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Conserved domains on  [gi|519083998|ref|WP_020239873|]
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MULTISPECIES: phosphoenolpyruvate--protein phosphotransferase [Escherichia]

Protein Classification

multiphosphoryl transfer protein( domain architecture ID 11449116)

multiphosphoryl transfer protein is a multifunctional protein that includes general (non sugar-specific) and sugar-specific components of the phosphoenolpyruvate-dependent sugar phosphotransferase system that catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PtsA COG1080
Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate ...
 117-680 0e+00

Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate transport and metabolism];


:

Pssm-ID: 440698 [Multi-domain]  Cd Length: 571  Bit Score: 656.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 117 LYGNVLASGVGVGTLTLLQSDSLD-SYRAIPASAQDS--TRLEHSLATLAEQLN---QQLRERDGESKT-ILSAHLSLIQ 189
Cdd:COG1080    1 LKGIAASPGIAIGKAFLLREEDLEvPEYTISPEDVEAeiARLEAALAKAREELEalrEKAPEDLGEEEAaIFDAHLLLLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 190 DDEFAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDIRDISEQLLHITWPElKPRNKLVLEKPTILVA 269
Cdd:COG1080   81 DPELIEEVEELIREGRYNAEWALKEVIEELAAQFEALDDEYLRERAADIRDVGRRVLRNLLGV-EAPDLSDLPEPVILVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 270 EDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPLDAIARYAGQPAVLDAQCGVLAINPNDAVSGYYQ 349
Cdd:COG1080  160 HDLTPSDTAQLDPSRVAGFVTDLGGRTSHTAILARSLGIPAVVGLGDALLLVKDGDLVIVDGDAGVVIVNPDEETLAEYR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 350 VAQTLADKRQKQQAQAAAQLAYSRDNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQQV 429
Cdd:COG1080  240 ERQAEYAAERAELARLRDLPAVTLDGVRVELAANIGLPEDAAAALENGAEGVGLFRTEFLFMDRDDLPTEEEQFEAYRAV 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 430 LLAAGDKPIIFRTMDIGGDKSIPYLNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQIL 509
Cdd:COG1080  320 AEAMGGRPVTIRTLDIGGDKPLPYLPLPKEENPFLGLRAIRLCLDRPELFRTQLRAILRASAHGNLRIMFPMISSVEELR 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 510 WVKGEIQKAIVELKRDGLRHAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPITPS 589
Cdd:COG1080  400 QAKALLEEAKAELRAEGIPFDEDIPVGIMIEVPAAALIADQLAKEVDFFSIGTNDLIQYTLAVDRGNEKVAYLYDPLHPA 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 590 FLRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDSEACRELARQACECRSAQE 669
Cdd:COG1080  480 VLRLIKMVIDAAHKAGKPVGVCGEMAGDPLATPLLLGLGLDELSMSPSSIPAVKAIIRRLDLAEARALAEKALALDTAEE 559

                        570
                 ....*....|.
gi 519083998 670 IEALLTAFTPE 680
Cdd:COG1080  560 VRALLEEFLAE 570
fruA TIGR00848
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family ...
 686-812 1.30e-51

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: 176.31  E-value: 1.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  686 LLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAK 765
Cdd:TIGR00848   1 LLNKDLIFLDQQFTSKEDVIKFLANKLLENGYISDTEEFLEDLLKREEEGTTGIGDGVAIPHAKSAAVKQPFVAIARLVK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 519083998  766 PIDWQSEMGE-VELVIMLTLG-ANEGMNHVKVFSQLARKLVNKNFRQSL 812
Cdd:TIGR00848  81 GVDWQSLDGKpVKLIFLIAVPkDEAGNTHLKALSQLARLLLNDEFRAKL 129
PtsH COG1925
HPr or related phosphotransfer protein [Signal transduction mechanisms, Carbohydrate transport ...
 1-87 6.05e-19

HPr or related phosphotransfer protein [Signal transduction mechanisms, Carbohydrate transport and metabolism];


:

Pssm-ID: 441528 [Multi-domain]  Cd Length: 88  Bit Score: 82.07  E-value: 6.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998   1 MLTIQFLCPLPNGLHARPAWELKEQCSQWQSEITFINhrQNAKADAKSSLALIGTGTLFNDSCSLNISGSDEEQARRVLE 80
Cdd:COG1925    1 MLEREVTIVNKLGLHARPAAKLVQLASKFDSEITVEK--GGKEVNAKSIMGLMSLGAKKGDEVTITAEGPDAEEALDALA 78


                 ....*..
gi 519083998  81 EYIQVRF 87
Cdd:COG1925   79 ALIESGF 85
 
Name Accession Description Interval E-value
PtsA COG1080
Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate ...
 117-680 0e+00

Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate transport and metabolism];


Pssm-ID: 440698 [Multi-domain]  Cd Length: 571  Bit Score: 656.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 117 LYGNVLASGVGVGTLTLLQSDSLD-SYRAIPASAQDS--TRLEHSLATLAEQLN---QQLRERDGESKT-ILSAHLSLIQ 189
Cdd:COG1080    1 LKGIAASPGIAIGKAFLLREEDLEvPEYTISPEDVEAeiARLEAALAKAREELEalrEKAPEDLGEEEAaIFDAHLLLLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 190 DDEFAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDIRDISEQLLHITWPElKPRNKLVLEKPTILVA 269
Cdd:COG1080   81 DPELIEEVEELIREGRYNAEWALKEVIEELAAQFEALDDEYLRERAADIRDVGRRVLRNLLGV-EAPDLSDLPEPVILVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 270 EDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPLDAIARYAGQPAVLDAQCGVLAINPNDAVSGYYQ 349
Cdd:COG1080  160 HDLTPSDTAQLDPSRVAGFVTDLGGRTSHTAILARSLGIPAVVGLGDALLLVKDGDLVIVDGDAGVVIVNPDEETLAEYR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 350 VAQTLADKRQKQQAQAAAQLAYSRDNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQQV 429
Cdd:COG1080  240 ERQAEYAAERAELARLRDLPAVTLDGVRVELAANIGLPEDAAAALENGAEGVGLFRTEFLFMDRDDLPTEEEQFEAYRAV 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 430 LLAAGDKPIIFRTMDIGGDKSIPYLNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQIL 509
Cdd:COG1080  320 AEAMGGRPVTIRTLDIGGDKPLPYLPLPKEENPFLGLRAIRLCLDRPELFRTQLRAILRASAHGNLRIMFPMISSVEELR 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 510 WVKGEIQKAIVELKRDGLRHAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPITPS 589
Cdd:COG1080  400 QAKALLEEAKAELRAEGIPFDEDIPVGIMIEVPAAALIADQLAKEVDFFSIGTNDLIQYTLAVDRGNEKVAYLYDPLHPA 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 590 FLRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDSEACRELARQACECRSAQE 669
Cdd:COG1080  480 VLRLIKMVIDAAHKAGKPVGVCGEMAGDPLATPLLLGLGLDELSMSPSSIPAVKAIIRRLDLAEARALAEKALALDTAEE 559

                        570
                 ....*....|.
gi 519083998 670 IEALLTAFTPE 680
Cdd:COG1080  560 VRALLEEFLAE 570
PRK11177 PRK11177
phosphoenolpyruvate-protein phosphotransferase PtsI;
121-681 4.14e-147

phosphoenolpyruvate-protein phosphotransferase PtsI;


Pssm-ID: 183017 [Multi-domain]  Cd Length: 575  Bit Score: 444.84  E-value: 4.14e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 121 VLAS-GVGVGTLTLLQSDSLD-SYRAIPASA--QDSTRLEHSLATLAEQLN---QQLRERDGESK-TILSAHLSLIQDDE 192
Cdd:PRK11177   5 ILASpGIAFGKALLLKEDEIViNRKKISADQvdQEVERFLSGRAKASAQLEaikTKAGETFGEEKeAIFEGHIMLLEDEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 193 FAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDIRDISEQLLhitwpelkpRNKLVL--------EKP 264
Cdd:PRK11177  85 LEQEIIALIKDKHMTADAAAHSVIEGQAKALEELDDEYLKERAADVRDIGKRLL---------KNILGLkiidlsaiQEE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 265 TILVAEDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPlDAIARYA-GQPAVLDAQCGVLAINPNDA 343
Cdd:PRK11177 156 VILVAADLTPSETAQLNLKKVLGFITDIGGRTSHTSIMARSLELPAIVGTG-NITKQVKnGDYLILDAVNNQIYVNPTNE 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 344 VSGYYQVAQT--LADKRQKQQAQAAAQLaySRDNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQE 421
Cdd:PRK11177 235 VIEELKAVQEqyASEKAELAKLKDLPAI--TLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFLFMDRDALPTEEE 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 422 QFEAYQQVLLAAGDKPIIFRTMDIGGDKSIPYLNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPM 501
Cdd:PRK11177 313 QFQAYKAVAEAMGSQAVIVRTMDIGGDKELPYMNLPKEENPFLGWRAIRIAMDRKEILHDQLRAILRASAFGKLRIMFPM 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 502 VHSLDQILWVKGEIQKAIVELKRDGLRHAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSP 581
Cdd:PRK11177 393 IISVEEVRELKAEIEILKQELRDEGKAFDESIEIGVMVETPAAAVIARHLAKEVDFFSIGTNDLTQYTLAVDRGNELISH 472

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 582 LYNPITPSFLRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDSEACRELARQA 661
Cdd:PRK11177 473 LYNPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNTNFEDAKALAEQA 552

                        570       580
                 ....*....|....*....|
gi 519083998 662 CECRSAQEIEALLTAFTPEE 681
Cdd:PRK11177 553 LAQPTADELMTLVNKFIEEK 572
PTS_I_fam TIGR01417
phosphoenolpyruvate-protein phosphotransferase; This model recognizes a distinct clade of ...
 117-674 4.84e-147

phosphoenolpyruvate-protein phosphotransferase; This model recognizes a distinct clade of phophoenolpyruvate (PEP)-dependent enzymes. Most members are known or deduced to function as the phosphoenolpyruvate-protein phosphotransferase (or enzyme I) of PTS sugar transport systems. However, some species with both a member of this family and a homolog of the phosphocarrier protein HPr lack a IIC component able to serve as a permease. An HPr homolog designated NPr has been implicated in the regulation of nitrogen assimilation, which demonstrates that not all phosphotransferase system components are associated directly with PTS transport.


Pssm-ID: 273611 [Multi-domain]  Cd Length: 565  Bit Score: 444.23  E-value: 4.84e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  117 LYGNVLASGVGVGTLTLLQSDSLD-SYRAIPASAQDST--RLEHSLATLAEQL----NQQLRERDGESKTILSAHLSLIQ 189
Cdd:TIGR01417   1 ISGIGVSPGIAIGKALLLKKPDLViDRKKISASQVDQEisRFLSARAKAKEDLetikTKAGKTFGQEKAAIFEAHILILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  190 DDEFAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDIRDISEQLL-HITWPELKprNKLVLEKPTILV 268
Cdd:TIGR01417  81 DPELTEEVIELIKKDHKNAEFAAHEVFEGQAKSLEEMDDEYLKERAADIRDIGNRLLgHLLGVKIS--DLSEIQDEVILV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  269 AEDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPLDAIARYAGQPAVLDAQCGVLAINP-NDAVSGY 347
Cdd:TIGR01417 159 AEDLTPSETAQLNLKYVKGFLTDAGGKTSHTAIMARSLEIPAIVGTKSVTSQVKNGDTVIIDGVKGIVIFNPsSETIDKY 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  348 YQVaQTLADKRQKQQAQAAAQLAYSRDNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQ 427
Cdd:TIGR01417 239 EAK-QEAVSSEKAELAKLKDKPAITLDGHQVELAANIGTVDDVEGAERNGGEGIGLFRTEFLYMSRDQLPTEEEQFAAYK 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  428 QVLLAAGDKPIIFRTMDIGGDKSIPYLNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQ 507
Cdd:TIGR01417 318 TVLEAMESDAVIVRTLDIGGDKELPYLNFPKEENPFLGYRAIRLALEREEILRTQLRAILRASAYGKLRIMFPMVATVEE 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  508 ILWVKGEIQKAIVELKRDGLRHAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPIT 587
Cdd:TIGR01417 398 IRAVKQELEEEKQELNDEGKAFDENIEVGVMIEIPSAALIADHLAKEVDFFSIGTNDLTQYTLAVDRGNDLISNLYQPYN 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  588 PSFLRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDSEACRELARQACECRSA 667
Cdd:TIGR01417 478 PAVLRLIKLVIDAAKAEGIWVGMCGEMAGDERAIPLLLGLGLRELSMSASSILRIKMIIRKLNIEECKSLAEKALAQPTT 557


                  ....*..
gi 519083998  668 QEIEALL 674
Cdd:TIGR01417 558 EEVHKLV 564
PEP-utilizers_C pfam02896
PEP-utilizing enzyme, PEP-binding domain; This entry represents a TIM barrel domain found at ...
 374-651 1.28e-122

PEP-utilizing enzyme, PEP-binding domain; This entry represents a TIM barrel domain found at the C terminus of a number of PEP (phosphoenolpyruvate)-utilizing proteins. In PPDK (Pyruvate phosphate dikinase) this C-terminal domain has been shown to be a PEP-binding domain.


Pssm-ID: 397163 [Multi-domain]  Cd Length: 292  Bit Score: 370.87  E-value: 1.28e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  374 DNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQQVLLAAGDKPIIFRTMDIGGDKSIPY 453
Cdd:pfam02896  16 DGTKIKVAANIGTPDDAEAALANGAEGIGLYRTEFLFMDRDELPTEDEQFEAYKGVLEAMNGRPVTVRTLDIGGDKELPY 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  454 LNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQILWVKGEIQKAIVELKRDGLRHaETI 533
Cdd:pfam02896  96 LEEPEEMNPFLGWRGIRIGLDRPELFRTQLRAILRASAFGNLRIMFPMVASVEELREAKAIIEEVKEELDAEVGFD-KDI 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  534 TLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPITPSFLRMLQQIVTTAHQRGKWVGICGE 613
Cdd:pfam02896 175 KVGIMIEVPSAALLADQLAKEVDFFSIGTNDLTQYTLAVDRDNERVAYLYDPLHPAVLRLIKEVIRAAHRHGKWVGICGE 254

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 519083998  614 LGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDS 651
Cdd:pfam02896 255 MAGDPSAVPLLVGLGLDEFSMSPDSVPRARALLAQIDR 292
fruA TIGR00848
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family ...
 686-812 1.30e-51

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: 176.31  E-value: 1.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  686 LLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAK 765
Cdd:TIGR00848   1 LLNKDLIFLDQQFTSKEDVIKFLANKLLENGYISDTEEFLEDLLKREEEGTTGIGDGVAIPHAKSAAVKQPFVAIARLVK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 519083998  766 PIDWQSEMGE-VELVIMLTLG-ANEGMNHVKVFSQLARKLVNKNFRQSL 812
Cdd:TIGR00848  81 GVDWQSLDGKpVKLIFLIAVPkDEAGNTHLKALSQLARLLLNDEFRAKL 129
PtsN COG1762
Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate ...
 686-829 1.18e-39

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: 143.45  E-value: 1.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 686 LLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAK 765
Cdd:COG1762    6 LLTPELILLDLEASSKEEAIEELAELLAEKGYVLDKEEYLEALLEREELGSTGIGPGIAIPHARPEGVKKPGIAVARLKE 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 519083998 766 PIDWQSEMGE-VELVIMLTLGANEGMNHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLETEL 829
Cdd:COG1762   86 PVDFGAMDGEpVDLVFLLAAPEDDSEEHLKLLAELARLLSDEEFREKLLNAKSPEEILELLKEAE 150
PTS_IIA_fru cd00211
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: ...
 690-825 2.23e-36

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: 133.46  E-value: 2.23e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 690 ENIFVDQDFSNKEQAIQFLCGNLGVNGRteHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAKPIDW 769
Cdd:cd00211    4 ENIRLNLKAKSKEEAIEELAQLLVAAGY--VEEEYIEALLEREKEGSTGIGNGIAIPHAKSEAVKKPGIAVLRLKEPVDF 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 519083998 770 QSEMGE-VELVIMltLGANEGMNHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLL 825
Cdd:cd00211   82 GSLDGQpVHLIFL--LAAPDSNEHLKALSQLARLLSDEEFVEQLLNAQSKEEILALL 136
PTS_EIIA_2 pfam00359
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
686-826 5.52e-34

Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;


Pssm-ID: 459780 [Multi-domain]  Cd Length: 139  Bit Score: 126.94  E-value: 5.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  686 LLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFEleEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAK 765
Cdd:pfam00359   1 LLDKELIFLNLEAKSKEEAIEFLADKLVEAGYVEPAYL--EAILEREKEGSTGIGNGIAIPHARSEAVKKPGIAVLTLKE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 519083998  766 PIDWQSEMGE-VELVIMLtLGANEGMNHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLE 826
Cdd:pfam00359  79 PVDFGSEDGKpVKLIFLL-AAPDNEASHLKILSQLARLLQDEEFVEKLLKAKDPEEILEILK 139
PRK09765 PRK09765
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional
 692-828 3.15e-20

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


Pssm-ID: 182066 [Multi-domain]  Cd Length: 631  Bit Score: 95.57  E-value: 3.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 692 IFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAKPIDWQS 771
Cdd:PRK09765  12 LCLNARFTSREEAIHALAQRLAALGKISSTEQFLEEVYRRESLGPTALGEGLAVPHGKTAAVKEAAFAVATLSEPLQWEG 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 772 --EMGEVELVIMLTLGANE-GMNHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLETE 828
Cdd:PRK09765  92 vdGPEAVDLIFLLAIPPNEaGTTHMQLLTALTTRLADDEIRARIQSATTPDELLSALDDK 151
PtsH COG1925
HPr or related phosphotransfer protein [Signal transduction mechanisms, Carbohydrate transport ...
 1-87 6.05e-19

HPr or related phosphotransfer protein [Signal transduction mechanisms, Carbohydrate transport and metabolism];


Pssm-ID: 441528 [Multi-domain]  Cd Length: 88  Bit Score: 82.07  E-value: 6.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998   1 MLTIQFLCPLPNGLHARPAWELKEQCSQWQSEITFINhrQNAKADAKSSLALIGTGTLFNDSCSLNISGSDEEQARRVLE 80
Cdd:COG1925    1 MLEREVTIVNKLGLHARPAAKLVQLASKFDSEITVEK--GGKEVNAKSIMGLMSLGAKKGDEVTITAEGPDAEEALDALA 78


                 ....*..
gi 519083998  81 EYIQVRF 87
Cdd:COG1925   79 ALIESGF 85
PTS-HPr_like cd00367
Histidine-containing phosphocarrier protein (HPr)-like proteins. HPr is a central component of ...
 5-83 6.95e-19

Histidine-containing phosphocarrier protein (HPr)-like proteins. HPr is a central component of the bacterial phosphoenolpyruvate sugar phosphotransferase system (PTS). The PTS catalyses the phosphorylation of sugar substrates during their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate is transferred to HPr by enzyme I (EI). Phospho-HPr then transfers the phosphoryl group to one of several sugar-specific phosphoprotein intermediates. The conserved histidine in the N-terminus of HPr serves as an acceptor for the phosphoryl group of EI. In addition to the phosphotransferase proteins HPr and E1, this family also includes the closely related Carbon Catabolite Repressor (CCR) proteins which use the same phosphorylation mechanism and interact with transcriptional regulators to control expression of genes coding for utilization of less favored carbon sources.


Pssm-ID: 238217 [Multi-domain]  Cd Length: 77  Bit Score: 81.40  E-value: 6.95e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 519083998   5 QFLCPLPNGLHARPAWELKEQCSQWQSEITFINHrqNAKADAKSSLALIGTGTLFNDSCSLNISGSDEEQARRVLEEYI 83
Cdd:cd00367    1 TVTITNPLGLHARPAALLVQLASKFKSDITLRKG--GRKANAKSILGLMSLGAKQGDEITLSAEGEDAEEALEALAELL 77
PTS-HPr pfam00381
PTS HPr component phosphorylation site;
5-84 2.27e-14

PTS HPr component phosphorylation site;


Pssm-ID: 459792 [Multi-domain]  Cd Length: 79  Bit Score: 68.57  E-value: 2.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998    5 QFLCPLPNGLHARPAWELKEQCSQWQSEITFINHrqNAKADAKSSLALIGTGTLFNDSCSLNISGSDEEQARRVLEEYIQ 84
Cdd:pfam00381   2 TVTITNPLGLHARPAALLVQLASKFDSDITLEKG--GKKVNAKSIMGLMSLGAKQGDEITISAEGEDEEEALEALAALLE 79
PTS_HPr_family TIGR01003
Phosphotransferase System HPr (HPr) Family; The HPr family are bacterial proteins (or domains ...
 11-83 6.06e-07

Phosphotransferase System HPr (HPr) Family; The HPr family are bacterial proteins (or domains of proteins) which function in phosphoryl transfer system (PTS) systems. They include energy-coupling components which catalyze sugar uptake via a group translocation mechanism. The functions of most of these proteins are not known, but they presumably function in PTS-related regulatory capacities. All seed members are stand-alone HPr proteins, although the model also recognizes HPr domains of PTS fusion proteins. This family includes the related NPr protein. [Signal transduction, PTS]


Pssm-ID: 273389 [Multi-domain]  Cd Length: 82  Bit Score: 47.64  E-value: 6.06e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 519083998   11 PNGLHARPAWELKEQCSQWQSEITFInhRQNAKADAKSSLALIGTGTLFNDSCSLNISGSDEEQARRVLEEYI 83
Cdd:TIGR01003  11 KVGLHARPAAILVKLASGFDSEITLT--KNGKEVNAKSIMGIMMLGAGQGTEVTVSADGEDEAEALEALAKLF 81
PRK13782 PRK13782
HPr family phosphocarrier protein;
10-84 2.45e-05

HPr family phosphocarrier protein;


Pssm-ID: 172320 [Multi-domain]  Cd Length: 82  Bit Score: 43.23  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  10 LPNGLHARPAWELKEQCSQWQSEItFInHRQNAKADAKS-----SLAlIGTGTlfndSCSLNISGSDEEQARRVLEEYIQ 84
Cdd:PRK13782  10 LKTGLQARPAALFVQEANRFHADI-FI-EKDGKKVNAKSimglmSLA-IGTGS----MITIITEGSDEEEALEALAAYVQ 82
PTS-HPr_Halo NF041319
phosphocarrier protein HPr;
13-81 6.27e-04

phosphocarrier protein HPr;


Pssm-ID: 469216 [Multi-domain]  Cd Length: 87  Bit Score: 39.58  E-value: 6.27e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  13 GLHARPAWELKEQCSQWQSEITFINHRQNAKA-DAKSSLALIGTGTLFNDSCSLNISGSDEEQARRVLEE 81
Cdd:NF041319  12 GLHARPASKFVETANEFDAEVTVGRADDDGDLvNAASMLAVTGLGVRHGEDVRLVAEGDDAEAALDALEA 81
 
Name Accession Description Interval E-value
PtsA COG1080
Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate ...
 117-680 0e+00

Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate transport and metabolism];


Pssm-ID: 440698 [Multi-domain]  Cd Length: 571  Bit Score: 656.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 117 LYGNVLASGVGVGTLTLLQSDSLD-SYRAIPASAQDS--TRLEHSLATLAEQLN---QQLRERDGESKT-ILSAHLSLIQ 189
Cdd:COG1080    1 LKGIAASPGIAIGKAFLLREEDLEvPEYTISPEDVEAeiARLEAALAKAREELEalrEKAPEDLGEEEAaIFDAHLLLLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 190 DDEFAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDIRDISEQLLHITWPElKPRNKLVLEKPTILVA 269
Cdd:COG1080   81 DPELIEEVEELIREGRYNAEWALKEVIEELAAQFEALDDEYLRERAADIRDVGRRVLRNLLGV-EAPDLSDLPEPVILVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 270 EDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPLDAIARYAGQPAVLDAQCGVLAINPNDAVSGYYQ 349
Cdd:COG1080  160 HDLTPSDTAQLDPSRVAGFVTDLGGRTSHTAILARSLGIPAVVGLGDALLLVKDGDLVIVDGDAGVVIVNPDEETLAEYR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 350 VAQTLADKRQKQQAQAAAQLAYSRDNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQQV 429
Cdd:COG1080  240 ERQAEYAAERAELARLRDLPAVTLDGVRVELAANIGLPEDAAAALENGAEGVGLFRTEFLFMDRDDLPTEEEQFEAYRAV 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 430 LLAAGDKPIIFRTMDIGGDKSIPYLNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQIL 509
Cdd:COG1080  320 AEAMGGRPVTIRTLDIGGDKPLPYLPLPKEENPFLGLRAIRLCLDRPELFRTQLRAILRASAHGNLRIMFPMISSVEELR 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 510 WVKGEIQKAIVELKRDGLRHAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPITPS 589
Cdd:COG1080  400 QAKALLEEAKAELRAEGIPFDEDIPVGIMIEVPAAALIADQLAKEVDFFSIGTNDLIQYTLAVDRGNEKVAYLYDPLHPA 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 590 FLRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDSEACRELARQACECRSAQE 669
Cdd:COG1080  480 VLRLIKMVIDAAHKAGKPVGVCGEMAGDPLATPLLLGLGLDELSMSPSSIPAVKAIIRRLDLAEARALAEKALALDTAEE 559

                        570
                 ....*....|.
gi 519083998 670 IEALLTAFTPE 680
Cdd:COG1080  560 VRALLEEFLAE 570
PRK11177 PRK11177
phosphoenolpyruvate-protein phosphotransferase PtsI;
121-681 4.14e-147

phosphoenolpyruvate-protein phosphotransferase PtsI;


Pssm-ID: 183017 [Multi-domain]  Cd Length: 575  Bit Score: 444.84  E-value: 4.14e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 121 VLAS-GVGVGTLTLLQSDSLD-SYRAIPASA--QDSTRLEHSLATLAEQLN---QQLRERDGESK-TILSAHLSLIQDDE 192
Cdd:PRK11177   5 ILASpGIAFGKALLLKEDEIViNRKKISADQvdQEVERFLSGRAKASAQLEaikTKAGETFGEEKeAIFEGHIMLLEDEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 193 FAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDIRDISEQLLhitwpelkpRNKLVL--------EKP 264
Cdd:PRK11177  85 LEQEIIALIKDKHMTADAAAHSVIEGQAKALEELDDEYLKERAADVRDIGKRLL---------KNILGLkiidlsaiQEE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 265 TILVAEDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPlDAIARYA-GQPAVLDAQCGVLAINPNDA 343
Cdd:PRK11177 156 VILVAADLTPSETAQLNLKKVLGFITDIGGRTSHTSIMARSLELPAIVGTG-NITKQVKnGDYLILDAVNNQIYVNPTNE 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 344 VSGYYQVAQT--LADKRQKQQAQAAAQLaySRDNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQE 421
Cdd:PRK11177 235 VIEELKAVQEqyASEKAELAKLKDLPAI--TLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFLFMDRDALPTEEE 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 422 QFEAYQQVLLAAGDKPIIFRTMDIGGDKSIPYLNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPM 501
Cdd:PRK11177 313 QFQAYKAVAEAMGSQAVIVRTMDIGGDKELPYMNLPKEENPFLGWRAIRIAMDRKEILHDQLRAILRASAFGKLRIMFPM 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 502 VHSLDQILWVKGEIQKAIVELKRDGLRHAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSP 581
Cdd:PRK11177 393 IISVEEVRELKAEIEILKQELRDEGKAFDESIEIGVMVETPAAAVIARHLAKEVDFFSIGTNDLTQYTLAVDRGNELISH 472

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 582 LYNPITPSFLRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDSEACRELARQA 661
Cdd:PRK11177 473 LYNPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNTNFEDAKALAEQA 552

                        570       580
                 ....*....|....*....|
gi 519083998 662 CECRSAQEIEALLTAFTPEE 681
Cdd:PRK11177 553 LAQPTADELMTLVNKFIEEK 572
PTS_I_fam TIGR01417
phosphoenolpyruvate-protein phosphotransferase; This model recognizes a distinct clade of ...
 117-674 4.84e-147

phosphoenolpyruvate-protein phosphotransferase; This model recognizes a distinct clade of phophoenolpyruvate (PEP)-dependent enzymes. Most members are known or deduced to function as the phosphoenolpyruvate-protein phosphotransferase (or enzyme I) of PTS sugar transport systems. However, some species with both a member of this family and a homolog of the phosphocarrier protein HPr lack a IIC component able to serve as a permease. An HPr homolog designated NPr has been implicated in the regulation of nitrogen assimilation, which demonstrates that not all phosphotransferase system components are associated directly with PTS transport.


Pssm-ID: 273611 [Multi-domain]  Cd Length: 565  Bit Score: 444.23  E-value: 4.84e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  117 LYGNVLASGVGVGTLTLLQSDSLD-SYRAIPASAQDST--RLEHSLATLAEQL----NQQLRERDGESKTILSAHLSLIQ 189
Cdd:TIGR01417   1 ISGIGVSPGIAIGKALLLKKPDLViDRKKISASQVDQEisRFLSARAKAKEDLetikTKAGKTFGQEKAAIFEAHILILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  190 DDEFAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDIRDISEQLL-HITWPELKprNKLVLEKPTILV 268
Cdd:TIGR01417  81 DPELTEEVIELIKKDHKNAEFAAHEVFEGQAKSLEEMDDEYLKERAADIRDIGNRLLgHLLGVKIS--DLSEIQDEVILV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  269 AEDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPLDAIARYAGQPAVLDAQCGVLAINP-NDAVSGY 347
Cdd:TIGR01417 159 AEDLTPSETAQLNLKYVKGFLTDAGGKTSHTAIMARSLEIPAIVGTKSVTSQVKNGDTVIIDGVKGIVIFNPsSETIDKY 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  348 YQVaQTLADKRQKQQAQAAAQLAYSRDNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQ 427
Cdd:TIGR01417 239 EAK-QEAVSSEKAELAKLKDKPAITLDGHQVELAANIGTVDDVEGAERNGGEGIGLFRTEFLYMSRDQLPTEEEQFAAYK 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  428 QVLLAAGDKPIIFRTMDIGGDKSIPYLNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQ 507
Cdd:TIGR01417 318 TVLEAMESDAVIVRTLDIGGDKELPYLNFPKEENPFLGYRAIRLALEREEILRTQLRAILRASAYGKLRIMFPMVATVEE 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  508 ILWVKGEIQKAIVELKRDGLRHAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPIT 587
Cdd:TIGR01417 398 IRAVKQELEEEKQELNDEGKAFDENIEVGVMIEIPSAALIADHLAKEVDFFSIGTNDLTQYTLAVDRGNDLISNLYQPYN 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  588 PSFLRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDSEACRELARQACECRSA 667
Cdd:TIGR01417 478 PAVLRLIKLVIDAAKAEGIWVGMCGEMAGDERAIPLLLGLGLRELSMSASSILRIKMIIRKLNIEECKSLAEKALAQPTT 557


                  ....*..
gi 519083998  668 QEIEALL 674
Cdd:TIGR01417 558 EEVHKLV 564
PEP-utilizers_C pfam02896
PEP-utilizing enzyme, PEP-binding domain; This entry represents a TIM barrel domain found at ...
 374-651 1.28e-122

PEP-utilizing enzyme, PEP-binding domain; This entry represents a TIM barrel domain found at the C terminus of a number of PEP (phosphoenolpyruvate)-utilizing proteins. In PPDK (Pyruvate phosphate dikinase) this C-terminal domain has been shown to be a PEP-binding domain.


Pssm-ID: 397163 [Multi-domain]  Cd Length: 292  Bit Score: 370.87  E-value: 1.28e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  374 DNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQQVLLAAGDKPIIFRTMDIGGDKSIPY 453
Cdd:pfam02896  16 DGTKIKVAANIGTPDDAEAALANGAEGIGLYRTEFLFMDRDELPTEDEQFEAYKGVLEAMNGRPVTVRTLDIGGDKELPY 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  454 LNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQILWVKGEIQKAIVELKRDGLRHaETI 533
Cdd:pfam02896  96 LEEPEEMNPFLGWRGIRIGLDRPELFRTQLRAILRASAFGNLRIMFPMVASVEELREAKAIIEEVKEELDAEVGFD-KDI 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  534 TLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPITPSFLRMLQQIVTTAHQRGKWVGICGE 613
Cdd:pfam02896 175 KVGIMIEVPSAALLADQLAKEVDFFSIGTNDLTQYTLAVDRDNERVAYLYDPLHPAVLRLIKEVIRAAHRHGKWVGICGE 254

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 519083998  614 LGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDS 651
Cdd:pfam02896 255 MAGDPSAVPLLVGLGLDEFSMSPDSVPRARALLAQIDR 292
PRK11061 PRK11061
phosphoenolpyruvate--protein phosphotransferase;
123-683 1.70e-92

phosphoenolpyruvate--protein phosphotransferase;


Pssm-ID: 182937 [Multi-domain]  Cd Length: 748  Bit Score: 306.92  E-value: 1.70e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 123 ASGVGVGTLtlLQSDSLDSYRAI-PASAQDSTRlEHSLATLA--EQLNQ--QLRER-----DGESKTILSAHLSLIQDDE 192
Cdd:PRK11061 177 SPGVAIAEG--WQDATQPLLEQVyPASTLDPAL-ERERLTGAleEAANEfrRYSKRfaagaQKETAAIFDLYSHLLNDPR 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 193 FAgniRRLMTEQHQGLGA--AIisnmEQVCAKLS---ASASD-YLRERVSDIRDISEQLL---------HITWPElkprn 257
Cdd:PRK11061 254 LR---RELFAEVDKGSVAewAV----KQVIEKFAeqfAALSDnYLRERAGDLRALGQRLLfhlddseqgPNAWPE----- 321

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 258 klvlekPTILVAEDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPLDAiARYAGQPAVLDAQCGVLA 337
Cdd:PRK11061 322 ------RFILVADELTATLLAELPQDRLAGVVVRDGAANSHAAILVRALGIPTVMGADIQP-SLLHQRLLIVDGYRGELL 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 338 INPNDAVSGYYQVAQTLADKRQKQQAQAAAQLAYSRDNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAP 417
Cdd:PRK11061 395 VDPEPVLLQEYQRLISEEIELSRLAEDDVNLPAQLKSGERIKVMLNAGLSAEHEEKLGSRVDGVGLYRTEIPFMLQSGFP 474

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 418 DEQEQFEAYQQVLLAAGDKPIIFRTMDIGGDKSIPYLNIpQEENPFLGYRAVRI---YPEfagLFRTQLRAILRA-ASFG 493
Cdd:PRK11061 475 SEEEQVAQYQGMLQMFPDKPVTLRTLDIGADKQLPYMPI-SEENPCLGWRGIRItldQPE---IFLIQVRAMLRAnAATG 550

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 494 NAQLMIPMVHSLDQILWVKGEIQKAIVELKRDGLRHAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVD 573
Cdd:PRK11061 551 NLSILLPMVTSIDEVDEARRLIDRAGREVEEMLGYEIPKPRIGIMIEVPSMVFMLPHLASRVDFISVGTNDLTQYLLAVD 630

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 574 RNNPRVSPLYNPITPSFLRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDSEA 653
Cdd:PRK11061 631 RNNTRVASLYDSLHPAMLRALKMIADEAEQHGLPVSLCGEMAGDPMGALLLIGLGYRHLSMNGRSVARVKYLLRHIDLAE 710

                        570       580       590
                 ....*....|....*....|....*....|
gi 519083998 654 CRELARQACECRSAQEIEALLTAFTPEEDV 683
Cdd:PRK11061 711 AENLAQRSLEAQLATEVRHQVAAFMERRGL 740
fruA TIGR00848
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family ...
 686-812 1.30e-51

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: 176.31  E-value: 1.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  686 LLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAK 765
Cdd:TIGR00848   1 LLNKDLIFLDQQFTSKEDVIKFLANKLLENGYISDTEEFLEDLLKREEEGTTGIGDGVAIPHAKSAAVKQPFVAIARLVK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 519083998  766 PIDWQSEMGE-VELVIMLTLG-ANEGMNHVKVFSQLARKLVNKNFRQSL 812
Cdd:TIGR00848  81 GVDWQSLDGKpVKLIFLIAVPkDEAGNTHLKALSQLARLLLNDEFRAKL 129
PRK06464 PRK06464
phosphoenolpyruvate synthase; Validated
 380-620 3.55e-44

phosphoenolpyruvate synthase; Validated


Pssm-ID: 235809 [Multi-domain]  Cd Length: 795  Bit Score: 171.47  E-value: 3.55e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 380 IAANIGTALEAPGAFANGAEGVGLFRTEML-----------YMDRDSAPDEQEQF------------EAYQQVL------ 430
Cdd:PRK06464 483 IMMNVGNPERAFDFAALPNDGVGLARLEFIinnmigvhplaLLEFDQQDADLKAEieeltagyaspeEFYVDKLaegiat 562

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 431 LAAG--DKPIIFRTMD---------IGGDKSIPylnipQEENPFLGYRAVRIY--PEFAGLFRTQLRAILRA---ASFGN 494
Cdd:PRK06464 563 VAAAfyPKPVIVRLSDfksneyanlIGGERYEP-----EEENPMLGFRGASRYlsESFREAFALECEAIKRVreeMGLTN 637

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 495 AQLMIPMVHSLDqilwvkgEIQKAIVELKRDGL-RHAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVD 573
Cdd:PRK06464 638 VEVMIPFVRTVE-------EAEKVIELLAENGLkRGENGLKVIMMCEIPSNALLAEEFLEYFDGFSIGSNDLTQLTLGLD 710

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 519083998 574 RNNPRVSPLYNPITPSFLRMLQQIVTTAHQRGKWVGICGElgGESRY 620
Cdd:PRK06464 711 RDSGLVAHLFDERNPAVKKLISMAIKAAKKAGKYVGICGQ--APSDH 755
PtsN COG1762
Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate ...
 686-829 1.18e-39

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: 143.45  E-value: 1.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 686 LLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAK 765
Cdd:COG1762    6 LLTPELILLDLEASSKEEAIEELAELLAEKGYVLDKEEYLEALLEREELGSTGIGPGIAIPHARPEGVKKPGIAVARLKE 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 519083998 766 PIDWQSEMGE-VELVIMLTLGANEGMNHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLETEL 829
Cdd:COG1762   86 PVDFGAMDGEpVDLVFLLAAPEDDSEEHLKLLAELARLLSDEEFREKLLNAKSPEEILELLKEAE 150
PTS_IIA_fru cd00211
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: ...
 690-825 2.23e-36

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: 133.46  E-value: 2.23e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 690 ENIFVDQDFSNKEQAIQFLCGNLGVNGRteHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAKPIDW 769
Cdd:cd00211    4 ENIRLNLKAKSKEEAIEELAQLLVAAGY--VEEEYIEALLEREKEGSTGIGNGIAIPHAKSEAVKKPGIAVLRLKEPVDF 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 519083998 770 QSEMGE-VELVIMltLGANEGMNHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLL 825
Cdd:cd00211   82 GSLDGQpVHLIFL--LAAPDSNEHLKALSQLARLLSDEEFVEQLLNAQSKEEILALL 136
PTS_EIIA_2 pfam00359
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
686-826 5.52e-34

Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;


Pssm-ID: 459780 [Multi-domain]  Cd Length: 139  Bit Score: 126.94  E-value: 5.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  686 LLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFEleEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAK 765
Cdd:pfam00359   1 LLDKELIFLNLEAKSKEEAIEFLADKLVEAGYVEPAYL--EAILEREKEGSTGIGNGIAIPHARSEAVKKPGIAVLTLKE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 519083998  766 PIDWQSEMGE-VELVIMLtLGANEGMNHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLE 826
Cdd:pfam00359  79 PVDFGSEDGKpVKLIFLL-AAPDNEASHLKILSQLARLLQDEEFVEKLLKAKDPEEILEILK 139
PRK11377 PRK11377
dihydroxyacetone kinase subunit M; Provisional
 11-338 3.09e-25

dihydroxyacetone kinase subunit M; Provisional


Pssm-ID: 183108 [Multi-domain]  Cd Length: 473  Bit Score: 110.22  E-value: 3.09e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  11 PNGLHARPAWELKEQCSQWQSEITFINHRQNAKADAKSSLALIGTgtLFNDSCSLNISGSDEEQARRVLEEYIQVRFIDS 90
Cdd:PRK11377 165 RNGLHVRPASRLVYTLSTFNADMLLEKNGKCVTPESLNQIALLQV--RYNDTLRLIAKGPEAEEALIAFRQLAEDNFGET 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  91 DSVQPTqaelTAHPLPRSLSclNPDLLYGNVLASGVGVGTLTLLQsDSLDSYRAIPASAQDstrlehsLATLAEQLNQQL 170
Cdd:PRK11377 243 EEVAPP----TLRPVPSPVS--GKAFYYQPVLCTVQAKSTLTVEE-EQERLRQAIDFTLLD-------LMTLTAKAEASG 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 171 RERDGeskTILSAHLSLIQDDEFAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDIRDISEQLL-HIT 249
Cdd:PRK11377 309 LDDIA---AIFSGHHTLLDDPELLAAASERLQHEHCTAEYAWQQVLKELSQQYQQLDDEYLQARYIDVDDLLHRTLvHLT 385

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 250 wpELKPRnKLVLEKPTILVAEDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGL--PLDAIAryAGQPA 327
Cdd:PRK11377 386 --QTKEE-LPQFNSPTILLAENIYPSTVLQLDPAVVKGICLSAGSPLSHSAIIARELGIGWICQQgeKLYAIQ--PEETL 460

                        330
                 ....*....|.
gi 519083998 328 VLDAQCGVLAI 338
Cdd:PRK11377 461 TLDVKTQRLNR 471
PRK09765 PRK09765
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional
 692-828 3.15e-20

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


Pssm-ID: 182066 [Multi-domain]  Cd Length: 631  Bit Score: 95.57  E-value: 3.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 692 IFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAKPIDWQS 771
Cdd:PRK09765  12 LCLNARFTSREEAIHALAQRLAALGKISSTEQFLEEVYRRESLGPTALGEGLAVPHGKTAAVKEAAFAVATLSEPLQWEG 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 772 --EMGEVELVIMLTLGANE-GMNHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLETE 828
Cdd:PRK09765  92 vdGPEAVDLIFLLAIPPNEaGTTHMQLLTALTTRLADDEIRARIQSATTPDELLSALDDK 151
MtlA2 COG4668
Mannitol/fructose-specific phosphotransferase system, IIA domain [Carbohydrate transport and ...
 685-826 3.03e-19

Mannitol/fructose-specific phosphotransferase system, IIA domain [Carbohydrate transport and metabolism];


Pssm-ID: 443705 [Multi-domain]  Cd Length: 143  Bit Score: 84.83  E-value: 3.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 685 PLLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFelEEDVWQREEIVTTGVGFGVAIPH----TKSQwIRHSSISI 760
Cdd:COG4668    2 LILTKENIRLNASAANKEEAIRLAGQLLVEAGYVEPEY--IDAMLEREAQVSTYLGNGIAIPHgtneAKDL-VLKTGISV 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 519083998 761 ARLAKPIDWqSEMGEVELVIMLTLGANEgmnHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLE 826
Cdd:COG4668   79 LQFPDGVDW-GDGNTVYLVIGIAAKSDE---HLEILRQLARVLSDEENVEKLAKATDAEEILALLT 140
PtsH COG1925
HPr or related phosphotransfer protein [Signal transduction mechanisms, Carbohydrate transport ...
 1-87 6.05e-19

HPr or related phosphotransfer protein [Signal transduction mechanisms, Carbohydrate transport and metabolism];


Pssm-ID: 441528 [Multi-domain]  Cd Length: 88  Bit Score: 82.07  E-value: 6.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998   1 MLTIQFLCPLPNGLHARPAWELKEQCSQWQSEITFINhrQNAKADAKSSLALIGTGTLFNDSCSLNISGSDEEQARRVLE 80
Cdd:COG1925    1 MLEREVTIVNKLGLHARPAAKLVQLASKFDSEITVEK--GGKEVNAKSIMGLMSLGAKKGDEVTITAEGPDAEEALDALA 78


                 ....*..
gi 519083998  81 EYIQVRF 87
Cdd:COG1925   79 ALIESGF 85
PTS-HPr_like cd00367
Histidine-containing phosphocarrier protein (HPr)-like proteins. HPr is a central component of ...
 5-83 6.95e-19

Histidine-containing phosphocarrier protein (HPr)-like proteins. HPr is a central component of the bacterial phosphoenolpyruvate sugar phosphotransferase system (PTS). The PTS catalyses the phosphorylation of sugar substrates during their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate is transferred to HPr by enzyme I (EI). Phospho-HPr then transfers the phosphoryl group to one of several sugar-specific phosphoprotein intermediates. The conserved histidine in the N-terminus of HPr serves as an acceptor for the phosphoryl group of EI. In addition to the phosphotransferase proteins HPr and E1, this family also includes the closely related Carbon Catabolite Repressor (CCR) proteins which use the same phosphorylation mechanism and interact with transcriptional regulators to control expression of genes coding for utilization of less favored carbon sources.


Pssm-ID: 238217 [Multi-domain]  Cd Length: 77  Bit Score: 81.40  E-value: 6.95e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 519083998   5 QFLCPLPNGLHARPAWELKEQCSQWQSEITFINHrqNAKADAKSSLALIGTGTLFNDSCSLNISGSDEEQARRVLEEYI 83
Cdd:cd00367    1 TVTITNPLGLHARPAALLVQLASKFKSDITLRKG--GRKANAKSILGLMSLGAKQGDEITLSAEGEDAEEALEALAELL 77
PRK09913 PRK09913
PTS fructose transporter subunit IIA;
685-808 2.11e-16

PTS fructose transporter subunit IIA;


Pssm-ID: 182141 [Multi-domain]  Cd Length: 148  Bit Score: 76.85  E-value: 2.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 685 PLLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLA 764
Cdd:PRK09913   2 AALTASCIDLNIQGNGAYSILKQLATIALQNGFITDSHQFLQTLLLREKMHSTGFGSGVAVPHGKSACVKQPFVLFARKA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 519083998 765 KPIDWQSEMGE-VELVIMLTLGANEGMNHVKVFSQLARKLVNKNF 808
Cdd:PRK09913  82 QAIDWQASDGEdVNCWICLGVPQSGEEDQVKIIGTLCRKIIHQDF 126
PEP-utilizers pfam00391
PEP-utilizing enzyme, mobile domain; This domain is a "swivelling" beta/beta/alpha domain ...
 261-334 1.49e-14

PEP-utilizing enzyme, mobile domain; This domain is a "swivelling" beta/beta/alpha domain which is thought to be mobile in all proteins known to contain it.


Pssm-ID: 459796 [Multi-domain]  Cd Length: 73  Bit Score: 68.98  E-value: 1.49e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 519083998  261 LEKPTILVAEDLTPSQFLslDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPLDAIARYAGQPAVLDAQCG 334
Cdd:pfam00391   2 LPEGVILVAPDTTPSDTA--GLDKAAGIVTERGGMTSHAAIVARELGIPAVVGVGDATILLKEGDLVTVDGSTG 73
PTS-HPr pfam00381
PTS HPr component phosphorylation site;
5-84 2.27e-14

PTS HPr component phosphorylation site;


Pssm-ID: 459792 [Multi-domain]  Cd Length: 79  Bit Score: 68.57  E-value: 2.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998    5 QFLCPLPNGLHARPAWELKEQCSQWQSEITFINHrqNAKADAKSSLALIGTGTLFNDSCSLNISGSDEEQARRVLEEYIQ 84
Cdd:pfam00381   2 TVTITNPLGLHARPAALLVQLASKFDSDITLEKG--GKKVNAKSIMGLMSLGAKQGDEITISAEGEDEEEALEALAALLE 79
PEP-utilizers_N pfam05524
PEP-utilizing enzyme, N-terminal;
123-234 1.99e-12

PEP-utilizing enzyme, N-terminal;


Pssm-ID: 461671 [Multi-domain]  Cd Length: 125  Bit Score: 64.94  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  123 ASGVGVGTLTLLQSDSLDSYRAIPASAQDS----TRLEHSLATLAEQLnQQLRER-----DGESKTILSAHLSLIQDDEF 193
Cdd:pfam05524   6 SPGIAIGKAVVLEEPELEVPDEREVPADDVeaeiARLEAALEAAREEL-EALAERaagelGEEEAAIFEAHLMMLEDPEL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 519083998  194 AGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRER 234
Cdd:pfam05524  85 LEEVEELIREGGLNAEAAVKEVVDEFAAMFEAMDDPYLRER 125
PTS_HPr_family TIGR01003
Phosphotransferase System HPr (HPr) Family; The HPr family are bacterial proteins (or domains ...
 11-83 6.06e-07

Phosphotransferase System HPr (HPr) Family; The HPr family are bacterial proteins (or domains of proteins) which function in phosphoryl transfer system (PTS) systems. They include energy-coupling components which catalyze sugar uptake via a group translocation mechanism. The functions of most of these proteins are not known, but they presumably function in PTS-related regulatory capacities. All seed members are stand-alone HPr proteins, although the model also recognizes HPr domains of PTS fusion proteins. This family includes the related NPr protein. [Signal transduction, PTS]


Pssm-ID: 273389 [Multi-domain]  Cd Length: 82  Bit Score: 47.64  E-value: 6.06e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 519083998   11 PNGLHARPAWELKEQCSQWQSEITFInhRQNAKADAKSSLALIGTGTLFNDSCSLNISGSDEEQARRVLEEYI 83
Cdd:TIGR01003  11 KVGLHARPAAILVKLASGFDSEITLT--KNGKEVNAKSIMGIMMLGAGQGTEVTVSADGEDEAEALEALAKLF 81
PRK15083 PRK15083
PTS system mannitol-specific transporter subunit IICBA; Provisional
 687-828 1.30e-06

PTS system mannitol-specific transporter subunit IICBA; Provisional


Pssm-ID: 237905 [Multi-domain]  Cd Length: 639  Bit Score: 51.98  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 687 LALENIFVDQDFSNKEQAIQFlCGNLGVNGRTEHPfELEEDVWQREEIVTTGVGFGVAIPH----TKSQWIRhSSISIAR 762
Cdd:PRK15083 497 LGAENIFLGLKAATKEEAIRF-AGEQLVKGGYVEP-EYVDAMLDREKLTSTYLGESIAVPHgtveAKDRVLK-TGVVFCQ 573

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 519083998 763 LAKPIDWQSEMGEV-ELVIMLTLGANEgmnHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLETE 828
Cdd:PRK15083 574 YPEGVRFGEEEDDIaRLVIGIAARNNE---HIQVITSLTNALDDESVIERLAHTTSVDEVLELLAGK 637
PRK10896 PRK10896
PTS IIA-like nitrogen regulatory protein PtsN;
726-816 2.00e-05

PTS IIA-like nitrogen regulatory protein PtsN;


Pssm-ID: 182818 [Multi-domain]  Cd Length: 154  Bit Score: 45.51  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 726 EDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISI-ARLAKPIDWQS-EMGEVELVIMLTLGANEGMNHVKVFSQLARKL 803
Cdd:PRK10896  51 EAILTREKMGSTGIGNGIAIPHGKLEEDTLRAVGVfVQLEQPIAFDAiDNQPVDLLFALLVPADQCKTHLHTLSLVAKRL 130

                         90
                 ....*....|...
gi 519083998 804 VNKNFRQSLFAAQ 816
Cdd:PRK10896 131 ADKTICRRLRAAQ 143
PRK13782 PRK13782
HPr family phosphocarrier protein;
10-84 2.45e-05

HPr family phosphocarrier protein;


Pssm-ID: 172320 [Multi-domain]  Cd Length: 82  Bit Score: 43.23  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  10 LPNGLHARPAWELKEQCSQWQSEItFInHRQNAKADAKS-----SLAlIGTGTlfndSCSLNISGSDEEQARRVLEEYIQ 84
Cdd:PRK13782  10 LKTGLQARPAALFVQEANRFHADI-FI-EKDGKKVNAKSimglmSLA-IGTGS----MITIITEGSDEEEALEALAAYVQ 82
PRK10850 PRK10850
phosphocarrier protein Hpr;
11-75 4.91e-05

phosphocarrier protein Hpr;


Pssm-ID: 182777 [Multi-domain]  Cd Length: 85  Bit Score: 42.42  E-value: 4.91e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 519083998  11 PNGLHARPAWELKEQCSQWQSEITFINHRQNAKadAKSSLALIGTGTLFNDSCSLNISGSDEEQA 75
Cdd:PRK10850  11 PNGLHTRPAAQFVKEAKGFTSEITVTSNGKSAS--AKSLFKLQTLGLTQGTVVTISAEGEDEQKA 73
PRK11109 PRK11109
fused PTS fructose transporter subunit IIA/HPr protein;
687-825 3.38e-04

fused PTS fructose transporter subunit IIA/HPr protein;


Pssm-ID: 236849 [Multi-domain]  Cd Length: 375  Bit Score: 43.78  E-value: 3.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 687 LALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFEleEDVWQREEIVTTGVGFGVAIPH----TKSQwIRHSSISIAR 762
Cdd:PRK11109   4 LSVQDIHLGQQAGNKEEAIRQVAAALTQAGNVAEGYV--DGMLAREQQTSTFLGNGIAIPHgttdTRDL-VLKTGVQVFQ 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 519083998 763 LAKPIDWqsemGE---VELVIMLTLGANEgmnHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLL 825
Cdd:PRK11109  81 FPQGVTW----GDgqtAYVAIGIAAKSDE---HLGLLRQLTHVLSDDSVAEQLKSATTAEELRALL 139
PTS-HPr_Halo NF041319
phosphocarrier protein HPr;
13-81 6.27e-04

phosphocarrier protein HPr;


Pssm-ID: 469216 [Multi-domain]  Cd Length: 87  Bit Score: 39.58  E-value: 6.27e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998  13 GLHARPAWELKEQCSQWQSEITFINHRQNAKA-DAKSSLALIGTGTLFNDSCSLNISGSDEEQARRVLEE 81
Cdd:NF041319  12 GLHARPASKFVETANEFDAEVTVGRADDDGDLvNAASMLAVTGLGVRHGEDVRLVAEGDDAEAALDALEA 81
PykA2 COG3848
Phosphohistidine swiveling domain of PEP-utilizing enzymes [Signal transduction mechanisms];
266-315 1.08e-03

Phosphohistidine swiveling domain of PEP-utilizing enzymes [Signal transduction mechanisms];


Pssm-ID: 443058  Cd Length: 321  Bit Score: 42.19  E-value: 1.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 519083998 266 ILVAEDLTPSqFLSlDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLP 315
Cdd:COG3848  245 ILVVPSTDAE-FVP-AIEKAAGIITEEGGLTSHAAIVGLELGIPVIVGAE 292
PRK13779 PRK13779
bifunctional PTS system fructose-specific transporter subunit IIA/HPr protein; Provisional
 687-828 2.68e-03

bifunctional PTS system fructose-specific transporter subunit IIA/HPr protein; Provisional


Pssm-ID: 237502 [Multi-domain]  Cd Length: 503  Bit Score: 41.01  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083998 687 LALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFelEEDVWQREEIVTTGVGFGVAIPH----TKSQwIRHSSISIAR 762
Cdd:PRK13779   4 LSESNIHLNAQAINKQQAIEMAAAALEQAGNVENGY--LQGMLARELQTSTFLGNGIAIPHgtldTRHM-VKNTGVQIFQ 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 519083998 763 LAKPIDWqSEMGEVELVIMLTLGANEgmnHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLETE 828
Cdd:PRK13779  81 FPQGIEW-GEGNIAYVVIGIAARSDE---HLSLLRQLTHVLSDEDTAAKLATLTDVKEFRAILMGE 142
 
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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