its ATP-binding activity. Rv2623 is thought to function as an ATP-dependent signaling intermediate in a pathway that promotes persistent infection. The universal stress protein Usp is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. Usp enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae Usp reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, although Usp lacks ATP-binding activity. Pssm-ID: 467509 Cd Length: 140 Bit Score: 90.16 E-value: 5.96e-24
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PRK15005 | PRK15005 | universal stress protein UspF; |
55-139 | 1.86e-04 | |||
universal stress protein UspF; Pssm-ID: 184967 [Multi-domain] Cd Length: 144 Bit Score: 39.40 E-value: 1.86e-04
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Name | Accession | Description | Interval | E-value | |||
UspA | COG0589 | Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms]; |
6-139 | 2.90e-29 | |||
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms]; Pssm-ID: 440354 Cd Length: 136 Bit Score: 103.85 E-value: 2.90e-29
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Usp | pfam00582 | Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ... |
8-140 | 1.00e-25 | |||
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. UspA enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae UspA reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, though UspA lacks ATP-binding activity. Pssm-ID: 425765 [Multi-domain] Cd Length: 137 Bit Score: 94.78 E-value: 1.00e-25
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USP_Rv2623_repeat1 | cd23944 | universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis ... |
8-140 | 5.96e-24 | |||
universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis universal stress protein Rv2623 regulates mycobacterial growth in vitro and in vivo and is required for the entry of the tubercle bacillus into the chronic phase of infection in the host. In addition Rv2623 binds ATP and the growth-regulatory attribute of this USP is dependent on its ATP-binding activity. Rv2623 is thought to function as an ATP-dependent signaling intermediate in a pathway that promotes persistent infection. The universal stress protein Usp is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. Usp enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae Usp reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, although Usp lacks ATP-binding activity. Pssm-ID: 467509 Cd Length: 140 Bit Score: 90.16 E-value: 5.96e-24
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USP-like | cd00293 | universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ... |
7-139 | 1.95e-23 | |||
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. USP enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae Usp reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, although USP lacks ATP-binding activity. Pssm-ID: 467483 [Multi-domain] Cd Length: 135 Bit Score: 88.94 E-value: 1.95e-23
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USP_At3g01520-like | cd23659 | universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ... |
7-140 | 5.76e-23 | |||
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and fungal proteins of unknown function, including Arabidopsis thaliana At3g01520. A. thaliana contains 44 USP domain-containing proteins; the USP domain is found either in a small protein with unknown physiological function or as an N-terminal portion of a multi-domain protein, usually a protein kinase. The gene At3g01520 of Arabidopsis thaliana encodes a 175-residue universal stress protein (USP)-like protein which is widely found in the genomes of bacteria, as well as fungi, protozoa, and plants. The bound AMP and conservation of residues in the ATP-binding loop suggest that the protein At3g01520 belongs to the ATP-binding USP subfamily. Universal stress proteins (USPs) are small cytoplasmic bacterial proteins whose expression is enhanced when the cell is exposed to stress agents. USP enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. Pssm-ID: 467505 Cd Length: 143 Bit Score: 87.68 E-value: 5.76e-23
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USP_Rv2623_repeat2 | cd23661 | universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis ... |
8-139 | 9.66e-19 | |||
universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis universal stress protein Rv2623 regulates mycobacterial growth in vitro and in vivo and is required for the entry of the tubercle bacillus into the chronic phase of infection in the host. In addition, Rv2623 binds ATP and the growth-regulatory attribute of this USP is dependent on its ATP-binding activity. Rv2623 is thought to function as an ATP-dependent signaling intermediate in a pathway that promotes persistent infection. The universal stress protein Usp is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. Usp enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae Usp reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, although Usp lacks ATP-binding activity. Pssm-ID: 467507 [Multi-domain] Cd Length: 133 Bit Score: 76.78 E-value: 9.66e-19
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PRK15005 | PRK15005 | universal stress protein UspF; |
55-139 | 1.86e-04 | |||
universal stress protein UspF; Pssm-ID: 184967 [Multi-domain] Cd Length: 144 Bit Score: 39.40 E-value: 1.86e-04
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USP-E_repeat2 | cd23660 | Universal stress protein E, repeat 2; UspE is a tandem-type USP that consists of two USP ... |
7-141 | 1.55e-03 | |||
Universal stress protein E, repeat 2; UspE is a tandem-type USP that consists of two USP domains. The UspE expression levels of Escherichia coli become elevated in response to oxidative stress and DNA damaging agents, including exposure to mitomycin C, cadmium, and hydrogen peroxide. The universal stress protein Usp is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. Usp enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. Pssm-ID: 467506 Cd Length: 148 Bit Score: 36.48 E-value: 1.55e-03
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USP-A-like | cd23657 | universal stress protein A and similar proteins; The universal stress protein UspA is a small ... |
7-141 | 7.98e-03 | |||
universal stress protein A and similar proteins; The universal stress protein UspA is a small cytoplasmic bacterial protein whose expression is enhanced several-fold when cellular viability is challenged with heat shock, nutrient starvation, stress agents which arrest cell growth, or DNA-damaging agents. UspA enhances the rate of cell survival during prolonged exposure to such conditions, suggesting that it asserts a general "stress endurance" activity. In general, these proteins form dimers and have domains for nucleotide binding activity. The crystal structure of Haemophilus influenzae UspA reveals an asymmetric dimer with a tertiary alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, but unlike MJ0577, it lacks ATP-binding activity. Pssm-ID: 467504 Cd Length: 138 Bit Score: 34.59 E-value: 7.98e-03
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PRK15456 | PRK15456 | universal stress protein UspG; Provisional |
57-139 | 8.22e-03 | |||
universal stress protein UspG; Provisional Pssm-ID: 185353 Cd Length: 142 Bit Score: 34.53 E-value: 8.22e-03
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Blast search parameters | ||||
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