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Conserved domains on  [gi|489828367|ref|WP_003732126|]
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BglG family transcription antiterminator LicT [Listeria monocytogenes]

Protein Classification

Bg1G family transcriptional antiterminator( domain architecture ID 1004078)

Bg1G family transcriptional antiterminator similar to Dickeya chrysanthemi beta-glucoside operon antiterminator that mediates the positive regulation of the beta-glucoside (arb) operon by functioning as a transcriptional antiterminator

CATH:  1.10.1790.10
Gene Ontology:  GO:0045893|GO:0003723

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09772 super family cl31605
transcriptional antiterminator BglG; Provisional
 1-274 1.67e-64

transcriptional antiterminator BglG; Provisional


The actual alignment was detected with superfamily member PRK09772:

Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 203.40  E-value: 1.67e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367   1 MRIERILNNNIVSAISEDAQELLILGKGLGFNSKVGDPINESKIEKVFELKDDTMD-KFKMIVNEIPIQFLEVTDDIVKL 79
Cdd:PRK09772   3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNgRLSELLSHIPLEVMATCDRIISL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367  80 FKMKTAKdISDVIYISLSDHLYFATQRLQENVVIENPLSWEVKRFYQEEYAVAKEAAKMVESKLEIELPDAEISNIALHF 159
Cdd:PRK09772  83 AQERLGK-LQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367 160 VNAEVDSDMNDVTHIMQLIQEIISIIKYHFNIEFDEESTNYYRFMTHLKFFCQRVIIGETIDEMDEFLYQTVKKSRGVIF 239
Cdd:PRK09772 162 VSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAW 241

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 489828367 240 DCIDKIGVFLEKNYQFTMSHSEQFYLALHIERLLK 274
Cdd:PRK09772 242 QCAERIAIFIGLQYQRKISPAEIMFLAINIERVRK 276
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-274 1.67e-64

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 203.40  E-value: 1.67e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367   1 MRIERILNNNIVSAISEDAQELLILGKGLGFNSKVGDPINESKIEKVFELKDDTMD-KFKMIVNEIPIQFLEVTDDIVKL 79
Cdd:PRK09772   3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNgRLSELLSHIPLEVMATCDRIISL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367  80 FKMKTAKdISDVIYISLSDHLYFATQRLQENVVIENPLSWEVKRFYQEEYAVAKEAAKMVESKLEIELPDAEISNIALHF 159
Cdd:PRK09772  83 AQERLGK-LQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367 160 VNAEVDSDMNDVTHIMQLIQEIISIIKYHFNIEFDEESTNYYRFMTHLKFFCQRVIIGETIDEMDEFLYQTVKKSRGVIF 239
Cdd:PRK09772 162 VSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAW 241

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 489828367 240 DCIDKIGVFLEKNYQFTMSHSEQFYLALHIERLLK 274
Cdd:PRK09772 242 QCAERIAIFIGLQYQRKISPAEIMFLAINIERVRK 276
BglG COG3711
Transcriptional antiterminator [Transcription];
44-279 6.81e-41

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 149.24  E-value: 6.81e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367  44 IEKVFELKDDTMDKFKMIVNEIPIQFLEVTDDIVKLFKMKTAKDISDVIYISLSDHLYFATQRLQENVVIE--NPLSWEV 121
Cdd:COG3711  153 AELLSELLSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKldNPLLWEI 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367 122 KRfyQEEYAVAKEAAKMVESKLEIELPDAEISNIALHFVNAEVDSDMN----DVTHIMQLIQEIISIIKYHFNIEFDEES 197
Cdd:COG3711  233 KK--PKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNElseiITLEITKLIKEIINIIEEELGIDLDEDS 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367 198 TNYYRFMTHLKFFCQRVIIGETIdemDEFLYQTVKKSRGVIFDCIDKIGVFLEKNYQFTMSHSEQFYLALHIERLLKRKN 277
Cdd:COG3711  311 LLYERLITHLKPAINRLKYGIPI---RNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQK 387


                 ..
gi 489828367 278 NQ 279
Cdd:COG3711  388 ES 389
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-55 2.82e-19

CAT RNA binding domain; This RNA binding domain is found at the amino terminus of transcriptional antitermination proteins such as BglG, SacY and LicT. These proteins control the expression of sugar metabolising operons in Gram+ and Gram- bacteria. This domain has been called the CAT (Co-AntiTerminator) domain. It binds as a dimer.to short Ribonucleotidic Anti-Terminator (RAT) hairpin, each monomer interacting symmetrically with both strands of the RAT hairpin. In the full-length protein, CAT is followed by two phosphorylatable PTS regulation domains that modulate the RNA binding activity of CAT. Upon activation, the dimeric proteins bind to RAT targets in the nascent mRNA, thereby preventing abortive dissociation of the RNA polymerase from the DNA template.


Pssm-ID: 215004  Cd Length: 55  Bit Score: 79.05  E-value: 2.82e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 489828367     1 MRIERILNNNIVSAISEDAQELLILGKGLGFNSKVGDPINESKIEKVFELKDDTM 55
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEED 55
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-55 1.36e-18

CAT RNA binding domain; This RNA binding domain is found at the amino terminus of transcriptional antitermination proteins such as BglG, SacY and LicT. These proteins control the expression of sugar metabolising operons in Gram+ and Gram- bacteria. This domain has been called the CAT (Co-AntiTerminator) domain. It binds as a dimer to short Ribonucleotidic Anti-Terminator (RAT) hairpin, each monomer interacting symmetrically with both strands of the RAT hairpin. In the full-length protein, CAT is followed by two phosphorylatable PTS regulation domains (pfam00874) that modulate the RNA binding activity of CAT. Upon activation, the dimeric proteins bind to RAT targets in the nascent mRNA, thereby preventing abortive dissociation of the RNA polymerase from the DNA template.


Pssm-ID: 460815  Cd Length: 56  Bit Score: 77.47  E-value: 1.36e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489828367    2 RIERILNNNIVSAISEDAQELLILGKGLGFNSKVGDPINESKIEKVFELKDDTM 55
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDEEE 54
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-274 1.67e-64

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 203.40  E-value: 1.67e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367   1 MRIERILNNNIVSAISEDAQELLILGKGLGFNSKVGDPINESKIEKVFELKDDTMD-KFKMIVNEIPIQFLEVTDDIVKL 79
Cdd:PRK09772   3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNgRLSELLSHIPLEVMATCDRIISL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367  80 FKMKTAKdISDVIYISLSDHLYFATQRLQENVVIENPLSWEVKRFYQEEYAVAKEAAKMVESKLEIELPDAEISNIALHF 159
Cdd:PRK09772  83 AQERLGK-LQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367 160 VNAEVDSDMNDVTHIMQLIQEIISIIKYHFNIEFDEESTNYYRFMTHLKFFCQRVIIGETIDEMDEFLYQTVKKSRGVIF 239
Cdd:PRK09772 162 VSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAW 241

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 489828367 240 DCIDKIGVFLEKNYQFTMSHSEQFYLALHIERLLK 274
Cdd:PRK09772 242 QCAERIAIFIGLQYQRKISPAEIMFLAINIERVRK 276
BglG COG3711
Transcriptional antiterminator [Transcription];
44-279 6.81e-41

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 149.24  E-value: 6.81e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367  44 IEKVFELKDDTMDKFKMIVNEIPIQFLEVTDDIVKLFKMKTAKDISDVIYISLSDHLYFATQRLQENVVIE--NPLSWEV 121
Cdd:COG3711  153 AELLSELLSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKldNPLLWEI 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367 122 KRfyQEEYAVAKEAAKMVESKLEIELPDAEISNIALHFVNAEVDSDMN----DVTHIMQLIQEIISIIKYHFNIEFDEES 197
Cdd:COG3711  233 KK--PKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNElseiITLEITKLIKEIINIIEEELGIDLDEDS 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367 198 TNYYRFMTHLKFFCQRVIIGETIdemDEFLYQTVKKSRGVIFDCIDKIGVFLEKNYQFTMSHSEQFYLALHIERLLKRKN 277
Cdd:COG3711  311 LLYERLITHLKPAINRLKYGIPI---RNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQK 387


                 ..
gi 489828367 278 NQ 279
Cdd:COG3711  388 ES 389
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-55 2.82e-19

CAT RNA binding domain; This RNA binding domain is found at the amino terminus of transcriptional antitermination proteins such as BglG, SacY and LicT. These proteins control the expression of sugar metabolising operons in Gram+ and Gram- bacteria. This domain has been called the CAT (Co-AntiTerminator) domain. It binds as a dimer.to short Ribonucleotidic Anti-Terminator (RAT) hairpin, each monomer interacting symmetrically with both strands of the RAT hairpin. In the full-length protein, CAT is followed by two phosphorylatable PTS regulation domains that modulate the RNA binding activity of CAT. Upon activation, the dimeric proteins bind to RAT targets in the nascent mRNA, thereby preventing abortive dissociation of the RNA polymerase from the DNA template.


Pssm-ID: 215004  Cd Length: 55  Bit Score: 79.05  E-value: 2.82e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 489828367     1 MRIERILNNNIVSAISEDAQELLILGKGLGFNSKVGDPINESKIEKVFELKDDTM 55
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFVLKDEED 55
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-55 1.36e-18

CAT RNA binding domain; This RNA binding domain is found at the amino terminus of transcriptional antitermination proteins such as BglG, SacY and LicT. These proteins control the expression of sugar metabolising operons in Gram+ and Gram- bacteria. This domain has been called the CAT (Co-AntiTerminator) domain. It binds as a dimer to short Ribonucleotidic Anti-Terminator (RAT) hairpin, each monomer interacting symmetrically with both strands of the RAT hairpin. In the full-length protein, CAT is followed by two phosphorylatable PTS regulation domains (pfam00874) that modulate the RNA binding activity of CAT. Upon activation, the dimeric proteins bind to RAT targets in the nascent mRNA, thereby preventing abortive dissociation of the RNA polymerase from the DNA template.


Pssm-ID: 460815  Cd Length: 56  Bit Score: 77.47  E-value: 1.36e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489828367    2 RIERILNNNIVSAISEDAQELLILGKGLGFNSKVGDPINESKIEKVFELKDDTM 55
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFVLKDEEE 54
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 75-162 7.64e-18

PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory domain found in bacterial transcriptional antiterminator such as BglG, SacY and LicT, as well as in activators such as MtlR and LevR. The PRD is phosphorylated on one or two conserved histidine residues. PRD-containing proteins are involved in the regulation of catabolic operons in Gram+ and Gram- bacteria and are often characterized by a short N-terminal effector domain that binds to either RNA (CAT-RBD for antiterminators pfam03123) or DNA (for activators), and a duplicated PRD module which is phosphorylated by the sugar phosphotransferase system (PTS) in response to the availability of carbon source. The phosphorylations modify the conformation and stability of the dimeric proteins and thereby the RNA- or DNA-binding activity of the effector domain. The structure of the LicT PRD domains has been solved in both the active (pdb:1h99) and inactive state (pdb:1tlv), revealing massive structural rearrangements upon activation.


Pssm-ID: 459973 [Multi-domain]  Cd Length: 90  Bit Score: 76.52  E-value: 7.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367   75 DIVKLFKMKTAKDI-SDVIYISLSDHLYFATQRLQENVVIENPLSWEVKRFYQEEYAVAKEAAKMVESKLEIELPDAEIS 153
Cdd:pfam00874   2 EIIELIEKKLGITFdDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIG 81


                  ....*....
gi 489828367  154 NIALHFVNA 162
Cdd:pfam00874  82 YIALHFLSA 90
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 179-272 2.90e-13

PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory domain found in bacterial transcriptional antiterminator such as BglG, SacY and LicT, as well as in activators such as MtlR and LevR. The PRD is phosphorylated on one or two conserved histidine residues. PRD-containing proteins are involved in the regulation of catabolic operons in Gram+ and Gram- bacteria and are often characterized by a short N-terminal effector domain that binds to either RNA (CAT-RBD for antiterminators pfam03123) or DNA (for activators), and a duplicated PRD module which is phosphorylated by the sugar phosphotransferase system (PTS) in response to the availability of carbon source. The phosphorylations modify the conformation and stability of the dimeric proteins and thereby the RNA- or DNA-binding activity of the effector domain. The structure of the LicT PRD domains has been solved in both the active (pdb:1h99) and inactive state (pdb:1tlv), revealing massive structural rearrangements upon activation.


Pssm-ID: 459973 [Multi-domain]  Cd Length: 90  Bit Score: 64.20  E-value: 2.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367  179 QEIISIIKYHFNIEFDEEStNYYRFMTHLKFFCQRVIIGETIDEmdeFLYQTVKKSRGVIFDCIDKIGVFLEKNYQFTMS 258
Cdd:pfam00874   1 EEIIELIEKKLGITFDDDI-LYIRLILHLAFAIERIKEGITIEN---PLLEEIKEKYPKEFEIAKKILEILEEELGIELP 76

                          90
                  ....*....|....
gi 489828367  259 HSEQFYLALHIERL 272
Cdd:pfam00874  77 EDEIGYIALHFLSA 90
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
39-171 5.18e-11

Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 62.83  E-value: 5.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367  39 INESKIEKVFELKDDTMDKFKM-----------IVNEIPIQFLEVTDDIVKLFKMKTAKDISDVIYISLSDHLYFATQRL 107
Cdd:COG3933  416 IDEEEINIIIEIDIDVHLLKFIyddnknfnkeeLAKIVDEDIINVVEEILELAEKKLGRKFSENFIYALSLHLSSFIERI 495

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489828367 108 QENVVIENPLSWEVKRFYQEEYAVAKEAAKMVESKLEIELPDAEISNIALHFVNAEVDSDMNDV 171
Cdd:COG3933  496 KEGKEIINPNLNEIKKKYPKEFKVAKEIKELIEQELDIEIPEDEVGFLTLFLVSLNENNESGKV 559
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 4-174 3.37e-04

Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];


Pssm-ID: 440834 [Multi-domain]  Cd Length: 835  Bit Score: 42.02  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367   4 ERILNNNIVSAISEDAQELlilgKGLGFNSKVGDPINESKIEKVFE---LKDDTMDKFKMIVNEIPIQFLEVTDDIVKLF 80
Cdd:COG1221  406 EYELPYNFYEIIEDKYEEL----KSEGLSEEEINKIISKDIESYFKkliFKLDKSNISEELLLIVVDEVIVNVVEIFEEA 481

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489828367  81 KMKTAKDISDVIYISLSDHLYFATQRLQENVVIENPLSWEVKRFYQEEYAVAKEAAKMVESKLEIELPDAEISNIALHFV 160
Cdd:COG1221  482 EKKLLRYNSSNLFIALSLHLLSTLLRIKKGKKIINPQLNEIKKKYYEEFILAAEAIKIIEEELKILIPDEEEGFILLLLI 561

                        170
                 ....*....|....
gi 489828367 161 NAEVDSDMNDVTHI 174
Cdd:COG1221  562 ELKEEKSLSENVIV 575
 
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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