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Conserved domains on  [gi|534601309|gb|EQN59106|]
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transcriptional antiterminator [Escherichia coli HVH 20 (4-5865042)]

Protein Classification

BglG family transcription antiterminator( domain architecture ID 11467243)

BglG family transcription antiterminator similar to Bacillus subtilis transcriptional regulator MtlR that positively regulates the expression of the mtlAFD operon, which is involved in the uptake and catabolism of mannitol

Gene Ontology:  GO:0006355|GO:0009401|GO:0008982
PubMed:  15802242|9305643

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BglG COG3711
Transcriptional antiterminator [Transcription];
20-502 2.39e-107

Transcriptional antiterminator [Transcription];


:

Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 332.98  E-value: 2.39e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309  20 EYTTIVTIAGYLNVSEKTIQRDLRLLEQWLGQWRINVEKRAGAGVMLSAENIADLLHLDHLLvaecEEIDCVMNNARRVK 99
Cdd:COG3711   10 NVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDDEQKEKLLQLLE----KSEDPLSPKERVAY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 100 IASQLLSETpNETSISKLSERYFISGASIVNDLRVIESWLAPLGLSLIRSPS-GTHIEGSEGQVRQAMALLINGIINHNE 178
Cdd:COG3711   86 ILLRLLLAG-DPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNyGIKLEGSELDIRKALAELLSELLSEND 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 179 pqgvvysrldpGSYKALVHYFGEEEVLFVQSLLLDMENELSWSLGEPYYVNIFTHILIMMYRNTHGNALSREEDQTRQY- 257
Cdd:COG3711  165 -----------LLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLLWEIk 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 258 DENIFNVASQMIHKIDQRIAHTLPDDEVWFIYQYIISSGvaIDGQKDVSIISHMQASNEARlitwRLITVFSDIVDCDFS 337
Cdd:COG3711  234 KPKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGAR--LNNDNELSEIITLEITKLIK----EIINIIEEELGIDLD 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 338 EDSALYDGLLVHIKPLINRLNYRIHIRNPLLEDIKAELADVWRLTQYVVNQVFKTWGeNAVSEDEVGYLTVHFQAAMERQ 417
Cdd:COG3711  308 EDSLLYERLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELG-IEIPEDEIGYLTLHFGAALERQ 386

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 418 --IARKRVLLVCSTGIGTSHLLKSRILRAFPEWTIVDVISAANLSQVLPDNIELIISTINLPTVtmPVAYVTAFFNDADI 495
Cdd:COG3711  387 keSKKKRVLVVCSSGIGTSRLLKSRLKKLFPEIEIIDVISYRELEEIDLEDYDLIISTVPLEDK--PVIVVSPLLTEEDI 464


                 ....*..
gi 534601309 496 KRVTEMV 502
Cdd:COG3711  465 EKIRKFL 471
 
Name Accession Description Interval E-value
BglG COG3711
Transcriptional antiterminator [Transcription];
20-502 2.39e-107

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 332.98  E-value: 2.39e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309  20 EYTTIVTIAGYLNVSEKTIQRDLRLLEQWLGQWRINVEKRAGAGVMLSAENIADLLHLDHLLvaecEEIDCVMNNARRVK 99
Cdd:COG3711   10 NVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDDEQKEKLLQLLE----KSEDPLSPKERVAY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 100 IASQLLSETpNETSISKLSERYFISGASIVNDLRVIESWLAPLGLSLIRSPS-GTHIEGSEGQVRQAMALLINGIINHNE 178
Cdd:COG3711   86 ILLRLLLAG-DPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNyGIKLEGSELDIRKALAELLSELLSEND 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 179 pqgvvysrldpGSYKALVHYFGEEEVLFVQSLLLDMENELSWSLGEPYYVNIFTHILIMMYRNTHGNALSREEDQTRQY- 257
Cdd:COG3711  165 -----------LLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLLWEIk 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 258 DENIFNVASQMIHKIDQRIAHTLPDDEVWFIYQYIISSGvaIDGQKDVSIISHMQASNEARlitwRLITVFSDIVDCDFS 337
Cdd:COG3711  234 KPKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGAR--LNNDNELSEIITLEITKLIK----EIINIIEEELGIDLD 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 338 EDSALYDGLLVHIKPLINRLNYRIHIRNPLLEDIKAELADVWRLTQYVVNQVFKTWGeNAVSEDEVGYLTVHFQAAMERQ 417
Cdd:COG3711  308 EDSLLYERLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELG-IEIPEDEIGYLTLHFGAALERQ 386

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 418 --IARKRVLLVCSTGIGTSHLLKSRILRAFPEWTIVDVISAANLSQVLPDNIELIISTINLPTVtmPVAYVTAFFNDADI 495
Cdd:COG3711  387 keSKKKRVLVVCSSGIGTSRLLKSRLKKLFPEIEIIDVISYRELEEIDLEDYDLIISTVPLEDK--PVIVVSPLLTEEDI 464


                 ....*..
gi 534601309 496 KRVTEMV 502
Cdd:COG3711  465 EKIRKFL 471
PTS_IIB_bgl_like cd05568
PTS_IIB_bgl_like: the PTS (phosphotransferase system) IIB domain of a family of sensory ...
 421-502 1.60e-23

PTS_IIB_bgl_like: the PTS (phosphotransferase system) IIB domain of a family of sensory systems composed of a membrane-bound sugar-sensor (similar to BglF) and a transcription antiterminator (similar to BglG) which regulate expression of genes involved in sugar utilization. The domain architecture of the IIB-containing protein includes a region N-terminal to the IIB domain which is homologous to the BglG transcription antiterminator with an RNA-binding domain followed by two homologous domains, PRD1 and PRD2 (PTS Regulation Domains). C-terminal to the IIB domain is a domain similar to the PTS IIA domain. In this system, the BglG-like region and the IIB and IIA-like domains are all expressed together as a single multidomain protein. The IIB domain fold includes a central four-stranded parallel open twisted beta-sheet flanked by alpha-helices on both sides. The seven major PTS systems with this IIB fold include this sensory system with similarity to the bacterial bgl system, chitobiose/lichenan, ascorbate, lactose, galactitol, mannitol, and fructose systems.


Pssm-ID: 99910  Cd Length: 85  Bit Score: 94.11  E-value: 1.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 421 KRVLLVCSTGIGTSHLLKSRILRAFPEWTIVDVISAANLSQVLPDNIELIISTINLPTVTMPVAYVTAFFNDADIKRVTE 500
Cdd:cd05568    1 KKALVVCPSGIGTSRLLKSKLKKLFPEIEIIDVISLRELEEVDLDDYDLIISTVPLEDTDKPVIVVSPILTEEDIKKIRK 80


                 ..
gi 534601309 501 MV 502
Cdd:cd05568   81 FI 82
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 323-413 1.16e-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: 66.51  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309  323 RLITVFSDIVDCDFSEDSaLYDGLLVHIKPLINRLNYRIHIRNPLLEDIKAELADVWRLTQYVVNQVFKTWGENaVSEDE 402
Cdd:pfam00874   2 EIIELIEKKLGITFDDDI-LYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIE-LPEDE 79

                          90
                  ....*....|.
gi 534601309  403 VGYLTVHFQAA 413
Cdd:pfam00874  80 IGYIALHFLSA 90
PRK11564 PRK11564
stationary phase inducible protein CsiE; Provisional
 262-425 2.92e-04

stationary phase inducible protein CsiE; Provisional


Pssm-ID: 236932 [Multi-domain]  Cd Length: 426  Bit Score: 43.46  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 262 FNVASQMIHKIDQRIAHTLPDDEVWFI----YQYIISSGVAIDGQKDVSIishMQASNearlitwRLITVFSDIVDCDFS 337
Cdd:PRK11564 185 FQLAQEIGRHWQRRVLQPPPLDEPLFLallfSMLRAPDPLRDAHQRDRRL---RQAIK-------RLVNRFRELGGVRFS 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 338 EDSALYDGLLVHIKPLINRLNYRIHIRNPLLEDIKAELADVWRLTQYVVNQVFKTWGEnAVSEDEVGYLTVHFQAAM--E 415
Cdd:PRK11564 255 DEQGLCDQLYTHLAQALERSLFAIGIDNTLPEEFARLYPRLLRTTRAALAGFEQEYGV-HFSDEEVGLVAVIFGAWLmqE 333

                        170
                 ....*....|
gi 534601309 416 RQIARKRVLL 425
Cdd:PRK11564 334 NDLHEKQILL 343
 
Name Accession Description Interval E-value
BglG COG3711
Transcriptional antiterminator [Transcription];
20-502 2.39e-107

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 332.98  E-value: 2.39e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309  20 EYTTIVTIAGYLNVSEKTIQRDLRLLEQWLGQWRINVEKRAGAGVMLSAENIADLLHLDHLLvaecEEIDCVMNNARRVK 99
Cdd:COG3711   10 NVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDDEQKEKLLQLLE----KSEDPLSPKERVAY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 100 IASQLLSETpNETSISKLSERYFISGASIVNDLRVIESWLAPLGLSLIRSPS-GTHIEGSEGQVRQAMALLINGIINHNE 178
Cdd:COG3711   86 ILLRLLLAG-DPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNyGIKLEGSELDIRKALAELLSELLSEND 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 179 pqgvvysrldpGSYKALVHYFGEEEVLFVQSLLLDMENELSWSLGEPYYVNIFTHILIMMYRNTHGNALSREEDQTRQY- 257
Cdd:COG3711  165 -----------LLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLLWEIk 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 258 DENIFNVASQMIHKIDQRIAHTLPDDEVWFIYQYIISSGvaIDGQKDVSIISHMQASNEARlitwRLITVFSDIVDCDFS 337
Cdd:COG3711  234 KPKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGAR--LNNDNELSEIITLEITKLIK----EIINIIEEELGIDLD 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 338 EDSALYDGLLVHIKPLINRLNYRIHIRNPLLEDIKAELADVWRLTQYVVNQVFKTWGeNAVSEDEVGYLTVHFQAAMERQ 417
Cdd:COG3711  308 EDSLLYERLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELG-IEIPEDEIGYLTLHFGAALERQ 386

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 418 --IARKRVLLVCSTGIGTSHLLKSRILRAFPEWTIVDVISAANLSQVLPDNIELIISTINLPTVtmPVAYVTAFFNDADI 495
Cdd:COG3711  387 keSKKKRVLVVCSSGIGTSRLLKSRLKKLFPEIEIIDVISYRELEEIDLEDYDLIISTVPLEDK--PVIVVSPLLTEEDI 464


                 ....*..
gi 534601309 496 KRVTEMV 502
Cdd:COG3711  465 EKIRKFL 471
PTS_IIB_bgl_like cd05568
PTS_IIB_bgl_like: the PTS (phosphotransferase system) IIB domain of a family of sensory ...
 421-502 1.60e-23

PTS_IIB_bgl_like: the PTS (phosphotransferase system) IIB domain of a family of sensory systems composed of a membrane-bound sugar-sensor (similar to BglF) and a transcription antiterminator (similar to BglG) which regulate expression of genes involved in sugar utilization. The domain architecture of the IIB-containing protein includes a region N-terminal to the IIB domain which is homologous to the BglG transcription antiterminator with an RNA-binding domain followed by two homologous domains, PRD1 and PRD2 (PTS Regulation Domains). C-terminal to the IIB domain is a domain similar to the PTS IIA domain. In this system, the BglG-like region and the IIB and IIA-like domains are all expressed together as a single multidomain protein. The IIB domain fold includes a central four-stranded parallel open twisted beta-sheet flanked by alpha-helices on both sides. The seven major PTS systems with this IIB fold include this sensory system with similarity to the bacterial bgl system, chitobiose/lichenan, ascorbate, lactose, galactitol, mannitol, and fructose systems.


Pssm-ID: 99910  Cd Length: 85  Bit Score: 94.11  E-value: 1.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 421 KRVLLVCSTGIGTSHLLKSRILRAFPEWTIVDVISAANLSQVLPDNIELIISTINLPTVTMPVAYVTAFFNDADIKRVTE 500
Cdd:cd05568    1 KKALVVCPSGIGTSRLLKSKLKKLFPEIEIIDVISLRELEEVDLDDYDLIISTVPLEDTDKPVIVVSPILTEEDIKKIRK 80


                 ..
gi 534601309 501 MV 502
Cdd:cd05568   81 FI 82
PTS_IIB cd00133
PTS_IIB: subunit IIB of enzyme II (EII) is the central energy-coupling domain of the ...
 422-500 1.48e-14

PTS_IIB: subunit IIB of enzyme II (EII) is the central energy-coupling domain of the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS). In the multienzyme PTS complex, EII is a carbohydrate-specific permease consisting of two cytoplasmic domains (IIA and IIB) and a transmembrane channel IIC domain. The IIB domain fold includes a central four-stranded parallel open twisted beta-sheet flanked by alpha-helices on both sides. The seven major PTS systems with this IIB fold include chitobiose/lichenan, ascorbate, lactose, galactitol, mannitol, fructose, and a sensory system with similarity to the bacterial bgl system. The PTS is found only in bacteria, where it catalyzes the transport and phosphorylation of numerous monosaccharides, disaccharides, polyols, amino sugars, and other sugar derivatives. The four proteins (domains) forming the PTS phosphorylation cascade (EI, HPr, EIIA, and EIIB), can phosphorylate or interact with numerous non-PTS proteins thereby regulating their activity.


Pssm-ID: 99904  Cd Length: 84  Bit Score: 68.82  E-value: 1.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 422 RVLLVCSTGIGTSHLLKSRILRAFPEWTIVDVISAANLSQVL-PDNIELIISTINLPT--VTMPVAYVTAFFNDADIKRV 498
Cdd:cd00133    1 KILVVCGSGIGSSSMLAEKLEKAAKELGIEVKVEAQGLSEVIdLADADLIISTVPLAArfLGKPVIVVSPLLNEKDGEKI 80


                 ..
gi 534601309 499 TE 500
Cdd:cd00133   81 LE 82
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 323-413 1.16e-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: 66.51  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309  323 RLITVFSDIVDCDFSEDSaLYDGLLVHIKPLINRLNYRIHIRNPLLEDIKAELADVWRLTQYVVNQVFKTWGENaVSEDE 402
Cdd:pfam00874   2 EIIELIEKKLGITFDDDI-LYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIE-LPEDE 79

                          90
                  ....*....|.
gi 534601309  403 VGYLTVHFQAA 413
Cdd:pfam00874  80 IGYIALHFLSA 90
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 208-295 1.38e-06

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: 46.48  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309  208 QSLLLDMENELSWSLGEPY-YVNIFTHILIMMYRNTHGNALSREE-DQTRQYDENIFNVASQMIHKIDQRIAHTLPDDEV 285
Cdd:pfam00874   1 EEIIELIEKKLGITFDDDIlYIRLILHLAFAIERIKEGITIENPLlEEIKEKYPKEFEIAKKILEILEEELGIELPEDEI 80

                          90
                  ....*....|
gi 534601309  286 WFIYQYIISS 295
Cdd:pfam00874  81 GYIALHFLSA 90
PTS_IIB pfam02302
PTS system, Lactose/Cellobiose specific IIB subunit; The bacterial phosphoenolpyruvate: sugar ...
 422-498 1.38e-04

PTS system, Lactose/Cellobiose specific IIB subunit; The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. The lactose/cellobiose-specific family are one of four structurally and functionally distinct group IIB PTS system cytoplasmic enzymes. The fold of IIB cellobiose shows similar structure to mammalian tyrosine phosphatases. This family also contains the fructose specific IIB subunit.


Pssm-ID: 396744  Cd Length: 92  Bit Score: 40.78  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309  422 RVLLVCSTGIGTSHLLKSRILRAFPEWTIVDVISAANLSQVLPDNIE----LIISTINLPTVTM--------PVAYVTAF 489
Cdd:pfam02302   1 KILTACGAGMATSLMAAEALEKAAKELGIVEAQGAAGVNELTAEDIAddadVVILAPDVAVEDLarfagkpvYVIPVKDA 80


                  ....*....
gi 534601309  490 FNDADIKRV 498
Cdd:pfam02302  81 LGMKDAEEV 89
PRK11564 PRK11564
stationary phase inducible protein CsiE; Provisional
 262-425 2.92e-04

stationary phase inducible protein CsiE; Provisional


Pssm-ID: 236932 [Multi-domain]  Cd Length: 426  Bit Score: 43.46  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 262 FNVASQMIHKIDQRIAHTLPDDEVWFI----YQYIISSGVAIDGQKDVSIishMQASNearlitwRLITVFSDIVDCDFS 337
Cdd:PRK11564 185 FQLAQEIGRHWQRRVLQPPPLDEPLFLallfSMLRAPDPLRDAHQRDRRL---RQAIK-------RLVNRFRELGGVRFS 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 338 EDSALYDGLLVHIKPLINRLNYRIHIRNPLLEDIKAELADVWRLTQYVVNQVFKTWGEnAVSEDEVGYLTVHFQAAM--E 415
Cdd:PRK11564 255 DEQGLCDQLYTHLAQALERSLFAIGIDNTLPEEFARLYPRLLRTTRAALAGFEQEYGV-HFSDEEVGLVAVIFGAWLmqE 333

                        170
                 ....*....|
gi 534601309 416 RQIARKRVLL 425
Cdd:PRK11564 334 NDLHEKQILL 343
PTS_IIB_galactitol cd05566
PTS_IIB_galactitol: subunit IIB of enzyme II (EII) of the galactitol-specific ...
 421-502 1.20e-03

PTS_IIB_galactitol: subunit IIB of enzyme II (EII) of the galactitol-specific phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS). In this system, EII is a galactitol-specific permease with two cytoplasmic domains (IIA and IIB) and a transmembrane channel IIC domain that are expressed on three distinct polypeptide chains, in contrast to other PTS sugar transporters. The three genes encoding these subunits (gatA, gatB, and gatC) comprise the gatCBA operon. Galactitol PTS permease takes up exogenous galactitol, releasing the phosphate ester into the cytoplasm in preparation for oxidation and further metabolism via a modified glycolytic pathway called the tagatose-6-phosphate glycolytic pathway. The IIB domain fold includes a central four-stranded parallel open twisted beta-sheet flanked by alpha-helices on both sides. The seven major PTS systems with this IIB fold include galactitol, chitobiose/lichenan, ascorbate, lactose, mannitol, fructose, and a sensory system with similarity to the bacterial bgl system.


Pssm-ID: 99908  Cd Length: 89  Bit Score: 37.90  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534601309 421 KRVLLVCSTGIGTSHLLKSRILRAFPEWTIVDVISAANLSQVLP--DNIELIISTINLP-TVTMPV----AYVTAFFNDA 493
Cdd:cd05566    1 KKILVACGTGVATSTVVASKVKELLKENGIDVKVEQCKIAEVPSllDDADLIVSTTKVPeDYGIPVinglPFLTGIGEDK 80


                 ....*....
gi 534601309 494 DIKRVTEMV 502
Cdd:cd05566   81 VYEEILEAL 89
Mga pfam05043
Mga helix-turn-helix domain; M regulator protein trans-acting positive regulator (Mga) is a ...
 103-169 1.36e-03

Mga helix-turn-helix domain; M regulator protein trans-acting positive regulator (Mga) is a DNA-binding protein that activates the expression of several important virulence genes in group A streptococcus in response to changing environmental conditions. This domain is found in the centre of the Mga proteins. This family also contains a number of bacterial RofA transcriptional regulators that seem to be largely restricted to streptococci. These proteins have been shown to regulate the expression of important bacterial adhesins. This is presumably a DNA-binding domain.


Pssm-ID: 428276 [Multi-domain]  Cd Length: 87  Bit Score: 37.98  E-value: 1.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 534601309  103 QLLSE--TPNETSISKLSERYFISGASIVNDLRVIESWLAPLGLSLIRSPSgtHIEGSEGQVRQAMALL 169
Cdd:pfam05043  20 QLLKYlfFEEFVSIKSLAQKLYISESTLYRKIKELNKLLKEFDLSIKKKNL--KLIGDEKQIRYFYALL 86
 
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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