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Conserved domains on  [gi|2230564695|ref|WP_247855225|]
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universal stress protein [Halomonas getboli]

Protein Classification

universal stress protein( domain architecture ID 10001747)

universal stress protein (USP) enhances the rate of cell survival during prolonged exposure to stress agents

CATH:  3.40.50.620
Gene Ontology:  GO:0042802
SCOP:  8083864

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
1-147 9.03e-39

Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];


:

Pssm-ID: 440354  Cd Length: 136  Bit Score: 127.73  E-value: 9.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230564695   1 MFKRIMVPVDGSKGAIKALDKAVALQRLTDAELYILCVFKHHSLLEASLSMIRperldipdDALKEYATEIAVQAKAHAA 80
Cdd:COG0589     1 MYKRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEELE--------EELREEAEEALEEAAERLE 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2230564695  81 ELGVPadkVRAFVKGGRPSRTIVRFARKRDCDLIVIGAQGTNGDKGLLLGSVSQRVAGSAHCPTLVV 147
Cdd:COG0589    73 EAGVE---VETVVREGDPAEAILEAAEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
 
Name Accession Description Interval E-value
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
1-147 9.03e-39

Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];


Pssm-ID: 440354  Cd Length: 136  Bit Score: 127.73  E-value: 9.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230564695   1 MFKRIMVPVDGSKGAIKALDKAVALQRLTDAELYILCVFKHHSLLEASLSMIRperldipdDALKEYATEIAVQAKAHAA 80
Cdd:COG0589     1 MYKRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEELE--------EELREEAEEALEEAAERLE 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2230564695  81 ELGVPadkVRAFVKGGRPSRTIVRFARKRDCDLIVIGAQGTNGDKGLLLGSVSQRVAGSAHCPTLVV 147
Cdd:COG0589    73 EAGVE---VETVVREGDPAEAILEAAEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
4-147 1.07e-31

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: 109.74  E-value: 1.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230564695   4 RIMVPVDGSKGAIKALDKAVALQRLTDAELYILCVfkhhslLEASLSMIRPERLDIPDDALKEYATEIAVQAKAHAAELG 83
Cdd:cd00293     1 KILVAVDGSEESERALEWALELAKRPGAELTLLHV------VDPPPSSSLSGGLEELADELKEEAEELLEEAKKLAEEAG 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2230564695  84 VpadKVRAFVKGGRPSRTIVRFARKRDCDLIVIGAQGTNGDKGLLLGSVSQRVAGSAHCPTLVV 147
Cdd:cd00293    75 V---EVETIVVEGDPAEAILEEAKELGADLIVMGSRGRSGLKRLLLGSVSEYVLRHAPCPVLVV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
5-147 9.45e-30

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: 104.80  E-value: 9.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230564695   5 IMVPVDGSKGAIKALDKAVALQRLTDAELYILCVFKHHSLLEASLsmirpERLDIPDDALKEYATEIAVQAKAHAAELGV 84
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAELILLHVIDPPPSGAASL-----ADESAEEEELELELAEAEALAAAAAAEAGG 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2230564695  85 PadKVRAFVKGGRPSRTIVRFARKRDCDLIVIGAQGTNGDKGLLLGSVSQRVAGSAHCPTLVV 147
Cdd:pfam00582  76 V--KVEVVVVVGDPAEEILEVAEEEDADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVV 136
PRK15005 PRK15005
universal stress protein UspF;
1-147 3.16e-09

universal stress protein UspF;


Pssm-ID: 184967 [Multi-domain]  Cd Length: 144  Bit Score: 52.11  E-value: 3.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230564695   1 MFKRIMVPVDGSKGAI--KALDKAVALQRLTDAELYILCV---FKHHSLLEASLSMIRPERldipdDALKEyatEIAVQA 75
Cdd:PRK15005    1 MNRTILVPIDISDSELtqRVISHVEAEAKIDDAEVHFLTVipsLPYYASLGLAYSAELPAM-----DDLKA---EAKSQL 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2230564695  76 KAHAAELGVPADKVRAFVKGGRPSRTIVRFARKRDCDLIVIgAQGTNGDKGLLLGSVSQRVAGSAHCPTLVV 147
Cdd:PRK15005   73 EEIIKKFKLPTDRVHVHVEEGSPKDRILELAKKIPADMIII-ASHRPDITTYLLGSNAAAVVRHAECSVLVV 143
 
Name Accession Description Interval E-value
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
1-147 9.03e-39

Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];


Pssm-ID: 440354  Cd Length: 136  Bit Score: 127.73  E-value: 9.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230564695   1 MFKRIMVPVDGSKGAIKALDKAVALQRLTDAELYILCVFKHHSLLEASLSMIRperldipdDALKEYATEIAVQAKAHAA 80
Cdd:COG0589     1 MYKRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEELE--------EELREEAEEALEEAAERLE 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2230564695  81 ELGVPadkVRAFVKGGRPSRTIVRFARKRDCDLIVIGAQGTNGDKGLLLGSVSQRVAGSAHCPTLVV 147
Cdd:COG0589    73 EAGVE---VETVVREGDPAEAILEAAEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
4-147 1.07e-31

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: 109.74  E-value: 1.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230564695   4 RIMVPVDGSKGAIKALDKAVALQRLTDAELYILCVfkhhslLEASLSMIRPERLDIPDDALKEYATEIAVQAKAHAAELG 83
Cdd:cd00293     1 KILVAVDGSEESERALEWALELAKRPGAELTLLHV------VDPPPSSSLSGGLEELADELKEEAEELLEEAKKLAEEAG 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2230564695  84 VpadKVRAFVKGGRPSRTIVRFARKRDCDLIVIGAQGTNGDKGLLLGSVSQRVAGSAHCPTLVV 147
Cdd:cd00293    75 V---EVETIVVEGDPAEAILEEAKELGADLIVMGSRGRSGLKRLLLGSVSEYVLRHAPCPVLVV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
5-147 9.45e-30

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: 104.80  E-value: 9.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230564695   5 IMVPVDGSKGAIKALDKAVALQRLTDAELYILCVFKHHSLLEASLsmirpERLDIPDDALKEYATEIAVQAKAHAAELGV 84
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAELILLHVIDPPPSGAASL-----ADESAEEEELELELAEAEALAAAAAAEAGG 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2230564695  85 PadKVRAFVKGGRPSRTIVRFARKRDCDLIVIGAQGTNGDKGLLLGSVSQRVAGSAHCPTLVV 147
Cdd:pfam00582  76 V--KVEVVVVVGDPAEEILEVAEEEDADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVV 136
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
3-147 2.00e-17

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: 73.42  E-value: 2.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230564695   3 KRIMVPVDGSKGAIKALDKAVA-LQRLTDaELYILCVFKHHSLLEASLSMIRPERLDIPDDALKEYATEIAVQAKAHAAE 81
Cdd:cd23659     1 RKVLIAVDGSEESEYALEWALEnLHRPGD-EVVLLHVIEPPSLPAASLGSGSEEWEALEEEAREKAEKLLEKYEKKLKEE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2230564695  82 LGVpadKVRAFVKGGRPSRTIVRFARKRDCDLIVIGAQGTNGDKGLLLGSVSQRVAGSAHCPTLVV 147
Cdd:cd23659    80 KGI---KVKVEVVAGDPGEVICKAAEELKADLIVMGSRGLGALKRTLLGSVSDYVVHHSPCPVLVV 142
USP-A-like cd23657
universal stress protein A and similar proteins; The universal stress protein UspA is a small ...
2-147 1.55e-13

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: 63.09  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230564695   2 FKRIMVPVDGSKGAIKALDKAVALQRLTDAELYILCVFKHHslleaslSMIRPERLDIPDDALKEYATEIAVQAKAHAAE 81
Cdd:cd23657     1 YKHILVAVDLSPESQSLVDKAVEIARENDAKLSLIHVDEDI-------SEYYTGLIDVDIAALQDLESTMLEEALKNLSE 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2230564695  82 L-GVPADKVraFVKGGRPSRTIVRFARKRDCDLIVIgaqGTNGDKGL-LLGSVSQRVAGSAHCPTLVV 147
Cdd:cd23657    74 LaGYPVDHT--FIGYGDLKEEILEVAKKHNVDLIVC---GHHGDFGLsLLGSSARAVLNSAPCDVLIV 136
PRK15005 PRK15005
universal stress protein UspF;
1-147 3.16e-09

universal stress protein UspF;


Pssm-ID: 184967 [Multi-domain]  Cd Length: 144  Bit Score: 52.11  E-value: 3.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230564695   1 MFKRIMVPVDGSKGAI--KALDKAVALQRLTDAELYILCV---FKHHSLLEASLSMIRPERldipdDALKEyatEIAVQA 75
Cdd:PRK15005    1 MNRTILVPIDISDSELtqRVISHVEAEAKIDDAEVHFLTVipsLPYYASLGLAYSAELPAM-----DDLKA---EAKSQL 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2230564695  76 KAHAAELGVPADKVRAFVKGGRPSRTIVRFARKRDCDLIVIgAQGTNGDKGLLLGSVSQRVAGSAHCPTLVV 147
Cdd:PRK15005   73 EEIIKKFKLPTDRVHVHVEEGSPKDRILELAKKIPADMIII-ASHRPDITTYLLGSNAAAVVRHAECSVLVV 143
USP_Rv2623_repeat2 cd23661
universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis ...
5-147 3.55e-09

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: 51.74  E-value: 3.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230564695   5 IMVPVDGSKGAIKALDKAVALQRLTDAELYILCVFKHHSLLEaSLSMIRPERLDIPDDALKEyatEIAVQAKAHaaelgv 84
Cdd:cd23661     2 VVVGVDGSPASELATEIAFDEASRRGVDLVALHAWSDMGPGG-FLGIDWRESEQDQERMLAE---RLAGWQERY------ 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2230564695  85 PADKVRAFVKGGRPSRTIVRFARKrdCDLIVIGAQGTNGDKGLLLGSVSQRVAGSAHCPTLVV 147
Cdd:cd23661    72 PDVHVHKVVVRDRPARVLLEASER--AQLVVVGSHGRGGFAGMLLGSVSRAVLHSAPCPVIVV 132
USP_Rv2623_repeat1 cd23944
universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis ...
5-147 9.48e-08

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: 48.17  E-value: 9.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230564695   5 IMVPVDGSKGAIKALDKAVALQRLTDAELYILCVFKhhSLLEASLSMIRPERLDipdDALKEYATEIAVQAK--AHAAEL 82
Cdd:cd23944     2 IIVGVDGSPASDAAVRWAAREAQLRQIPLTLVHVVP--PVVVSWPEGPRPAEVL---DWQQDEARQVIEQARkvAEEASG 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2230564695  83 GVPADKVRAFVKGGRPSRTIVRFARkrDCDLIVIGAQGTNGDKGLLLGSVSQRVAGSAHCPTLVV 147
Cdd:cd23944    77 EGPPVKVETEIVPGSPVPTLVEASR--DATMVVVGSRGIGALAGLLLGSVSTSLVRHAHCPVAVI 139
USP-E_repeat2 cd23660
Universal stress protein E, repeat 2; UspE is a tandem-type USP that consists of two USP ...
58-146 2.77e-04

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: 38.79  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2230564695  58 DIPDDALKEYATEIAVQA----KAHAAELGVPADKVRafVKGGRPSRTIVRFARKRDCDLIVIGAQGTNGDKGLLLGSVS 133
Cdd:cd23660    55 ELPEFDPTEYVDAIRGRHleamKALRQKFGIDEEQTH--VLEGLPEEVIPDFAEELDADIVVLGTVARTGLSGALIGNTA 132
                          90
                  ....*....|...
gi 2230564695 134 QRVAGSAHCPTLV 146
Cdd:cd23660   133 EHVLDHLNCDLLA 145
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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