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Conserved domains on  [gi|1206084635|gb|ARY90491|]
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transcription antiterminator BglG [Lacticaseibacillus casei]

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];
8-592 8.50e-94

Transcriptional antiterminator [Transcription];


:

Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 301.78  E-value: 8.50e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635   8 ILDFLLKH-GTVHYDQIAEATGLSERTVGNYLNRLDADLSPYAVKLVRKRNVGVSLDGPADQKAHLLRSIHGQEGFTSQT 86
Cdd:COG3711     1 ILKILLKNnNVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDDEQKEKLLQLLEKSEDPLSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635  87 AREHYLMIKLLLTNRPYTLSKLADDLFVSRRTIDNDFKSVKRVFRENHVTVQTSR-TGIQVTASESRRRHMLAKLLRGYW 165
Cdd:COG3711    81 ERVAYILLRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPnYGIKLEGSELDIRKALAELLSELL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 166 GESlsvakqkdgevvqqIQLPAYLNHLVNPATTKAVMQSLAEFLKQSDLIFSDYVLQSLAIHLIIACERpKKAAPAPVHP 245
Cdd:COG3711   161 SEN--------------DLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKR-IKKGKYIKLD 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 246 APLLPETK---------QLLTLVTKHVHRTLDNADAQQINAHIAAILdRQVSDAPAASIEEQAAPVLRQ--QIAGWLTGI 314
Cdd:COG3711   226 NPLLWEIKkpkeyeiakEILKLIEERLGISLPEDEIGYIALHLLGAR-LNNDNELSEIITLEITKLIKEiiNIIEEELGI 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 315 --SPDTRLLEDLSVHLSGALARISRGMTIPNPYTEEIKRNFPMAFDAAAQLSMAVAKRYHVTLNDDESGFLALHFESFFE 392
Cdd:COG3711   305 dlDEDSLLYERLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALE 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 393 RQHAADRISTVVVCSSGVGTSRLLAQRLEERFREkLVITRTIGLADLMRQTIPET-LIISTVPIQGMrqPVVIVNPLLLQ 471
Cdd:COG3711   385 RQKESKKKRVLVVCSSGIGTSRLLKSRLKKLFPE-IEIIDVISYRELEEIDLEDYdLIISTVPLEDK--PVIVVSPLLTE 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 472 HDIEKVAQQADRLRFGTDgdaflslldpKLVLPNLPQTDQHAAMQVMIRQLTKNGVFEDETLPLKLAEDREKLATTAMRL 551
Cdd:COG3711   462 EDIEKIRKFLKQIKKKLA----------KILFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEELEEII 531
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 1206084635 552 VAIPHISPEMVQRPAIALGLAPEGIEWSGQKVKVVFFLALN 592
Cdd:COG3711   532 IIIVIAIPIIIIIIIAIIVLAAEEPGVIKLILVLLLLLILI 572
 
Name Accession Description Interval E-value
BglG COG3711
Transcriptional antiterminator [Transcription];
8-592 8.50e-94

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 301.78  E-value: 8.50e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635   8 ILDFLLKH-GTVHYDQIAEATGLSERTVGNYLNRLDADLSPYAVKLVRKRNVGVSLDGPADQKAHLLRSIHGQEGFTSQT 86
Cdd:COG3711     1 ILKILLKNnNVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDDEQKEKLLQLLEKSEDPLSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635  87 AREHYLMIKLLLTNRPYTLSKLADDLFVSRRTIDNDFKSVKRVFRENHVTVQTSR-TGIQVTASESRRRHMLAKLLRGYW 165
Cdd:COG3711    81 ERVAYILLRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPnYGIKLEGSELDIRKALAELLSELL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 166 GESlsvakqkdgevvqqIQLPAYLNHLVNPATTKAVMQSLAEFLKQSDLIFSDYVLQSLAIHLIIACERpKKAAPAPVHP 245
Cdd:COG3711   161 SEN--------------DLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKR-IKKGKYIKLD 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 246 APLLPETK---------QLLTLVTKHVHRTLDNADAQQINAHIAAILdRQVSDAPAASIEEQAAPVLRQ--QIAGWLTGI 314
Cdd:COG3711   226 NPLLWEIKkpkeyeiakEILKLIEERLGISLPEDEIGYIALHLLGAR-LNNDNELSEIITLEITKLIKEiiNIIEEELGI 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 315 --SPDTRLLEDLSVHLSGALARISRGMTIPNPYTEEIKRNFPMAFDAAAQLSMAVAKRYHVTLNDDESGFLALHFESFFE 392
Cdd:COG3711   305 dlDEDSLLYERLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALE 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 393 RQHAADRISTVVVCSSGVGTSRLLAQRLEERFREkLVITRTIGLADLMRQTIPET-LIISTVPIQGMrqPVVIVNPLLLQ 471
Cdd:COG3711   385 RQKESKKKRVLVVCSSGIGTSRLLKSRLKKLFPE-IEIIDVISYRELEEIDLEDYdLIISTVPLEDK--PVIVVSPLLTE 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 472 HDIEKVAQQADRLRFGTDgdaflslldpKLVLPNLPQTDQHAAMQVMIRQLTKNGVFEDETLPLKLAEDREKLATTAMRL 551
Cdd:COG3711   462 EDIEKIRKFLKQIKKKLA----------KILFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEELEEII 531
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 1206084635 552 VAIPHISPEMVQRPAIALGLAPEGIEWSGQKVKVVFFLALN 592
Cdd:COG3711   532 IIIVIAIPIIIIIIIAIIVLAAEEPGVIKLILVLLLLLILI 572
PTS_IIB_bgl_like cd05568
PTS_IIB_bgl_like: the PTS (phosphotransferase system) IIB domain of a family of sensory ...
400-484 5.67e-19

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: 81.78  E-value: 5.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 400 ISTVVVCSSGVGTSRLLAQRLEERFREKLVItRTIGLADLMRQTIPET-LIISTVPIQGMRQPVVIVNPLLLQHDIEKVA 478
Cdd:cd05568     1 KKALVVCPSGIGTSRLLKSKLKKLFPEIEII-DVISLRELEEVDLDDYdLIISTVPLEDTDKPVIVVSPILTEEDIKKIR 79

                  ....*.
gi 1206084635 479 QQADRL 484
Cdd:cd05568    80 KFIKKL 85
PTS_EIIA_2 pfam00359
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
496-633 1.30e-18

Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;


Pssm-ID: 459780 [Multi-domain]  Cd Length: 139  Bit Score: 82.64  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 496 LLDPKLVLPNLPQTDQHAAMQVMIRQLTKNGVFEDetlplKLAED---REKLATTAMR-LVAIPHISPEMVQRPAIALGL 571
Cdd:pfam00359   1 LLDKELIFLNLEAKSKEEAIEFLADKLVEAGYVEP-----AYLEAileREKEGSTGIGnGIAIPHARSEAVKKPGIAVLT 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1206084635 572 APEGIEWS---GQKVKVVFFLalnaAAPDDQR---RIYQVMNRMIDDRLFCEKLAQSPTPASALRILS 633
Cdd:pfam00359  76 LKEPVDFGsedGKPVKLIFLL----AAPDNEAshlKILSQLARLLQDEEFVEKLLKAKDPEEILEILK 139
fruA TIGR00848
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family ...
496-599 2.69e-11

PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Fru family is a large and complex family which includes several sequenced fructose and mannitol-specific permeases as well as several putative PTS permeases of unknown specificities. The fructose permeases of this family phosphorylate fructose on the 1-position. Those of family 4.6 phosphorylate fructose on the 6-position. The Fru family PTS systems typically have 3 domains, IIA, IIB and IIC, which may be found as 1 or more proteins. The fructose and mannitol transporters form separate phylogenetic clusters in this family. This model is specific for the IIA domain of the fructose PTS transporters. Also similar to the Enzyme IIA Fru subunits of the PTS, but included in TIGR01419 rather than this model, is enzyme IIA Ntr (nitrogen), also called PtsN, found in E. coli and other organisms, which may play a solely regulatory role. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]


Pssm-ID: 273298 [Multi-domain]  Cd Length: 129  Bit Score: 61.14  E-value: 2.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 496 LLDPKLVLPNLPQTDQHAAMQVMIRQLTKNGVFEDETLPLKLAEDREKLATTAMRL-VAIPHISPEMVQRPAIALGLAPE 574
Cdd:TIGR00848   1 LLNKDLIFLDQQFTSKEDVIKFLANKLLENGYISDTEEFLEDLLKREEEGTTGIGDgVAIPHAKSAAVKQPFVAIARLVK 80
                          90       100
                  ....*....|....*....|....*...
gi 1206084635 575 GIEWS---GQKVKVVFFLALNAAAPDDQ 599
Cdd:TIGR00848  81 GVDWQsldGKPVKLIFLIAVPKDEAGNT 108
PRK09765 PRK09765
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional
493-634 9.05e-07

PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional


Pssm-ID: 182066 [Multi-domain]  Cd Length: 631  Bit Score: 52.04  E-value: 9.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 493 FLSLLDPKLVLPNLPQTDQHAAMQVMIRQLTKNGVFEDETLPLKLAEDREKLATTAM-RLVAIPHISPEMVQRPAIALGL 571
Cdd:PRK09765    3 LTTLTHRDLLCLNARFTSREEAIHALAQRLAALGKISSTEQFLEEVYRRESLGPTALgEGLAVPHGKTAAVKEAAFAVAT 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1206084635 572 APEGIEWSG----QKVKVVFFLALnaaaPDDQ------RRIYQVMNRMIDDRLFcEKLAQSPTPASALRILSE 634
Cdd:PRK09765   83 LSEPLQWEGvdgpEAVDLIFLLAI----PPNEagtthmQLLTALTTRLADDEIR-ARIQSATTPDELLSALDD 150
 
Name Accession Description Interval E-value
BglG COG3711
Transcriptional antiterminator [Transcription];
8-592 8.50e-94

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 301.78  E-value: 8.50e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635   8 ILDFLLKH-GTVHYDQIAEATGLSERTVGNYLNRLDADLSPYAVKLVRKRNVGVSLDGPADQKAHLLRSIHGQEGFTSQT 86
Cdd:COG3711     1 ILKILLKNnNVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDDEQKEKLLQLLEKSEDPLSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635  87 AREHYLMIKLLLTNRPYTLSKLADDLFVSRRTIDNDFKSVKRVFRENHVTVQTSR-TGIQVTASESRRRHMLAKLLRGYW 165
Cdd:COG3711    81 ERVAYILLRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPnYGIKLEGSELDIRKALAELLSELL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 166 GESlsvakqkdgevvqqIQLPAYLNHLVNPATTKAVMQSLAEFLKQSDLIFSDYVLQSLAIHLIIACERpKKAAPAPVHP 245
Cdd:COG3711   161 SEN--------------DLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKR-IKKGKYIKLD 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 246 APLLPETK---------QLLTLVTKHVHRTLDNADAQQINAHIAAILdRQVSDAPAASIEEQAAPVLRQ--QIAGWLTGI 314
Cdd:COG3711   226 NPLLWEIKkpkeyeiakEILKLIEERLGISLPEDEIGYIALHLLGAR-LNNDNELSEIITLEITKLIKEiiNIIEEELGI 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 315 --SPDTRLLEDLSVHLSGALARISRGMTIPNPYTEEIKRNFPMAFDAAAQLSMAVAKRYHVTLNDDESGFLALHFESFFE 392
Cdd:COG3711   305 dlDEDSLLYERLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALE 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 393 RQHAADRISTVVVCSSGVGTSRLLAQRLEERFREkLVITRTIGLADLMRQTIPET-LIISTVPIQGMrqPVVIVNPLLLQ 471
Cdd:COG3711   385 RQKESKKKRVLVVCSSGIGTSRLLKSRLKKLFPE-IEIIDVISYRELEEIDLEDYdLIISTVPLEDK--PVIVVSPLLTE 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 472 HDIEKVAQQADRLRFGTDgdaflslldpKLVLPNLPQTDQHAAMQVMIRQLTKNGVFEDETLPLKLAEDREKLATTAMRL 551
Cdd:COG3711   462 EDIEKIRKFLKQIKKKLA----------KILFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEELEEII 531
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 1206084635 552 VAIPHISPEMVQRPAIALGLAPEGIEWSGQKVKVVFFLALN 592
Cdd:COG3711   532 IIIVIAIPIIIIIIIAIIVLAAEEPGVIKLILVLLLLLILI 572
PtsN COG1762
Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate ...
495-635 1.32e-23

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: 97.23  E-value: 1.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 495 SLLDPKLVLPNLPQTDQHAAMQVMIRQLTKNGVFEDETLPLKLAEDREKLATTAM-RLVAIPHISPEMVQRPAIALGLAP 573
Cdd:COG1762     5 DLLTPELILLDLEASSKEEAIEELAELLAEKGYVLDKEEYLEALLEREELGSTGIgPGIAIPHARPEGVKKPGIAVARLK 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1206084635 574 EGIEWS---GQKVKVVFFLALNAAAPDDQRRIYQVMNRMIDDRLFCEKLAQSPTPASALRILSEY 635
Cdd:COG1762    85 EPVDFGamdGEPVDLVFLLAAPEDDSEEHLKLLAELARLLSDEEFREKLLNAKSPEEILELLKEA 149
PTS_IIB_bgl_like cd05568
PTS_IIB_bgl_like: the PTS (phosphotransferase system) IIB domain of a family of sensory ...
400-484 5.67e-19

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: 81.78  E-value: 5.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 400 ISTVVVCSSGVGTSRLLAQRLEERFREKLVItRTIGLADLMRQTIPET-LIISTVPIQGMRQPVVIVNPLLLQHDIEKVA 478
Cdd:cd05568     1 KKALVVCPSGIGTSRLLKSKLKKLFPEIEII-DVISLRELEEVDLDDYdLIISTVPLEDTDKPVIVVSPILTEEDIKKIR 79

                  ....*.
gi 1206084635 479 QQADRL 484
Cdd:cd05568    80 KFIKKL 85
PTS_EIIA_2 pfam00359
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
496-633 1.30e-18

Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;


Pssm-ID: 459780 [Multi-domain]  Cd Length: 139  Bit Score: 82.64  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 496 LLDPKLVLPNLPQTDQHAAMQVMIRQLTKNGVFEDetlplKLAED---REKLATTAMR-LVAIPHISPEMVQRPAIALGL 571
Cdd:pfam00359   1 LLDKELIFLNLEAKSKEEAIEFLADKLVEAGYVEP-----AYLEAileREKEGSTGIGnGIAIPHARSEAVKKPGIAVLT 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1206084635 572 APEGIEWS---GQKVKVVFFLalnaAAPDDQR---RIYQVMNRMIDDRLFCEKLAQSPTPASALRILS 633
Cdd:pfam00359  76 LKEPVDFGsedGKPVKLIFLL----AAPDNEAshlKILSQLARLLQDEEFVEKLLKAKDPEEILEILK 139
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
317-389 3.93e-16

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: 73.83  E-value: 3.93e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1206084635 317 DTRLLEDLSVHLSGALARISRGMTIPNPYTEEIKRNFPMAFDAAAQLSMAVAKRYHVTLNDDESGFLALHFES 389
Cdd:pfam00874  17 DDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIGYIALHFLS 89
PTS_IIA_fru cd00211
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: ...
497-632 3.73e-13

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: 66.82  E-value: 3.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 497 LDPKLVLPNLPQTDQHAAMQVMIRQLTKNGVFEDETLplKLAEDREKLATTAM-RLVAIPHISPEMVQRPAIALGLAPEG 575
Cdd:cd00211     1 LTKENIRLNLKAKSKEEAIEELAQLLVAAGYVEEEYI--EALLEREKEGSTGIgNGIAIPHAKSEAVKKPGIAVLRLKEP 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 576 IEWS---GQKVKVVFFLAlnAAAPDDQRRIYQVMNRMIDDRLFCEKLAQSPTPASALRIL 632
Cdd:cd00211    79 VDFGsldGQPVHLIFLLA--APDSNEHLKALSQLARLLSDEEFVEQLLNAQSKEEILALL 136
PTS_IIB cd00133
PTS_IIB: subunit IIB of enzyme II (EII) is the central energy-coupling domain of the ...
403-481 1.11e-11

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: 61.12  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 403 VVVCSSGVGTSRLLAQRLEERFrEKLVITRTIGLADLMRQTIPET--LIISTVPIQGMRQ--PVVIVNPLLLQHDIEKVA 478
Cdd:cd00133     3 LVVCGSGIGSSSMLAEKLEKAA-KELGIEVKVEAQGLSEVIDLADadLIISTVPLAARFLgkPVIVVSPLLNEKDGEKIL 81

                  ...
gi 1206084635 479 QQA 481
Cdd:cd00133    82 EKL 84
fruA TIGR00848
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family ...
496-599 2.69e-11

PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Fru family is a large and complex family which includes several sequenced fructose and mannitol-specific permeases as well as several putative PTS permeases of unknown specificities. The fructose permeases of this family phosphorylate fructose on the 1-position. Those of family 4.6 phosphorylate fructose on the 6-position. The Fru family PTS systems typically have 3 domains, IIA, IIB and IIC, which may be found as 1 or more proteins. The fructose and mannitol transporters form separate phylogenetic clusters in this family. This model is specific for the IIA domain of the fructose PTS transporters. Also similar to the Enzyme IIA Fru subunits of the PTS, but included in TIGR01419 rather than this model, is enzyme IIA Ntr (nitrogen), also called PtsN, found in E. coli and other organisms, which may play a solely regulatory role. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]


Pssm-ID: 273298 [Multi-domain]  Cd Length: 129  Bit Score: 61.14  E-value: 2.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 496 LLDPKLVLPNLPQTDQHAAMQVMIRQLTKNGVFEDETLPLKLAEDREKLATTAMRL-VAIPHISPEMVQRPAIALGLAPE 574
Cdd:TIGR00848   1 LLNKDLIFLDQQFTSKEDVIKFLANKLLENGYISDTEEFLEDLLKREEEGTTGIGDgVAIPHAKSAAVKQPFVAIARLVK 80
                          90       100
                  ....*....|....*....|....*...
gi 1206084635 575 GIEWS---GQKVKVVFFLALNAAAPDDQ 599
Cdd:TIGR00848  81 GVDWQsldGKPVKLIFLIAVPKDEAGNT 108
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
324-394 8.22e-09

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 58.98  E-value: 8.22e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1206084635 324 LSVHLSGALARISRGMTIPNPYTEEIKRNFPMAFDAAAQLSMAVAKRYHVTLNDDESGFLALHFESFFERQ 394
Cdd:COG3933   484 LSLHLSSFIERIKEGKEIINPNLNEIKKKYPKEFKVAKEIKELIEQELDIEIPEDEVGFLTLFLVSLNENN 554
PRK09765 PRK09765
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional
493-634 9.05e-07

PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional


Pssm-ID: 182066 [Multi-domain]  Cd Length: 631  Bit Score: 52.04  E-value: 9.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 493 FLSLLDPKLVLPNLPQTDQHAAMQVMIRQLTKNGVFEDETLPLKLAEDREKLATTAM-RLVAIPHISPEMVQRPAIALGL 571
Cdd:PRK09765    3 LTTLTHRDLLCLNARFTSREEAIHALAQRLAALGKISSTEQFLEEVYRRESLGPTALgEGLAVPHGKTAAVKEAAFAVAT 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1206084635 572 APEGIEWSG----QKVKVVFFLALnaaaPDDQ------RRIYQVMNRMIDDRLFcEKLAQSPTPASALRILSE 634
Cdd:PRK09765   83 LSEPLQWEGvdgpEAVDLIFLLAI----PPNEagtthmQLLTALTTRLADDEIR-ARIQSATTPDELLSALDD 150
PRK09913 PRK09913
PTS fructose transporter subunit IIA;
505-624 7.86e-05

PTS fructose transporter subunit IIA;


Pssm-ID: 182141 [Multi-domain]  Cd Length: 148  Bit Score: 43.34  E-value: 7.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 505 NLPQTDQHAAMQVMIRQLTKNGVFEDETLPLKLAEDREKLATTAM-RLVAIPHISPEMVQRPAIALGLAPEGIEWS---G 580
Cdd:PRK09913   12 NIQGNGAYSILKQLATIALQNGFITDSHQFLQTLLLREKMHSTGFgSGVAVPHGKSACVKQPFVLFARKAQAIDWQasdG 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1206084635 581 QKVKVVFFLALNAAAPDDQRRIYQVMNRMIDDRLFCEKLAQSPT 624
Cdd:PRK09913   92 EDVNCWICLGVPQSGEEDQVKIIGTLCRKIIHQDFIHQLKQGDT 135
PTS_IIB pfam02302
PTS system, Lactose/Cellobiose specific IIB subunit; The bacterial phosphoenolpyruvate: sugar ...
403-480 2.54e-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: 40.39  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206084635 403 VVVCSSGVGTSRLLAQRLEERFREKLVITRTI--GLADLMRQTIPET--LIISTVPI--------QGMRQPVVIVNPLLL 470
Cdd:pfam02302   3 LTACGAGMATSLMAAEALEKAAKELGIVEAQGaaGVNELTAEDIADDadVVILAPDVavedlarfAGKPVYVIPVKDALG 82
                          90
                  ....*....|
gi 1206084635 471 QHDIEKVAQQ 480
Cdd:pfam02302  83 MKDAEEVLEK 92
PRK09772 PRK09772
transcriptional antiterminator BglG; Provisional
324-389 2.61e-04

transcriptional antiterminator BglG; Provisional


Pssm-ID: 170086 [Multi-domain]  Cd Length: 278  Bit Score: 43.16  E-value: 2.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1206084635 324 LSVHLSGALARISRGMTIPNPYTEEIKRNFPMAFDAAAQLSMAVAKRYHVTLNDDESGFLALHFES 389
Cdd:PRK09772   98 LTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHLVS 163
HTH_Mga pfam08280
M protein trans-acting positive regulator (MGA) HTH domain; Mga is a DNA-binding protein that ...
5-41 6.76e-03

M protein trans-acting positive regulator (MGA) HTH domain; 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.


Pssm-ID: 311953 [Multi-domain]  Cd Length: 59  Bit Score: 35.28  E-value: 6.76e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1206084635   5 KLLILDFLLKHGTVHYDQIAEATGLSERTVGNYLNRL 41
Cdd:pfam08280   7 KLKLLELLTENKWITLDELAEELGLSELTLKSDISEL 43
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
3-41 6.88e-03

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 34.72  E-value: 6.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1206084635   3 DKKLLILDFLLKHGTVHYDQIAEATGLSERTVGNYLNRL 41
Cdd:pfam13412   1 ETDRKILNLLQENPRISQRELAERLGLSPSTVNRRLKRL 39
 
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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