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Conserved domains on  [gi|485777446|ref|WP_001400766|]
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phosphoenolpyruvate--protein phosphotransferase [Escherichia coli]

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: 657.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 117 LYGnVPAS-GVGVGTLTLLQSDSLD-SYRAIPASAQDS--TRLEHSLATLAEQLN---QQLRERDGESKT-ILSAHLSLI 188
Cdd:COG1080    1 LKG-IAASpGIAIGKAFLLREEDLEvPEYTISPEDVEAeiARLEAALAKAREELEalrEKAPEDLGEEEAaIFDAHLLLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 189 QDDEFAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDIRDISEQLLHITWPElKPRNKLVLEKPTILV 268
Cdd:COG1080   80 EDPELIEEVEELIREGRYNAEWALKEVIEELAAQFEALDDEYLRERAADIRDVGRRVLRNLLGV-EAPDLSDLPEPVILV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 269 AEDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPLDAIARYAGQPAVLDAQCGVLAINPNDAVSGYY 348
Cdd:COG1080  159 AHDLTPSDTAQLDPSRVAGFVTDLGGRTSHTAILARSLGIPAVVGLGDALLLVKDGDLVIVDGDAGVVIVNPDEETLAEY 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 349 QVAQTLADKRQKQQAQAAAQLAYSRDNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQQ 428
Cdd:COG1080  239 RERQAEYAAERAELARLRDLPAVTLDGVRVELAANIGLPEDAAAALENGAEGVGLFRTEFLFMDRDDLPTEEEQFEAYRA 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 429 VLLAAGDKPIIFRTMDIGGDKSIPYLNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQI 508
Cdd:COG1080  319 VAEAMGGRPVTIRTLDIGGDKPLPYLPLPKEENPFLGLRAIRLCLDRPELFRTQLRAILRASAHGNLRIMFPMISSVEEL 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 509 LWVKGEIQKAIVELKRDGLRYAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPITP 588
Cdd:COG1080  399 RQAKALLEEAKAELRAEGIPFDEDIPVGIMIEVPAAALIADQLAKEVDFFSIGTNDLIQYTLAVDRGNEKVAYLYDPLHP 478

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 589 SFLRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDSEACRELARQACECRSAQ 668
Cdd:COG1080  479 AVLRLIKMVIDAAHKAGKPVGVCGEMAGDPLATPLLLGLGLDELSMSPSSIPAVKAIIRRLDLAEARALAEKALALDTAE 558

                        570
                 ....*....|..
gi 485777446 669 EIEALLTAFTPE 680
Cdd:COG1080  559 EVRALLEEFLAE 570
fruA TIGR00848
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family ...
 686-812 2.62e-50

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: 172.84  E-value: 2.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  686 LLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAK 765
Cdd:TIGR00848   1 LLNKDLIFLDQQFTSKEDVIKFLANKLLENGYISDTEEFLEDLLKREEEGTTGIGDGVAIPHAKSAAVKQPFVAIARLVK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 485777446  766 PIGWQSEMGE-VELVIMLTLG-ANEGMNHVKVFSQLARKLVNKNFRQSL 812
Cdd:TIGR00848  81 GVDWQSLDGKpVKLIFLIAVPkDEAGNTHLKALSQLARLLLNDEFRAKL 129
PtsH COG1925
HPr or related phosphotransfer protein [Signal transduction mechanisms, Carbohydrate transport ...
 1-87 8.88e-18

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


:

Pssm-ID: 441528 [Multi-domain]  Cd Length: 88  Bit Score: 78.61  E-value: 8.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446   1 MLTIQFLCPLPNGLHARPAWELKEQCSQWQSEITFINhrQNAKADAKSSLALIGTGTLFNDSCSLNISDSDEEQARRVLE 80
Cdd:COG1925    1 MLEREVTIVNKLGLHARPAAKLVQLASKFDSEITVEK--GGKEVNAKSIMGLMSLGAKKGDEVTITAEGPDAEEALDALA 78


                 ....*..
gi 485777446  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: 657.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 117 LYGnVPAS-GVGVGTLTLLQSDSLD-SYRAIPASAQDS--TRLEHSLATLAEQLN---QQLRERDGESKT-ILSAHLSLI 188
Cdd:COG1080    1 LKG-IAASpGIAIGKAFLLREEDLEvPEYTISPEDVEAeiARLEAALAKAREELEalrEKAPEDLGEEEAaIFDAHLLLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 189 QDDEFAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDIRDISEQLLHITWPElKPRNKLVLEKPTILV 268
Cdd:COG1080   80 EDPELIEEVEELIREGRYNAEWALKEVIEELAAQFEALDDEYLRERAADIRDVGRRVLRNLLGV-EAPDLSDLPEPVILV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 269 AEDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPLDAIARYAGQPAVLDAQCGVLAINPNDAVSGYY 348
Cdd:COG1080  159 AHDLTPSDTAQLDPSRVAGFVTDLGGRTSHTAILARSLGIPAVVGLGDALLLVKDGDLVIVDGDAGVVIVNPDEETLAEY 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 349 QVAQTLADKRQKQQAQAAAQLAYSRDNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQQ 428
Cdd:COG1080  239 RERQAEYAAERAELARLRDLPAVTLDGVRVELAANIGLPEDAAAALENGAEGVGLFRTEFLFMDRDDLPTEEEQFEAYRA 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 429 VLLAAGDKPIIFRTMDIGGDKSIPYLNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQI 508
Cdd:COG1080  319 VAEAMGGRPVTIRTLDIGGDKPLPYLPLPKEENPFLGLRAIRLCLDRPELFRTQLRAILRASAHGNLRIMFPMISSVEEL 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 509 LWVKGEIQKAIVELKRDGLRYAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPITP 588
Cdd:COG1080  399 RQAKALLEEAKAELRAEGIPFDEDIPVGIMIEVPAAALIADQLAKEVDFFSIGTNDLIQYTLAVDRGNEKVAYLYDPLHP 478

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 589 SFLRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDSEACRELARQACECRSAQ 668
Cdd:COG1080  479 AVLRLIKMVIDAAHKAGKPVGVCGEMAGDPLATPLLLGLGLDELSMSPSSIPAVKAIIRRLDLAEARALAEKALALDTAE 558

                        570
                 ....*....|..
gi 485777446 669 EIEALLTAFTPE 680
Cdd:COG1080  559 EVRALLEEFLAE 570
PRK11177 PRK11177
phosphoenolpyruvate-protein phosphotransferase PtsI;
163-681 2.04e-147

phosphoenolpyruvate-protein phosphotransferase PtsI;


Pssm-ID: 183017 [Multi-domain]  Cd Length: 575  Bit Score: 445.61  E-value: 2.04e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 163 AEQLN---QQLRERDGESK-TILSAHLSLIQDDEFAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDI 238
Cdd:PRK11177  51 SAQLEaikTKAGETFGEEKeAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHSVIEGQAKALEELDDEYLKERAADV 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 239 RDISEQLLhitwpelkpRNKLVL--------EKPTILVAEDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPV 310
Cdd:PRK11177 131 RDIGKRLL---------KNILGLkiidlsaiQEEVILVAADLTPSETAQLNLKKVLGFITDIGGRTSHTSIMARSLELPA 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 311 LSGLPlDAIARYA-GQPAVLDAQCGVLAINPNDAVSGYYQVAQT--LADKRQKQQAQAAAQLaySRDNKRIDIAANIGTA 387
Cdd:PRK11177 202 IVGTG-NITKQVKnGDYLILDAVNNQIYVNPTNEVIEELKAVQEqyASEKAELAKLKDLPAI--TLDGHQVEVCANIGTV 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 388 LEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQQVLLAAGDKPIIFRTMDIGGDKSIPYLNIPQEENPFLGYR 467
Cdd:PRK11177 279 RDVEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFQAYKAVAEAMGSQAVIVRTMDIGGDKELPYMNLPKEENPFLGWR 358

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 468 AVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQILWVKGEIQKAIVELKRDGLRYAETITLGIMVEVPSVCYI 547
Cdd:PRK11177 359 AIRIAMDRKEILHDQLRAILRASAFGKLRIMFPMIISVEEVRELKAEIEILKQELRDEGKAFDESIEIGVMVETPAAAVI 438

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 548 IDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPITPSFLRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGL 627
Cdd:PRK11177 439 ARHLAKEVDFFSIGTNDLTQYTLAVDRGNELISHLYNPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGM 518

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 485777446 628 GLDELSMSSPRIPAVKSQLRQLDSEACRELARQACECRSAQEIEALLTAFTPEE 681
Cdd:PRK11177 519 GLDEFSMSAISIPRIKKIIRNTNFEDAKALAEQALAQPTADELMTLVNKFIEEK 572
PTS_I_fam TIGR01417
phosphoenolpyruvate-protein phosphotransferase; This model recognizes a distinct clade of ...
 121-674 3.40e-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: 444.62  E-value: 3.40e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  121 VPAS-GVGVGTLTLLQSDSLD-SYRAIPASAQDST--RLEHSLATLAEQL----NQQLRERDGESKTILSAHLSLIQDDE 192
Cdd:TIGR01417   4 IGVSpGIAIGKALLLKKPDLViDRKKISASQVDQEisRFLSARAKAKEDLetikTKAGKTFGQEKAAIFEAHILILEDPE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  193 FAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDIRDISEQLL-HITWPELKprNKLVLEKPTILVAED 271
Cdd:TIGR01417  84 LTEEVIELIKKDHKNAEFAAHEVFEGQAKSLEEMDDEYLKERAADIRDIGNRLLgHLLGVKIS--DLSEIQDEVILVAED 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  272 LTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPLDAIARYAGQPAVLDAQCGVLAINP-NDAVSGYYQV 350
Cdd:TIGR01417 162 LTPSETAQLNLKYVKGFLTDAGGKTSHTAIMARSLEIPAIVGTKSVTSQVKNGDTVIIDGVKGIVIFNPsSETIDKYEAK 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  351 aQTLADKRQKQQAQAAAQLAYSRDNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQQVL 430
Cdd:TIGR01417 242 -QEAVSSEKAELAKLKDKPAITLDGHQVELAANIGTVDDVEGAERNGGEGIGLFRTEFLYMSRDQLPTEEEQFAAYKTVL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  431 LAAGDKPIIFRTMDIGGDKSIPYLNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQILW 510
Cdd:TIGR01417 321 EAMESDAVIVRTLDIGGDKELPYLNFPKEENPFLGYRAIRLALEREEILRTQLRAILRASAYGKLRIMFPMVATVEEIRA 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  511 VKGEIQKAIVELKRDGLRYAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPITPSF 590
Cdd:TIGR01417 401 VKQELEEEKQELNDEGKAFDENIEVGVMIEIPSAALIADHLAKEVDFFSIGTNDLTQYTLAVDRGNDLISNLYQPYNPAV 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  591 LRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDSEACRELARQACECRSAQEI 670
Cdd:TIGR01417 481 LRLIKLVIDAAKAEGIWVGMCGEMAGDERAIPLLLGLGLRELSMSASSILRIKMIIRKLNIEECKSLAEKALAQPTTEEV 560


                  ....
gi 485777446  671 EALL 674
Cdd:TIGR01417 561 HKLV 564
PEP-utilizers_C pfam02896
PEP-utilizing enzyme, PEP-binding domain; This entry represents a TIM barrel domain found at ...
 374-651 8.82e-123

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: 371.25  E-value: 8.82e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  374 DNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQQVLLAAGDKPIIFRTMDIGGDKSIPY 453
Cdd:pfam02896  16 DGTKIKVAANIGTPDDAEAALANGAEGIGLYRTEFLFMDRDELPTEDEQFEAYKGVLEAMNGRPVTVRTLDIGGDKELPY 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  454 LNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQILWVKGEIQKAIVELkRDGLRYAETI 533
Cdd:pfam02896  96 LEEPEEMNPFLGWRGIRIGLDRPELFRTQLRAILRASAFGNLRIMFPMVASVEELREAKAIIEEVKEEL-DAEVGFDKDI 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  534 TLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPITPSFLRMLQQIVTTAHQRGKWVGICGE 613
Cdd:pfam02896 175 KVGIMIEVPSAALLADQLAKEVDFFSIGTNDLTQYTLAVDRDNERVAYLYDPLHPAVLRLIKEVIRAAHRHGKWVGICGE 254

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 485777446  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 2.62e-50

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: 172.84  E-value: 2.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  686 LLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAK 765
Cdd:TIGR00848   1 LLNKDLIFLDQQFTSKEDVIKFLANKLLENGYISDTEEFLEDLLKREEEGTTGIGDGVAIPHAKSAAVKQPFVAIARLVK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 485777446  766 PIGWQSEMGE-VELVIMLTLG-ANEGMNHVKVFSQLARKLVNKNFRQSL 812
Cdd:TIGR00848  81 GVDWQSLDGKpVKLIFLIAVPkDEAGNTHLKALSQLARLLLNDEFRAKL 129
PtsN COG1762
Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate ...
 686-829 2.14e-38

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: 139.99  E-value: 2.14e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 686 LLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAK 765
Cdd:COG1762    6 LLTPELILLDLEASSKEEAIEELAELLAEKGYVLDKEEYLEALLEREELGSTGIGPGIAIPHARPEGVKKPGIAVARLKE 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485777446 766 PIGWQSEMGE-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 1.53e-35

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: 131.14  E-value: 1.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 690 ENIFVDQDFSNKEQAIQFLCGNLGVNGRteHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAKPIGW 769
Cdd:cd00211    4 ENIRLNLKAKSKEEAIEELAQLLVAAGY--VEEEYIEALLEREKEGSTGIGNGIAIPHAKSEAVKKPGIAVLRLKEPVDF 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 485777446 770 QSEMGE-VELVIMltLGANEGMNHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLL 825
Cdd:cd00211   82 GSLDGQpVHLIFL--LAAPDSNEHLKALSQLARLLSDEEFVEQLLNAQSKEEILALL 136
PTS_EIIA_2 pfam00359
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
686-826 8.68e-33

Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;


Pssm-ID: 459780 [Multi-domain]  Cd Length: 139  Bit Score: 123.47  E-value: 8.68e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  686 LLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFEleEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAK 765
Cdd:pfam00359   1 LLDKELIFLNLEAKSKEEAIEFLADKLVEAGYVEPAYL--EAILEREKEGSTGIGNGIAIPHARSEAVKKPGIAVLTLKE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 485777446  766 PIGWQSEMGE-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 4.42e-20

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


Pssm-ID: 182066 [Multi-domain]  Cd Length: 631  Bit Score: 95.19  E-value: 4.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 692 IFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAKPIGWQS 771
Cdd:PRK09765  12 LCLNARFTSREEAIHALAQRLAALGKISSTEQFLEEVYRRESLGPTALGEGLAVPHGKTAAVKEAAFAVATLSEPLQWEG 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 772 --EMGEVELVIMLTLGANE-GMNHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLETE 828
Cdd:PRK09765  92 vdGPEAVDLIFLLAIPPNEaGTTHMQLLTALTTRLADDEIRARIQSATTPDELLSALDDK 151
PtsH COG1925
HPr or related phosphotransfer protein [Signal transduction mechanisms, Carbohydrate transport ...
 1-87 8.88e-18

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


Pssm-ID: 441528 [Multi-domain]  Cd Length: 88  Bit Score: 78.61  E-value: 8.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446   1 MLTIQFLCPLPNGLHARPAWELKEQCSQWQSEITFINhrQNAKADAKSSLALIGTGTLFNDSCSLNISDSDEEQARRVLE 80
Cdd:COG1925    1 MLEREVTIVNKLGLHARPAAKLVQLASKFDSEITVEK--GGKEVNAKSIMGLMSLGAKKGDEVTITAEGPDAEEALDALA 78


                 ....*..
gi 485777446  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 1.33e-17

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: 77.93  E-value: 1.33e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 485777446   5 QFLCPLPNGLHARPAWELKEQCSQWQSEITFINHrqNAKADAKSSLALIGTGTLFNDSCSLNISDSDEEQARRVLEEYI 83
Cdd:cd00367    1 TVTITNPLGLHARPAALLVQLASKFKSDITLRKG--GRKANAKSILGLMSLGAKQGDEITLSAEGEDAEEALEALAELL 77
PTS-HPr pfam00381
PTS HPr component phosphorylation site;
5-84 3.76e-13

PTS HPr component phosphorylation site;


Pssm-ID: 459792 [Multi-domain]  Cd Length: 79  Bit Score: 65.10  E-value: 3.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446    5 QFLCPLPNGLHARPAWELKEQCSQWQSEITFINHrqNAKADAKSSLALIGTGTLFNDSCSLNISDSDEEQARRVLEEYIQ 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 9.94e-06

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: 44.18  E-value: 9.94e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 485777446   11 PNGLHARPAWELKEQCSQWQSEITFInhRQNAKADAKSSLALIGTGTLFNDSCSLNISDSDEEQARRVLEEYI 83
Cdd:TIGR01003  11 KVGLHARPAAILVKLASGFDSEITLT--KNGKEVNAKSIMGIMMLGAGQGTEVTVSADGEDEAEALEALAKLF 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: 657.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 117 LYGnVPAS-GVGVGTLTLLQSDSLD-SYRAIPASAQDS--TRLEHSLATLAEQLN---QQLRERDGESKT-ILSAHLSLI 188
Cdd:COG1080    1 LKG-IAASpGIAIGKAFLLREEDLEvPEYTISPEDVEAeiARLEAALAKAREELEalrEKAPEDLGEEEAaIFDAHLLLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 189 QDDEFAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDIRDISEQLLHITWPElKPRNKLVLEKPTILV 268
Cdd:COG1080   80 EDPELIEEVEELIREGRYNAEWALKEVIEELAAQFEALDDEYLRERAADIRDVGRRVLRNLLGV-EAPDLSDLPEPVILV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 269 AEDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPLDAIARYAGQPAVLDAQCGVLAINPNDAVSGYY 348
Cdd:COG1080  159 AHDLTPSDTAQLDPSRVAGFVTDLGGRTSHTAILARSLGIPAVVGLGDALLLVKDGDLVIVDGDAGVVIVNPDEETLAEY 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 349 QVAQTLADKRQKQQAQAAAQLAYSRDNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQQ 428
Cdd:COG1080  239 RERQAEYAAERAELARLRDLPAVTLDGVRVELAANIGLPEDAAAALENGAEGVGLFRTEFLFMDRDDLPTEEEQFEAYRA 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 429 VLLAAGDKPIIFRTMDIGGDKSIPYLNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQI 508
Cdd:COG1080  319 VAEAMGGRPVTIRTLDIGGDKPLPYLPLPKEENPFLGLRAIRLCLDRPELFRTQLRAILRASAHGNLRIMFPMISSVEEL 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 509 LWVKGEIQKAIVELKRDGLRYAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPITP 588
Cdd:COG1080  399 RQAKALLEEAKAELRAEGIPFDEDIPVGIMIEVPAAALIADQLAKEVDFFSIGTNDLIQYTLAVDRGNEKVAYLYDPLHP 478

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 589 SFLRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDSEACRELARQACECRSAQ 668
Cdd:COG1080  479 AVLRLIKMVIDAAHKAGKPVGVCGEMAGDPLATPLLLGLGLDELSMSPSSIPAVKAIIRRLDLAEARALAEKALALDTAE 558

                        570
                 ....*....|..
gi 485777446 669 EIEALLTAFTPE 680
Cdd:COG1080  559 EVRALLEEFLAE 570
PRK11177 PRK11177
phosphoenolpyruvate-protein phosphotransferase PtsI;
163-681 2.04e-147

phosphoenolpyruvate-protein phosphotransferase PtsI;


Pssm-ID: 183017 [Multi-domain]  Cd Length: 575  Bit Score: 445.61  E-value: 2.04e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 163 AEQLN---QQLRERDGESK-TILSAHLSLIQDDEFAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDI 238
Cdd:PRK11177  51 SAQLEaikTKAGETFGEEKeAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHSVIEGQAKALEELDDEYLKERAADV 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 239 RDISEQLLhitwpelkpRNKLVL--------EKPTILVAEDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPV 310
Cdd:PRK11177 131 RDIGKRLL---------KNILGLkiidlsaiQEEVILVAADLTPSETAQLNLKKVLGFITDIGGRTSHTSIMARSLELPA 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 311 LSGLPlDAIARYA-GQPAVLDAQCGVLAINPNDAVSGYYQVAQT--LADKRQKQQAQAAAQLaySRDNKRIDIAANIGTA 387
Cdd:PRK11177 202 IVGTG-NITKQVKnGDYLILDAVNNQIYVNPTNEVIEELKAVQEqyASEKAELAKLKDLPAI--TLDGHQVEVCANIGTV 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 388 LEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQQVLLAAGDKPIIFRTMDIGGDKSIPYLNIPQEENPFLGYR 467
Cdd:PRK11177 279 RDVEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFQAYKAVAEAMGSQAVIVRTMDIGGDKELPYMNLPKEENPFLGWR 358

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 468 AVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQILWVKGEIQKAIVELKRDGLRYAETITLGIMVEVPSVCYI 547
Cdd:PRK11177 359 AIRIAMDRKEILHDQLRAILRASAFGKLRIMFPMIISVEEVRELKAEIEILKQELRDEGKAFDESIEIGVMVETPAAAVI 438

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 548 IDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPITPSFLRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGL 627
Cdd:PRK11177 439 ARHLAKEVDFFSIGTNDLTQYTLAVDRGNELISHLYNPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGM 518

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 485777446 628 GLDELSMSSPRIPAVKSQLRQLDSEACRELARQACECRSAQEIEALLTAFTPEE 681
Cdd:PRK11177 519 GLDEFSMSAISIPRIKKIIRNTNFEDAKALAEQALAQPTADELMTLVNKFIEEK 572
PTS_I_fam TIGR01417
phosphoenolpyruvate-protein phosphotransferase; This model recognizes a distinct clade of ...
 121-674 3.40e-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: 444.62  E-value: 3.40e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  121 VPAS-GVGVGTLTLLQSDSLD-SYRAIPASAQDST--RLEHSLATLAEQL----NQQLRERDGESKTILSAHLSLIQDDE 192
Cdd:TIGR01417   4 IGVSpGIAIGKALLLKKPDLViDRKKISASQVDQEisRFLSARAKAKEDLetikTKAGKTFGQEKAAIFEAHILILEDPE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  193 FAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDIRDISEQLL-HITWPELKprNKLVLEKPTILVAED 271
Cdd:TIGR01417  84 LTEEVIELIKKDHKNAEFAAHEVFEGQAKSLEEMDDEYLKERAADIRDIGNRLLgHLLGVKIS--DLSEIQDEVILVAED 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  272 LTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPLDAIARYAGQPAVLDAQCGVLAINP-NDAVSGYYQV 350
Cdd:TIGR01417 162 LTPSETAQLNLKYVKGFLTDAGGKTSHTAIMARSLEIPAIVGTKSVTSQVKNGDTVIIDGVKGIVIFNPsSETIDKYEAK 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  351 aQTLADKRQKQQAQAAAQLAYSRDNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQQVL 430
Cdd:TIGR01417 242 -QEAVSSEKAELAKLKDKPAITLDGHQVELAANIGTVDDVEGAERNGGEGIGLFRTEFLYMSRDQLPTEEEQFAAYKTVL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  431 LAAGDKPIIFRTMDIGGDKSIPYLNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQILW 510
Cdd:TIGR01417 321 EAMESDAVIVRTLDIGGDKELPYLNFPKEENPFLGYRAIRLALEREEILRTQLRAILRASAYGKLRIMFPMVATVEEIRA 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  511 VKGEIQKAIVELKRDGLRYAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPITPSF 590
Cdd:TIGR01417 401 VKQELEEEKQELNDEGKAFDENIEVGVMIEIPSAALIADHLAKEVDFFSIGTNDLTQYTLAVDRGNDLISNLYQPYNPAV 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  591 LRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDSEACRELARQACECRSAQEI 670
Cdd:TIGR01417 481 LRLIKLVIDAAKAEGIWVGMCGEMAGDERAIPLLLGLGLRELSMSASSILRIKMIIRKLNIEECKSLAEKALAQPTTEEV 560


                  ....
gi 485777446  671 EALL 674
Cdd:TIGR01417 561 HKLV 564
PEP-utilizers_C pfam02896
PEP-utilizing enzyme, PEP-binding domain; This entry represents a TIM barrel domain found at ...
 374-651 8.82e-123

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: 371.25  E-value: 8.82e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  374 DNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAPDEQEQFEAYQQVLLAAGDKPIIFRTMDIGGDKSIPY 453
Cdd:pfam02896  16 DGTKIKVAANIGTPDDAEAALANGAEGIGLYRTEFLFMDRDELPTEDEQFEAYKGVLEAMNGRPVTVRTLDIGGDKELPY 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  454 LNIPQEENPFLGYRAVRIYPEFAGLFRTQLRAILRAASFGNAQLMIPMVHSLDQILWVKGEIQKAIVELkRDGLRYAETI 533
Cdd:pfam02896  96 LEEPEEMNPFLGWRGIRIGLDRPELFRTQLRAILRASAFGNLRIMFPMVASVEELREAKAIIEEVKEEL-DAEVGFDKDI 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  534 TLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVDRNNPRVSPLYNPITPSFLRMLQQIVTTAHQRGKWVGICGE 613
Cdd:pfam02896 175 KVGIMIEVPSAALLADQLAKEVDFFSIGTNDLTQYTLAVDRDNERVAYLYDPLHPAVLRLIKEVIRAAHRHGKWVGICGE 254

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 485777446  614 LGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDS 651
Cdd:pfam02896 255 MAGDPSAVPLLVGLGLDEFSMSPDSVPRARALLAQIDR 292
PRK11061 PRK11061
phosphoenolpyruvate--protein phosphotransferase;
123-683 2.51e-92

phosphoenolpyruvate--protein phosphotransferase;


Pssm-ID: 182937 [Multi-domain]  Cd Length: 748  Bit Score: 306.54  E-value: 2.51e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 123 ASGVGVGTLtlLQSDSLDSYRAI-PASAQDSTRlEHSLATLA--EQLNQ--QLRER-----DGESKTILSAHLSLIQDDE 192
Cdd:PRK11061 177 SPGVAIAEG--WQDATQPLLEQVyPASTLDPAL-ERERLTGAleEAANEfrRYSKRfaagaQKETAAIFDLYSHLLNDPR 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 193 FAgniRRLMTEQHQGLGA--AIisnmEQVCAKLS---ASASD-YLRERVSDIRDISEQLL---------HITWPElkprn 257
Cdd:PRK11061 254 LR---RELFAEVDKGSVAewAV----KQVIEKFAeqfAALSDnYLRERAGDLRALGQRLLfhlddseqgPNAWPE----- 321

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 258 klvlekPTILVAEDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPLDAiARYAGQPAVLDAQCGVLA 337
Cdd:PRK11061 322 ------RFILVADELTATLLAELPQDRLAGVVVRDGAANSHAAILVRALGIPTVMGADIQP-SLLHQRLLIVDGYRGELL 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 338 INPNDAVSGYYQVAQTLADKRQKQQAQAAAQLAYSRDNKRIDIAANIGTALEAPGAFANGAEGVGLFRTEMLYMDRDSAP 417
Cdd:PRK11061 395 VDPEPVLLQEYQRLISEEIELSRLAEDDVNLPAQLKSGERIKVMLNAGLSAEHEEKLGSRVDGVGLYRTEIPFMLQSGFP 474

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 418 DEQEQFEAYQQVLLAAGDKPIIFRTMDIGGDKSIPYLNIpQEENPFLGYRAVRI---YPEfagLFRTQLRAILRA-ASFG 493
Cdd:PRK11061 475 SEEEQVAQYQGMLQMFPDKPVTLRTLDIGADKQLPYMPI-SEENPCLGWRGIRItldQPE---IFLIQVRAMLRAnAATG 550

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 494 NAQLMIPMVHSLDQILWVKGEIQKAIVELKRDGLRYAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVD 573
Cdd:PRK11061 551 NLSILLPMVTSIDEVDEARRLIDRAGREVEEMLGYEIPKPRIGIMIEVPSMVFMLPHLASRVDFISVGTNDLTQYLLAVD 630

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 574 RNNPRVSPLYNPITPSFLRMLQQIVTTAHQRGKWVGICGELGGESRYLPLLLGLGLDELSMSSPRIPAVKSQLRQLDSEA 653
Cdd:PRK11061 631 RNNTRVASLYDSLHPAMLRALKMIADEAEQHGLPVSLCGEMAGDPMGALLLIGLGYRHLSMNGRSVARVKYLLRHIDLAE 710

                        570       580       590
                 ....*....|....*....|....*....|
gi 485777446 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 2.62e-50

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: 172.84  E-value: 2.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  686 LLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAK 765
Cdd:TIGR00848   1 LLNKDLIFLDQQFTSKEDVIKFLANKLLENGYISDTEEFLEDLLKREEEGTTGIGDGVAIPHAKSAAVKQPFVAIARLVK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 485777446  766 PIGWQSEMGE-VELVIMLTLG-ANEGMNHVKVFSQLARKLVNKNFRQSL 812
Cdd:TIGR00848  81 GVDWQSLDGKpVKLIFLIAVPkDEAGNTHLKALSQLARLLLNDEFRAKL 129
PRK06464 PRK06464
phosphoenolpyruvate synthase; Validated
 380-620 1.98e-43

phosphoenolpyruvate synthase; Validated


Pssm-ID: 235809 [Multi-domain]  Cd Length: 795  Bit Score: 169.16  E-value: 1.98e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 380 IAANIGTALEAPGAFANGAEGVGLFRTEML-----------YMDRDSAPDEQEQF------------EAYQQVL------ 430
Cdd:PRK06464 483 IMMNVGNPERAFDFAALPNDGVGLARLEFIinnmigvhplaLLEFDQQDADLKAEieeltagyaspeEFYVDKLaegiat 562

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 431 LAAG--DKPIIFRTMD---------IGGDKSIPylnipQEENPFLGYRAVRIY--PEFAGLFRTQLRAILRA---ASFGN 494
Cdd:PRK06464 563 VAAAfyPKPVIVRLSDfksneyanlIGGERYEP-----EEENPMLGFRGASRYlsESFREAFALECEAIKRVreeMGLTN 637

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 495 AQLMIPMVHSLDqilwvkgEIQKAIVELKRDGL-RYAETITLGIMVEVPSVCYIIDHFCDEVDFFSIGSNDMTQYLYAVD 573
Cdd:PRK06464 638 VEVMIPFVRTVE-------EAEKVIELLAENGLkRGENGLKVIMMCEIPSNALLAEEFLEYFDGFSIGSNDLTQLTLGLD 710

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 485777446 574 RNNPRVSPLYNPITPSFLRMLQQIVTTAHQRGKWVGICGElgGESRY 620
Cdd:PRK06464 711 RDSGLVAHLFDERNPAVKKLISMAIKAAKKAGKYVGICGQ--APSDH 755
PtsN COG1762
Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate ...
 686-829 2.14e-38

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: 139.99  E-value: 2.14e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 686 LLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAK 765
Cdd:COG1762    6 LLTPELILLDLEASSKEEAIEELAELLAEKGYVLDKEEYLEALLEREELGSTGIGPGIAIPHARPEGVKKPGIAVARLKE 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485777446 766 PIGWQSEMGE-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 1.53e-35

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: 131.14  E-value: 1.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 690 ENIFVDQDFSNKEQAIQFLCGNLGVNGRteHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAKPIGW 769
Cdd:cd00211    4 ENIRLNLKAKSKEEAIEELAQLLVAAGY--VEEEYIEALLEREKEGSTGIGNGIAIPHAKSEAVKKPGIAVLRLKEPVDF 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 485777446 770 QSEMGE-VELVIMltLGANEGMNHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLL 825
Cdd:cd00211   82 GSLDGQpVHLIFL--LAAPDSNEHLKALSQLARLLSDEEFVEQLLNAQSKEEILALL 136
PTS_EIIA_2 pfam00359
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
686-826 8.68e-33

Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;


Pssm-ID: 459780 [Multi-domain]  Cd Length: 139  Bit Score: 123.47  E-value: 8.68e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  686 LLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFEleEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAK 765
Cdd:pfam00359   1 LLDKELIFLNLEAKSKEEAIEFLADKLVEAGYVEPAYL--EAILEREKEGSTGIGNGIAIPHARSEAVKKPGIAVLTLKE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 485777446  766 PIGWQSEMGE-VELVIMLtLGANEGMNHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLE 826
Cdd:pfam00359  79 PVDFGSEDGKpVKLIFLL-AAPDNEASHLKILSQLARLLQDEEFVEKLLKAKDPEEILEILK 139
PRK11377 PRK11377
dihydroxyacetone kinase subunit M; Provisional
 11-338 2.84e-23

dihydroxyacetone kinase subunit M; Provisional


Pssm-ID: 183108 [Multi-domain]  Cd Length: 473  Bit Score: 104.06  E-value: 2.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  11 PNGLHARPAWELKEQCSQWQSEITFINHRQNAKADAKSSLALIgtGTLFNDSCSLNISDSDEEQARRVLEEYIQVRFIDS 90
Cdd:PRK11377 165 RNGLHVRPASRLVYTLSTFNADMLLEKNGKCVTPESLNQIALL--QVRYNDTLRLIAKGPEAEEALIAFRQLAEDNFGET 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  91 DSVQPTqaelTAHPLPRSLSrlNPDLLYGNVPASGVGVGTLTLLQsDSLDSYRAIPASAQDstrlehsLATLAEQLNQQL 170
Cdd:PRK11377 243 EEVAPP----TLRPVPSPVS--GKAFYYQPVLCTVQAKSTLTVEE-EQERLRQAIDFTLLD-------LMTLTAKAEASG 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 171 RERDGeskTILSAHLSLIQDDEFAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRERVSDIRDISEQLL-HIT 249
Cdd:PRK11377 309 LDDIA---AIFSGHHTLLDDPELLAAASERLQHEHCTAEYAWQQVLKELSQQYQQLDDEYLQARYIDVDDLLHRTLvHLT 385

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 250 wpELKPRnKLVLEKPTILVAEDLTPSQFLSLDLKNLAGMILEKTGRTSHTLILARASAIPVLSGL--PLDAIAryAGQPA 327
Cdd:PRK11377 386 --QTKEE-LPQFNSPTILLAENIYPSTVLQLDPAVVKGICLSAGSPLSHSAIIARELGIGWICQQgeKLYAIQ--PEETL 460

                        330
                 ....*....|.
gi 485777446 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 4.42e-20

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


Pssm-ID: 182066 [Multi-domain]  Cd Length: 631  Bit Score: 95.19  E-value: 4.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 692 IFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLAKPIGWQS 771
Cdd:PRK09765  12 LCLNARFTSREEAIHALAQRLAALGKISSTEQFLEEVYRRESLGPTALGEGLAVPHGKTAAVKEAAFAVATLSEPLQWEG 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 772 --EMGEVELVIMLTLGANE-GMNHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLETE 828
Cdd:PRK09765  92 vdGPEAVDLIFLLAIPPNEaGTTHMQLLTALTTRLADDEIRARIQSATTPDELLSALDDK 151
PtsH COG1925
HPr or related phosphotransfer protein [Signal transduction mechanisms, Carbohydrate transport ...
 1-87 8.88e-18

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


Pssm-ID: 441528 [Multi-domain]  Cd Length: 88  Bit Score: 78.61  E-value: 8.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446   1 MLTIQFLCPLPNGLHARPAWELKEQCSQWQSEITFINhrQNAKADAKSSLALIGTGTLFNDSCSLNISDSDEEQARRVLE 80
Cdd:COG1925    1 MLEREVTIVNKLGLHARPAAKLVQLASKFDSEITVEK--GGKEVNAKSIMGLMSLGAKKGDEVTITAEGPDAEEALDALA 78


                 ....*..
gi 485777446  81 EYIQVRF 87
Cdd:COG1925   79 ALIESGF 85
MtlA2 COG4668
Mannitol/fructose-specific phosphotransferase system, IIA domain [Carbohydrate transport and ...
 685-826 9.05e-18

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


Pssm-ID: 443705 [Multi-domain]  Cd Length: 143  Bit Score: 80.59  E-value: 9.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 685 PLLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFelEEDVWQREEIVTTGVGFGVAIPH----TKSQwIRHSSISI 760
Cdd:COG4668    2 LILTKENIRLNASAANKEEAIRLAGQLLVEAGYVEPEY--IDAMLEREAQVSTYLGNGIAIPHgtneAKDL-VLKTGISV 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 485777446 761 ARLAKPIGWqSEMGEVELVIMLTLGANEgmnHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLE 826
Cdd:COG4668   79 LQFPDGVDW-GDGNTVYLVIGIAAKSDE---HLEILRQLARVLSDEENVEKLAKATDAEEILALLT 140
PTS-HPr_like cd00367
Histidine-containing phosphocarrier protein (HPr)-like proteins. HPr is a central component of ...
 5-83 1.33e-17

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: 77.93  E-value: 1.33e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 485777446   5 QFLCPLPNGLHARPAWELKEQCSQWQSEITFINHrqNAKADAKSSLALIGTGTLFNDSCSLNISDSDEEQARRVLEEYI 83
Cdd:cd00367    1 TVTITNPLGLHARPAALLVQLASKFKSDITLRKG--GRKANAKSILGLMSLGAKQGDEITLSAEGEDAEEALEALAELL 77
PRK09913 PRK09913
PTS fructose transporter subunit IIA;
685-808 1.69e-15

PTS fructose transporter subunit IIA;


Pssm-ID: 182141 [Multi-domain]  Cd Length: 148  Bit Score: 74.54  E-value: 1.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 685 PLLALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFELEEDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISIARLA 764
Cdd:PRK09913   2 AALTASCIDLNIQGNGAYSILKQLATIALQNGFITDSHQFLQTLLLREKMHSTGFGSGVAVPHGKSACVKQPFVLFARKA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 485777446 765 KPIGWQSEMGE-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 1.37e-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: 69.36  E-value: 1.37e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 485777446  261 LEKPTILVAEDLTPSQFLslDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLPLDAIARYAGQPAVLDAQCG 334
Cdd:pfam00391   2 LPEGVILVAPDTTPSDTA--GLDKAAGIVTERGGMTSHAAIVARELGIPAVVGVGDATILLKEGDLVTVDGSTG 73
PTS-HPr pfam00381
PTS HPr component phosphorylation site;
5-84 3.76e-13

PTS HPr component phosphorylation site;


Pssm-ID: 459792 [Multi-domain]  Cd Length: 79  Bit Score: 65.10  E-value: 3.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446    5 QFLCPLPNGLHARPAWELKEQCSQWQSEITFINHrqNAKADAKSSLALIGTGTLFNDSCSLNISDSDEEQARRVLEEYIQ 84
Cdd:pfam00381   2 TVTITNPLGLHARPAALLVQLASKFDSDITLEKG--GKKVNAKSIMGLMSLGAKQGDEITISAEGEDEEEALEALAALLE 79
PEP-utilizers_N pfam05524
PEP-utilizing enzyme, N-terminal;
121-234 6.99e-13

PEP-utilizing enzyme, N-terminal;


Pssm-ID: 461671 [Multi-domain]  Cd Length: 125  Bit Score: 66.10  E-value: 6.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446  121 VPAS-GVGVGTLTLLQSDSLDSYRAIPASAQDS----TRLEHSLATLAEQLnQQLRER-----DGESKTILSAHLSLIQD 190
Cdd:pfam05524   3 IGASpGIAIGKAVVLEEPELEVPDEREVPADDVeaeiARLEAALEAAREEL-EALAERaagelGEEEAAIFEAHLMMLED 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 485777446  191 DEFAGNIRRLMTEQHQGLGAAIISNMEQVCAKLSASASDYLRER 234
Cdd:pfam05524  82 PELLEEVEELIREGGLNAEAAVKEVVDEFAAMFEAMDDPYLRER 125
PRK15083 PRK15083
PTS system mannitol-specific transporter subunit IICBA; Provisional
 687-828 1.57e-06

PTS system mannitol-specific transporter subunit IICBA; Provisional


Pssm-ID: 237905 [Multi-domain]  Cd Length: 639  Bit Score: 51.59  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 687 LALENIFVDQDFSNKEQAIQFlCGNLGVNGRTEHPfELEEDVWQREEIVTTGVGFGVAIPH----TKSQWIRhSSISIAR 762
Cdd:PRK15083 497 LGAENIFLGLKAATKEEAIRF-AGEQLVKGGYVEP-EYVDAMLDREKLTSTYLGESIAVPHgtveAKDRVLK-TGVVFCQ 573

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 485777446 763 LAKPIGWQSEMGEV-ELVIMLTLGANEgmnHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLETE 828
Cdd:PRK15083 574 YPEGVRFGEEEDDIaRLVIGIAARNNE---HIQVITSLTNALDDESVIERLAHTTSVDEVLELLAGK 637
PTS_HPr_family TIGR01003
Phosphotransferase System HPr (HPr) Family; The HPr family are bacterial proteins (or domains ...
 11-83 9.94e-06

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: 44.18  E-value: 9.94e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 485777446   11 PNGLHARPAWELKEQCSQWQSEITFInhRQNAKADAKSSLALIGTGTLFNDSCSLNISDSDEEQARRVLEEYI 83
Cdd:TIGR01003  11 KVGLHARPAAILVKLASGFDSEITLT--KNGKEVNAKSIMGIMMLGAGQGTEVTVSADGEDEAEALEALAKLF 81
PRK10896 PRK10896
PTS IIA-like nitrogen regulatory protein PtsN;
726-816 1.25e-05

PTS IIA-like nitrogen regulatory protein PtsN;


Pssm-ID: 182818 [Multi-domain]  Cd Length: 154  Bit Score: 45.90  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 726 EDVWQREEIVTTGVGFGVAIPHTKSQWIRHSSISI-ARLAKPIGWQS-EMGEVELVIMLTLGANEGMNHVKVFSQLARKL 803
Cdd:PRK10896  51 EAILTREKMGSTGIGNGIAIPHGKLEEDTLRAVGVfVQLEQPIAFDAiDNQPVDLLFALLVPADQCKTHLHTLSLVAKRL 130

                         90
                 ....*....|...
gi 485777446 804 VNKNFRQSLFAAQ 816
Cdd:PRK10896 131 ADKTICRRLRAAQ 143
PykA2 COG3848
Phosphohistidine swiveling domain of PEP-utilizing enzymes [Signal transduction mechanisms];
266-315 1.09e-03

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


Pssm-ID: 443058  Cd Length: 321  Bit Score: 42.19  E-value: 1.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 485777446 266 ILVAEDLTPSqFLSlDLKNLAGMILEKTGRTSHTLILARASAIPVLSGLP 315
Cdd:COG3848  245 ILVVPSTDAE-FVP-AIEKAAGIITEEGGLTSHAAIVGLELGIPVIVGAE 292
PRK11109 PRK11109
fused PTS fructose transporter subunit IIA/HPr protein;
687-825 1.26e-03

fused PTS fructose transporter subunit IIA/HPr protein;


Pssm-ID: 236849 [Multi-domain]  Cd Length: 375  Bit Score: 41.86  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 687 LALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFEleEDVWQREEIVTTGVGFGVAIPH----TKSQwIRHSSISIAR 762
Cdd:PRK11109   4 LSVQDIHLGQQAGNKEEAIRQVAAALTQAGNVAEGYV--DGMLAREQQTSTFLGNGIAIPHgttdTRDL-VLKTGVQVFQ 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 485777446 763 LAKPIGWqsemGE---VELVIMLTLGANEgmnHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLL 825
Cdd:PRK11109  81 FPQGVTW----GDgqtAYVAIGIAAKSDE---HLGLLRQLTHVLSDDSVAEQLKSATTAEELRALL 139
PRK13779 PRK13779
bifunctional PTS system fructose-specific transporter subunit IIA/HPr protein; Provisional
 687-828 7.99e-03

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


Pssm-ID: 237502 [Multi-domain]  Cd Length: 503  Bit Score: 39.47  E-value: 7.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485777446 687 LALENIFVDQDFSNKEQAIQFLCGNLGVNGRTEHPFelEEDVWQREEIVTTGVGFGVAIPH----TKSQwIRHSSISIAR 762
Cdd:PRK13779   4 LSESNIHLNAQAINKQQAIEMAAAALEQAGNVENGY--LQGMLARELQTSTFLGNGIAIPHgtldTRHM-VKNTGVQIFQ 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 485777446 763 LAKPIGWqSEMGEVELVIMLTLGANEgmnHVKVFSQLARKLVNKNFRQSLFAAQDAQSILTLLETE 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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