|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10682 |
PRK10682 |
putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional |
1-369 |
0e+00 |
|
putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional
Pssm-ID: 182645 [Multi-domain] Cd Length: 370 Bit Score: 753.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 1 MVTQRKKWLSGVVAGLLMAASVTA-SAEEKTLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGSTGYD 79
Cdd:PRK10682 1 MTALNKKWLSGLVAGALMAVSVGTlAAEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 80 LVVPSSNFLERQSQAGIFEPLDKSKMPNYKNLDPEMLKLVAHNDKDNKYGIPYLMVTTGIGYNVDKVKAALGKDAPVDSW 159
Cdd:PRK10682 81 LVVPSASFLERQLTAGVFQPLDKSKLPNWKNLDPELLKLVAKHDPDNKYAMPYMWATTGIGYNVDKVKAVLGEDAPVDSW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 160 DLILKPENLEKLKSCGVSFLDAPSEVYATVLHYLGKDPNSTNAADYTGAANDLLLKLRPNIRYFHSSQYINDLANGDICV 239
Cdd:PRK10682 161 DLVLKPENLEKLKSCGVSFLDAPEEIFATVLNYLGKDPNSTKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 240 AIGWSGDVMQAANRAKEAKNGVNVAYAIPKEGALTYFDMFAMPADAKNKDAAYQFLNFLMKPDVMAGISNYVYYANAVKD 319
Cdd:PRK10682 241 AIGWAGDVWQASNRAKEAKNGVNVSYSIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPDVIAHISDHVFYANANKA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 727169280 320 STPLVNAEVRNNPNVYPPADLRAKLFTLNVQSPKLDRVITRAWTKVKSGK 369
Cdd:PRK10682 321 ATPLVSAEVRDNPGIYPPADVRAKLFTLKVQDPKIDRVRTRAWTKVKSGK 370
|
|
| PBP2_PotF |
cd13659 |
The periplasmic substrate-binding component of an ABC putrescine transport system and related ... |
30-362 |
0e+00 |
|
The periplasmic substrate-binding component of an ABC putrescine transport system and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic substrate-binding domain that serves as the primary polyamine receptor of ABC-type putrescine-preferential transporter from gram-negative bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270377 [Multi-domain] Cd Length: 331 Bit Score: 540.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGSTGYDLVVPSSNFLERQSQAGIFEPLDKSKMPNYK 109
Cdd:cd13659 1 TLNVYNWSDYIAPDTLEDFEKETGIKVVYDTYDSNEELEAKLLAGGSGYDLVVPSANFLGRQIKAGALQKLDKSKLPNWK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 110 NLDPEMLKLVAHNDKDNKYGIPYLMVTTGIGYNVDKVKAALGKDAPvDSWDLILKPENLEKLKSCGVSFLDAPSEVYATV 189
Cdd:cd13659 81 NLDPLLLKLLAAVDPGNRYAVPYMWGTTGIAYNVDKVKAALGDDLP-DSWDLVFDPENLSKLKSCGVSVLDSPEEVFPAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 190 LHYLGKDPNSTNAADYtGAANDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWSGDVMQAANRAKEAKNGVNVAYAIPK 269
Cdd:cd13659 160 LNYLGLDPNSTDPEDI-KAAEDLLKKVRPYVRYFHSSKYINDLANGEICVAIGWSGDAVQAAQRAKEAGNGVTLEYVIPK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 270 EGALTYFDMFAMPADAKNKDAAYQFLNFLMKPDVMAGISNYVYYANAVKDSTPLVNAEVRNNPNVYPPADLRAKLFTLNV 349
Cdd:cd13659 239 EGANLWFDMFAIPADAKNPDNAYRFINYLMRPEVIAKISNYVNYANANKAATPLVDEAIKDDPAIYPPEEVLKKLYALPP 318
|
330
....*....|...
gi 727169280 350 QSPKLDRVITRAW 362
Cdd:cd13659 319 LSAKVQRALTRAW 331
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
5-366 |
2.24e-147 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 420.47 E-value: 2.24e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 5 RKKWLS--GVVAGLLMAASVTASAEEKTLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGSTGYDLVV 82
Cdd:COG0687 3 RRSLLGlaAAALAAALAGGAPAAAAEGTLNVYNWGGYIDPDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAGGSGYDVVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 83 PSSNFLERQSQAGIFEPLDKSKMPNYKNLDPEMLKLvaHNDKDNKYGIPYLMVTTGIGYNVDKVKaalgkdAPVDSWDLI 162
Cdd:COG0687 83 PSDYFVARLIKAGLLQPLDKSKLPNLANLDPRFKDP--PFDPGNVYGVPYTWGTTGIAYNTDKVK------EPPTSWADL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 163 LKPENLEKlkscgVSFLDAPSEVYATVLHYLGKDPNSTNAADYTgAANDLLLKLRPNIRYFHSS--QYINDLANGDICVA 240
Cdd:COG0687 155 WDPEYKGK-----VALLDDPREVLGAALLYLGYDPNSTDPADLD-AAFELLIELKPNVRAFWSDgaEYIQLLASGEVDLA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 241 IGWSGDVMQAANRakeaknGVNVAYAIPKEGALTYFDMFAMPADAKNKDAAYQFLNFLMKPDVMAGISNYVYYANAVKDS 320
Cdd:COG0687 229 VGWSGDALALRAE------GPPIAYVIPKEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAA 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 727169280 321 TPLVNAEVRNNPNVYPPADLRAKLFTLNVQSPKLDRVITRAWTKVK 366
Cdd:COG0687 303 RELLPPELAANPAIYPPEEVLDKLEFWNPLPPENRELYTRRWTEIK 348
|
|
| PBP2_PotD_PotF_like |
cd13590 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
30-362 |
2.90e-122 |
|
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270308 [Multi-domain] Cd Length: 315 Bit Score: 355.39 E-value: 2.90e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGS-TGYDLVVPSSNFLERQSQAGIFEPLDKSKMPNY 108
Cdd:cd13590 1 ELNIYNWSDYIDPEVLKAFEKETGVKVNYDTYDSNEEMLAKLRAGGgSGYDLVVPSDYMVERLIKQGLLEPLDHSKLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 109 KNLDPEMLKLvaHNDKDNKYGIPYLMVTTGIGYNVDKVKAalgkdaPVDSWDLILKPENLeklkSCGVSFLDAPSEVYAT 188
Cdd:cd13590 81 KNLDPQFLNP--PYDPGNRYSVPYQWGTTGIAYNKDKVKE------PPTSWDLDLWDPAL----KGRIAMLDDAREVLGA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 189 VLHYLGKDPNSTNAADyTGAANDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWSGDVMQAANRAKeakngvNVAYAIP 268
Cdd:cd13590 149 ALLALGYSPNTTDPAE-LAAAAELLIKQKPNVRAFDSDSYVQDLASGEIWLAQAWSGDALQANRENP------NLKFVIP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 269 KEGALTYFDMFAMPADAKNKDAAYQFLNFLMKPDVMAGISNYVYYANAVKDSTPLVNAEVRNNPNVYPPADLRAKLFTLN 348
Cdd:cd13590 222 KEGGLLWVDNMAIPKGAPNPELAHAFINFLLDPEVAAKNAEYIGYATPNKAALELLPPELLDNPALYPPIEPLAKLLTFK 301
|
330
....*....|....
gi 727169280 349 VQSPKLDRVITRAW 362
Cdd:cd13590 302 DVDGEALELYDRIW 315
|
|
| PBP2_polyamines |
cd13523 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
30-309 |
2.07e-100 |
|
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding proteins that function as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270241 [Multi-domain] Cd Length: 268 Bit Score: 297.81 E-value: 2.07e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMA-GSTGYDLVVPSSNFLERQSQAGIFEPLDKSKMPNY 108
Cdd:cd13523 1 TVVIYTWGGYLPQDIIDPFEKETGIKVVVDTAANSERMIKKLSAgGSGGFDLVTPSDSYTSRQLGVGLMQPIDKSLLPSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 109 KNLDPEMLKLVAHNDKDNKYGIPYLMVTTGIGYNVDKVKaalgkdAPVDSWdlilKPENLEKLKSCGVSFLDAPSEVYAT 188
Cdd:cd13523 81 ATLDPHLTLAAVLTVPGKKYGVPYQWGATGLVYNTDKVK------APPKSY----AADLDDPKYKGRVSFSDIPRETFAM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 189 VLHYLGKDPNSTNAADYTGAANDLLLKLRPNIRYFHS--SQYINDLANGDICVAIGWSGDVMQAANRakeaknGVNVAYA 266
Cdd:cd13523 151 ALANLGADGNEELYPDFTDAAAALLKELKPNVKKYWSnaSQPANLLLNGEVVLAMAWLGSGFKLKQA------GAPIEFV 224
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 727169280 267 IPKEGALTYFDMFAMPADAKNKDAAYQFLNFLMKPDVMAGISN 309
Cdd:cd13523 225 VPKEGAVGWLDTFAVPANAPNKDGAYKLLNALLRPKVAAAVAA 267
|
|
| PBP2_PotD_PotF_like_3 |
cd13664 |
TThe periplasmic substrate-binding component of an uncharacterized active transport system ... |
30-362 |
5.51e-80 |
|
TThe periplasmic substrate-binding component of an uncharacterized active transport system closely related to spermidine and putrescine transporters; contains the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270382 [Multi-domain] Cd Length: 315 Bit Score: 247.66 E-value: 5.51e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGSTGYDLVVPSSNFLERQSQAGIFEPLDKSKMPNYK 109
Cdd:cd13664 1 ELNLYNWTDYTSPELLDKFEKETGIKVTLDTYDSNETLLAKLKAGGQGYDVVVPSDSFVPILIKEGLLEPLDKSQLTNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 110 NLDPEMLKLVAhnDKDNKYGIPYLMVTTGIGYNVDKVkaalgkDAPVDSWDLILKPENLEKLKscgVSFLDAPSEVYATV 189
Cdd:cd13664 81 NIDPRWRKPDF--DPGNEYSIPWQWGTTGFAVDTAVY------DGDIDDYSVIFQPPEELKGK---IAMVDSMNEVVNAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 190 LHYLGKDPNSTNAADYTgAANDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWSGDVMQAanRAKEAkngvNVAYAIPK 269
Cdd:cd13664 150 IYYLGGPICTTDPKLMR-KVRDLLLEQKPHVKAYDSDGIVERMASGDVAAHVDWNGASLRA--RRQNP----SLAYAYPK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 270 EGALTYFDMFAMPADAKNKDAAYQFLNFLMKPDVMAGISNYVYYANAVKDSTPLVNAEVRNNPNVYPPADLRAKLFTLNV 349
Cdd:cd13664 223 EGVLIWSDNLVIPKGAPNYENARTFLNFIMEPENAALQSNFAGYANAITGAEKFMDDPLKDAPALEIPPPEGSRLKFSTL 302
|
330
....*....|...
gi 727169280 350 QSPKLDRVITRAW 362
Cdd:cd13664 303 CPPKAEKLQSRIW 315
|
|
| PBP2_PotD |
cd13660 |
The periplasmic substrate-binding component of an active spermidine-preferential transport ... |
30-339 |
9.02e-67 |
|
The periplasmic substrate-binding component of an active spermidine-preferential transport system; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that serves as the primary polyamine receptor of ABC-type spermindine-preferential transport system from gram-negative bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270378 [Multi-domain] Cd Length: 315 Bit Score: 213.60 E-value: 9.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKL-MAGSTGYDLVVPSSNFLERQSQAGIFEPLDKSKMPNY 108
Cdd:cd13660 1 TLNFYNWSEYVPPELLEQFTKETGIKVILSTYESNETMYAKVkLYKDGAYDLVVPSTYYVDKMRKEGLIQKIDKSKITNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 109 KNLDPEMLKlvAHNDKDNKYGIPYLMVTTGIGYNVDkvkaALGKDApVDSWDLILKPENLEKLkscgvSFLDAPSEVYAT 188
Cdd:cd13660 81 SNIDPDFLN--QPFDPNNDYSIPYIWGATALAVNGD----AVDGKS-VTSWADLWKPEYKGKL-----LLTDDAREVFQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 189 VLHYLGKDPNSTNAADYTGAANDLLlKLRPNIRYFHSSQYINDLANGDICVAIGWSGDVMQAANRAKeakngvNVAYAIP 268
Cdd:cd13660 149 ALRKLGYSGNTKDPEEIEAAFEELK-KLMPNVAAFDSDNPANPYMEGEVALGMIWNGSAFVARQANK------PIHVVWP 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727169280 269 KEGALTYFDMFAMPADAKNKDAAYQFLNFLMKPDVMAGISNYVYYANAVKDSTPLVNAEVRNNPNVYPPAD 339
Cdd:cd13660 222 KEGGIFWMDSFAIPANAKNKEGALKFINFLLRPDVSKQIAETIGYPTPNLKARKLLSPEVANNKIVYPSAE 292
|
|
| PBP2_PotD_PotF_like_2 |
cd13663 |
The periplasmic substrate-binding component of an uncharacterized active transport system ... |
30-366 |
2.34e-66 |
|
The periplasmic substrate-binding component of an uncharacterized active transport system closely related to spermidine and putrescine transporters; contains the type 2 periplasmic binding fold; This group represents the periplasmic substrate-binding domain that serves as a primary polyamine receptor of an uncharacterized ABC-type transport system from gram-negative bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270381 [Multi-domain] Cd Length: 323 Bit Score: 212.92 E-value: 2.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGSTGYDLVVPSSNFLERQSQAGIFEPLDKSKMPNYK 109
Cdd:cd13663 1 TLKVYNWGEYIDPDLIDDFEKETGIKVNYETFDSNEEMYTKIKTGGTSYDVIVPSDYMIEKLIKEDLLQPLDYSKLPNVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 110 ---NLDPEMLKLVAhnDKDNKYGIPYLMVTTGIGYNVDKVkaalgKDAPVDSWDLILKPENLEKlkscgVSFLDAPSEVY 186
Cdd:cd13663 81 kniNIQPDLLNLAF--DPINEYSVPYFWGTLGIVYNKTKV-----SLEELSWWNILWNKKYKGK-----ILMYDSPRDAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 187 ATVLHYLGKDPNSTNaADYTGAANDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWSGDVMQAANRAKeakngvNVAYA 266
Cdd:cd13663 149 MVALKALGYSLNTTN-PDEIEEAKDWLIKQKPNVKAFVVDEIKDLMINGNADIAVTYSGDAAYAMEENE------NLDYV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 267 IPKEGALTYFDMFAMPADAKNKDAAYQFLNFLMKPDvmAGISNYVYyanaVKDSTPLVNAE--------VRNNPNVYPPA 338
Cdd:cd13663 222 IPKEGSNLWFDNWVIPKNAKNVDLAYKFINFLLRPD--NALKNAEY----VGYSTPNAAAEellpeeesIKDDKIFYPDE 295
|
330 340
....*....|....*....|....*...
gi 727169280 339 DLRAKLFTLNVQSPKLDRVITRAWTKVK 366
Cdd:cd13663 296 DIYKKCEVFKYLGGDAKKEYNDLWLEVK 323
|
|
| potD |
PRK09501 |
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed |
6-343 |
5.07e-65 |
|
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed
Pssm-ID: 181913 [Multi-domain] Cd Length: 348 Bit Score: 210.16 E-value: 5.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 6 KKWLSGVVAGLLMAASVTASA--EEKTLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGSTG-YDLVV 82
Cdd:PRK09501 2 KKWSRHLLAAGALALGMSAAHadDNNTLYFYNWTEYVPPGLLEQFTKETGIKVIYSTYESNETMYAKLKTYKDGaYDLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 83 PSSNFLERQSQAGIFEPLDKSKMPNYKNLDPEMLKlvAHNDKDNKYGIPYLMVTTGIGYNVDKVKAalgkdAPVDSWDLI 162
Cdd:PRK09501 82 PSTYYVDKMRKEGMIQKIDKSKLTNFSNLDPDMLN--KPFDPNNDYSIPYIWGATAIGVNSDAIDP-----KSVTSWADL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 163 LKPENLEKLkscgvSFLDAPSEVYATVLHYLGKDPNSTNAADYTGAANDlLLKLRPNIRYFHSSQYINDLANGDICVAIG 242
Cdd:PRK09501 155 WKPEYKGSL-----LLTDDAREVFQMALRKLGYSGNTTDPKEIEAAYNE-LKKLMPNVAAFNSDNPANPYMEGEVNLGMI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 243 WSGdvmqAANRAKEAKNGVNVAYaiPKEGALTYFDMFAMPADAKNKDAAYQFLNFLMKPDVMAGISNYVYYANAVKDSTP 322
Cdd:PRK09501 229 WNG----SAFVARQAGTPIDVVW--PKEGGIFWMDSLAIPANAKNKEGALKLINFLLRPDVAKQVAETIGYPTPNLAARK 302
|
330 340
....*....|....*....|.
gi 727169280 323 LVNAEVRNNPNVYPPADLRAK 343
Cdd:PRK09501 303 LLSPEVANDKSLYPDAETIKK 323
|
|
| PBP2_polyamine_1 |
cd13588 |
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
30-317 |
1.99e-61 |
|
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that functions as the primary high-affinity receptor of an uncharactertized ABC-type polyamine transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270306 [Multi-domain] Cd Length: 279 Bit Score: 198.67 E-value: 1.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGSTGYDLVVPSSNFLERQSQAGIFEPLDKSKMPNYK 109
Cdd:cd13588 1 ELNVLTWPGYADPDWVTAFEEATGCKVVVKFFGSEDEMVAKLRSGGGDYDVVTPSGDALLRLIAAGLVQPIDTSKIPNYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 110 NLDPEMLKLVAHNDKDNKYGIPYLMVTTGIGYNVDKVKAalgkdAPVDSWDLILKPENLEKlkscgVSFLDAPSEVYATV 189
Cdd:cd13588 81 NIDPRLRNLPWLTVDGKVYGVPYDWGANGLAYNTKKVKT-----PPTSWLALLWDPKYKGR-----VAARDDPIDAIADA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 190 LHYLGKDPNSTNAADYTGAANDLLLKLRPNIR-YFHSS-QYINDLANGDICVAIGWSGdvmqAANRAKeaKNGVNVAYAI 267
Cdd:cd13588 151 ALYLGQDPPFNLTDEQLDAVKAKLREQRPLVRkYWSDGaELVQLFANGEVVAATAWSG----QVNALQ--KAGKPVAYVI 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 727169280 268 PKEGALTYFDMFAMPADAKNKDAAYQFLNFLMKPDVMAGISNYVYYANAV 317
Cdd:cd13588 225 PKEGATGWVDTWMILKDAKNPDCAYKWLNYMLSPKVQAAVAEWTGYAPSN 274
|
|
| PBP2_TpPotD_like |
cd13662 |
The periplasmic substrate-binding component of an ABC-type polyamine transport system from ... |
30-346 |
1.45e-58 |
|
The periplasmic substrate-binding component of an ABC-type polyamine transport system from Treponema pallidum and related proteins; contains the type 2 periplasmic binding fold; This group includes the polyamine-binding component of an ABC-type polyamine transport system from Treponema pallidum and closely related proteins, which is homologous to the spermidine-preferring periplasmic substrate-binding protein component (PotD)of ABC transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270380 Cd Length: 312 Bit Score: 192.35 E-value: 1.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGSTGYDLVVPSSNFLERQSQAGIFEPLDKSKMPNYK 109
Cdd:cd13662 1 VLYIYNWTYYIPDKVIEDFEKETGIRVVYDYYASNEEMYAKLKIGGGGYDIVSPSGDYVSIMKKEGLLEKLDKSKLPNVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 110 NLDPEMLKLVAHNDKDNKYGIPYLMVTTGIGYNVDKVkaalgKDAPVDsWDLILKpenlEKLKScGVSFLDAPSEVYATV 189
Cdd:cd13662 81 EEKDNLMEASKIYDPGLEYSVPYMFGATGIAVNKKIV-----KNYFRK-WSIFLR----EDLAG-RMTMLDDMREVIGAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 190 LHYLG--KDPNSTNAADytgAANDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWSGDVMQAANRAKEAkngvNVAYAI 267
Cdd:cd13662 150 LAYLGypVDSKDIEQLE---EAKEVILSWKKNLAKFDSNSYGKGFASGDFWVVHGYAEDVFYEVPEEEEE----KFDFFI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 268 PKEGALT-YFDMFAMPADAKNKDAAYQFLNFLMKPDVMAGISNYVYYANAVKDstplVNAEVRNNPNVYPPADL-RAKLF 345
Cdd:cd13662 223 PEGAASMmYIDSFVIPKGSKHKDNAYKFINFILRPENYAEILDVLGNPSIIKE----AEKKSQKKPIIYAEEDLkNSKLP 298
|
.
gi 727169280 346 T 346
Cdd:cd13662 299 G 299
|
|
| PBP2_polyamine_RpCGA009 |
cd13589 |
The periplasmic-binding component of an uncharacterized ABC transport system from ... |
48-314 |
1.43e-41 |
|
The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270307 [Multi-domain] Cd Length: 268 Bit Score: 146.60 E-value: 1.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 48 FQKETGIKVVYDVFDSNEVLeGKLMA--GSTGYDLVVPSSNFLERQSQAGIFEPLDKSKMPNYKNLD-PEMLKlvahndk 124
Cdd:cd13589 23 FEKETGIKVVYDTGTSADRL-AKLQAqaGNPQWDVVDLDDGDAARAIAEGLLEPLDYSKIPNAAKDKaPAALK------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 125 dNKYGIPYLMVTTGIGYNVDKVKAalgkdaPVDSWDLiLKPENLEKLKSCGVSFLDAPSEVYAtVLHYLGKDPNSTNAAd 204
Cdd:cd13589 95 -TGYGVGYTLYSTGIAYNTDKFKE------PPTSWWL-ADFWDVGKFPGPRILNTSGLALLEA-ALLADGVDPYPLDVD- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 205 ytgAANDLLLKLRPNIRYFHSS--QYINDLANGDICVAIGWSGdvmqaanRAKEA-KNGVNVAYAIPKEGALTYFDMFAM 281
Cdd:cd13589 165 ---RAFAKLKELKPNVVTWWTSgaQLAQLLQSGEVDMAPAWNG-------RAQALiDAGAPVAFVWPKEGAILGPDTLAI 234
|
250 260 270
....*....|....*....|....*....|...
gi 727169280 282 PADAKNKDAAYQFLNFLMKPDVMAGISNYVYYA 314
Cdd:cd13589 235 VKGAPNKELAMKFINFALSPEVQAALAEALGYG 267
|
|
| PBP2_polyamine_2 |
cd13587 |
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
30-320 |
5.19e-34 |
|
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This family represents the periplasmic binding domain that functions as the primary polyamine receptor of an uncharacterized ABC-type transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270305 [Multi-domain] Cd Length: 292 Bit Score: 127.16 E-value: 5.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMA-GSTGYDLVVPSSNFLERQSQAGIFEPLDKSKMpNY 108
Cdd:cd13587 1 TLRILTWAGYAPEDLLEKFENETGIKVQVTTSNNNEEMISKLRAtGGGGFDLAQPSQRIAPNYEEFGLYQPIDESKI-KV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 109 KNLDPEMLKLVAHND--KDNKYGIPYLMVTTGIGYNVDKvkaalGKDAPVDSWDLILKPENLEKlkscgVSF-LDAPSEV 185
Cdd:cd13587 80 AQFPPSLLESTKLGTtiNGKRYAVPFDWGTEGLTVNSTK-----APDVSGFSYGDLWAPEYAGK-----VAYrLKSPLTG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 186 YATVLHYLGKDPnSTNAADYTGAAN---------DLLLKLRPNIRYF--HSSQYINDLANGDICVAIGWSGdvmqaaNRA 254
Cdd:cd13587 150 LGLYADATGEDP-FNRYLDYKDEAKyqkildqvlQFLIERKANVKAYwnNADEALAAFRSGGCVIGQTWDS------TGL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727169280 255 KEAKNGVNVAYAIPKEGALTYFDMFAMPADAKNKDAAYQFLNFLMKPDVMAGISNYVYYANAVKDS 320
Cdd:cd13587 223 KLNRENPPIDYGAPKEGALGWIDTFAIPAKAENVDQAYAFINFMLRPEIAAMFTNATGYNTAAVGA 288
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
46-334 |
5.89e-28 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 110.57 E-value: 5.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 46 AKFQKETGIKVVYDVFDSNEvLEGKLM----AGSTG-YDLVVPSSNFLERQSQAGIFEPLDKSkmPNYKNLDPemlKLVA 120
Cdd:pfam13416 4 KAFEKKTGVTVEVEPQASND-LQAKLLaaaaAGNAPdLDVVWIAADQLATLAEAGLLADLSDV--DNLDDLPD---ALDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 121 HNDKDNKYGIPYLMVT-TGIGYNVDKVKAAlgkDAPVDSWDLILkpENLEKLKSCgVSFLDAPSEVYATVLHYLGKDPNS 199
Cdd:pfam13416 78 AGYDGKLYGVPYAASTpTVLYYNKDLLKKA---GEDPKTWDELL--AAAAKLKGK-TGLTDPATGWLLWALLADGVDLTD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 200 TN-AADYTGAANDLLLKLRPNIRYF-HSSQYINDLANGDICVAIGWSGDVmqaanrAKEAKNGVNVAYAIPKEGALTYFD 277
Cdd:pfam13416 152 DGkGVEALDEALAYLKKLKDNGKVYnTGADAVQLFANGEVAMTVNGTWAA------AAAKKAGKKLGAVVPKDGSFLGGK 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 727169280 278 MFAMPADAKNKD-AAYQFLNFLMKPDVMAGISNYVYYANAVKDSTPlvNAEVRNNPNV 334
Cdd:pfam13416 226 GLVVPAGAKDPRlAALDFIKFLTSPENQAALAEDTGYIPANKSAAL--SDEVKADPAL 281
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
5-305 |
5.55e-24 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 101.27 E-value: 5.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 5 RKKWLSGVVAGLLMAA-------SVTASAEEKTLHVYNWSDYIAP---DTLAKFQKET-GIKVVYDVFDSNEVLEgKL-- 71
Cdd:COG1653 2 RRLALALAAALALALAacggggsGAAAAAGKVTLTVWHTGGGEAAaleALIKEFEAEHpGIKVEVESVPYDDYRT-KLlt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 72 -MAGSTGYDLVVPSSNFLERQSQAGIFEPLD---KSKMPNYKNLDPEMLKLVAHNDKdnKYGIPYLMVTTGIGYNVDKVK 147
Cdd:COG1653 81 aLAAGNAPDVVQVDSGWLAEFAAAGALVPLDdllDDDGLDKDDFLPGALDAGTYDGK--LYGVPFNTDTLGLYYNKDLFE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 148 AAlGKDAPvDSWD-LIlkpENLEKLKS----CGVSFLDAPSEVYATVLHYLGKDP-NSTNAADYTGAAN----DLLLKLR 217
Cdd:COG1653 159 KA-GLDPP-KTWDeLL---AAAKKLKAkdgvYGFALGGKDGAAWLDLLLSAGGDLyDEDGKPAFDSPEAvealEFLKDLV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 218 ------PNIRYFHSSQYINDLANGDicVAIGWSGDvmQAANRAKEAKNGVNVAYA-IP------KEGALTYFDMFAMPAD 284
Cdd:COG1653 234 kdgyvpPGALGTDWDDARAAFASGK--AAMMINGS--WALGALKDAAPDFDVGVApLPggpggkKPASVLGGSGLAIPKG 309
|
330 340
....*....|....*....|.
gi 727169280 285 AKNKDAAYQFLNFLMKPDVMA 305
Cdd:COG1653 310 SKNPEAAWKFLKFLTSPEAQA 330
|
|
| PBP2_PotD_PotF_like_1 |
cd13661 |
The periplasmic substrate-binding component of an uncharacterized active transport system ... |
128-343 |
3.23e-23 |
|
The periplasmic substrate-binding component of an uncharacterized active transport system closely related to spermidine and putrescine transporters; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that serves as a primary polyamine receptor of an uncharacterized ABC-type transport system from plants and plant-symbiotic cyanobacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270379 [Multi-domain] Cd Length: 319 Bit Score: 98.64 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 128 YGIPYLMVTTGIGYNVDKVKAALGKdaPVDsWDLILKPEnlekLKScGVSFLDAPSEVYATVLHYLGKdpnSTNAADYTG 207
Cdd:cd13661 81 WAVPYRWGTTVIAYRKDKLKKLGWD--PID-WSDLWRPE----LAG-RIAMVDSPREVIGLVLKKLGA---SYNTAEVPG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 208 AANDL---LLKLRPNIRYFHSSQYINDLANGDICVAIGWSGDVMQAANRAKeakngvNVAYAIPKEGALTYFDMFAMPAD 284
Cdd:cd13661 150 GREALeerLAALRRQVKLYSSNNYLQALLLGDVWVAVGWSQDIIPLARRYS------NLAVVIPRSGTSLWADLWVIPAG 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727169280 285 AKNKD-------AAYQFLNFLMKP--------DVMAGISNYVYYANAVKD-STPLVNAEVRNNPNVYPPADLRAK 343
Cdd:cd13661 224 SDFGGrvrgpspLLSQWIDFCLQParatqfaqLSFGGASPLILDGPSLTPpEATRKLKLDTNLVLGLPPDEILAK 298
|
|
| AfuA |
COG1840 |
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
44-364 |
3.26e-21 |
|
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 92.31 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 44 TLAKFQKETGIKVVYDVFDSNEVLEgKLMA--GSTGYDLV-VPSSNFLERQSQAGIFEPLdksKMPNYKNLDPEMlklva 120
Cdd:COG1840 1 LLEAFEKKTGIKVNVVRGGSGELLA-RLKAegGNPPADVVwSGDADALEQLANEGLLQPY---KSPELDAIPAEF----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 121 hNDKDNKYgIPYLMVTTGIGYNVDKVKAalgKDAPvDSWDLILKPENLEKL-------KSCGVSFLdapsevyATVLHYL 193
Cdd:COG1840 72 -RDPDGYW-FGFSVRARVIVYNTDLLKE---LGVP-KSWEDLLDPEYKGKIamadpssSGTGYLLV-------AALLQAF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 194 GKDpnstnaadytgAANDLLLKLRPNIRYF--HSSQYINDLANGDICVAIGWSGDVmqaanrAKEAKNGVNVAYAIPKEG 271
Cdd:COG1840 139 GEE-----------KGWEWLKGLAANGARVtgSSSAVAKAVASGEVAIGIVNSYYA------LRAKAKGAPVEVVFPEDG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 272 ALTYFDMFAMPADAKNKDAAYQFLNFLMKPDVMAgisnyvYYANAvkdstplvNAEVRNNPNVYPPADLRA----KLFTL 347
Cdd:COG1840 202 TLVNPSGAAILKGAPNPEAAKLFIDFLLSDEGQE------LLAEE--------GYEYPVRPDVEPPEGLPPlgelKLIDD 267
|
330
....*....|....*..
gi 727169280 348 NVQSPKLDRVITRAWTK 364
Cdd:COG1840 268 DDKAAENREELLELWDE 284
|
|
| SBP_bac_6 |
pfam13343 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
78-332 |
2.20e-17 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 463852 [Multi-domain] Cd Length: 247 Bit Score: 80.48 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 78 YDLVVPSSN------FLERQSQAGIFEPLDKSKMPNYknldPEMLKLVAHNDKDNKYgIPYLMVTTGIGYNVDKVKaalG 151
Cdd:pfam13343 4 PDIILSAGDlffdkrFLEKFIEEGLFQPLDSANLPNV----PKDFDDEGLRDPDGYY-TPYGVGPLVIAYNKERLG---G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 152 KDAPVdSWDLILKPEnlekLKSCGVSFLDAPSEVYATVLHYLGKDPNSTNAAdytgaanDLLLKLRPNIRYFHSSQYIND 231
Cdd:pfam13343 76 RPVPR-SWADLLDPE----YKGKVALPGPNVGDLFNALLLALYKDFGEDGVR-------KLARNLKANLHPAQMVKAAGR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 232 LANGD--ICVAIGWSGDVMQAanrakeakNGVNVAYAIPKEGALTYFDMFAMPADakNKDAAYQFLNFLMKPDVMAGISN 309
Cdd:pfam13343 144 LESGEpaVYLMPYFFADILPR--------KKKNVEVVWPEDGALVSPIFMLVKKG--KKELADPLIDFLLSPEVQAILAK 213
|
250 260
....*....|....*....|...
gi 727169280 310 YvYYANAVKDSTPLVNAEVRNNP 332
Cdd:pfam13343 214 A-GLVFPVVLNPAVDNPLPEGAP 235
|
|
| PBP2_Fbp_like_1 |
cd13544 |
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ... |
28-340 |
3.04e-15 |
|
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270262 [Multi-domain] Cd Length: 292 Bit Score: 75.33 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 28 EKTLHVYNWSDYIAPdTLAKFQKETGIKVVYdVFDSNEVLEGKLMA--GSTGYDLVV--PSSNFLERQSQaGIFEPLdks 103
Cdd:cd13544 1 ELTVYTSLEEEEAKA-ILEAFKKDTGIKVEF-VRLSTGEALARLEAekGNPQADVWFggTADAHIQAKKE-GLLEPY--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 104 KMPNYKNLDPEmlklvahnDKDNK-YGIPYLMVTTGIGYNVDKVKAaLGKDAPvDSWDLILKPEnlekLK---------S 173
Cdd:cd13544 75 KSPNADKIPAK--------FKDPDgYWTGIYLGPLGFGVNTDELKE-KGLPVP-KSWEDLLNPE----YKgeivmpnpaS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 174 CGVSFLdapseVYATVLHYLGKDpnstnaadytgAANDLLLKLRPNIRYFHSSQY--INDLANGDICVAIGWSGDVMqaa 251
Cdd:cd13544 141 SGTAYT-----FLASLIQLMGED-----------EAWEYLKKLNKNVGQYTKSGSapAKLVASGEAAIGISFLHDAL--- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 252 nraKEAKNGVNVAYAIPKEGalTYFDM--FAMPADAKNKDAAYQFLNFLMKPDVMAGISNYVYYANAVKDSTPLVNAEVR 329
Cdd:cd13544 202 ---KLKEQGYPIKIIFPKEG--TGYEIeaVAIIKGAKNPEAAKAFIDWALSKEAQELLAKVGSYAIPTNPDAKPPEIAPD 276
|
330
....*....|.
gi 727169280 330 NNPNVYPPADL 340
Cdd:cd13544 277 LKKDKLIKYDF 287
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
5-334 |
8.17e-15 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 74.99 E-value: 8.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 5 RKKWLSGVVAGLLMAASVTA-------------SAEEKTLHVYNWSDYIAP--DTLAKFQKETGIKVVYDVFDSNEVLEG 69
Cdd:COG2182 2 KRRLLAALALALALALALAAcgsgssssgsssaAGAGGTLTVWVDDDEAEAleEAAAAFEEEPGIKVKVVEVPWDDLREK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 70 KLMAGSTGY--DLVVPSSNFLERQSQAGIFEPLDKSKmPNYKNLDPEMLKLVAHNDKdnKYGIPYLMVTTGIGYNVDKVK 147
Cdd:COG2182 82 LTTAAPAGKgpDVFVGAHDWLGELAEAGLLAPLDDDL-ADKDDFLPAALDAVTYDGK--LYGVPYAVETLALYYNKDLVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 148 AalgkDAPVdSWDLILkpENLEKLKSCGVS-FLDAPSEVYATVL-------HYLGKDPNSTNAADYTGAAN----DLLLK 215
Cdd:COG2182 159 A----EPPK-TWDELI--AAAKKLTAAGKYgLAYDAGDAYYFYPflaafggYLFGKDGDDPKDVGLNSPGAvaalEYLKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 216 LRPNiRYFHSS----QYINDLANGDICVAIG--WsgdvmqAANRAKEAKnGVNVAYA-IPK----EGALTYF--DMFAMP 282
Cdd:COG2182 232 LIKD-GVLPADadydAADALFAEGKAAMIINgpW------AAADLKKAL-GIDYGVApLPTlaggKPAKPFVgvKGFGVS 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 727169280 283 ADAKNKDAAYQFLNFLMKPDVMAGISNYVYYANAVKDStpLVNAEVRNNPNV 334
Cdd:COG2182 304 AYSKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAA--AEDAEVKADPLI 353
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
45-305 |
3.51e-14 |
|
Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.
Pssm-ID: 460248 [Multi-domain] Cd Length: 294 Bit Score: 72.06 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 45 LAKFQKE-TGIKVVYDVFDSNEV---LEGKLMAGSTGYDLVVPSSNFLERQSQAGIFEPLDKSKMPNYKNLDPEmlklva 120
Cdd:pfam01547 14 VKEFEKEhPGIKVEVESVGSGSLaqkLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYLVLGVPK------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 121 hndkdnKYGIPYLMVTTGIGYNVDKVKAAlgKDAPVDSWD--LILKPENLEKLKS-CGVSFLDAPSEVYATVLHYL---- 193
Cdd:pfam01547 88 ------LYGVPLAAETLGLIYNKDLFKKA--GLDPPKTWDelLEAAKKLKEKGKSpGGAGGGDASGTLGYFTLALLaslg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 194 -------GKDPNSTNAADYTGAANDLLLKLR-------PNIRYFHSSQYINDLANGDICVAIGWSGDVMQAANRAKEA-- 257
Cdd:pfam01547 160 gplfdkdGGGLDNPEAVDAITYYVDLYAKVLllkklknPGVAGADGREALALFEQGKAAMGIVGPWAALAANKVKLKVaf 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 727169280 258 -----KNGVNVAYAIP--KEGALTYFDMFAMPADAKNKDAAYQFLNFLMKPDVMA 305
Cdd:pfam01547 240 aapapDPKGDVGYAPLpaGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQA 294
|
|
| PBP2_Fe3_thiamine_like |
cd13518 |
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ... |
30-303 |
5.31e-13 |
|
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. On the other hand, thiamin is an essential cofactor in all living systems. Thiamin diphosphate (ThDP)-dependent enzymes play an important role in carbohydrate and branched-chain amino acid metabolism. Most prokaryotes, plants, and fungi can synthesize thiamin, but it is not synthesized in vertebrates. These periplasmic domains have high affinities for their respective substrates and serve as the primary receptor for transport. After binding iron and thiamine with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The iron- and thiamine-binding proteins belong to the PBPI2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270236 [Multi-domain] Cd Length: 260 Bit Score: 68.10 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 30 TLHVYNWSDYI-APDTLAKFQKETGIKVVYdVFDSNEVLEGKLMA--GSTGYDLVVPSSNF-LERQSQAGIFEPLDkskm 105
Cdd:cd13518 1 ELVVYTASDRDfAEPVLKAFEEKTGIKVKA-VYDGTGELANRLIAekNNPQADVFWGGEIIaLEALKEEGLLEPYT---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 106 PNYKNLDPEMLKlvahnDKDNKYgIPYLMVTTGIGYNVDKVKaalGKDAPVDSWDLiLKPENLEKLKSCGVSFLDAPSEV 185
Cdd:cd13518 76 PKVIEAIPADYR-----DPDGYW-VGFAARARVFIYNTDKLK---EPDLPKSWDDL-LDPKWKGKIVYPTPLRSGTGLTH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 186 YATVLHYLGKDPnstnaadytgAANDLLLKLRPNIRYFHSSQYINDL-ANGDICVAIGWSGDVMQAANRakeaknGVNVA 264
Cdd:cd13518 146 VAALLQLMGEEK----------GGWYLLKLLANNGKPVAGNSDAYDLvAKGEVAVGLTDTYYAARAAAK------GEPVE 209
|
250 260 270
....*....|....*....|....*....|....*....
gi 727169280 265 YAIPKEGALTYFDMFAMPADAKNKDAAYQFLNFLMKPDV 303
Cdd:cd13518 210 IVYPDQGALVIPEGVALLKGAPNPEAAKKFIDFLLSPEG 248
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
45-345 |
4.46e-12 |
|
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270303 [Multi-domain] Cd Length: 383 Bit Score: 66.66 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 45 LAKFQKE-TGIKVVYDVFDSNEVLEgKLM---AGSTGYDLVVPSSNFLERQSQAGIFEPLDK--SKMPNYKNLDPEMLKL 118
Cdd:cd13585 20 IDAFEKEnPGVKVEVVPVPYDDYWT-KLTtaaAAGTAPDVFYVDGPWVPEFASNGALLDLDDyiEKDGLDDDFPPGLLDA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 119 VAHNDKdnKYGIPYLMVTTGIGYNVDKVKAALGKDAPVDSWDLIL---KPENLEKLKSCGVSFlDAPSEVYATVLHYL-- 193
Cdd:cd13585 99 GTYDGK--LYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLeaaKKLTDKKGGQYGFAL-RGGSGGQTQWYPFLws 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 194 --GK--DPNSTNAADYTGAANDLLLKLR--------PNIRYFHSSQYINDLANGDicVAIGWSGDVMqaANRAKEAKNGV 261
Cdd:cd13585 176 ngGDllDEDDGKATLNSPEAVEALQFYVdlykdgvaPSSATTGGDEAVDLFASGK--VAMMIDGPWA--LGTLKDSKVKF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 262 NVAYA-IP-----KEGALTYFDMFAMPADAKNKDAAYQFLNFLMKPDVMAGISNYVYYANAVKDSTPLVNAEVRNNPNVY 335
Cdd:cd13585 252 KWGVApLPagpggKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAASAAAPDAKPALALA 331
|
330
....*....|
gi 727169280 336 PPADLRAKLF 345
Cdd:cd13585 332 AAADALAAAV 341
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
45-369 |
5.33e-12 |
|
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold; This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270451 [Multi-domain] Cd Length: 385 Bit Score: 66.55 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 45 LAKFQKE-TGIKVVYDVFDSNEVLEGKLMA---GSTGYDLVVPSSNFLERQSQAGIFEPLD---KSKMPNYKNLDPEMLK 117
Cdd:cd14748 20 VDEFNKShPDIKVKAVYQGSYDDTLTKLLAalaAGTAPDVAQVDASWVAQLADSGALEPLDdyiDKDGVDDDDFYPAALD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 118 LVAHNDKdnKYGIPYLMVTTGIGYNVDKVKAA-LGKDAPVDSWD--------LILKPENLEK-----------------L 171
Cdd:cd14748 100 AGTYDGK--LYGLPFDTSTPVLYYNKDLFEEAgLDPEKPPKTWDeleeaakkLKDKGGKTGRygfalppgdggwtfqalL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 172 KSCGVSFLDA-PSEVYATvlhylgkDPNSTNAADYtgaANDLLLKlRPNIRYFHSSQYINDLANGDICVAIGWSGDVmqa 250
Cdd:cd14748 178 WQNGGDLLDEdGGKVTFN-------SPEGVEALEF---LVDLVGK-DGVSPLNDWGDAQDAFISGKVAMTINGTWSL--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 251 aNRAKEAKNGVNVAYA-IP-----KEGALTYFDMFAMPAD-AKNKDAAYQFLNFLMKPDVMAGISNYVYYANAVKDSTPL 323
Cdd:cd14748 244 -AGIRDKGAGFEYGVApLPagkgkKGATPAGGASLVIPKGsSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRKSAAED 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 727169280 324 VNAEVRNNPNVYPPAD---LRAKLFTLNVQSPKLDRVITRAWTKVKSGK 369
Cdd:cd14748 323 PEEFLAENPNYKVAVDqldYAKPWGPPVPNGAEIRDELNEALEAALLGK 371
|
|
| PBP2_Fbp_like_2 |
cd13547 |
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
30-302 |
3.11e-10 |
|
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270265 [Multi-domain] Cd Length: 259 Bit Score: 59.93 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 30 TLHVYNwSDY--IAPDTLAKF-QKETGIKVvyDVFDSNEvleGKLM--------AGSTGYDLV-VPSSNFLERQSQAGIF 97
Cdd:cd13547 1 KLVVYT-SMPedLANALVEAFeKKYPGVKV--EVFRAGT---GKLMaklaaeaeAGNPQADVLwVADPPTAEALKKEGLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 98 EPlDKSKmPNYKNLDPEMlklvahnDKDNKYgIPYLMVTTGIGYNVDKVkaalGKDAPVDSWDLiLKPEnleklkscgvs 177
Cdd:cd13547 75 LP-YKSP-EADAIPAPFY-------DKDGYY-YGTRLSAMGIAYNTDKV----PEEAPKSWADL-TKPK----------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 178 fldapsevyatvlhYLGK----DPNstnaadYTGAANDLL--LKLRPNIR--YFH------------SSQYINDLANGDI 237
Cdd:cd13547 129 --------------YKGQivmpDPL------YSGAALDLVaaLADKYGLGweYFEklkengvkveggNGQVLDAVASGER 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727169280 238 CVAIGwsGDVMqaANRAKEAKNGVNVAYaiPKEGALTYFDMFAMPADAKNKDAAYQFLNFLMKPD 302
Cdd:cd13547 189 PAGVG--VDYN--ALRAKEKGSPLEVIY--PEEGTVVIPSPIAILKGSKNPEAAKAFVDFLLSPE 247
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
46-369 |
1.69e-09 |
|
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; possesses type 2 periplasmic binding fold; This group represents the periplasmic component of an ABC transport system XBP1 that shows preference for xylo-oligosaccharides in the order of xylotriose > xylobiose > xylotetraose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270452 [Multi-domain] Cd Length: 388 Bit Score: 58.93 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 46 AKFQKET-GIKVVYDVF---DSNEVLEgKLMAGSTGYDLV-VPSSNFLERQSQAGIFEPLDKsKMPNYKNLDPEMLKLVA 120
Cdd:cd14749 22 ADFEKENpNIKVKVVVFpydNYKTKLK-TAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPLTD-YLDPNGVDKRFLPGLAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 121 HNDKDNK-YGIPYLMVTTGIGYNVDKVKAALGKDAPvDSWDLILKPENLEKLKSCGV-------SFLDAPSEVYATVLHY 192
Cdd:cd14749 100 AVTFNGKvYGIPFAARALALFYNKDLFEEAGGVKPP-KTWDELIEAAKKDKFKAKGQtgfglllGAQGGHWYFQYLVRQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 193 LG-------------KDPNSTNAADYtgaANDLLLK--LRPNIRYFHSSQYINDLANGDICVAIGWSGDVmqAANRAKEA 257
Cdd:cd14749 179 GGgplsddgsgkatfNDPAFVQALQK---LQDLVKAgaFQEGFEGIDYDDAGQAFAQGKAAMNIGGSWDL--GAIKAGEP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 258 KNGVNVAyAIP--KEGALT-----YFDMFAMPADAKNKDAAYQFLNFLMKPDVMA------GISNYVYYANAVKDSTPLV 324
Cdd:cd14749 254 GGKIGVF-PFPtvGKGAQTstiggSDWAIAISANGKKKEAAVKFLKYLTSPEVMKqyledvGLLPAKEVVAKDEDPDPVA 332
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 727169280 325 ----NAEVRNNPNVYPPADlraklFTLNVQSPKLDRVITRAWTKVKSGK 369
Cdd:cd14749 333 ilgpFADVLNAAGSTPFLD-----EYWPAAAQVHKDAVQKLLTGKIDPE 376
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
36-339 |
2.87e-08 |
|
The periplasmic-binding component of ABC transport systems specific for maltose and related polysaccharides; possess type 2 periplasmic binding fold; This subfamily represents the periplasmic binding component of ABC transport systems involved in uptake of polysaccharides including maltose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270304 [Multi-domain] Cd Length: 367 Bit Score: 54.99 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 36 WSDYIAPD-----TLAKFQKETGIKVVYdVFDSNEVLEGKLM-AGSTGY--DLVVPSSNFLERQSQAGIFEPLDKSKMPN 107
Cdd:cd13586 5 WTDEDGELeylkeLAEEFEKKYGIKVEV-VYVDSGDTREKFItAGPAGKgpDVFFGPHDWLGELAAAGLLAPIPEYLAVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 108 YKNLDPEMLKLVAhndkDNK-YGIPYLMVTTGIGYNVDKVKaalgkdAPVDSWDLIL---KPENLEKLKSCGVSFLDAPS 183
Cdd:cd13586 84 IKNLPVALAAVTY----NGKlYGVPVSVETIALFYNKDLVP------EPPKTWEELIalaKKFNDKAGGKYGFAYDQTNP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 184 EVYATVL-----HYLGKDPNSTNAadyTGAANDLLLKlrpNIRYFHSSQYINDL----ANGDICVAIGWSGDV-MQ---- 249
Cdd:cd13586 154 YFSYPFLaafggYVFGENGGDPTD---IGLNNEGAVK---GLKFIKDLKKKYKVlppdLDYDIADALFKEGKAaMIingp 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 250 -AANRAKEAknGVNVAYA-IPK----EGALTYFD--MFAMPADAKNKDAAYQFLNFLMKPDVMAGISNYVYYANAVKDSt 321
Cdd:cd13586 228 wDLADYKDA--GINFGVApLPTlpggKQAAPFVGvqGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALKDA- 304
|
330
....*....|....*...
gi 727169280 322 pLVNAEVRNNPNVYPPAD 339
Cdd:cd13586 305 -LNDAAVKNDPLVKAFAE 321
|
|
| PBP2_TbpA |
cd13545 |
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ... |
30-315 |
3.27e-06 |
|
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding fold superfamily; Thiamin-binding protein TbpA is the periplasmic component of ABC-type transporter in E. coli, while the transmembrane permease and ATPase are ThiP and ThiQ, respectively. Thiamin (vitamin B1) is an essential confactor in all living systems that most prokaryotes, plants, and fungi can synthesized thiamin. However, in vertebrates, thiamine cannot be synthesized and must therefore be obtained through dietary absorption. In addition to thiamin biosynthesis, most organisms can import thiamin using specific transporters. After binding thiamine with high affinity, TbpA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The thiamine-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270263 [Multi-domain] Cd Length: 269 Bit Score: 48.06 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 30 TLHVY-----NWSDYIAPDTLAKFQKETGIKV-VYDVFDSNEVLE-GKLMAGSTGYDLVVP-SSNFLERQSQAGIFEPLD 101
Cdd:cd13545 1 TLTVYtydsfVGEWGPGPEVKAEFEKETGCKVeFVKPGDAGELLNrLILEKNNPRADVVLGlDNNLLSRALKEGLFEPYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 102 KSKMPNYknldPEMLKLVAhndkdNKYGIPYLMVTTGIGYNVDKVKaalgkDAPVDSWDLiLKPEnLEKL--------KS 173
Cdd:cd13545 81 SPALDVV----PEVPVFDP-----EDRLIPYDYGYLAFNYDKKKFK-----EPPLSLEDL-TAPE-YKGLivvqdprtSS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 174 CGVSFLdapsevYATVLHYlGKDpnstnaaDYtgaandlllklrpniryfhsSQYINDLANGDICVAIGWS--------- 244
Cdd:cd13545 145 PGLGFL------LWTIAVF-GEE-------GY--------------------LEYWKKLKANGVTVTPGWSeayglfttg 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727169280 245 -GDVM--QAANRAKEAKNGVNVAYA--IPKEGALTYFDMFAMPADAKNKDAAYQFLNFLMKPDVMAGI--SNYVYYAN 315
Cdd:cd13545 191 eAPMVvsYATSPAYHVYYEKDLRYTavIFPEGHYRQVEGAGILKGAKNPELAKKFVDFLLSPEFQEVIpeTNWMFPVN 268
|
|
| PBP2_AEPn_like |
cd13548 |
Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member ... |
43-322 |
1.79e-05 |
|
Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270266 [Multi-domain] Cd Length: 310 Bit Score: 46.02 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 43 DTLAKFQKETGIKVVYDVFDSNEVLE-GKLMAGSTGYDLVVPSSNFLERQSQAGIFEPldkSKMPNYKNldPEMLKlvah 121
Cdd:cd13548 16 DEFAAFTKATGITVNYVEAGSGEVVErAAKEKSNPQADVLVTLPPFIQQAAQMGLLQP---YQSDAAKN--PAIIK---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 122 nDKDNKYgIPYLMVTTGIGYNVDKVKaalgkdAPVDSWDLILKPENLEKLKSCGVSFLDAPSEVYATVLHYLGKDpnstn 201
Cdd:cd13548 87 -AEDGTY-APLVNNYFSFIYNSAVLK------NAPKTFADLLDPKYKGKIQYSTPGQAGDGMAVLLLTTHLMGSD----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 202 aadytgAANDLLLKLRPNIRyFHSSQ--YINDLAN-GDICVAigwSGDVMQAANRAKEAKNGVNVAYA-----IPKEGAL 273
Cdd:cd13548 154 ------AAFAYLAKLQQNNV-GPSAStgKLTALVSkGEISVA---NGDLQMNLAQMEHANPNKKIFWPakaggQRSTFAL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 727169280 274 TYFdmFAMPADAKNKDAAYQFLNFLMKPDVMAGISNYVYYANAVKDSTP 322
Cdd:cd13548 224 PYG--IGLVKGAPNADNGKKLIDFLLSKEAQSKVPDMAWGMPVRTDVTP 270
|
|
| PRK15046 |
PRK15046 |
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional |
3-322 |
2.22e-05 |
|
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
Pssm-ID: 237887 [Multi-domain] Cd Length: 349 Bit Score: 45.83 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 3 TQRKKWLSGVVAGLLMAASVTASAEeKTLHVY------NWSDyiapDTLAKFQKETGIKVVYDVFDSNEVLE-GKLMAGS 75
Cdd:PRK15046 10 AAAMKLAAAAAAAAFGGGAAPAWAA-DAVTVYsadgleDWYQ----DVFPAFTKATGIKVNYVEAGSGEVVNrAAKEKSN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 76 TGYDLVVPSSNFLERQSQAGIFEPLDKSkmpNYKNLDPemlklvAHNDKDNKYgIPYLMVTTGIGYNVDKVkaalgKDAP 155
Cdd:PRK15046 85 PQADVLVTLPPFIQQAAAEGLLQPYSSV---NAKAVPA------IAKDADGTY-APFVNNYLSFIYNPKVL-----KTAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 156 vDSWDLILKPENLEKLKscgvsfldapsevYAT---------VL----HYLGKDPnstnAADYtgaandlLLKLRPNIRy 222
Cdd:PRK15046 150 -ATWADLLDPKFKGKLQ-------------YSTpgqagdgtaVLlltfHLMGKDK----AFDY-------LAKLQANNV- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 223 FHSSQ--YINDLAN-GDICVAigwSGDVMQaaNRAKEAKNGVNVAYAIPKEG-------ALTYfdMFAMPADAKNKDAAY 292
Cdd:PRK15046 204 GPSKStgKLTPLVSkGEIYVA---NGDLQM--NLAQAEHGGPNVKIFFPAKDggerstfALPY--VIGLVKGAPNSENGK 276
|
330 340 350
....*....|....*....|....*....|
gi 727169280 293 QFLNFLMKPDVMAGISNYVYYANAVKDSTP 322
Cdd:PRK15046 277 KLIDFLLSKEAQTKVSDMAWGIPVRTDVPP 306
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
94-305 |
8.14e-05 |
|
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270450 [Multi-domain] Cd Length: 386 Bit Score: 44.23 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 94 AGIFEPLDkSKMPNYKNLDPEMLKLVAHNDKDNK-YGIPYLMVTTGIGYNVDKVKAALGKDAPVDsWD-----LILKPEN 167
Cdd:cd14747 72 MGALEDLT-PYLEDLGGDKDLFPGLVDTGTVDGKyYGVPWYADTRALFYRTDLLKKAGGDEAPKT-WDeleaaAKKIKAD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 168 LEK----------------------------LKSCGVSFLDAPsEVYATVLHYlgkdpnsTNAADYTGAANDLLLKlrpn 219
Cdd:cd14747 150 GPDvsgfaipgkndvwhnalpfvwgaggdlaTKDKWKATLDSP-EAVAGLEFY-------TSLYQKGLSPKSTLEN---- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 220 iryfhSSQYINDLANGDICVAIGWSGDVMQAANRAKEAKNGVNVAyAIP---KEGALTYF---DMfAMPADAKNKDAAYQ 293
Cdd:cd14747 218 -----SADVEQAFANGKVAMIISGPWEIGAIREAGPDLAGKWGVA-PLPggpGGGSPSFAggsNL-AVFKGSKNKDLAWK 290
|
250
....*....|..
gi 727169280 294 FLNFLMKPDVMA 305
Cdd:cd14747 291 FIEFLSSPENQA 302
|
|
| PBP2_BitB |
cd13546 |
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ... |
30-303 |
8.58e-05 |
|
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270264 [Multi-domain] Cd Length: 258 Bit Score: 43.79 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 30 TLHVY--NWSDYIAPdTLAKFQKETGIKVvydvfdsnevlegKLMAGSTGyDLVVPSSNflERQS-QAGIFEPLDKSKMP 106
Cdd:cd13546 1 TLVVYspNSEEIIEP-IIKEFEEKPGIKV-------------EVVTGGTG-ELLARIKA--EADNpQADVMWGGGIETLE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 107 NYKNL-----DPEMLKLVAHNDKDNKYGIPYLMVTTGIGYNVDKVKAAlgkDAPVdSWDLILKPenleKLKscgvsflda 181
Cdd:cd13546 64 AYKDLfepyeSPEAAAIPDAYKSPEGLWTGFSVLPVVLMVNTDLVKNI---GAPK-GWKDLLDP----KWK--------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 182 psevyatvlhylGK----DPNSTNAAdYT---------GAANDLLLKLRPN--IRYFHSSQYINDLANGDICVAIGWSgd 246
Cdd:cd13546 127 ------------GKiafaDPNKSGSA-YTilytilklyGGAWEYIEKLLDNlgVILSSSSAVYKAVADGEYAVGLTYE-- 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 727169280 247 vmqaANRAKEAKNGVNVAYAIPKEGalTYFDMFAMP--ADAKNKDAAYQFLNFLMKPDV 303
Cdd:cd13546 192 ----DAAYKYVAGGAPVKIVYPKEG--TTAVPDGVAivKGAKNPENAKKFIDFLLSKEV 244
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
47-334 |
2.23e-04 |
|
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold; This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270376 [Multi-domain] Cd Length: 372 Bit Score: 42.86 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 47 KFQKETGIKVVYDVFDSNEVLEGKLMAGSTGY--DLVVPSSNFLERQSQAGIFEP--LDKSKMpnyKNLDPEMLKLVAHN 122
Cdd:cd13658 21 QYTKKTGVKVKLVEVDQLDQLEKLSLDGPAGKgpDVMVAPHDRIGSAVLQGLLSPikLSKDKK---KGFTDQALKALTYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 123 DKdnKYGIPYLMVTTGIGYNVDKVKAALgkdAPVDSWDLILKPENLEKLKSCGVSFlDAPSEVYATVL-----HYLGKDP 197
Cdd:cd13658 98 GK--LYGLPAAVETLALYYNKDLVKNAP---KTFDELEALAKDLTKEKGKQYGFLA-DATNFYYSYGLlagngGYIFKKN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 198 NSTNAADYTGAANDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWSGDVMQ------AANRAKEAKNGVNVAyAIPKEG 271
Cdd:cd13658 172 GSDLDINDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAvidgpwAIQEYQEAGVNYGVA-PLPTLP 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727169280 272 ALTYFDMFA------MPADAKNKDAAYQFLNFLMKPDVMagisnYVYY--ANAVKDSTPLVN-AEVRNNPNV 334
Cdd:cd13658 251 NGKPMAPFLgvkgwyLSAYSKHKEWAQKFMEFLTSKENL-----KKRYdeTNEIPPRKDVRSdPEIKNNPLT 317
|
|
| SBP_bac_11 |
pfam13531 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
46-302 |
2.26e-04 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 463911 [Multi-domain] Cd Length: 225 Bit Score: 42.25 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 46 AKFQKETGIKVVYDVFDSNEVLegKLMAGSTGYDLVVPSSnflerqsqagifepldkSKMPNyknldpemlKLVAHNDKD 125
Cdd:pfam13531 17 AAFEAETGVKVVVSYGGSGKLA--KQIANGAPADVFISAD-----------------SAWLD---------KLAAAGLVV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 126 NKYGIPYlmvttgiGYNVDKVKAALGKDAPVDSWDLILKPenleklkscGVSFldapseVYAtvlhylgkDPNSTNAADY 205
Cdd:pfam13531 69 PGSRVPL-------AYSPLVIAVPKGNPKDISGLADLLKP---------GVRL------AVA--------DPKTAPSGRA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 206 TGA---ANDLLLKLRPNIRYF--HSSQYINDLANGDICVAIGWSGDVMQAANRAKEAkngvnvAYAIPKEGALTYFDMFA 280
Cdd:pfam13531 119 ALElleKAGLLKALEKKVVVLgeNVRQALTAVASGEADAGIVYLSEALFPENGPGLE------VVPLPEDLNLPLDYPAA 192
|
250 260
....*....|....*....|..
gi 727169280 281 MPADAKNKDAAYQFLNFLMKPD 302
Cdd:pfam13531 193 VLKKAAHPEAARAFLDFLLSPE 214
|
|
| PBP2_Fbp_like_3 |
cd13549 |
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
36-299 |
4.02e-04 |
|
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270267 [Multi-domain] Cd Length: 263 Bit Score: 41.67 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 36 WSDYIApdTLAKFQKETGIKVVYDVFDSNEVLeGKLMA--GSTGYDLVVPSSNFLERQSQAGIFEPLdkskMPNYKNLDP 113
Cdd:cd13549 11 WADWGT--QLKAFKKRTGIQIPYDNKNSGQAL-AALIAerARPVADVAYYGVAFGIQAVAQGVVQPY----KPAHWDEIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 114 EMLKlvahnDKDNKYgipYLMVTTGIGYNVDkVKAALGKDAPvDSWDLILKPENLEKlkscgVSFLDAPS----EVYATV 189
Cdd:cd13549 84 EGLK-----DPDGKW---FAIHSGTLGFIVN-VDALGGKPVP-KSWADLLKPEYKGM-----VGYLDPRSafvgYVGAVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 190 LHYL--GKDPNSTNAADYtgaandlLLKLRPNIRYFHSSQYINDLANGDICVAIGWSGDvmqaANRAKEaKNGVNVAYAI 267
Cdd:cd13549 149 VNQAmgGSLDNFGPGIDY-------FKKLHKNGPIVPKQTAYARVLSGEIPILIDYDFN----AYRAKY-TDKANVAFVI 216
|
250 260 270
....*....|....*....|....*....|..
gi 727169280 268 PKEGALTYFDMFAMPADAKNKDAAYQFLNFLM 299
Cdd:cd13549 217 PKEGSVVVPYVMSLVKNAPNPNNGKKVLDFIM 248
|
|
| ModA |
COG0725 |
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ... |
5-305 |
2.22e-03 |
|
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, periplasmic Mo-binding protein ModA is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440489 [Multi-domain] Cd Length: 253 Bit Score: 39.08 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 5 RKKWLSGVVAGLLMAASVTASAEEKTLHVYNWSDYIAP-DTLAK-FQKET-GIKVVYdVFdsnevlegklmaGSTGYdlv 81
Cdd:COG0725 1 RRLLLLALLLLALLLAGASAAAAAAELTVFAAASLKEAlEELAAaFEKEHpGVKVEL-SF------------GGSGA--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 82 vpssnfLERQSQAG----IFEPLDKSKMPnyknldpemlKLVAHNDKDNKYGIPYLMVTTGIGYNvdkvkaalgKDAPVD 157
Cdd:COG0725 65 ------LARQIEQGapadVFISADEKYMD----------KLAKKGLILAGSRVVFATNRLVLAVP---------KGNPAD 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 158 swdlilkPENLEKLKSCGVSF-LDAPSEV----YA-TVLHYLGkdpnstnaadytgaandLLLKLRPNIRYF-HSSQYIN 230
Cdd:COG0725 120 -------ISSLEDLAKPGVRIaIGDPKTVpygkYAkEALEKAG-----------------LWDALKPKLVLGeNVRQVLA 175
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727169280 231 DLANGDICVAIGWSGDVMQAAnrakeaknGVNVAYAIPKE--GALTYfdMFAMPADAKNKDAAYQFLNFLMKPDVMA 305
Cdd:COG0725 176 YVESGEADAGIVYLSDALAAK--------GVLVVVELPAElyAPIVY--PAAVLKGAKNPEAAKAFLDFLLSPEAQA 242
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
36-327 |
6.00e-03 |
|
The periplasmic-binding component of ABC transport systems specific for maltose and related oligosaccharides; possess type 2 periplasmic binding fold; This family represents the periplasmic binding component of ABC transport systems involved in uptake of oligosaccharides including maltose, trehalose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270240 [Multi-domain] Cd Length: 368 Bit Score: 38.16 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 36 WSDYIAPD------TLAKFQKET-GIKV--VYDVFDSNEVLEGKLMAGSTGYDLVVPSSNFLERQSQAGIFEPLDKSKMP 106
Cdd:cd13522 5 WHQYDTGEnqavneLIAKFEKAYpGITVevTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDEYVSK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 107 NYKNLdPEMLKLVAHNDKdnKYGIPYLMVTTGIGYNVDKVkaalgKDAPVDSWDLILKPENLEKLKScGVSFLDAPSEVY 186
Cdd:cd13522 85 SGKYA-PNTIAAMKLNGK--LYGVPVSVGAHLMYYNKKLV-----PKNPPKTWQELIALAQGLKAKN-VWGLVYNQNEPY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 187 ATVLH------YLGKDPNSTN--AADYTGAANDL--LLKLRpniryfHSSQYINDLANGDIC--------VAIGWSGDVM 248
Cdd:cd13522 156 FFAAWiggfggQVFKANNGKNnpTLDTPGAVEALqfLVDLK------SKYKIMPPETDYSIAdalfkagkAAMIINGPWD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169280 249 QAANRAKEAKN-GV-------NVAYAIPKEGALTYFdmfaMPADAKNKDAAYQFLNFLMKPDVMAGISNYVYYANA---V 317
Cdd:cd13522 230 LGDYRQALKINlGVaplptfsGTKHAAPFVGGKGFG----INKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDIPAnlqA 305
|
330
....*....|
gi 727169280 318 KDSTPLVNAE 327
Cdd:cd13522 306 YESPAVQNKP 315
|
|
| |
