NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|544960492|ref|WP_021365146|]
View 

BglG family transcription antiterminator [Clostridioides difficile]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
BglG COG3711
Transcriptional antiterminator [Transcription];
24-660 9.24e-90

Transcriptional antiterminator [Transcription];


:

Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 291.76  E-value: 9.24e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492  24 TLEQFSNVLGVSTRTIRNYINQINRELKDGIAKIVKNEKGTYSIRIEDESKlieivNFNRGKLSNFINLNSPDERINYVL 103
Cdd:COG3711   13 TAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDDEQK-----EKLLQLLEKSEDPLSPKERVAYIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 104 DILTMTNNPITIDDLAEEICIGRTTLIKDLKKADRILAEYDLELKRKPNIGMILVGEEMDIRLLVLDRLYENY-IDVLEN 182
Cdd:COG3711   88 LRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNYGIKLEGSELDIRKALAELLSELLsENDLLS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 183 VNQINLIKDYDIECLRDELKKLFKKEELYITEQVLRDVERYIIMSVLRNLNGYKFEKIDKRFEVIRCSDEYTLGLKLKAL 262
Cdd:COG3711  168 LLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLLWEIKKPKEYEIAKEILKL 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 263 LEKIFNIVLNEKETIFLTMPLIGRKapSTKLALSSIKINDSVKEVVDEVTSFLLETSGIDFKEDKKLIENLEYHLYFALN 342
Cdd:COG3711  248 IEERLGISLPEDEIGYIALHLLGAR--LNNDNELSEIITLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAIN 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 343 RMRFNIRVKNPLLQEIKERYTFPYSVAKIAAMIIEEKFDLKICDHEIGYIALHFGSYFEKNSRKvlNVNRVAVVCGTGLG 422
Cdd:COG3711  326 RLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKES--KKKRVLVVCSSGIG 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 423 TAQLIRIKIGKILGESVEVNTFSDIEAKANldLLKYYDLVFTTVDFKidlDVPIFRVNALFNEESIKKeienaillknsi 502
Cdd:COG3711  404 TSRLLKSRLKKLFPEIEIIDVISYRELEEI--DLEDYDLIISTVPLE---DKPVIVVSPLLTEEDIEK------------ 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 503 nlksIKKIEKNtpFIGKLIEEDKFFILNKSTFMENLEDMLEKLVHKGIIDIEFKKKVLKREKKSSTALDNYIALPHSVNT 582
Cdd:COG3711  467 ----IRKFLKQ--IKKKLAKILFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEELEEIIIIIVIAIPI 540
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544960492 583 NGENLYLAFGILEKPVVWDTKEIRIIILMIIPDKNVDSTDLIIKSYEEVLEVGRDKKMVEELAKVKSFDEFYKIITKR 660
Cdd:COG3711  541 IIIIIIAIIVLAAEEPGVIKLILVLLLLLILIILLEDDEALLVILLLLLLLIESSLLLLLLLELLLELELELLILLLL 618
 
Name Accession Description Interval E-value
BglG COG3711
Transcriptional antiterminator [Transcription];
24-660 9.24e-90

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 291.76  E-value: 9.24e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492  24 TLEQFSNVLGVSTRTIRNYINQINRELKDGIAKIVKNEKGTYSIRIEDESKlieivNFNRGKLSNFINLNSPDERINYVL 103
Cdd:COG3711   13 TAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDDEQK-----EKLLQLLEKSEDPLSPKERVAYIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 104 DILTMTNNPITIDDLAEEICIGRTTLIKDLKKADRILAEYDLELKRKPNIGMILVGEEMDIRLLVLDRLYENY-IDVLEN 182
Cdd:COG3711   88 LRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNYGIKLEGSELDIRKALAELLSELLsENDLLS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 183 VNQINLIKDYDIECLRDELKKLFKKEELYITEQVLRDVERYIIMSVLRNLNGYKFEKIDKRFEVIRCSDEYTLGLKLKAL 262
Cdd:COG3711  168 LLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLLWEIKKPKEYEIAKEILKL 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 263 LEKIFNIVLNEKETIFLTMPLIGRKapSTKLALSSIKINDSVKEVVDEVTSFLLETSGIDFKEDKKLIENLEYHLYFALN 342
Cdd:COG3711  248 IEERLGISLPEDEIGYIALHLLGAR--LNNDNELSEIITLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAIN 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 343 RMRFNIRVKNPLLQEIKERYTFPYSVAKIAAMIIEEKFDLKICDHEIGYIALHFGSYFEKNSRKvlNVNRVAVVCGTGLG 422
Cdd:COG3711  326 RLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKES--KKKRVLVVCSSGIG 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 423 TAQLIRIKIGKILGESVEVNTFSDIEAKANldLLKYYDLVFTTVDFKidlDVPIFRVNALFNEESIKKeienaillknsi 502
Cdd:COG3711  404 TSRLLKSRLKKLFPEIEIIDVISYRELEEI--DLEDYDLIISTVPLE---DKPVIVVSPLLTEEDIEK------------ 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 503 nlksIKKIEKNtpFIGKLIEEDKFFILNKSTFMENLEDMLEKLVHKGIIDIEFKKKVLKREKKSSTALDNYIALPHSVNT 582
Cdd:COG3711  467 ----IRKFLKQ--IKKKLAKILFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEELEEIIIIIVIAIPI 540
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544960492 583 NGENLYLAFGILEKPVVWDTKEIRIIILMIIPDKNVDSTDLIIKSYEEVLEVGRDKKMVEELAKVKSFDEFYKIITKR 660
Cdd:COG3711  541 IIIIIIAIIVLAAEEPGVIKLILVLLLLLILIILLEDDEALLVILLLLLLLIESSLLLLLLLELLLELELELLILLLL 618
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
310-399 9.47e-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: 69.97  E-value: 9.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492  310 EVTSFLLETSGIDFKEDKkLIENLEYHLYFALNRMRFNIRVKNPLLQEIKERYTFPYSVAKIAAMIIEEKFDLKICDHEI 389
Cdd:pfam00874   2 EIIELIEKKLGITFDDDI-LYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEI 80
                          90
                  ....*....|
gi 544960492  390 GYIALHFGSY 399
Cdd:pfam00874  81 GYIALHFLSA 90
PTS_IIB_bgl_like cd05568
PTS_IIB_bgl_like: the PTS (phosphotransferase system) IIB domain of a family of sensory ...
412-496 3.22e-14

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: 68.30  E-value: 3.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 412 RVAVVCGTGLGTAQLIRIKIGKILGESVEVNTFSDIEAKaNLDLLKyYDLVFTTVDFKiDLDVPIFRVNALFNEESIKKe 491
Cdd:cd05568    2 KALVVCPSGIGTSRLLKSKLKKLFPEIEIIDVISLRELE-EVDLDD-YDLIISTVPLE-DTDKPVIVVSPILTEEDIKK- 77

                 ....*
gi 544960492 492 IENAI 496
Cdd:cd05568   78 IRKFI 82
PRK11564 PRK11564
stationary phase inducible protein CsiE; Provisional
317-399 2.45e-05

stationary phase inducible protein CsiE; Provisional


Pssm-ID: 236932 [Multi-domain]  Cd Length: 426  Bit Score: 47.31  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 317 ETSGIDFKEDKKLIENLEYHLYFALNRMRFNIRVKNPLLQEIKERYTFPYSVAKIAAMIIEEKFDLKICDHEIGYIALHF 396
Cdd:PRK11564 247 ELGGVRFSDEQGLCDQLYTHLAQALERSLFAIGIDNTLPEEFARLYPRLLRTTRAALAGFEQEYGVHFSDEEVGLVAVIF 326

                 ...
gi 544960492 397 GSY 399
Cdd:PRK11564 327 GAW 329
 
Name Accession Description Interval E-value
BglG COG3711
Transcriptional antiterminator [Transcription];
24-660 9.24e-90

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 291.76  E-value: 9.24e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492  24 TLEQFSNVLGVSTRTIRNYINQINRELKDGIAKIVKNEKGTYSIRIEDESKlieivNFNRGKLSNFINLNSPDERINYVL 103
Cdd:COG3711   13 TAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDDEQK-----EKLLQLLEKSEDPLSPKERVAYIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 104 DILTMTNNPITIDDLAEEICIGRTTLIKDLKKADRILAEYDLELKRKPNIGMILVGEEMDIRLLVLDRLYENY-IDVLEN 182
Cdd:COG3711   88 LRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNYGIKLEGSELDIRKALAELLSELLsENDLLS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 183 VNQINLIKDYDIECLRDELKKLFKKEELYITEQVLRDVERYIIMSVLRNLNGYKFEKIDKRFEVIRCSDEYTLGLKLKAL 262
Cdd:COG3711  168 LLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLLWEIKKPKEYEIAKEILKL 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 263 LEKIFNIVLNEKETIFLTMPLIGRKapSTKLALSSIKINDSVKEVVDEVTSFLLETSGIDFKEDKKLIENLEYHLYFALN 342
Cdd:COG3711  248 IEERLGISLPEDEIGYIALHLLGAR--LNNDNELSEIITLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPAIN 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 343 RMRFNIRVKNPLLQEIKERYTFPYSVAKIAAMIIEEKFDLKICDHEIGYIALHFGSYFEKNSRKvlNVNRVAVVCGTGLG 422
Cdd:COG3711  326 RLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKES--KKKRVLVVCSSGIG 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 423 TAQLIRIKIGKILGESVEVNTFSDIEAKANldLLKYYDLVFTTVDFKidlDVPIFRVNALFNEESIKKeienaillknsi 502
Cdd:COG3711  404 TSRLLKSRLKKLFPEIEIIDVISYRELEEI--DLEDYDLIISTVPLE---DKPVIVVSPLLTEEDIEK------------ 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 503 nlksIKKIEKNtpFIGKLIEEDKFFILNKSTFMENLEDMLEKLVHKGIIDIEFKKKVLKREKKSSTALDNYIALPHSVNT 582
Cdd:COG3711  467 ----IRKFLKQ--IKKKLAKILFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEELEEIIIIIVIAIPI 540
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544960492 583 NGENLYLAFGILEKPVVWDTKEIRIIILMIIPDKNVDSTDLIIKSYEEVLEVGRDKKMVEELAKVKSFDEFYKIITKR 660
Cdd:COG3711  541 IIIIIIAIIVLAAEEPGVIKLILVLLLLLILIILLEDDEALLVILLLLLLLIESSLLLLLLLELLLELELELLILLLL 618
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
310-399 9.47e-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: 69.97  E-value: 9.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492  310 EVTSFLLETSGIDFKEDKkLIENLEYHLYFALNRMRFNIRVKNPLLQEIKERYTFPYSVAKIAAMIIEEKFDLKICDHEI 389
Cdd:pfam00874   2 EIIELIEKKLGITFDDDI-LYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEI 80
                          90
                  ....*....|
gi 544960492  390 GYIALHFGSY 399
Cdd:pfam00874  81 GYIALHFLSA 90
PTS_IIB_bgl_like cd05568
PTS_IIB_bgl_like: the PTS (phosphotransferase system) IIB domain of a family of sensory ...
412-496 3.22e-14

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: 68.30  E-value: 3.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 412 RVAVVCGTGLGTAQLIRIKIGKILGESVEVNTFSDIEAKaNLDLLKyYDLVFTTVDFKiDLDVPIFRVNALFNEESIKKe 491
Cdd:cd05568    2 KALVVCPSGIGTSRLLKSKLKKLFPEIEIIDVISLRELE-EVDLDD-YDLIISTVPLE-DTDKPVIVVSPILTEEDIKK- 77

                 ....*
gi 544960492 492 IENAI 496
Cdd:cd05568   78 IRKFI 82
PTS_IIB cd00133
PTS_IIB: subunit IIB of enzyme II (EII) is the central energy-coupling domain of the ...
412-495 5.31e-09

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: 53.41  E-value: 5.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 412 RVAVVCGTGLGTAQLIRIKIGKILGESVEVNTFSDIEAKANLDLLKyYDLVFTTVDFKI-DLDVPIFRVNALFNEESIKK 490
Cdd:cd00133    1 KILVVCGSGIGSSSMLAEKLEKAAKELGIEVKVEAQGLSEVIDLAD-ADLIISTVPLAArFLGKPVIVVSPLLNEKDGEK 79

                 ....*
gi 544960492 491 EIENA 495
Cdd:cd00133   80 ILEKL 84
SgaB COG3414
Phosphotransferase system, galactitol-specific IIB component [Carbohydrate transport and ...
412-500 6.34e-09

Phosphotransferase system, galactitol-specific IIB component [Carbohydrate transport and metabolism];


Pssm-ID: 442640  Cd Length: 94  Bit Score: 53.64  E-value: 6.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 412 RVAVVCGTGLGTAQLIRIKIGKILGE---SVEVNTFSDIEAKANLDLlkyYDLVFTTVDFKIDLDVPIFRV---NALFNE 485
Cdd:COG3414    3 KILVVCGSGLGTSTMLKMKIEKVLKElgiDAEVEHCDVSSAKSKADD---ADLIVTTTDLAEELGIPVINViplLNGIDK 79
                         90
                 ....*....|....*
gi 544960492 486 ESIKKEIENAILLKN 500
Cdd:COG3414   80 DEIKEKLLEALKELG 94
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
105-410 8.93e-09

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 58.59  E-value: 8.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 105 ILTMTNNPITIDDLAEEICIGRTTLIKDLKKADRILAEYDLELKRKPNIGMILVGEEMDIRLLVLDRLYENYIDVLENVN 184
Cdd:COG3933  262 RIRIIIILPRLPILERRERERLLLLLFEFEEEEIRIIKILIVLLLALLLLLLYVNNLGQLGLLKLLIKAAAAAALAKAIK 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 185 QINLIKDYDIEC-------LRDELKKLFKKEELYITEQVLRDVERYIIMSVLRNLNGYKFEKIDKRFEVIRcsdeytlgl 257
Cdd:COG3933  342 EATIILRLLSKLlklllllLLNERLLLLELKILIEPLDIFFDSSASSDESDESEEDENLYEIIEIKKKLLL--------- 412
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 258 KLKALLEKIFNIVLNEKETIFLTMPLIGRKAPSTKLALSSIkiNDSVKEVVDEVTSFLLETSGIDFkeDKKLIENLEYHL 337
Cdd:COG3933  413 ELGIDEEEINIIIEIDIDVHLLKFIYDDNKNFNKEELAKIV--DEDIINVVEEILELAEKKLGRKF--SENFIYALSLHL 488
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544960492 338 YFALNRMRFNIRVKNPLLQEIKERYTFPYSVAKIAAMIIEEKFDLKICDHEIGYIALHFGSYFEKNSRKVLNV 410
Cdd:COG3933  489 SSFIERIKEGKEIINPNLNEIKKKYPKEFKVAKEIKELIEQELDIEIPEDEVGFLTLFLVSLNENNESGKVGV 561
PtsN COG1762
Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate ...
517-659 1.19e-08

Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 441368 [Multi-domain]  Cd Length: 150  Bit Score: 54.47  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 517 IGKLIEEDKFFI-LNKSTFMENLEDMLEKLVHKGIIDI--EFKKKVLKREKKSSTALDNYIALPHSVNTNGENLYLAFGI 593
Cdd:COG1762    3 LSDLLTPELILLdLEASSKEEAIEELAELLAEKGYVLDkeEYLEALLEREELGSTGIGPGIAIPHARPEGVKKPGIAVAR 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544960492 594 LEKPVVWDTKEiriiilmiipDKNVD----------STDLIIKSYEEVLEVGRDKKMVEELAKVKSFDEFYKIITK 659
Cdd:COG1762   83 LKEPVDFGAMD----------GEPVDlvfllaapedDSEEHLKLLAELARLLSDEEFREKLLNAKSPEEILELLKE 148
PTS_EIIA_2 pfam00359
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
538-657 2.44e-08

Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;


Pssm-ID: 459780 [Multi-domain]  Cd Length: 139  Bit Score: 52.98  E-value: 2.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492  538 LEDMLEKLVHKGIIDIEFKKKVLKREKKSSTALDNYIALPHSVNTNGENLYLAFGILEKPVVWDTKEIRIIIL---MIIP 614
Cdd:pfam00359  20 IEFLADKLVEAGYVEPAYLEAILEREKEGSTGIGNGIAIPHARSEAVKKPGIAVLTLKEPVDFGSEDGKPVKLiflLAAP 99
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 544960492  615 DKNVDSTDLIiksyEEVLEVGRDKKMVEELAKVKSFDEFYKII 657
Cdd:pfam00359 100 DNEASHLKIL----SQLARLLQDEEFVEKLLKAKDPEEILEIL 138
PTS_IIA_fru cd00211
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: ...
538-657 1.80e-06

PTS_IIA, PTS system, fructose/mannitol specific IIA 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. This family is one of four structurally and functionally distinct group IIA PTS system cytoplasmic enzymes, necessary for the uptake of carbohydrates across the cytoplasmic membrane and their phosphorylation.


Pssm-ID: 238129 [Multi-domain]  Cd Length: 136  Bit Score: 47.56  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 538 LEDMLEKLVHKGIIDIEFKKKVLKREKKSSTALDNYIALPHSVNTNGENLYLAFGILEKPVVWDTKEiriiilmiipDKN 617
Cdd:cd00211   19 IEELAQLLVAAGYVEEEYIEALLEREKEGSTGIGNGIAIPHAKSEAVKKPGIAVLRLKEPVDFGSLD----------GQP 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 544960492 618 VdstDLII-------KSYEEVL----EVGRDKKMVEELAKVKSFDEFYKII 657
Cdd:cd00211   89 V---HLIFllaapdsNEHLKALsqlaRLLSDEEFVEQLLNAQSKEEILALL 136
PRK11564 PRK11564
stationary phase inducible protein CsiE; Provisional
317-399 2.45e-05

stationary phase inducible protein CsiE; Provisional


Pssm-ID: 236932 [Multi-domain]  Cd Length: 426  Bit Score: 47.31  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 317 ETSGIDFKEDKKLIENLEYHLYFALNRMRFNIRVKNPLLQEIKERYTFPYSVAKIAAMIIEEKFDLKICDHEIGYIALHF 396
Cdd:PRK11564 247 ELGGVRFSDEQGLCDQLYTHLAQALERSLFAIGIDNTLPEEFARLYPRLLRTTRAALAGFEQEYGVHFSDEEVGLVAVIF 326

                 ...
gi 544960492 397 GSY 399
Cdd:PRK11564 327 GAW 329
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
294-398 7.86e-05

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 45.08  E-value: 7.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 294 ALSSIKINDSVKEVV-----------DEVTSFLLETSGidfKEDKKLIENLEYHLYFALNRMRFNIRVKNPLLQEIKERY 362
Cdd:PRK09772  51 ALSSHELNGRLSELLshiplevmatcDRIISLAQERLG---KLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLY 127
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 544960492 363 TFPYSVAKIAAMIIEEKFDLKICDHEIGYIALHFGS 398
Cdd:PRK09772 128 PKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHLVS 163
Mga pfam05043
Mga helix-turn-helix domain; M regulator protein trans-acting positive regulator (Mga) is a ...
97-166 8.79e-05

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: 41.44  E-value: 8.79e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492   97 ERINYVLDILTMTNNPITIDDLAEEICIGRTTLIKDLKKADRILAEYDLELKRKPNigmILVGEEMDIRL 166
Cdd:pfam05043  15 ESLKFQLLKYLFFEEFVSIKSLAQKLYISESTLYRKIKELNKLLKEFDLSIKKKNL---KLIGDEKQIRY 81
PTS_IIB pfam02302
PTS system, Lactose/Cellobiose specific IIB subunit; The bacterial phosphoenolpyruvate: sugar ...
412-493 1.02e-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: 41.55  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492  412 RVAVVCGTGLGTAQLIRIKIGKILGE--SVEVNTFSDIEAKANLDLLKYYDLVFTTVDFKI-------DLDVPIFRVNAL 482
Cdd:pfam02302   1 KILTACGAGMATSLMAAEALEKAAKElgIVEAQGAAGVNELTAEDIADDADVVILAPDVAVedlarfaGKPVYVIPVKDA 80
                          90
                  ....*....|.
gi 544960492  483 FNEESIKKEIE 493
Cdd:pfam02302  81 LGMKDAEEVLE 91
PTS_IIB_ascorbate cd05563
PTS_IIB_ascorbate: subunit IIB of enzyme II (EII) of the L-ascorbate-specific ...
412-496 1.62e-04

PTS_IIB_ascorbate: subunit IIB of enzyme II (EII) of the L-ascorbate-specific phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS). In this system, EII is an L-ascorbate-specific permease with two cytoplasmic subunits (IIA and IIB) and a transmembrane channel IIC subunit. Subunits IIA, IIB, and IIC are encoded by the sgaA, sgaB, and sgaT genes of the E. coli sgaTBA operon. In some bacteria, the IIB (SgaB) domain is fused C-terminal to the IIA (SgaT) 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 ascorbate, chitobiose/lichenan, lactose, galactitol, mannitol, fructose, and a sensory system with similarity to the bacterial bgl system.


Pssm-ID: 99905  Cd Length: 86  Bit Score: 40.59  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544960492 412 RVAVVCGTGLGTAQLIRIKIGKIL---GESVEVNTFSDIEAKANLdllkyYDLVFTTVDFKIDL---DVPIFRVNALFNE 485
Cdd:cd05563    1 KILAVCGSGLGSSLMLKMNVEKVLkelGIEAEVEHTDLGSAKASS-----ADIIVTSKDLASLLadgGAKVIGLKNIMDK 75
                         90
                 ....*....|.
gi 544960492 486 ESIKKEIENAI 496
Cdd:cd05563   76 NEIKEKLLEAL 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH