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Conserved domains on  [gi|488218259|ref|WP_002289467|]
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MULTISPECIES: universal stress protein [Enterococcus]

Protein Classification

universal stress protein( domain architecture ID 10456834)

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

CATH:  3.40.50.620
Gene Ontology:  GO:0005524

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];
4-145 1.33e-36

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


:

Pssm-ID: 440354  Cd Length: 136  Bit Score: 122.34  E-value: 1.33e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259   4 TYRNILVAIDGSEKAEKAFLEAITIAKRNQATLHILYVNEVTgnyfGDFAFVTTSLQEELDEVAENQMKEHRNLAIEKGL 83
Cdd:COG0589    1 MYKRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPP----PSAAAGPEELEEELREEAEEALEEAAERLEEAGV 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488218259  84 tDIETYVLYGYPKTLIANFhESKEPIDLIVMGATGLNAVERALVGSTTSYVVNHASCNVMVV 145
Cdd:COG0589   77 -EVETVVREGDPAEAILEA-AEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
 
Name Accession Description Interval E-value
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
4-145 1.33e-36

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 122.34  E-value: 1.33e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259   4 TYRNILVAIDGSEKAEKAFLEAITIAKRNQATLHILYVNEVTgnyfGDFAFVTTSLQEELDEVAENQMKEHRNLAIEKGL 83
Cdd:COG0589    1 MYKRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPP----PSAAAGPEELEEELREEAEEALEEAAERLEEAGV 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488218259  84 tDIETYVLYGYPKTLIANFhESKEPIDLIVMGATGLNAVERALVGSTTSYVVNHASCNVMVV 145
Cdd:COG0589   77 -EVETVVREGDPAEAILEA-AEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
7-145 3.10e-33

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: 113.60  E-value: 3.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259   7 NILVAIDGSEKAEKAFLEAITIAKRNQATLHILYVNEVTgnYFGDFAFVTTSLQEELDEVAENQMKEHRNLAIEKGLtDI 86
Cdd:cd00293    1 KILVAVDGSEESERALEWALELAKRPGAELTLLHVVDPP--PSSSLSGGLEELADELKEEAEELLEEAKKLAEEAGV-EV 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488218259  87 ETYVLYGYPKTLIANfHESKEPIDLIVMGATGLNAVERALVGSTTSYVVNHASCNVMVV 145
Cdd:cd00293   78 ETIVVEGDPAEAILE-EAKELGADLIVMGSRGRSGLKRLLLGSVSEYVLRHAPCPVLVV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
8-146 4.00e-33

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: 113.66  E-value: 4.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259    8 ILVAIDGSEKAEKAFLEAITIAKRNQATLHILYVNEVTGNYFGDFAFVTTSLQEELDEVAENQmKEHRNLAIEKGLTDIE 87
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAELILLHVIDPPPSGAASLADESAEEEELELELAEAE-ALAAAAAAEAGGVKVE 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488218259   88 TYVLYGYPKTLIANFHESKEpIDLIVMGATGLNAVERALVGSTTSYVVNHASCNVMVVK 146
Cdd:pfam00582  80 VVVVVGDPAEEILEVAEEED-ADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
PRK15005 PRK15005
universal stress protein UspF;
5-146 1.43e-06

universal stress protein UspF;


Pssm-ID: 184967 [Multi-domain]  Cd Length: 144  Bit Score: 44.79  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259   5 YRNILVAIDGSEK--AEKAFLEAITIAKRNQATLHILYVNEvTGNYFGDFAFVTTS---LQEELDEVAENQMKE---HRN 76
Cdd:PRK15005   2 NRTILVPIDISDSelTQRVISHVEAEAKIDDAEVHFLTVIP-SLPYYASLGLAYSAelpAMDDLKAEAKSQLEEiikKFK 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259  77 LAIEKgltdIETYVLYGYPKTLIANFHEsKEPIDLIVMgATGLNAVERALVGSTTSYVVNHASCNVMVVK 146
Cdd:PRK15005  81 LPTDR----VHVHVEEGSPKDRILELAK-KIPADMIII-ASHRPDITTYLLGSNAAAVVRHAECSVLVVR 144
 
Name Accession Description Interval E-value
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
4-145 1.33e-36

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 122.34  E-value: 1.33e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259   4 TYRNILVAIDGSEKAEKAFLEAITIAKRNQATLHILYVNEVTgnyfGDFAFVTTSLQEELDEVAENQMKEHRNLAIEKGL 83
Cdd:COG0589    1 MYKRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPP----PSAAAGPEELEEELREEAEEALEEAAERLEEAGV 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488218259  84 tDIETYVLYGYPKTLIANFhESKEPIDLIVMGATGLNAVERALVGSTTSYVVNHASCNVMVV 145
Cdd:COG0589   77 -EVETVVREGDPAEAILEA-AEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
7-145 3.10e-33

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: 113.60  E-value: 3.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259   7 NILVAIDGSEKAEKAFLEAITIAKRNQATLHILYVNEVTgnYFGDFAFVTTSLQEELDEVAENQMKEHRNLAIEKGLtDI 86
Cdd:cd00293    1 KILVAVDGSEESERALEWALELAKRPGAELTLLHVVDPP--PSSSLSGGLEELADELKEEAEELLEEAKKLAEEAGV-EV 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488218259  87 ETYVLYGYPKTLIANfHESKEPIDLIVMGATGLNAVERALVGSTTSYVVNHASCNVMVV 145
Cdd:cd00293   78 ETIVVEGDPAEAILE-EAKELGADLIVMGSRGRSGLKRLLLGSVSEYVLRHAPCPVLVV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
8-146 4.00e-33

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: 113.66  E-value: 4.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259    8 ILVAIDGSEKAEKAFLEAITIAKRNQATLHILYVNEVTGNYFGDFAFVTTSLQEELDEVAENQmKEHRNLAIEKGLTDIE 87
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAELILLHVIDPPPSGAASLADESAEEEELELELAEAE-ALAAAAAAEAGGVKVE 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488218259   88 TYVLYGYPKTLIANFHESKEpIDLIVMGATGLNAVERALVGSTTSYVVNHASCNVMVVK 146
Cdd:pfam00582  80 VVVVVGDPAEEILEVAEEED-ADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
6-146 2.97e-26

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: 96.15  E-value: 2.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259   6 RNILVAIDGSEKAEKAFLEAITIAKRNQATLHILYVNE---VTGNYFGDFAFVTTSLQEELDEVAENQMKEHRNLAIEKG 82
Cdd:cd23659    1 RKVLIAVDGSEESEYALEWALENLHRPGDEVVLLHVIEppsLPAASLGSGSEEWEALEEEAREKAEKLLEKYEKKLKEEK 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488218259  83 LTDIETYVLYGYPKTLIANFHEsKEPIDLIVMGATGLNAVERALVGSTTSYVVNHASCNVMVVK 146
Cdd:cd23659   81 GIKVKVEVVAGDPGEVICKAAE-ELKADLIVMGSRGLGALKRTLLGSVSDYVVHHSPCPVLVVR 143
USP-E_repeat2 cd23660
Universal stress protein E, repeat 2; UspE is a tandem-type USP that consists of two USP ...
5-146 2.31e-14

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: 65.75  E-value: 2.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259   5 YRNILVAID-GSEKAEKAFL------EAITIAKRNQATLHILYVNEVTgnyfgdFAFVTTSLQEELDEVAENQMKEH--- 74
Cdd:cd23660    1 GGRILVAVDpSNEEEYHEDLnlrlieLAYSLAAQLKAELHLVSAWPVT------PENIAIELPEFDPTEYVDAIRGRhle 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488218259  75 --RNLAIEKGLTDIETYVLYGYPKTLIANFHEsKEPIDLIVMGATGLNAVERALVGSTTSYVVNHASCNVMVVK 146
Cdd:cd23660   75 amKALRQKFGIDEEQTHVLEGLPEEVIPDFAE-ELDADIVVLGTVARTGLSGALIGNTAEHVLDHLNCDLLALK 147
USP-A-like cd23657
universal stress protein A and similar proteins; The universal stress protein UspA is a small ...
5-146 1.07e-12

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: 61.17  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259   5 YRNILVAIDGSEKAEKAFLEAITIAKRNQATLHILYVNEVTGNYFGDFAFVTTSLQEELDEVAENQMKehRNLAIEKGLT 84
Cdd:cd23657    1 YKHILVAVDLSPESQSLVDKAVEIARENDAKLSLIHVDEDISEYYTGLIDVDIAALQDLESTMLEEAL--KNLSELAGYP 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488218259  85 DIETYVLYGYPKTLIANFHEsKEPIDLIVMGATGLNAVerALVGSTTSYVVNHASCNVMVVK 146
Cdd:cd23657   79 VDHTFIGYGDLKEEILEVAK-KHNVDLIVCGHHGDFGL--SLLGSSARAVLNSAPCDVLIVP 137
USP_Rv2623_repeat1 cd23944
universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis ...
8-145 6.72e-12

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: 58.95  E-value: 6.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259   8 ILVAIDGSEKAEKAFLEAITIAKRNQATL---HILYVNEVTGNYFGDFAFVTTSLQEELDEVAENQMKEHRNLAIEKGLT 84
Cdd:cd23944    2 IIVGVDGSPASDAAVRWAAREAQLRQIPLtlvHVVPPVVVSWPEGPRPAEVLDWQQDEARQVIEQARKVAEEASGEGPPV 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488218259  85 DIETYVLYGYP-KTLIanfhESKEPIDLIVMGATGLNAVERALVGSTTSYVVNHASCNVMVV 145
Cdd:cd23944   82 KVETEIVPGSPvPTLV----EASRDATMVVVGSRGIGALAGLLLGSVSTSLVRHAHCPVAVI 139
PRK15005 PRK15005
universal stress protein UspF;
5-146 1.43e-06

universal stress protein UspF;


Pssm-ID: 184967 [Multi-domain]  Cd Length: 144  Bit Score: 44.79  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259   5 YRNILVAIDGSEK--AEKAFLEAITIAKRNQATLHILYVNEvTGNYFGDFAFVTTS---LQEELDEVAENQMKE---HRN 76
Cdd:PRK15005   2 NRTILVPIDISDSelTQRVISHVEAEAKIDDAEVHFLTVIP-SLPYYASLGLAYSAelpAMDDLKAEAKSQLEEiikKFK 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259  77 LAIEKgltdIETYVLYGYPKTLIANFHEsKEPIDLIVMgATGLNAVERALVGSTTSYVVNHASCNVMVVK 146
Cdd:PRK15005  81 LPTDR----VHVHVEEGSPKDRILELAK-KIPADMIII-ASHRPDITTYLLGSNAAAVVRHAECSVLVVR 144
USP_Rv2623_repeat2 cd23661
universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis ...
8-146 7.84e-05

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: 40.19  E-value: 7.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259   8 ILVAIDGSEKAEKAFLEAITIAKRNQATLHILYvnevTGNYFGDFAFVT----TSLQEELDEVAEN---QMKEHRNLAIE 80
Cdd:cd23661    2 VVVGVDGSPASELATEIAFDEASRRGVDLVALH----AWSDMGPGGFLGidwrESEQDQERMLAERlagWQERYPDVHVH 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488218259  81 KgltdietYVLYGYPKTLIAnfhESKEPIDLIVMGATGLNAVERALVGSTTSYVVNHASCNVMVVK 146
Cdd:cd23661   78 K-------VVVRDRPARVLL---EASERAQLVVVGSHGRGGFAGMLLGSVSRAVLHSAPCPVIVVR 133
PRK11175 PRK11175
universal stress protein UspE; Provisional
6-146 1.28e-03

universal stress protein UspE; Provisional


Pssm-ID: 236871 [Multi-domain]  Cd Length: 305  Bit Score: 37.55  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259   6 RNILVAID-GSEKAEKAFL------EAITIAKR-NQATLHIlyVNevtgnyfgdfAFVTT--SLQEELDEVA-------- 67
Cdd:PRK11175 153 GKILVAVNvASEEPYHDALneklveEAIDLAEQlNHAEVHL--VN----------AYPVTpiNIAIELPEFDpsvyndai 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259  68 ----ENQMKEHRNlaiEKGLTDIETYVLYGYPKTLIAnfhESKEPID--LIVMGA---TGLNAverALVGSTTSYVVNHA 138
Cdd:PRK11175 221 rgqhLLAMKALRQ---KFGIDEEQTHVEEGLPEEVIP---DLAEHLDaeLVILGTvgrTGLSA---AFLGNTAEHVIDHL 291

                 ....*...
gi 488218259 139 SCNVMVVK 146
Cdd:PRK11175 292 NCDLLAIK 299
USP_KdpD-like cd01987
USP domain of the osmosensitive K+ channel histidine kinase family; The KdpDE two component ...
8-139 4.09e-03

USP domain of the osmosensitive K+ channel histidine kinase family; The KdpDE two component system is widespread in bacteria and archaea; it controls potassium homeostasis and virulence by regulating the transcription of multiple genes, including a kdpFABC operon, which encodes a high-affinity P-type ATPase transporter. The KdpD histidine kinase (HK, EC:2.7.13.3) contain an N-terminal sensory cytoplasmic region (NTR) composed of KdpD' and universal stress protein (USP) domains, a canonical transmembrane domain, and a cytoplasmic C-terminal region with a transmitter GAF domain and an EnvZ-like catalytic HK domain. Proteins containing the USP domain are induced by many environmental stressors such as nutrient starvation, drought, extreme temperatures, high salinity, and the presence of uncouplers, antibiotics, and metals. It enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity.


Pssm-ID: 467491 [Multi-domain]  Cd Length: 124  Bit Score: 35.30  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488218259   8 ILVAIDGSEKAEKAFLEAITIAKRNQATLHILYvnevtgnyfgdfafVTTSLQEELDEVAENQMKEHRNLAIEKGltdIE 87
Cdd:cd01987    2 ILVCISSSPTSEKLIRRAARLAERLNGELTAVY--------------VETPEESRLDEESQRRLLTNLKLAEELG---AE 64
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488218259  88 TYVLYG--YPKTLIAnFHESKEpIDLIVMGATGLNAVERALVGSTTSYVVNHAS 139
Cdd:cd01987   65 VVSVEGddVAEAIVE-FARERN-VTQIVLGQSRRRRWRRLFKGSLVDRLLREAP 116
 
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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