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Conserved domains on  [gi|779968003|ref|WP_045414935|]
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MULTISPECIES: universal stress protein UspF [Enterobacter cloacae complex]

Protein Classification

adenine nucleotide alpha hydrolase family protein( domain architecture ID 188)

AANH (adenine nucleotide alpha hydrolase) family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AANH_superfamily super family cl00292
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ...
 1-144 1.14e-81

Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


The actual alignment was detected with superfamily member PRK15005:

Pssm-ID: 469708 [Multi-domain]  Cd Length: 144  Bit Score: 236.62  E-value: 1.14e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003   1 MYNSILVPIDISEDSLTHMVIPFVQAHTALNTAKVHFLTVIPSLPYYSSLGLAYPAEMPKMKEFQHAALARLDEIVKQFK 80
Cdd:PRK15005   1 MNRTILVPIDISDSELTQRVISHVEAEAKIDDAEVHFLTVIPSLPYYASLGLAYSAELPAMDDLKAEAKSQLEEIIKKFK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 779968003  81 IPADKIQTHAVTGSPKDQILKLADTIGADLIIIASHKPDISTYLLGSNAAAVVRHAKCPVLVVR 144
Cdd:PRK15005  81 LPTDRVHVHVEEGSPKDRILELAKKIPADMIIIASHRPDITTYLLGSNAAAVVRHAECSVLVVR 144
 
Name Accession Description Interval E-value
PRK15005 PRK15005
universal stress protein UspF;
1-144 1.14e-81

universal stress protein UspF;


Pssm-ID: 184967 [Multi-domain]  Cd Length: 144  Bit Score: 236.62  E-value: 1.14e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003   1 MYNSILVPIDISEDSLTHMVIPFVQAHTALNTAKVHFLTVIPSLPYYSSLGLAYPAEMPKMKEFQHAALARLDEIVKQFK 80
Cdd:PRK15005   1 MNRTILVPIDISDSELTQRVISHVEAEAKIDDAEVHFLTVIPSLPYYASLGLAYSAELPAMDDLKAEAKSQLEEIIKKFK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 779968003  81 IPADKIQTHAVTGSPKDQILKLADTIGADLIIIASHKPDISTYLLGSNAAAVVRHAKCPVLVVR 144
Cdd:PRK15005  81 LPTDRVHVHVEEGSPKDRILELAKKIPADMIIIASHRPDITTYLLGSNAAAVVRHAECSVLVVR 144
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
1-143 1.13e-32

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 112.32  E-value: 1.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003   1 MYNSILVPIDISEDSltHMVIPFVQAHTALNTAKVHFLTVIPSLPYYSSLGLAYPAEMpkmkefQHAALARLDEIVKQFK 80
Cdd:COG0589    1 MYKRILVPTDGSEEA--ERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEELEEEL------REEAEEALEEAAERLE 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 779968003  81 IPADKIQTHAVTGSPKDQILKLADTIGADLIIIASH-KPDISTYLLGSNAAAVVRHAKCPVLVV 143
Cdd:COG0589   73 EAGVEVETVVREGDPAEAILEAAEELDADLIVMGSRgRSGLRRLLLGSVAERVLRHAPCPVLVV 136
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
 5-143 8.59e-28

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: 99.73  E-value: 8.59e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003   5 ILVPIDISEDSltHMVIPFVQAHTALNTAKVHFLTVIPSLPYYSSLGLAYPAEmpkmKEFQHAALARLDEIVKQFKIPAD 84
Cdd:cd00293    2 ILVAVDGSEES--ERALEWALELAKRPGAELTLLHVVDPPPSSSLSGGLEELA----DELKEEAEELLEEAKKLAEEAGV 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003  85 KIQTHAVTGSPKDQILKLADTIGADLIIIASHKPD-ISTYLLGSNAAAVVRHAKCPVLVV 143
Cdd:cd00293   76 EVETIVVEGDPAEAILEEAKELGADLIVMGSRGRSgLKRLLLGSVSEYVLRHAPCPVLVV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 5-144 4.05e-24

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: 90.54  E-value: 4.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003    5 ILVPIDISEDSLThmVIPFVQAHTALNTAKVHFLTVIPSLPYYSSLGLAYPAEmpKMKEFQHAALARLDEIVKQFKIPAD 84
Cdd:pfam00582   1 ILVAVDGSEESKR--ALEWAAELAKARGAELILLHVIDPPPSGAASLADESAE--EEELELELAEAEALAAAAAAEAGGV 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 779968003   85 KIQTHAVTGSPKDQILKLADTIGADLIIIASHKPD-ISTYLLGSNAAAVVRHAKCPVLVVR 144
Cdd:pfam00582  77 KVEVVVVVGDPAEEILEVAEEEDADLIVMGSRGRSgLSRLLLGSVAEYVLRHAPCPVLVVR 137
 
Name Accession Description Interval E-value
PRK15005 PRK15005
universal stress protein UspF;
1-144 1.14e-81

universal stress protein UspF;


Pssm-ID: 184967 [Multi-domain]  Cd Length: 144  Bit Score: 236.62  E-value: 1.14e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003   1 MYNSILVPIDISEDSLTHMVIPFVQAHTALNTAKVHFLTVIPSLPYYSSLGLAYPAEMPKMKEFQHAALARLDEIVKQFK 80
Cdd:PRK15005   1 MNRTILVPIDISDSELTQRVISHVEAEAKIDDAEVHFLTVIPSLPYYASLGLAYSAELPAMDDLKAEAKSQLEEIIKKFK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 779968003  81 IPADKIQTHAVTGSPKDQILKLADTIGADLIIIASHKPDISTYLLGSNAAAVVRHAKCPVLVVR 144
Cdd:PRK15005  81 LPTDRVHVHVEEGSPKDRILELAKKIPADMIIIASHRPDITTYLLGSNAAAVVRHAECSVLVVR 144
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
1-143 1.13e-32

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 112.32  E-value: 1.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003   1 MYNSILVPIDISEDSltHMVIPFVQAHTALNTAKVHFLTVIPSLPYYSSLGLAYPAEMpkmkefQHAALARLDEIVKQFK 80
Cdd:COG0589    1 MYKRILVPTDGSEEA--ERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEELEEEL------REEAEEALEEAAERLE 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 779968003  81 IPADKIQTHAVTGSPKDQILKLADTIGADLIIIASH-KPDISTYLLGSNAAAVVRHAKCPVLVV 143
Cdd:COG0589   73 EAGVEVETVVREGDPAEAILEAAEELDADLIVMGSRgRSGLRRLLLGSVAERVLRHAPCPVLVV 136
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
 5-143 8.59e-28

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: 99.73  E-value: 8.59e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003   5 ILVPIDISEDSltHMVIPFVQAHTALNTAKVHFLTVIPSLPYYSSLGLAYPAEmpkmKEFQHAALARLDEIVKQFKIPAD 84
Cdd:cd00293    2 ILVAVDGSEES--ERALEWALELAKRPGAELTLLHVVDPPPSSSLSGGLEELA----DELKEEAEELLEEAKKLAEEAGV 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003  85 KIQTHAVTGSPKDQILKLADTIGADLIIIASHKPD-ISTYLLGSNAAAVVRHAKCPVLVV 143
Cdd:cd00293   76 EVETIVVEGDPAEAILEEAKELGADLIVMGSRGRSgLKRLLLGSVSEYVLRHAPCPVLVV 135
PRK15456 PRK15456
universal stress protein UspG; Provisional
 1-144 1.51e-26

universal stress protein UspG; Provisional


Pssm-ID: 185353  Cd Length: 142  Bit Score: 96.93  E-value: 1.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003   1 MYNSILVPIDISEDSLTHMVIPFVQaHTALNTAKVHFLTVipsLPYYSSLGLA-YPAEMPKMKE-FQHAALARLDEIVKQ 78
Cdd:PRK15456   1 MYKTIIMPVDVFEMELSDKAVRHAE-FLAQDDGVIHLLHV---LPGSASLSLHrFAADVRRFEEhLQHEAEERLQTMVSH 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779968003  79 FKIPADKIQTHAVTGSPKDQILKLADTIGADLIIIASHKPDISTYLLGSNAAAVVRHAKCPVLVVR 144
Cdd:PRK15456  77 FTIDPSRIKQHVRFGSVRDEVNELAEELGADVVVIGSRNPSISTHLLGSNASSVIRHANLPVLVVR 142
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 5-144 4.05e-24

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: 90.54  E-value: 4.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003    5 ILVPIDISEDSLThmVIPFVQAHTALNTAKVHFLTVIPSLPYYSSLGLAYPAEmpKMKEFQHAALARLDEIVKQFKIPAD 84
Cdd:pfam00582   1 ILVAVDGSEESKR--ALEWAAELAKARGAELILLHVIDPPPSGAASLADESAE--EEELELELAEAEALAAAAAAEAGGV 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 779968003   85 KIQTHAVTGSPKDQILKLADTIGADLIIIASHKPD-ISTYLLGSNAAAVVRHAKCPVLVVR 144
Cdd:pfam00582  77 KVEVVVVVGDPAEEILEVAEEEDADLIVMGSRGRSgLSRLLLGSVAEYVLRHAPCPVLVVR 137
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
 5-144 6.15e-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: 72.27  E-value: 6.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003   5 ILVPIDISEDS-------LTHMVIPfvqahtalnTAKVHFLTVIPSLPYYSSLGLAYPAEMPKM-KEFQHAALARLDEIV 76
Cdd:cd23659    3 VLIAVDGSEESeyalewaLENLHRP---------GDEVVLLHVIEPPSLPAASLGSGSEEWEALeEEAREKAEKLLEKYE 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003  77 KQFKIPAD-KIQTHAVTGSPKDQILKLADTIGADLIIIASH-KPDISTYLLGSNAAAVVRHAKCPVLVVR 144
Cdd:cd23659   74 KKLKEEKGiKVKVEVVAGDPGEVICKAAEELKADLIVMGSRgLGALKRTLLGSVSDYVVHHSPCPVLVVR 143
USP-A-like cd23657
universal stress protein A and similar proteins; The universal stress protein UspA is a small ...
 2-144 1.07e-09

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: 53.08  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003   2 YNSILVPIDISEDSltHMVIPFVQAHTALNTAKVHFLTVIPSLPYYsslglAYPAEMPKMKEFQHAALARLDEIVKQFK- 80
Cdd:cd23657    1 YKHILVAVDLSPES--QSLVDKAVEIARENDAKLSLIHVDEDISEY-----YTGLIDVDIAALQDLESTMLEEALKNLSe 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 779968003  81 -IPADKIQTHAVTGSPKDQILKLADTIGADLIIIASHKPDISTyLLGSNAAAVVRHAKCPVLVVR 144
Cdd:cd23657   74 lAGYPVDHTFIGYGDLKEEILEVAKKHNVDLIVCGHHGDFGLS-LLGSSARAVLNSAPCDVLIVP 137
USP-E_repeat2 cd23660
Universal stress protein E, repeat 2; UspE is a tandem-type USP that consists of two USP ...
 5-142 5.06e-07

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: 46.11  E-value: 5.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003   5 ILVPIDISE-----DSLTHMVIPFVQAHTALNTAKVHFLTVIPSLP--YYSSLGLAYPAEMPKMKEFQHaaLARLDEIVK 77
Cdd:cd23660    4 ILVAVDPSNeeeyhEDLNLRLIELAYSLAAQLKAELHLVSAWPVTPenIAIELPEFDPTEYVDAIRGRH--LEAMKALRQ 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779968003  78 QFKIPADkiQTHAVTGSPKDQILKLADTIGADLIIIAS-HKPDISTYLLGSNAAAVVRHAKCPVLV 142
Cdd:cd23660   82 KFGIDEE--QTHVLEGLPEEVIPDFAEELDADIVVLGTvARTGLSGALIGNTAEHVLDHLNCDLLA 145
USP_Rv2623_repeat2 cd23661
universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis ...
 78-144 6.21e-06

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: 42.88  E-value: 6.21e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 779968003  78 QFKIPADKIQTHAVTGSPKDQILKLADTigADLIIIASH-KPDISTYLLGSNAAAVVRHAKCPVLVVR 144
Cdd:cd23661   68 QERYPDVHVHKVVVRDRPARVLLEASER--AQLVVVGSHgRGGFAGMLLGSVSRAVLHSAPCPVIVVR 133
PRK11175 PRK11175
universal stress protein UspE; Provisional
 4-144 5.69e-04

universal stress protein UspE; Provisional


Pssm-ID: 236871 [Multi-domain]  Cd Length: 305  Bit Score: 38.71  E-value: 5.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003   4 SILVPIDI-SEDSlthmvipfvqAHTALNTAKVHFLTVIPSLPYYSSLGL--AYPA-------EMPkmkEF--------- 64
Cdd:PRK11175 154 KILVAVNVaSEEP----------YHDALNEKLVEEAIDLAEQLNHAEVHLvnAYPVtpiniaiELP---EFdpsvyndai 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003  65 --QHaaLARLDEIVKQFKIPADkiQTHAVTGSPKDQILKLADTIGADLIIIAS-HKPDISTYLLGSNAAAVVRHAKCPVL 141
Cdd:PRK11175 221 rgQH--LLAMKALRQKFGIDEE--QTHVEEGLPEEVIPDLAEHLDAELVILGTvGRTGLSAAFLGNTAEHVIDHLNCDLL 296


                 ...
gi 779968003 142 VVR 144
Cdd:PRK11175 297 AIK 299
USP_Rv2623_repeat1 cd23944
universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis ...
 82-144 7.00e-04

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: 37.38  E-value: 7.00e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 779968003  82 PADKIQTHAVTGSPKDQILKLADtiGADLIIIASH-KPDISTYLLGSNAAAVVRHAKCPVLVVR 144
Cdd:cd23944   79 PPVKVETEIVPGSPVPTLVEASR--DATMVVVGSRgIGALAGLLLGSVSTSLVRHAHCPVAVIH 140
USP_NhaS5_C cd01988
C-terminal USP domain(s) of Na(+)/H(+) antiporter NhaS5 and similar proteins; Na(+)/H(+) ...
 66-144 1.26e-03

C-terminal USP domain(s) of Na(+)/H(+) antiporter NhaS5 and similar proteins; Na(+)/H(+) exchange proteins eject protons from cells, effectively eliminating excess acid from actively metabolizing cells. Na(+)/H(+) exchange activity is also crucial for the regulation of cell volume, and for the reabsorption of NaCl across renal, intestinal, and other epithelia. These antiporters exchange Na(+) for H(+) in an electroneutral manner, and this activity is carried out by a family of Na(+)/H(+) exchangers, or NHEs, which are known to be present in both prokaryotic and eukaryotic cells. These exchangers are highly-regulated (glyco)phosphoproteins, which, based on their primary structure, appear to contain 10-12 membrane-spanning regions (M) at the N-terminus and a large cytoplasmic region at the C-terminus. The transmembrane regions M3-M12 share identity with other members of the family. The M6 and M7 regions are highly conserved. This is thought to be the region that is involved in the transport of sodium and hydrogen ions. The C-terminal region contains one or two domains that show homology with universal stress protein (USP), 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: 467492  Cd Length: 125  Bit Score: 36.71  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779968003  66 HAALARLDEIVKQFKiPADKIQTHAVTGS-PKDQILKLADTIgADLIIIASHKPDISTYLLGSNAAAVVRHAKCPVLVVR 144
Cdd:cd01988   48 EQAEQRFEELMELLN-GVNVHPIVRISHSvAARVTAREAKSF-ADLIVMGWRRTFLGNVLLGSTIDKVLMKAPTDVAVTR 125
 
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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