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Conserved domains on  [gi|1731153413|ref|WP_148411517|]
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transcription antiterminator [Enterococcus sp. T0168A.B-11]

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];
8-659 2.68e-111

Transcriptional antiterminator [Transcription];


:

Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 348.00  E-value: 2.68e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413   8 LLRYLIDHrKEYVTSQRLASELLLSDRTIRNYLQRIKELVEENGGKIIAKPGYGYQLHILQRLtfdlflsrQEIVPGYAR 87
Cdd:COG3711     1 ILKILLKN-NNVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDDEQ--------KEKLLQLLE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413  88 EPQGFYESEDRQKYILNQLLLEDAILFMDDLAEELYISRSSLTKDMQEIKERLISYSLKIVSKHGQGIWIEGEERNRRHF 167
Cdd:COG3711    72 KSEDPLSPKERVAYILLRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNYGIKLEGSELDIRKA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 168 IMDTFFGNHYGNSLKEYLGQSrFFTDISFEELVIIILDETREAKLKVSDFIIQNLSLHLALGIKRLREGFEIKELGIE-Q 246
Cdd:COG3711   152 LAELLSELLSENDLLSLLLLK-LIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLlW 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 247 EVSDRVEYQVAQRIVQRIEVIADVSFPQEEIAYLTLHLMA----KSNHRENKNDQELSKEVAKVLKRLSQEFRFSLIEDH 322
Cdd:COG3711   231 EIKKPKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGarlnNDNELSEIITLEITKLIKEIINIIEEELGIDLDEDS 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 323 QLFNGLLDHLSPMMIRLSRGIRIENPLTEEIKEENPKVFEAVKTHFSNMPALKNYTINEDEWAYLALHLMAALEKERATH 402
Cdd:COG3711   311 LLYERLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKESK 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 403 KLHALIICATGYGSAQLLKNRVVSEFgKNITVVNVKGYYEINETTLKGIDLIISSIDLStmffKIPVLHVSIFLNEDDVH 482
Cdd:COG3711   391 KKRVLVVCSSGIGTSRLLKSRLKKLF-PEIEIIDVISYRELEEIDLEDYDLIISTVPLE----DKPVIVVSPLLTEEDIE 465

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 483 KIRKVIgesipyhssdrpipafslqQKKQIYTEQLSEKFFKTYTYEPKKEEVLHDLLQKLSINEEEGYIREMRKQIQQRE 562
Cdd:COG3711   466 KIRKFL-------------------KQIKKKLAKILFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEE 526

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 563 SMGQIIfsdtvaVPHPAVPVGIETKIAVALIPSVMQWNQYQGIHFVFLVSPSYIENEGITVVTKAIVRLVDQLNVQQEIL 642
Cdd:COG3711   527 LEEIII------IIVIAIPIIIIIIIAIIVLAAEEPGVIKLILVLLLLLILIILLEDDEALLVILLLLLLLIESSLLLLL 600

                         650
                  ....*....|....*..
gi 1731153413 643 AEPIFKNFSSKFIKLIE 659
Cdd:COG3711   601 LLELLLELELELLILLL 617
 
Name Accession Description Interval E-value
BglG COG3711
Transcriptional antiterminator [Transcription];
8-659 2.68e-111

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 348.00  E-value: 2.68e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413   8 LLRYLIDHrKEYVTSQRLASELLLSDRTIRNYLQRIKELVEENGGKIIAKPGYGYQLHILQRLtfdlflsrQEIVPGYAR 87
Cdd:COG3711     1 ILKILLKN-NNVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDDEQ--------KEKLLQLLE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413  88 EPQGFYESEDRQKYILNQLLLEDAILFMDDLAEELYISRSSLTKDMQEIKERLISYSLKIVSKHGQGIWIEGEERNRRHF 167
Cdd:COG3711    72 KSEDPLSPKERVAYILLRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNYGIKLEGSELDIRKA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 168 IMDTFFGNHYGNSLKEYLGQSrFFTDISFEELVIIILDETREAKLKVSDFIIQNLSLHLALGIKRLREGFEIKELGIE-Q 246
Cdd:COG3711   152 LAELLSELLSENDLLSLLLLK-LIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLlW 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 247 EVSDRVEYQVAQRIVQRIEVIADVSFPQEEIAYLTLHLMA----KSNHRENKNDQELSKEVAKVLKRLSQEFRFSLIEDH 322
Cdd:COG3711   231 EIKKPKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGarlnNDNELSEIITLEITKLIKEIINIIEEELGIDLDEDS 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 323 QLFNGLLDHLSPMMIRLSRGIRIENPLTEEIKEENPKVFEAVKTHFSNMPALKNYTINEDEWAYLALHLMAALEKERATH 402
Cdd:COG3711   311 LLYERLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKESK 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 403 KLHALIICATGYGSAQLLKNRVVSEFgKNITVVNVKGYYEINETTLKGIDLIISSIDLStmffKIPVLHVSIFLNEDDVH 482
Cdd:COG3711   391 KKRVLVVCSSGIGTSRLLKSRLKKLF-PEIEIIDVISYRELEEIDLEDYDLIISTVPLE----DKPVIVVSPLLTEEDIE 465

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 483 KIRKVIgesipyhssdrpipafslqQKKQIYTEQLSEKFFKTYTYEPKKEEVLHDLLQKLSINEEEGYIREMRKQIQQRE 562
Cdd:COG3711   466 KIRKFL-------------------KQIKKKLAKILFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEE 526

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 563 SMGQIIfsdtvaVPHPAVPVGIETKIAVALIPSVMQWNQYQGIHFVFLVSPSYIENEGITVVTKAIVRLVDQLNVQQEIL 642
Cdd:COG3711   527 LEEIII------IIVIAIPIIIIIIIAIIVLAAEEPGVIKLILVLLLLLILIILLEDDEALLVILLLLLLLIESSLLLLL 600

                         650
                  ....*....|....*..
gi 1731153413 643 AEPIFKNFSSKFIKLIE 659
Cdd:COG3711   601 LLELLLELELELLILLL 617
PTS_IIB_bgl_like cd05568
PTS_IIB_bgl_like: the PTS (phosphotransferase system) IIB domain of a family of sensory ...
 404-488 8.13e-20

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: 84.09  E-value: 8.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 404 LHALIICATGYGSAQLLKNRVVSEFGkNITVVNVKGYYEINETTLKGIDLIISSIDLStmFFKIPVLHVSIFLNEDDVHK 483
Cdd:cd05568     1 KKALVVCPSGIGTSRLLKSKLKKLFP-EIEIIDVISLRELEEVDLDDYDLIISTVPLE--DTDKPVIVVSPILTEEDIKK 77


                  ....*
gi 1731153413 484 IRKVI 488
Cdd:cd05568    78 IRKFI 82
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 305-394 5.19e-14

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: 67.66  E-value: 5.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 305 KVLKRLSQEFRFSLiEDHQLFNGLLDHLSPMMIRLSRGIRIENPLTEEIKEENPKVFEAVKTHFSNMPALKNYTINEDEW 384
Cdd:pfam00874   2 EIIELIEKKLGITF-DDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEI 80

                          90
                  ....*....|
gi 1731153413 385 AYLALHLMAA 394
Cdd:pfam00874  81 GYIALHFLSA 90
Trans_reg_C smart00862
Transcriptional regulatory protein, C terminal; This domain is almost always found associated ...
 4-64 3.84e-04

Transcriptional regulatory protein, C terminal; This domain is almost always found associated with the response regulator receiver domain. It may play a role in DNA binding.


Pssm-ID: 214866 [Multi-domain]  Cd Length: 76  Bit Score: 39.46  E-value: 3.84e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1731153413    4 KEKLLLRYLIDHRKEYVTSQRLASEL-----LLSDRTIRNYLQRIKELVEENGGK--IIAKPGYGYQL 64
Cdd:smart00862   9 KEFRLLELLLRNPGRVVSREELLEAVwgddeDVDDNTLDVHISRLRKKLEDDGDPrlIETVRGVGYRL 76
PRK09765 PRK09765
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional
 531-633 6.87e-04

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


Pssm-ID: 182066 [Multi-domain]  Cd Length: 631  Bit Score: 42.80  E-value: 6.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 531 KEEVLHDLLQKL----SINEEEGYIREmrkqIQQRESMGQIIFSDTVAVPHPAVPVGIETKIAVALIPSVMQWNQYQG-- 604
Cdd:PRK09765   21 REEAIHALAQRLaalgKISSTEQFLEE----VYRRESLGPTALGEGLAVPHGKTAAVKEAAFAVATLSEPLQWEGVDGpe 96

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1731153413 605 -IHFVFL--VSPSYIENEGITVVTKAIVRLVD 633
Cdd:PRK09765   97 aVDLIFLlaIPPNEAGTTHMQLLTALTTRLAD 128
fruA TIGR00848
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family ...
 531-600 3.06e-03

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: 38.41  E-value: 3.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1731153413 531 KEEVLHDLLQKLSINeeeGYIREMR---KQIQQRESMGQIIFSDTVAVPHPAVPVGIETKIAVALIPSVMQWN 600
Cdd:TIGR00848  16 KEDVIKFLANKLLEN---GYISDTEeflEDLLKREEEGTTGIGDGVAIPHAKSAAVKQPFVAIARLVKGVDWQ 85
 
Name Accession Description Interval E-value
BglG COG3711
Transcriptional antiterminator [Transcription];
8-659 2.68e-111

Transcriptional antiterminator [Transcription];


Pssm-ID: 442925 [Multi-domain]  Cd Length: 618  Bit Score: 348.00  E-value: 2.68e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413   8 LLRYLIDHrKEYVTSQRLASELLLSDRTIRNYLQRIKELVEENGGKIIAKPGYGYQLHILQRLtfdlflsrQEIVPGYAR 87
Cdd:COG3711     1 ILKILLKN-NNVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDDEQ--------KEKLLQLLE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413  88 EPQGFYESEDRQKYILNQLLLEDAILFMDDLAEELYISRSSLTKDMQEIKERLISYSLKIVSKHGQGIWIEGEERNRRHF 167
Cdd:COG3711    72 KSEDPLSPKERVAYILLRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNYGIKLEGSELDIRKA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 168 IMDTFFGNHYGNSLKEYLGQSrFFTDISFEELVIIILDETREAKLKVSDFIIQNLSLHLALGIKRLREGFEIKELGIE-Q 246
Cdd:COG3711   152 LAELLSELLSENDLLSLLLLK-LIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLlW 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 247 EVSDRVEYQVAQRIVQRIEVIADVSFPQEEIAYLTLHLMA----KSNHRENKNDQELSKEVAKVLKRLSQEFRFSLIEDH 322
Cdd:COG3711   231 EIKKPKEYEIAKEILKLIEERLGISLPEDEIGYIALHLLGarlnNDNELSEIITLEITKLIKEIINIIEEELGIDLDEDS 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 323 QLFNGLLDHLSPMMIRLSRGIRIENPLTEEIKEENPKVFEAVKTHFSNMPALKNYTINEDEWAYLALHLMAALEKERATH 402
Cdd:COG3711   311 LLYERLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKESK 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 403 KLHALIICATGYGSAQLLKNRVVSEFgKNITVVNVKGYYEINETTLKGIDLIISSIDLStmffKIPVLHVSIFLNEDDVH 482
Cdd:COG3711   391 KKRVLVVCSSGIGTSRLLKSRLKKLF-PEIEIIDVISYRELEEIDLEDYDLIISTVPLE----DKPVIVVSPLLTEEDIE 465

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 483 KIRKVIgesipyhssdrpipafslqQKKQIYTEQLSEKFFKTYTYEPKKEEVLHDLLQKLSINEEEGYIREMRKQIQQRE 562
Cdd:COG3711   466 KIRKFL-------------------KQIKKKLAKILFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEE 526

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 563 SMGQIIfsdtvaVPHPAVPVGIETKIAVALIPSVMQWNQYQGIHFVFLVSPSYIENEGITVVTKAIVRLVDQLNVQQEIL 642
Cdd:COG3711   527 LEEIII------IIVIAIPIIIIIIIAIIVLAAEEPGVIKLILVLLLLLILIILLEDDEALLVILLLLLLLIESSLLLLL 600

                         650
                  ....*....|....*..
gi 1731153413 643 AEPIFKNFSSKFIKLIE 659
Cdd:COG3711   601 LLELLLELELELLILLL 617
PTS_IIB_bgl_like cd05568
PTS_IIB_bgl_like: the PTS (phosphotransferase system) IIB domain of a family of sensory ...
 404-488 8.13e-20

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: 84.09  E-value: 8.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 404 LHALIICATGYGSAQLLKNRVVSEFGkNITVVNVKGYYEINETTLKGIDLIISSIDLStmFFKIPVLHVSIFLNEDDVHK 483
Cdd:cd05568     1 KKALVVCPSGIGTSRLLKSKLKKLFP-EIEIIDVISLRELEEVDLDDYDLIISTVPLE--DTDKPVIVVSPILTEEDIKK 77


                  ....*
gi 1731153413 484 IRKVI 488
Cdd:cd05568    78 IRKFI 82
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 305-394 5.19e-14

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: 67.66  E-value: 5.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 305 KVLKRLSQEFRFSLiEDHQLFNGLLDHLSPMMIRLSRGIRIENPLTEEIKEENPKVFEAVKTHFSNMPALKNYTINEDEW 384
Cdd:pfam00874   2 EIIELIEKKLGITF-DDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEI 80

                          90
                  ....*....|
gi 1731153413 385 AYLALHLMAA 394
Cdd:pfam00874  81 GYIALHFLSA 90
PTS_IIB cd00133
PTS_IIB: subunit IIB of enzyme II (EII) is the central energy-coupling domain of the ...
 405-488 1.31e-13

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: 66.51  E-value: 1.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 405 HALIICATGYGSAQLLKNRVVSEFGKNITVVNVKgYYEINE-TTLKGIDLIISSIDLSTMFFKIPVLHVSIFLNEDDVHK 483
Cdd:cd00133     1 KILVVCGSGIGSSSMLAEKLEKAAKELGIEVKVE-AQGLSEvIDLADADLIISTVPLAARFLGKPVIVVSPLLNEKDGEK 79


                  ....*
gi 1731153413 484 IRKVI 488
Cdd:cd00133    80 ILEKL 84
PRD pfam00874
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ...
 214-286 1.26e-08

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: 52.64  E-value: 1.26e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1731153413 214 VSDFIIQNLSLHLALGIKRLREGFEIKELgIEQEVSD--RVEYQVAQRIVQRIEVIADVSFPQEEIAYLTLHLMA 286
Cdd:pfam00874  16 DDDILYIRLILHLAFAIERIKEGITIENP-LLEEIKEkyPKEFEIAKKILEILEEELGIELPEDEIGYIALHFLS 89
HTH_11 pfam08279
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
 8-62 1.13e-06

HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.


Pssm-ID: 429896 [Multi-domain]  Cd Length: 52  Bit Score: 45.89  E-value: 1.13e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1731153413   8 LLRYLIDHRkEYVTSQRLASELLLSDRTIRNYLQRIKELveenGGKIIAKPGYGY 62
Cdd:pfam08279   3 ILQLLLEAR-GPISGQELAEKLGVSRRTIRRDIKILEEL----GVPIEAEPGRGY 52
Mga pfam05043
Mga helix-turn-helix domain; M regulator protein trans-acting positive regulator (Mga) is a ...
 96-172 3.33e-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: 42.60  E-value: 3.33e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1731153413  96 EDRQKYILNQLLLEDAILFMDDLAEELYISRSSLTKDMQEIKERLISYSLKIVSKHGQgiwIEGEERNRRHFIMDTF 172
Cdd:pfam05043  14 KESLKFQLLKYLFFEEFVSIKSLAQKLYISESTLYRKIKELNKLLKEFDLSIKKKNLK---LIGDEKQIRYFYALLF 87
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
99-297 1.30e-04

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 45.11  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413  99 QKYILNQLLLEDAILFMDDLAEELYISRSSLTKDMQEIKERLISYSLKIVSKHGqgiwiEGEERNRRHFIMDT------F 172
Cdd:COG3933   362 LNERLLLLELKILIEPLDIFFDSSASSDESDESEEDENLYEIIEIKKKLLLELG-----IDEEEINIIIEIDIdvhllkF 436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 173 FGNHYGNSLKEYLGQSRFFTDISFEELVIIILDEtrEAKLKVSDFIIQNLSLHLALGIKRLREGFEIKELGIEQEVSDRV 252
Cdd:COG3933   437 IYDDNKNFNKEELAKIVDEDIINVVEEILELAEK--KLGRKFSENFIYALSLHLSSFIERIKEGKEIINPNLNEIKKKYP 514

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1731153413 253 -EYQVAQRIVQRIEVIADVSFPQEEIAYLTLHLmaKSNHRENKNDQ 297
Cdd:COG3933   515 kEFKVAKEIKELIEQELDIEIPEDEVGFLTLFL--VSLNENNESGK 558
Trans_reg_C pfam00486
Transcriptional regulatory protein, C terminal;
4-64 3.63e-04

Transcriptional regulatory protein, C terminal;


Pssm-ID: 425712 [Multi-domain]  Cd Length: 77  Bit Score: 39.42  E-value: 3.63e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731153413   4 KEKLLLRYLIDHRKEYVTSQRLASEL-----LLSDRTIRNYLQRIKELVEENGGK---IIAKPGYGYQL 64
Cdd:pfam00486   9 KEFKLLELLAENPGRVVSREQLLEEVwgedyDVDDNTVDVHISRLRKKLEDDPRDprlIKTVRGVGYRL 77
Trans_reg_C smart00862
Transcriptional regulatory protein, C terminal; This domain is almost always found associated ...
 4-64 3.84e-04

Transcriptional regulatory protein, C terminal; This domain is almost always found associated with the response regulator receiver domain. It may play a role in DNA binding.


Pssm-ID: 214866 [Multi-domain]  Cd Length: 76  Bit Score: 39.46  E-value: 3.84e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1731153413    4 KEKLLLRYLIDHRKEYVTSQRLASEL-----LLSDRTIRNYLQRIKELVEENGGK--IIAKPGYGYQL 64
Cdd:smart00862   9 KEFRLLELLLRNPGRVVSREELLEAVwgddeDVDDNTLDVHISRLRKKLEDDGDPrlIETVRGVGYRL 76
PtsN COG1762
Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate ...
 531-643 4.19e-04

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: 40.99  E-value: 4.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 531 KEEVLHDLLQKLS----INEEEGYIREMRKqiqqRESMGQIIFSDTVAVPHPAVPVGIETKIAVALIPSVMQWNQYQG-- 604
Cdd:COG1762    21 KEEAIEELAELLAekgyVLDKEEYLEALLE----REELGSTGIGPGIAIPHARPEGVKKPGIAVARLKEPVDFGAMDGep 96

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1731153413 605 IHFVFLVSPSYIENEGITVVTKAIVRLVDQLNVQQEILA 643
Cdd:COG1762    97 VDLVFLLAAPEDDSEEHLKLLAELARLLSDEEFREKLLN 135
PTS_IIB pfam02302
PTS system, Lactose/Cellobiose specific IIB subunit; The bacterial phosphoenolpyruvate: sugar ...
 406-486 6.03e-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: 39.24  E-value: 6.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 406 ALIICATGYGSAQLLKNRVVSEFgKNITVVNVKGYYEINETTLKGI----DLIISSIDLST----MFFKIPVLHVSI--F 475
Cdd:pfam02302   2 ILTACGAGMATSLMAAEALEKAA-KELGIVEAQGAAGVNELTAEDIaddaDVVILAPDVAVedlaRFAGKPVYVIPVkdA 80

                          90
                  ....*....|.
gi 1731153413 476 LNEDDVHKIRK 486
Cdd:pfam02302  81 LGMKDAEEVLE 91
PRK09765 PRK09765
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional
 531-633 6.87e-04

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


Pssm-ID: 182066 [Multi-domain]  Cd Length: 631  Bit Score: 42.80  E-value: 6.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 531 KEEVLHDLLQKL----SINEEEGYIREmrkqIQQRESMGQIIFSDTVAVPHPAVPVGIETKIAVALIPSVMQWNQYQG-- 604
Cdd:PRK09765   21 REEAIHALAQRLaalgKISSTEQFLEE----VYRRESLGPTALGEGLAVPHGKTAAVKEAAFAVATLSEPLQWEGVDGpe 96

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1731153413 605 -IHFVFL--VSPSYIENEGITVVTKAIVRLVD 633
Cdd:PRK09765   97 aVDLIFLlaIPPNEAGTTHMQLLTALTTRLAD 128
YobV COG2378
Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains ...
 1-82 1.80e-03

Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains [Transcription];


Pssm-ID: 441945 [Multi-domain]  Cd Length: 314  Bit Score: 40.83  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413   1 MKQKEKL--LLRYLIDHRkeYVTSQRLASELLLSDRTIRNYLQRIKELveenGGKIIAKPG--YGYQLHILQRLTfDLFL 76
Cdd:COG2378     1 MSRLERLlaLLQLLQSRR--GVTAAELAERLEVSERTIYRDIDALREL----GVPIEAERGrgGGYRLRDGYRLP-PLML 73


                  ....*.
gi 1731153413  77 SRQEIV 82
Cdd:COG2378    74 TEEEAL 79
LevR COG3933
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
289-410 2.62e-03

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


Pssm-ID: 443134 [Multi-domain]  Cd Length: 916  Bit Score: 40.87  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 289 NHRENKNDQELSKEVAKVLKRLSQEFrFSLIE-------DHQLFNGLLDHLSPMMIRLSRGIRIENPLTEEIKEENPKVF 361
Cdd:COG3933   439 DDNKNFNKEELAKIVDEDIINVVEEI-LELAEkklgrkfSENFIYALSLHLSSFIERIKEGKEIINPNLNEIKKKYPKEF 517

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1731153413 362 EAVKtHFSNMPALK-NYTINEDEWAYLALhLMAALEKERATHKLHALIIC 410
Cdd:COG3933   518 KVAK-EIKELIEQElDIEIPEDEVGFLTL-FLVSLNENNESGKVGVIVLA 565
fruA TIGR00848
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family ...
 531-600 3.06e-03

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: 38.41  E-value: 3.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1731153413 531 KEEVLHDLLQKLSINeeeGYIREMR---KQIQQRESMGQIIFSDTVAVPHPAVPVGIETKIAVALIPSVMQWN 600
Cdd:TIGR00848  16 KEDVIKFLANKLLEN---GYISDTEeflEDLLKREEEGTTGIGDGVAIPHAKSAAVKQPFVAIARLVKGVDWQ 85
PTS_EIIA_2 pfam00359
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
517-611 3.19e-03

Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;


Pssm-ID: 459780 [Multi-domain]  Cd Length: 139  Bit Score: 38.34  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153413 517 LSEKFFKTYTYEPKKEEVLHDLLQKLsinEEEGYI-REMRKQIQQRESMGQIIFSDTVAVPHPAVPVGIETKIAVALIPS 595
Cdd:pfam00359   2 LDKELIFLNLEAKSKEEAIEFLADKL---VEAGYVePAYLEAILEREKEGSTGIGNGIAIPHARSEAVKKPGIAVLTLKE 78

                          90
                  ....*....|....*...
gi 1731153413 596 VMQWNQYQG--IHFVFLV 611
Cdd:pfam00359  79 PVDFGSEDGkpVKLIFLL 96
 
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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