NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|757520552|ref|WP_042783774|]
View 

MULTISPECIES: BglG family transcription antiterminator LicT [Serratia]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK09772 super family cl31605
transcriptional antiterminator BglG; Provisional
 1-276 1.29e-93

transcriptional antiterminator BglG; Provisional


The actual alignment was detected with superfamily member PRK09772:

Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 277.74  E-value: 1.29e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552   1 MKIAKILNNNVVITLDDRQAETVVMGKGIGFKKKPGDTLDESLIEKVFTHNGGEIAERYKELLAEIPLACVTTADRIITL 80
Cdd:PRK09772   3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552  81 ARERLpGKLHNIVYITLTDHIHFALQRHAQGLDIKNALLWEIKKLYPAEFAVGLEALALIAQRLDTALPEDEAGFIALHL 160
Cdd:PRK09772  83 AQERL-GKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552 161 VNAQLNDEMHNTLHITRVMQEILNLVKYHFRFDYNEESLSYHRFVTHLKFFAQRLLGKNYVDSDDDSLYQVVKEKYRESF 240
Cdd:PRK09772 162 VSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAW 241

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 757520552 241 ACAGKINRHIEKHYQHQLTTEEMMFLTIHIERVRSE 276
Cdd:PRK09772 242 QCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-276 1.29e-93

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 277.74  E-value: 1.29e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552   1 MKIAKILNNNVVITLDDRQAETVVMGKGIGFKKKPGDTLDESLIEKVFTHNGGEIAERYKELLAEIPLACVTTADRIITL 80
Cdd:PRK09772   3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552  81 ARERLpGKLHNIVYITLTDHIHFALQRHAQGLDIKNALLWEIKKLYPAEFAVGLEALALIAQRLDTALPEDEAGFIALHL 160
Cdd:PRK09772  83 AQERL-GKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552 161 VNAQLNDEMHNTLHITRVMQEILNLVKYHFRFDYNEESLSYHRFVTHLKFFAQRLLGKNYVDSDDDSLYQVVKEKYRESF 240
Cdd:PRK09772 162 VSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAW 241

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 757520552 241 ACAGKINRHIEKHYQHQLTTEEMMFLTIHIERVRSE 276
Cdd:PRK09772 242 QCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
BglG COG3711
Transcriptional antiterminator [Transcription];
43-281 1.45e-49

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 172.74  E-value: 1.45e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552  43 LIEKVFTHNGGEIAERYKELLAEIPLACVTTADRIITLARERLPGKLHNIVYITLTDHIHFALQRHAQGLDIK--NALLW 120
Cdd:COG3711  151 ALAELLSELLSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKldNPLLW 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552 121 EIKKlyPAEFAVGLEALALIAQRLDTALPEDEAGFIALHLVNAQLNDEMH----NTLHITRVMQEILNLVKYHFRFDYNE 196
Cdd:COG3711  231 EIKK--PKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNElseiITLEITKLIKEIINIIEEELGIDLDE 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552 197 ESLSYHRFVTHLKFFAQRLLGKNYVDsddDSLYQVVKEKYRESFACAGKINRHIEKHYQHQLTTEEMMFLTIHIERVRSE 276
Cdd:COG3711  309 DSLLYERLITHLKPAINRLKYGIPIR---NPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALER 385


                 ....*
gi 757520552 277 SEEKP 281
Cdd:COG3711  386 QKESK 390
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-49 2.02e-23

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: 90.23  E-value: 2.02e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 757520552     1 MKIAKILNNNVVITLDDRQAETVVMGKGIGFKKKPGDTLDESLIEKVFT 49
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFV 49
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-49 2.02e-23

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: 90.18  E-value: 2.02e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 757520552    2 KIAKILNNNVVITLDDRQAETVVMGKGIGFKKKPGDTLDESLIEKVFT 49
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFV 48
 
Name Accession Description Interval E-value
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
 1-276 1.29e-93

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 277.74  E-value: 1.29e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552   1 MKIAKILNNNVVITLDDRQAETVVMGKGIGFKKKPGDTLDESLIEKVFTHNGGEIAERYKELLAEIPLACVTTADRIITL 80
Cdd:PRK09772   3 MQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552  81 ARERLpGKLHNIVYITLTDHIHFALQRHAQGLDIKNALLWEIKKLYPAEFAVGLEALALIAQRLDTALPEDEAGFIALHL 160
Cdd:PRK09772  83 AQERL-GKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552 161 VNAQLNDEMHNTLHITRVMQEILNLVKYHFRFDYNEESLSYHRFVTHLKFFAQRLLGKNYVDSDDDSLYQVVKEKYRESF 240
Cdd:PRK09772 162 VSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAW 241

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 757520552 241 ACAGKINRHIEKHYQHQLTTEEMMFLTIHIERVRSE 276
Cdd:PRK09772 242 QCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKE 277
BglG COG3711
Transcriptional antiterminator [Transcription];
43-281 1.45e-49

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 172.74  E-value: 1.45e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552  43 LIEKVFTHNGGEIAERYKELLAEIPLACVTTADRIITLARERLPGKLHNIVYITLTDHIHFALQRHAQGLDIK--NALLW 120
Cdd:COG3711  151 ALAELLSELLSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKldNPLLW 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552 121 EIKKlyPAEFAVGLEALALIAQRLDTALPEDEAGFIALHLVNAQLNDEMH----NTLHITRVMQEILNLVKYHFRFDYNE 196
Cdd:COG3711  231 EIKK--PKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNElseiITLEITKLIKEIINIIEEELGIDLDE 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552 197 ESLSYHRFVTHLKFFAQRLLGKNYVDsddDSLYQVVKEKYRESFACAGKINRHIEKHYQHQLTTEEMMFLTIHIERVRSE 276
Cdd:COG3711  309 DSLLYERLITHLKPAINRLKYGIPIR---NPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALER 385


                 ....*
gi 757520552 277 SEEKP 281
Cdd:COG3711  386 QKESK 390
CAT_RBD smart01061
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 1-49 2.02e-23

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: 90.23  E-value: 2.02e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 757520552     1 MKIAKILNNNVVITLDDRQAETVVMGKGIGFKKKPGDTLDESLIEKVFT 49
Cdd:smart01061   1 MRIKKVLNNNVVLAEDENGQEVIVMGKGIGFGKKKGDLIDESKIEKIFV 49
CAT_RBD pfam03123
CAT RNA binding domain; This RNA binding domain is found at the amino terminus of ...
 2-49 2.02e-23

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: 90.18  E-value: 2.02e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 757520552    2 KIAKILNNNVVITLDDRQAETVVMGKGIGFKKKPGDTLDESLIEKVFT 49
Cdd:pfam03123   1 KIKKVLNNNVVLAKDDNGEEVILMGKGIGFGKKKGDLIDESKIEKIFV 48
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 91-163 3.31e-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: 77.29  E-value: 3.31e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757520552   91 NIVYITLTDHIHFALQRHAQGLDIKNALLWEIKKLYPAEFAVGLEALALIAQRLDTALPEDEAGFIALHLVNA 163
Cdd:pfam00874  18 DILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIGYIALHFLSA 90
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 180-272 5.30e-15

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: 68.82  E-value: 5.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552  180 QEILNLVKYHFRFDYNEESLsYHRFVTHLKFFAQRLLGKNYVDsddDSLYQVVKEKYRESFACAGKINRHIEKHYQHQLT 259
Cdd:pfam00874   1 EEIIELIEKKLGITFDDDIL-YIRLILHLAFAIERIKEGITIE---NPLLEEIKEKYPKEFEIAKKILEILEEELGIELP 76

                          90
                  ....*....|...
gi 757520552  260 TEEMMFLTIHIER 272
Cdd:pfam00874  77 EDEIGYIALHFLS 89
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
39-172 6.31e-12

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 65.52  E-value: 6.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552  39 LDESLIEKVFTHNGGEIAERYKELLAEIPLACVTTADRIITLARERLPGKLHNIVYITLTDHIHFALQRHAQGLDIKNAL 118
Cdd:COG3933  426 EIDIDVHLLKFIYDDNKNFNKEELAKIVDEDIINVVEEILELAEKKLGRKFSENFIYALSLHLSSFIERIKEGKEIINPN 505

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 757520552 119 LWEIKKLYPAEFAVGLEALALIAQRLDTALPEDEAGFIALHLVNAQLNDEMHNT 172
Cdd:COG3933  506 LNEIKKKYPKEFKVAKEIKELIEQELDIEIPEDEVGFLTLFLVSLNENNESGKV 559
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 75-175 4.66e-03

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: 38.55  E-value: 4.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757520552  75 DRIITLARERLPGKLHNIVYITLTDHIHFALQRHAQGLDIKNALLWEIKKLYPAEFAVGLEALALIAQRLDTALPEDEAG 154
Cdd:COG1221  475 VEIFEEAEKKLLRYNSSNLFIALSLHLLSTLLRIKKGKKIINPQLNEIKKKYYEEFILAAEAIKIIEEELKILIPDEEEG 554

                         90       100
                 ....*....|....*....|.
gi 757520552 155 FIALHLVNAQLNDEMHNTLHI 175
Cdd:COG1221  555 FILLLLIELKEEKSLSENVIV 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH