|
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: 749.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 1 MVTQRKKWLSGVVAGLLMAASVTA-SAEEKTLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGSTGYD 79
Cdd:PRK10682 1 MTALNKKWLSGLVAGALMAVSVGTlAAEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 80 LVVPSSNFLERQSQAGIFEPLDKSKIPNYKNLDPEMLKLVAHNDKDNKYGIPYMMVTTGIGYNVDKVKAALGKDAPVNSW 159
Cdd:PRK10682 81 LVVPSASFLERQLTAGVFQPLDKSKLPNWKNLDPELLKLVAKHDPDNKYAMPYMWATTGIGYNVDKVKAVLGEDAPVDSW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 160 DLIFKPENLEKLKSCGVSFLDAPSEVYATVLHYLGKDPNSTNAADYTGAANDLLLKLRPNIRYFHSSQYINDLANGDICV 239
Cdd:PRK10682 161 DLVLKPENLEKLKSCGVSFLDAPEEIFATVLNYLGKDPNSTKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 240 AIGWSGDVMQAANRAKEAKNGVNVAYAIPKEGALTYFDMFAMPADAKSKDAAYQFLNFLLKPDVMADISNHIYYANAVKD 319
Cdd:PRK10682 241 AIGWAGDVWQASNRAKEAKNGVNVSYSIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPDVIAHISDHVFYANANKA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 727179692 320 STPLVNAEVRDNPNVYPPADLRAKLFTLNVQSPKLDRVITRAWTKVKSGK 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: 542.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGSTGYDLVVPSSNFLERQSQAGIFEPLDKSKIPNYK 109
Cdd:cd13659 1 TLNVYNWSDYIAPDTLEDFEKETGIKVVYDTYDSNEELEAKLLAGGSGYDLVVPSANFLGRQIKAGALQKLDKSKLPNWK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 110 NLDPEMLKLVAHNDKDNKYGIPYMMVTTGIGYNVDKVKAALGKDAPvNSWDLIFKPENLEKLKSCGVSFLDAPSEVYATV 189
Cdd:cd13659 81 NLDPLLLKLLAAVDPGNRYAVPYMWGTTGIAYNVDKVKAALGDDLP-DSWDLVFDPENLSKLKSCGVSVLDSPEEVFPAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 190 LHYLGKDPNSTNAADYtGAANDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWSGDVMQAANRAKEAKNGVNVAYAIPK 269
Cdd:cd13659 160 LNYLGLDPNSTDPEDI-KAAEDLLKKVRPYVRYFHSSKYINDLANGEICVAIGWSGDAVQAAQRAKEAGNGVTLEYVIPK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 270 EGALTYFDMFAMPADAKSKDAAYQFLNFLLKPDVMADISNHIYYANAVKDSTPLVNAEVRDNPNVYPPADLRAKLFTLNV 349
Cdd:cd13659 239 EGANLWFDMFAIPADAKNPDNAYRFINYLMRPEVIAKISNYVNYANANKAATPLVDEAIKDDPAIYPPEEVLKKLYALPP 318
|
330
....*....|...
gi 727179692 350 QSPKLDRVITRAW 362
Cdd:cd13659 319 LSAKVQRALTRAW 331
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
5-366 |
8.46e-148 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 421.24 E-value: 8.46e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 5 RKKWLS--GVVAGLLMAASVTASAEEKTLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGSTGYDLVV 82
Cdd:COG0687 3 RRSLLGlaAAALAAALAGGAPAAAAEGTLNVYNWGGYIDPDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAGGSGYDVVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 83 PSSNFLERQSQAGIFEPLDKSKIPNYKNLDPEMLKLvaHNDKDNKYGIPYMMVTTGIGYNVDKVKaalgkdAPVNSWDLI 162
Cdd:COG0687 83 PSDYFVARLIKAGLLQPLDKSKLPNLANLDPRFKDP--PFDPGNVYGVPYTWGTTGIAYNTDKVK------EPPTSWADL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 163 FKPENLEKlkscgVSFLDAPSEVYATVLHYLGKDPNSTNAADYTgAANDLLLKLRPNIRYFHSS--QYINDLANGDICVA 240
Cdd:COG0687 155 WDPEYKGK-----VALLDDPREVLGAALLYLGYDPNSTDPADLD-AAFELLIELKPNVRAFWSDgaEYIQLLASGEVDLA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 241 IGWSGDVMQAANRakeaknGVNVAYAIPKEGALTYFDMFAMPADAKSKDAAYQFLNFLLKPDVMADISNHIYYANAVKDS 320
Cdd:COG0687 229 VGWSGDALALRAE------GPPIAYVIPKEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAA 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 727179692 321 TPLVNAEVRDNPNVYPPADLRAKLFTLNVQSPKLDRVITRAWTKVK 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 |
3.23e-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: 355.00 E-value: 3.23e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGS-TGYDLVVPSSNFLERQSQAGIFEPLDKSKIPNY 108
Cdd:cd13590 1 ELNIYNWSDYIDPEVLKAFEKETGVKVNYDTYDSNEEMLAKLRAGGgSGYDLVVPSDYMVERLIKQGLLEPLDHSKLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 109 KNLDPEMLKLvaHNDKDNKYGIPYMMVTTGIGYNVDKVKAalgkdaPVNSWDLIFKPENLeklkSCGVSFLDAPSEVYAT 188
Cdd:cd13590 81 KNLDPQFLNP--PYDPGNRYSVPYQWGTTGIAYNKDKVKE------PPTSWDLDLWDPAL----KGRIAMLDDAREVLGA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 189 VLHYLGKDPNSTNAADyTGAANDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWSGDVMQAANRAKeakngvNVAYAIP 268
Cdd:cd13590 149 ALLALGYSPNTTDPAE-LAAAAELLIKQKPNVRAFDSDSYVQDLASGEIWLAQAWSGDALQANRENP------NLKFVIP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 269 KEGALTYFDMFAMPADAKSKDAAYQFLNFLLKPDVMADISNHIYYANAVKDSTPLVNAEVRDNPNVYPPADLRAKLFTLN 348
Cdd:cd13590 222 KEGGLLWVDNMAIPKGAPNPELAHAFINFLLDPEVAAKNAEYIGYATPNKAALELLPPELLDNPALYPPIEPLAKLLTFK 301
|
330
....*....|....
gi 727179692 349 VQSPKLDRVITRAW 362
Cdd:cd13590 302 DVDGEALELYDRIW 315
|
|
| PBP2_polyamines |
cd13523 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
30-310 |
7.33e-102 |
|
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: 301.66 E-value: 7.33e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMA-GSTGYDLVVPSSNFLERQSQAGIFEPLDKSKIPNY 108
Cdd:cd13523 1 TVVIYTWGGYLPQDIIDPFEKETGIKVVVDTAANSERMIKKLSAgGSGGFDLVTPSDSYTSRQLGVGLMQPIDKSLLPSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 109 KNLDPEMLKLVAHNDKDNKYGIPYMMVTTGIGYNVDKVKAalgkdAPVNSWDLIFKPENleklkSCGVSFLDAPSEVYAT 188
Cdd:cd13523 81 ATLDPHLTLAAVLTVPGKKYGVPYQWGATGLVYNTDKVKA-----PPKSYAADLDDPKY-----KGRVSFSDIPRETFAM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 189 VLHYLGKDPNSTNAADYTGAANDLLLKLRPNIRYFHS--SQYINDLANGDICVAIGWSGDVMQAANRakeaknGVNVAYA 266
Cdd:cd13523 151 ALANLGADGNEELYPDFTDAAAALLKELKPNVKKYWSnaSQPANLLLNGEVVLAMAWLGSGFKLKQA------GAPIEFV 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 727179692 267 IPKEGALTYFDMFAMPADAKSKDAAYQFLNFLLKPDVMADISNH 310
Cdd:cd13523 225 VPKEGAVGWLDTFAVPANAPNKDGAYKLLNALLRPKVAAAVAAT 268
|
|
| PBP2_PotD_PotF_like_3 |
cd13664 |
TThe periplasmic substrate-binding component of an uncharacterized active transport system ... |
30-362 |
6.84e-77 |
|
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: 239.57 E-value: 6.84e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGSTGYDLVVPSSNFLERQSQAGIFEPLDKSKIPNYK 109
Cdd:cd13664 1 ELNLYNWTDYTSPELLDKFEKETGIKVTLDTYDSNETLLAKLKAGGQGYDVVVPSDSFVPILIKEGLLEPLDKSQLTNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 110 NLDPEMLKLVAhnDKDNKYGIPYMMVTTGIGYNVDKVkaalgkDAPVNSWDLIFKPENLEKLKscgVSFLDAPSEVYATV 189
Cdd:cd13664 81 NIDPRWRKPDF--DPGNEYSIPWQWGTTGFAVDTAVY------DGDIDDYSVIFQPPEELKGK---IAMVDSMNEVVNAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 190 LHYLGKDPNSTNAADYTgAANDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWSGDVMQAanRAKEAkngvNVAYAIPK 269
Cdd:cd13664 150 IYYLGGPICTTDPKLMR-KVRDLLLEQKPHVKAYDSDGIVERMASGDVAAHVDWNGASLRA--RRQNP----SLAYAYPK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 270 EGALTYFDMFAMPADAKSKDAAYQFLNFLLKPDVMADISNHIYYANAVKDSTPLVNAEVRDNPNVYPPADLRAKLFTLNV 349
Cdd:cd13664 223 EGVLIWSDNLVIPKGAPNYENARTFLNFIMEPENAALQSNFAGYANAITGAEKFMDDPLKDAPALEIPPPEGSRLKFSTL 302
|
330
....*....|...
gi 727179692 350 QSPKLDRVITRAW 362
Cdd:cd13664 303 CPPKAEKLQSRIW 315
|
|
| PBP2_PotD |
cd13660 |
The periplasmic substrate-binding component of an active spermidine-preferential transport ... |
30-339 |
1.50e-68 |
|
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: 218.22 E-value: 1.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKL-MAGSTGYDLVVPSSNFLERQSQAGIFEPLDKSKIPNY 108
Cdd:cd13660 1 TLNFYNWSEYVPPELLEQFTKETGIKVILSTYESNETMYAKVkLYKDGAYDLVVPSTYYVDKMRKEGLIQKIDKSKITNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 109 KNLDPEMLKlvAHNDKDNKYGIPYMMVTTGIGYNVDkvkaALGKDApVNSWDLIFKPENLEKLkscgvSFLDAPSEVYAT 188
Cdd:cd13660 81 SNIDPDFLN--QPFDPNNDYSIPYIWGATALAVNGD----AVDGKS-VTSWADLWKPEYKGKL-----LLTDDAREVFQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 189 VLHYLGKDPNSTNAADYTGAANDLLlKLRPNIRYFHSSQYINDLANGDICVAIGWSGDVMQAANRAKeakngvNVAYAIP 268
Cdd:cd13660 149 ALRKLGYSGNTKDPEEIEAAFEELK-KLMPNVAAFDSDNPANPYMEGEVALGMIWNGSAFVARQANK------PIHVVWP 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727179692 269 KEGALTYFDMFAMPADAKSKDAAYQFLNFLLKPDVMADISNHIYYANAVKDSTPLVNAEVRDNPNVYPPAD 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 |
1.50e-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: 213.31 E-value: 1.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGSTGYDLVVPSSNFLERQSQAGIFEPLDKSKIPNYK 109
Cdd:cd13663 1 TLKVYNWGEYIDPDLIDDFEKETGIKVNYETFDSNEEMYTKIKTGGTSYDVIVPSDYMIEKLIKEDLLQPLDYSKLPNVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 110 ---NLDPEMLKLVAhnDKDNKYGIPYMMVTTGIGYNVDKVkaalgKDAPVNSWDLIFKPENLEKlkscgVSFLDAPSEVY 186
Cdd:cd13663 81 kniNIQPDLLNLAF--DPINEYSVPYFWGTLGIVYNKTKV-----SLEELSWWNILWNKKYKGK-----ILMYDSPRDAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 187 ATVLHYLGKDPNSTNaADYTGAANDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWSGDVMQAANRAKeakngvNVAYA 266
Cdd:cd13663 149 MVALKALGYSLNTTN-PDEIEEAKDWLIKQKPNVKAFVVDEIKDLMINGNADIAVTYSGDAAYAMEENE------NLDYV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 267 IPKEGALTYFDMFAMPADAKSKDAAYQFLNFLLKPDvmadisnhIYYANA--VKDSTPLVNAE--------VRDNPNVYP 336
Cdd:cd13663 222 IPKEGSNLWFDNWVIPKNAKNVDLAYKFINFLLRPD--------NALKNAeyVGYSTPNAAAEellpeeesIKDDKIFYP 293
|
330 340 350
....*....|....*....|....*....|
gi 727179692 337 PADLRAKLFTLNVQSPKLDRVITRAWTKVK 366
Cdd:cd13663 294 DEDIYKKCEVFKYLGGDAKKEYNDLWLEVK 323
|
|
| potD |
PRK09501 |
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed |
6-343 |
2.58e-65 |
|
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed
Pssm-ID: 181913 [Multi-domain] Cd Length: 348 Bit Score: 210.93 E-value: 2.58e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 6 KKWLSGVVAGLLMAASVTASA--EEKTLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGSTG-YDLVV 82
Cdd:PRK09501 2 KKWSRHLLAAGALALGMSAAHadDNNTLYFYNWTEYVPPGLLEQFTKETGIKVIYSTYESNETMYAKLKTYKDGaYDLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 83 PSSNFLERQSQAGIFEPLDKSKIPNYKNLDPEMLKlvAHNDKDNKYGIPYMMVTTGIGYNVDKVKAalgkdAPVNSWDLI 162
Cdd:PRK09501 82 PSTYYVDKMRKEGMIQKIDKSKLTNFSNLDPDMLN--KPFDPNNDYSIPYIWGATAIGVNSDAIDP-----KSVTSWADL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 163 FKPENLEKLkscgvSFLDAPSEVYATVLHYLGKDPNSTNAADYTGAANDlLLKLRPNIRYFHSSQYINDLANGDICVAIG 242
Cdd:PRK09501 155 WKPEYKGSL-----LLTDDAREVFQMALRKLGYSGNTTDPKEIEAAYNE-LKKLMPNVAAFNSDNPANPYMEGEVNLGMI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 243 WSGdvmqAANRAKEAKNGVNVAYaiPKEGALTYFDMFAMPADAKSKDAAYQFLNFLLKPDVMADISNHIYYANAVKDSTP 322
Cdd:PRK09501 229 WNG----SAFVARQAGTPIDVVW--PKEGGIFWMDSLAIPANAKNKEGALKLINFLLRPDVAKQVAETIGYPTPNLAARK 302
|
330 340
....*....|....*....|.
gi 727179692 323 LVNAEVRDNPNVYPPADLRAK 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 |
5.75e-63 |
|
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: 202.53 E-value: 5.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGSTGYDLVVPSSNFLERQSQAGIFEPLDKSKIPNYK 109
Cdd:cd13588 1 ELNVLTWPGYADPDWVTAFEEATGCKVVVKFFGSEDEMVAKLRSGGGDYDVVTPSGDALLRLIAAGLVQPIDTSKIPNYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 110 NLDPEMLKLVAHNDKDNKYGIPYMMVTTGIGYNVDKVKAalgkdAPVNSWDLIFKPENLEKlkscgVSFLDAPSEVYATV 189
Cdd:cd13588 81 NIDPRLRNLPWLTVDGKVYGVPYDWGANGLAYNTKKVKT-----PPTSWLALLWDPKYKGR-----VAARDDPIDAIADA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 190 LHYLGKDPNSTNAADYTGAANDLLLKLRPNIR-YFHSS-QYINDLANGDICVAIGWSGdvmqAANRAKeaKNGVNVAYAI 267
Cdd:cd13588 151 ALYLGQDPPFNLTDEQLDAVKAKLREQRPLVRkYWSDGaELVQLFANGEVVAATAWSG----QVNALQ--KAGKPVAYVI 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 727179692 268 PKEGALTYFDMFAMPADAKSKDAAYQFLNFLLKPDVMADISNHIYYANAV 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 |
3.17e-59 |
|
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: 193.89 E-value: 3.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMAGSTGYDLVVPSSNFLERQSQAGIFEPLDKSKIPNYK 109
Cdd:cd13662 1 VLYIYNWTYYIPDKVIEDFEKETGIRVVYDYYASNEEMYAKLKIGGGGYDIVSPSGDYVSIMKKEGLLEKLDKSKLPNVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 110 NLDPEMLKLVAHNDKDNKYGIPYMMVTTGIGYNvdkvKAALGKDApvNSWDlIFkpeNLEKLKScGVSFLDAPSEVYATV 189
Cdd:cd13662 81 EEKDNLMEASKIYDPGLEYSVPYMFGATGIAVN----KKIVKNYF--RKWS-IF---LREDLAG-RMTMLDDMREVIGAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 190 LHYLG--KDPNSTNAADytgAANDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWSGDVMQAANRAKEAkngvNVAYAI 267
Cdd:cd13662 150 LAYLGypVDSKDIEQLE---EAKEVILSWKKNLAKFDSNSYGKGFASGDFWVVHGYAEDVFYEVPEEEEE----KFDFFI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 268 PKEGALT-YFDMFAMPADAKSKDAAYQFLNFLLKPDVMADISNHIYYANAVKDstplVNAEVRDNPNVYPPADL-RAKLF 345
Cdd:cd13662 223 PEGAASMmYIDSFVIPKGSKHKDNAYKFINFILRPENYAEILDVLGNPSIIKE----AEKKSQKKPIIYAEEDLkNSKLP 298
|
.
gi 727179692 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 |
3.20e-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: 145.83 E-value: 3.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 48 FQKETGIKVVYDVFDSNEVLeGKLMA--GSTGYDLVVPSSNFLERQSQAGIFEPLDKSKIPNYKNLD-PEMLKlvahndk 124
Cdd:cd13589 23 FEKETGIKVVYDTGTSADRL-AKLQAqaGNPQWDVVDLDDGDAARAIAEGLLEPLDYSKIPNAAKDKaPAALK------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 125 dNKYGIPYMMVTTGIGYNVDKVKAalgkdaPVNSWDLiFKPENLEKLKSCGVSFLDAPSEVYAtVLHYLGKDPNSTNAAd 204
Cdd:cd13589 95 -TGYGVGYTLYSTGIAYNTDKFKE------PPTSWWL-ADFWDVGKFPGPRILNTSGLALLEA-ALLADGVDPYPLDVD- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 205 ytgAANDLLLKLRPNIRYFHSS--QYINDLANGDICVAIGWSGdvmqaanRAKEA-KNGVNVAYAIPKEGALTYFDMFAM 281
Cdd:cd13589 165 ---RAFAKLKELKPNVVTWWTSgaQLAQLLQSGEVDMAPAWNG-------RAQALiDAGAPVAFVWPKEGAILGPDTLAI 234
|
250 260 270
....*....|....*....|....*....|...
gi 727179692 282 PADAKSKDAAYQFLNFLLKPDVMADISNHIYYA 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 |
5.39e-33 |
|
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: 124.47 E-value: 5.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 30 TLHVYNWSDYIAPDTLAKFQKETGIKVVYDVFDSNEVLEGKLMA-GSTGYDLVVPSSNFLERQSQAGIFEPLDKSKIpNY 108
Cdd:cd13587 1 TLRILTWAGYAPEDLLEKFENETGIKVQVTTSNNNEEMISKLRAtGGGGFDLAQPSQRIAPNYEEFGLYQPIDESKI-KV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 109 KNLDPEMLKLVAHND--KDNKYGIPYMMVTTGIGYNVDKvkaalGKDAPVNSWDLIFKPENLEKlkscgVSF-LDAPSEV 185
Cdd:cd13587 80 AQFPPSLLESTKLGTtiNGKRYAVPFDWGTEGLTVNSTK-----APDVSGFSYGDLWAPEYAGK-----VAYrLKSPLTG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 186 YATVLHYLGKDPnSTNAADYTGAAN---------DLLLKLRPNIRYF--HSSQYINDLANGDICVAIGWSGdvmqaaNRA 254
Cdd:cd13587 150 LGLYADATGEDP-FNRYLDYKDEAKyqkildqvlQFLIERKANVKAYwnNADEALAAFRSGGCVIGQTWDS------TGL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727179692 255 KEAKNGVNVAYAIPKEGALTYFDMFAMPADAKSKDAAYQFLNFLLKPDVMADISNHIYYANAVKDS 320
Cdd:cd13587 223 KLNRENPPIDYGAPKEGALGWIDTFAIPAKAENVDQAYAFINFMLRPEIAAMFTNATGYNTAAVGA 288
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
46-334 |
5.71e-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: 5.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 46 AKFQKETGIKVVYDVFDSNEvLEGKLM----AGSTG-YDLVVPSSNFLERQSQAGIFEPLDKskIPNYKNLDPemlKLVA 120
Cdd:pfam13416 4 KAFEKKTGVTVEVEPQASND-LQAKLLaaaaAGNAPdLDVVWIAADQLATLAEAGLLADLSD--VDNLDDLPD---ALDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 121 HNDKDNKYGIPYMMVT-TGIGYNVDKVKAAlgkDAPVNSWDLIFkpENLEKLKSCgVSFLDAPSEVYATVLHYLGKDPNS 199
Cdd:pfam13416 78 AGYDGKLYGVPYAASTpTVLYYNKDLLKKA---GEDPKTWDELL--AAAAKLKGK-TGLTDPATGWLLWALLADGVDLTD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 200 TN-AADYTGAANDLLLKLRPNIRYF-HSSQYINDLANGDICVAIGWSGDVmqaanrAKEAKNGVNVAYAIPKEGALTYFD 277
Cdd:pfam13416 152 DGkGVEALDEALAYLKKLKDNGKVYnTGADAVQLFANGEVAMTVNGTWAA------AAAKKAGKKLGAVVPKDGSFLGGK 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 727179692 278 MFAMPADAKSKD-AAYQFLNFLLKPDVMADISNHIYYANAVKDSTPlvNAEVRDNPNV 334
Cdd:pfam13416 226 GLVVPAGAKDPRlAALDFIKFLTSPENQAALAEDTGYIPANKSAAL--SDEVKADPAL 281
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
5-309 |
1.64e-23 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 100.12 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 5 RKKWLSGVVAGLLMAA-------SVTASAEEKTLHVYNWSDYIAP---DTLAKFQKET-GIKVVYDVFDSNEVLEgKL-- 71
Cdd:COG1653 2 RRLALALAAALALALAacggggsGAAAAAGKVTLTVWHTGGGEAAaleALIKEFEAEHpGIKVEVESVPYDDYRT-KLlt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 72 -MAGSTGYDLVVPSSNFLERQSQAGIFEPLD---KSKIPNYKNLDPEMLKLVAHNDKdnKYGIPYMMVTTGIGYNVDKVK 147
Cdd:COG1653 81 aLAAGNAPDVVQVDSGWLAEFAAAGALVPLDdllDDDGLDKDDFLPGALDAGTYDGK--LYGVPFNTDTLGLYYNKDLFE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 148 AAlGKDAPvNSWD-LIfkpENLEKLKS----CGVSFLDAPSEVYATVLHYLGKDP-NSTNAADYTGAAN----DLLLKLR 217
Cdd:COG1653 159 KA-GLDPP-KTWDeLL---AAAKKLKAkdgvYGFALGGKDGAAWLDLLLSAGGDLyDEDGKPAFDSPEAvealEFLKDLV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 218 ------PNIRYFHSSQYINDLANGDicVAIGWSGDvmQAANRAKEAKNGVNVAYA-IP------KEGALTYFDMFAMPAD 284
Cdd:COG1653 234 kdgyvpPGALGTDWDDARAAFASGK--AAMMINGS--WALGALKDAAPDFDVGVApLPggpggkKPASVLGGSGLAIPKG 309
|
330 340
....*....|....*....|....*
gi 727179692 285 AKSKDAAYQFLNFLLKPDVMADISN 309
Cdd:COG1653 310 SKNPEAAWKFLKFLTSPEAQAKWDA 334
|
|
| PBP2_PotD_PotF_like_1 |
cd13661 |
The periplasmic substrate-binding component of an uncharacterized active transport system ... |
128-343 |
5.84e-22 |
|
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: 94.79 E-value: 5.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 128 YGIPYMMVTTGIGYNVDKVKAALGKDApvnSWDLIFKPEnlekLKScGVSFLDAPSEVYATVLHYLGKdpnSTNAADYTG 207
Cdd:cd13661 81 WAVPYRWGTTVIAYRKDKLKKLGWDPI---DWSDLWRPE----LAG-RIAMVDSPREVIGLVLKKLGA---SYNTAEVPG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 208 AANDL---LLKLRPNIRYFHSSQYINDLANGDICVAIGWSGDVMQAANRAKeakngvNVAYAIPKEGALTYFDMFAMPAD 284
Cdd:cd13661 150 GREALeerLAALRRQVKLYSSNNYLQALLLGDVWVAVGWSQDIIPLARRYS------NLAVVIPRSGTSLWADLWVIPAG 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727179692 285 AKSKD-------AAYQFLNFLLKP--------DVMADISNHIYYANAVKD-STPLVNAEVRDNPNVYPPADLRAK 343
Cdd:cd13661 224 SDFGGrvrgpspLLSQWIDFCLQParatqfaqLSFGGASPLILDGPSLTPpEATRKLKLDTNLVLGLPPDEILAK 298
|
|
| AfuA |
COG1840 |
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
44-364 |
3.18e-20 |
|
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 89.22 E-value: 3.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 44 TLAKFQKETGIKVVYDVFDSNEVLEgKLMA--GSTGYDLV-VPSSNFLERQSQAGIFEPLdksKIPNYKNLDPEMlklva 120
Cdd:COG1840 1 LLEAFEKKTGIKVNVVRGGSGELLA-RLKAegGNPPADVVwSGDADALEQLANEGLLQPY---KSPELDAIPAEF----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 121 hNDKDNKYgIPYMMVTTGIGYNVDKVKAalgKDAPVNSWDLIfKPENLEKL-------KSCGVSFLdapsevyATVLHYL 193
Cdd:COG1840 72 -RDPDGYW-FGFSVRARVIVYNTDLLKE---LGVPKSWEDLL-DPEYKGKIamadpssSGTGYLLV-------AALLQAF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 194 GKDpnstnaadytgAANDLLLKLRPNIRYF--HSSQYINDLANGDICVAIGWSGDVmqaanrAKEAKNGVNVAYAIPKEG 271
Cdd:COG1840 139 GEE-----------KGWEWLKGLAANGARVtgSSSAVAKAVASGEVAIGIVNSYYA------LRAKAKGAPVEVVFPEDG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 272 ALTYFDMFAMPADAKSKDAAYQFLNFLLKPDVMAdisnhiYYANAvkdstplvNAEVRDNPNVYPPADLRA----KLFTL 347
Cdd:COG1840 202 TLVNPSGAAILKGAPNPEAAKLFIDFLLSDEGQE------LLAEE--------GYEYPVRPDVEPPEGLPPlgelKLIDD 267
|
330
....*....|....*..
gi 727179692 348 NVQSPKLDRVITRAWTK 364
Cdd:COG1840 268 DDKAAENREELLELWDE 284
|
|
| SBP_bac_6 |
pfam13343 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
78-332 |
2.03e-18 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 463852 [Multi-domain] Cd Length: 247 Bit Score: 83.56 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 78 YDLVVPSSN------FLERQSQAGIFEPLDKSKIPNYknldPEMLKLVAHNDKDNKYgIPYMMVTTGIGYNVDKVKaalG 151
Cdd:pfam13343 4 PDIILSAGDlffdkrFLEKFIEEGLFQPLDSANLPNV----PKDFDDEGLRDPDGYY-TPYGVGPLVIAYNKERLG---G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 152 KDAPVnSWDLIFKPEnlekLKSCGVSFLDAPSEVYATVLHYLGKDPNSTNAAdytgaanDLLLKLRPNIRYFHSSQYIND 231
Cdd:pfam13343 76 RPVPR-SWADLLDPE----YKGKVALPGPNVGDLFNALLLALYKDFGEDGVR-------KLARNLKANLHPAQMVKAAGR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 232 LANGD--ICVAIGWSGDVMQAanrakeakNGVNVAYAIPKEGALTYFDMFAMPADAksKDAAYQFLNFLLKPDVMADISn 309
Cdd:pfam13343 144 LESGEpaVYLMPYFFADILPR--------KKKNVEVVWPEDGALVSPIFMLVKKGK--KELADPLIDFLLSPEVQAILA- 212
|
250 260
....*....|....*....|...
gi 727179692 310 HIYYANAVKDSTPLVNAEVRDNP 332
Cdd:pfam13343 213 KAGLVFPVVLNPAVDNPLPEGAP 235
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
5-326 |
1.54e-14 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 74.22 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 5 RKKWLSGVVAGLLMAASVTA-------------SAEEKTLHVYNWSDYIAP--DTLAKFQKETGIKVVYDVFDSNEVLEG 69
Cdd:COG2182 2 KRRLLAALALALALALALAAcgsgssssgsssaAGAGGTLTVWVDDDEAEAleEAAAAFEEEPGIKVKVVEVPWDDLREK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 70 KLMAGSTGY--DLVVPSSNFLERQSQAGIFEPLDKSkIPNYKNLDPEMLKLVAHNDKdnKYGIPYMMVTTGIGYNVDKVK 147
Cdd:COG2182 82 LTTAAPAGKgpDVFVGAHDWLGELAEAGLLAPLDDD-LADKDDFLPAALDAVTYDGK--LYGVPYAVETLALYYNKDLVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 148 AalgkdAPVNSWD-LIfkpENLEKLKSCGVS-FLDAPSEVYATVL-------HYLGKDPNSTNAADYTGAAN----DLLL 214
Cdd:COG2182 159 A-----EPPKTWDeLI---AAAKKLTAAGKYgLAYDAGDAYYFYPflaafggYLFGKDGDDPKDVGLNSPGAvaalEYLK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 215 KLRPNiRYFHSS----QYINDLANGDICVAIG--WsgdvmqAANRAKEAKnGVNVAYA-IPK----EGALTYF--DMFAM 281
Cdd:COG2182 231 DLIKD-GVLPADadydAADALFAEGKAAMIINgpW------AAADLKKAL-GIDYGVApLPTlaggKPAKPFVgvKGFGV 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 727179692 282 PADAKSKDAAYQFLNFLLKPDV---MADISNHI-----YYANAVKDSTPLVNA 326
Cdd:COG2182 303 SAYSKNKEAAQEFAEYLTSPEAqkaLFEATGRIpankaAAEDAEVKADPLIAA 355
|
|
| PBP2_Fbp_like_1 |
cd13544 |
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ... |
28-341 |
5.89e-14 |
|
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: 71.48 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 28 EKTLHVYNWSDYIAPdTLAKFQKETGIKVVYdVFDSNEVLEGKLMA--GSTGYDLVV--PSSNFLERQSQaGIFEPLdks 103
Cdd:cd13544 1 ELTVYTSLEEEEAKA-ILEAFKKDTGIKVEF-VRLSTGEALARLEAekGNPQADVWFggTADAHIQAKKE-GLLEPY--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 104 KIPNYKNLDPEmlklvahnDKDNK-YGIPYMMVTTGIGYNVDKVKaALGKDAPVnSWDLIFKPEnlekLK---------S 173
Cdd:cd13544 75 KSPNADKIPAK--------FKDPDgYWTGIYLGPLGFGVNTDELK-EKGLPVPK-SWEDLLNPE----YKgeivmpnpaS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 174 CGVSFLdapseVYATVLHYLGKDpnstnaadytgAANDLLLKLRPNIRYFHSSQY--INDLANGDICVAIGWSGDVMqaa 251
Cdd:cd13544 141 SGTAYT-----FLASLIQLMGED-----------EAWEYLKKLNKNVGQYTKSGSapAKLVASGEAAIGISFLHDAL--- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 252 nraKEAKNGVNVAYAIPKEGalTYFDM--FAMPADAKSKDAAYQFLNFLLKPDVMADISnhiyyanAVKDSTPLVNAEVR 329
Cdd:cd13544 202 ---KLKEQGYPIKIIFPKEG--TGYEIeaVAIIKGAKNPEAAKAFIDWALSKEAQELLA-------KVGSYAIPTNPDAK 269
|
330
....*....|..
gi 727179692 330 DNPNVYPPADLR 341
Cdd:cd13544 270 PPEIAPDLKKDK 281
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
45-305 |
8.92e-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: 70.91 E-value: 8.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 45 LAKFQKE-TGIKVVYDVFDSNEV---LEGKLMAGSTGYDLVVPSSNFLERQSQAGIFEPLDKSKIPNYKNLDPEmlklva 120
Cdd:pfam01547 14 VKEFEKEhPGIKVEVESVGSGSLaqkLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYLVLGVPK------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 121 hndkdnKYGIPYMMVTTGIGYNVDKVKAAlgKDAPVNSWD--LIFKPENLEKLKS-CGVSFLDAPSEVYATVLHYL---- 193
Cdd:pfam01547 88 ------LYGVPLAAETLGLIYNKDLFKKA--GLDPPKTWDelLEAAKKLKEKGKSpGGAGGGDASGTLGYFTLALLaslg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 194 -------GKDPNSTNAADYTGAANDLLLKLR-------PNIRYFHSSQYINDLANGDICVAIGWSGDVMQAANRAKEA-- 257
Cdd:pfam01547 160 gplfdkdGGGLDNPEAVDAITYYVDLYAKVLllkklknPGVAGADGREALALFEQGKAAMGIVGPWAALAANKVKLKVaf 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 727179692 258 -----KNGVNVAYAIP--KEGALTYFDMFAMPADAKSKDAAYQFLNFLLKPDVMA 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 |
1.27e-12 |
|
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: 66.94 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 30 TLHVYNWSDYI-APDTLAKFQKETGIKVVYdVFDSNEVLEGKLMA--GSTGYDLVVPSSNF-LERQSQAGIFEPLDkski 105
Cdd:cd13518 1 ELVVYTASDRDfAEPVLKAFEEKTGIKVKA-VYDGTGELANRLIAekNNPQADVFWGGEIIaLEALKEEGLLEPYT---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 106 PNYKNLDPEMLKlvahnDKDNKYgIPYMMVTTGIGYNVDKVKaalGKDAPVnSWDLIFKPENLEKLKSCGVSFLDAPSEV 185
Cdd:cd13518 76 PKVIEAIPADYR-----DPDGYW-VGFAARARVFIYNTDKLK---EPDLPK-SWDDLLDPKWKGKIVYPTPLRSGTGLTH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 186 YATVLHYLGKDPnstnaadytgAANDLLLKLRPNIRYFHSSQYINDL-ANGDICVAIGWSGDVMQAANRakeaknGVNVA 264
Cdd:cd13518 146 VAALLQLMGEEK----------GGWYLLKLLANNGKPVAGNSDAYDLvAKGEVAVGLTDTYYAARAAAK------GEPVE 209
|
250 260 270
....*....|....*....|....*....|....*....
gi 727179692 265 YAIPKEGALTYFDMFAMPADAKSKDAAYQFLNFLLKPDV 303
Cdd:cd13518 210 IVYPDQGALVIPEGVALLKGAPNPEAAKKFIDFLLSPEG 248
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
45-369 |
1.67e-11 |
|
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: 65.01 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 45 LAKFQKE-TGIKVVYDVFDSNEVLEGKLMA---GSTGYDLVVPSSNFLERQSQAGIFEPLD---KSKIPNYKNLDPEMLK 117
Cdd:cd14748 20 VDEFNKShPDIKVKAVYQGSYDDTLTKLLAalaAGTAPDVAQVDASWVAQLADSGALEPLDdyiDKDGVDDDDFYPAALD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 118 LVAHNDKdnKYGIPYMMVTTGIGYNVDKVKAA-LGKDAPVNSWD--------LIFKPENLEK-----------------L 171
Cdd:cd14748 100 AGTYDGK--LYGLPFDTSTPVLYYNKDLFEEAgLDPEKPPKTWDeleeaakkLKDKGGKTGRygfalppgdggwtfqalL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 172 KSCGVSFLDA-PSEVYATvlhylgkDPNSTNAADYtgaANDLLLKlRPNIRYFHSSQYINDLANGDICVAIGWSGDVmqa 250
Cdd:cd14748 178 WQNGGDLLDEdGGKVTFN-------SPEGVEALEF---LVDLVGK-DGVSPLNDWGDAQDAFISGKVAMTINGTWSL--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 251 aNRAKEAKNGVNVAYA-IP-----KEGALTYFDMFAMPAD-AKSKDAAYQFLNFLLKPDVMADISNHIYYANAVKDSTPL 323
Cdd:cd14748 244 -AGIRDKGAGFEYGVApLPagkgkKGATPAGGASLVIPKGsSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRKSAAED 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 727179692 324 VNAEVRDNPNVYPPAD---LRAKLFTLNVQSPKLDRVITRAWTKVKSGK 369
Cdd:cd14748 323 PEEFLAENPNYKVAVDqldYAKPWGPPVPNGAEIRDELNEALEAALLGK 371
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
45-345 |
7.75e-10 |
|
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: 59.73 E-value: 7.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 45 LAKFQKE-TGIKVVYDVFDSNEVLEgKLM---AGSTGYDLVVPSSNFLERQSQAGIFEPLDK--SKIPNYKNLDPEMLKL 118
Cdd:cd13585 20 IDAFEKEnPGVKVEVVPVPYDDYWT-KLTtaaAAGTAPDVFYVDGPWVPEFASNGALLDLDDyiEKDGLDDDFPPGLLDA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 119 VAHNDKdnKYGIPYMMVTTGIGYNVDKVKAALGKDAPVNSWDLIF---KPENLEKLKSCGVSFlDAPSEVYATVLHYL-- 193
Cdd:cd13585 99 GTYDGK--LYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLeaaKKLTDKKGGQYGFAL-RGGSGGQTQWYPFLws 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 194 --GK--DPNSTNAADYTGAANDLLLKLR--------PNIRYFHSSQYINDLANGDicVAIGWSGDVMqaANRAKEAKNGV 261
Cdd:cd13585 176 ngGDllDEDDGKATLNSPEAVEALQFYVdlykdgvaPSSATTGGDEAVDLFASGK--VAMMIDGPWA--LGTLKDSKVKF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 262 NVAYA-IP-----KEGALTYFDMFAMPADAKSKDAAYQFLNFLLKPDVMADISNHIYYANAVKDSTPLVNAEVRDNPNVY 335
Cdd:cd13585 252 KWGVApLPagpggKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAASAAAPDAKPALALA 331
|
330
....*....|
gi 727179692 336 PPADLRAKLF 345
Cdd:cd13585 332 AAADALAAAV 341
|
|
| PBP2_Fbp_like_2 |
cd13547 |
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
30-302 |
2.68e-09 |
|
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: 57.23 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 30 TLHVYNwSDY--IAPDTLAKF-QKETGIKVvyDVFDSNEvleGKLM--------AGSTGYDLV-VPSSNFLERQSQAGIF 97
Cdd:cd13547 1 KLVVYT-SMPedLANALVEAFeKKYPGVKV--EVFRAGT---GKLMaklaaeaeAGNPQADVLwVADPPTAEALKKEGLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 98 EPLdksKIPNYKNLDPEMLklvahnDKDNKYgIPYMMVTTGIGYNVDKVkaalGKDAPVNSWDLIfKPEnleklkscgvs 177
Cdd:cd13547 75 LPY---KSPEADAIPAPFY------DKDGYY-YGTRLSAMGIAYNTDKV----PEEAPKSWADLT-KPK----------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 178 fldapsevyatvlhYLGK----DPNstnaadYTGAANDLL--LKLRPNIR--YFH------------SSQYINDLANGDI 237
Cdd:cd13547 129 --------------YKGQivmpDPL------YSGAALDLVaaLADKYGLGweYFEklkengvkveggNGQVLDAVASGER 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727179692 238 CVAIGwsGDVMqaANRAKEAKNGVNVAYaiPKEGALTYFDMFAMPADAKSKDAAYQFLNFLLKPD 302
Cdd:cd13547 189 PAGVG--VDYN--ALRAKEKGSPLEVIY--PEEGTVVIPSPIAILKGSKNPEAAKAFVDFLLSPE 247
|
|
| TbpA |
COG4143 |
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ... |
5-344 |
8.76e-08 |
|
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and metabolism];
Pssm-ID: 443315 [Multi-domain] Cd Length: 343 Bit Score: 53.31 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 5 RKKWLSGVVAGLLMAA--SVTASAEEKTLHVYNWSDYIA-----PDTLAKFQKETGIKVVYDVFDS-----NE-VLEGKl 71
Cdd:COG4143 4 RTFLLAAALALALALAgcSGAAAAAKPTLTVYTYDSFASewgpgPWLKAAFEAECGCTLEFVAPGDggellNRlRLEGA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 72 magSTGYDLVVP-SSNFLERQSQAGIFEPLDkskIPNYKNLDPEmLKLvahndKDNKYGIPYmmvTTG---IGYNVDKVK 147
Cdd:COG4143 83 ---NPKADVVLGlDNNLLARALDTGLFAPHG---VDALDALALP-LAW-----DPDDRFVPY---DYGyfaFVYDKTKLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 148 AAlgkdapvnswdlifkPENLEKLkscgvsfLDAPSE---VYatvlhylgKDP-NSTnaadyTGAAndLLLKlrpNIRYF 223
Cdd:COG4143 148 NP---------------PESLEDL-------VDPEYKdklVV--------QDPrTST-----PGLA--FLLW---TIAAY 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 224 ---HSSQYINDLANGDICVAIGWS--------GD---VM-----QAANRAKEAKNGvNVAYAIPKEGALTYFDMFAMPAD 284
Cdd:COG4143 188 gedGALDYWQKLADNGVTVTKGWSeayglflkGEapmVLsystsPAYHVIAEGDKD-RYAAALFDEGHYRQVEGAGVLAG 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727179692 285 AKSKDAAYQFLNFLLKPDVMADI--SNHIYYANavkDSTPL-----VNAEVRDNPNVYPPADLRAKL 344
Cdd:COG4143 267 AKNPELARKFLDFLLSPEFQAEIptRNWMYPAV---EDVELpeafdEYAPVPEKPLTFDPDEIAANR 330
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
36-164 |
2.40e-07 |
|
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: 51.91 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 36 WSDYIAPD-----TLAKFQKETGIKVVYdVFDSNEVLEGKLM-AGSTGY--DLVVPSSNFLERQSQAGIFEPLDKSKIPN 107
Cdd:cd13586 5 WTDEDGELeylkeLAEEFEKKYGIKVEV-VYVDSGDTREKFItAGPAGKgpDVFFGPHDWLGELAAAGLLAPIPEYLAVK 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 727179692 108 YKNLDPEMLKLVAhndkDNK-YGIPYMMVTTGIGYNVDKVKaalgkdAPVNSWDLIFK 164
Cdd:cd13586 84 IKNLPVALAAVTY----NGKlYGVPVSVETIALFYNKDLVP------EPPKTWEELIA 131
|
|
| PBP2_TbpA |
cd13545 |
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ... |
30-308 |
6.59e-05 |
|
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: 44.21 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 30 TLHVY-----NWSDYIAPDTLAKFQKETGIKV-VYDVFDSNEVLE-GKLMAGSTGYDLVVP-SSNFLERQSQAGIFEPLD 101
Cdd:cd13545 1 TLTVYtydsfVGEWGPGPEVKAEFEKETGCKVeFVKPGDAGELLNrLILEKNNPRADVVLGlDNNLLSRALKEGLFEPYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 102 K---SKIPNYKNLDPemlklvahndkdNKYGIPYMMVTTGIGYNVDKVkaalgKDAPVNSWDLIfKPEnLEKL------- 171
Cdd:cd13545 81 SpalDVVPEVPVFDP------------EDRLIPYDYGYLAFNYDKKKF-----KEPPLSLEDLT-APE-YKGLivvqdpr 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 172 -KSCGVSFLdapsevYATVLHYlGKDpnstnaaDYtgaandlllklrpniryfhsSQYINDLANGDICVAIGWS------ 244
Cdd:cd13545 142 tSSPGLGFL------LWTIAVF-GEE-------GY--------------------LEYWKKLKANGVTVTPGWSeayglf 187
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727179692 245 ----GDVM--QAANRAKEAKNGVNVAYA--IPKEGALTYFDMFAMPADAKSKDAAYQFLNFLLKPDVMADIS 308
Cdd:cd13545 188 ttgeAPMVvsYATSPAYHVYYEKDLRYTavIFPEGHYRQVEGAGILKGAKNPELAKKFVDFLLSPEFQEVIP 259
|
|
| SBP_bac_11 |
pfam13531 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
196-302 |
7.37e-04 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 463911 [Multi-domain] Cd Length: 225 Bit Score: 40.71 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 196 DPNSTNAADYTGA---ANDLLLKLRPNIRYF--HSSQYINDLANGDICVAIGWSGDVMQAANRAKEAkngvnvAYAIPKE 270
Cdd:pfam13531 109 DPKTAPSGRAALElleKAGLLKALEKKVVVLgeNVRQALTAVASGEADAGIVYLSEALFPENGPGLE------VVPLPED 182
|
90 100 110
....*....|....*....|....*....|..
gi 727179692 271 GALTYFDMFAMPADAKSKDAAYQFLNFLLKPD 302
Cdd:pfam13531 183 LNLPLDYPAAVLKKAAHPEAARAFLDFLLSPE 214
|
|
| PBP2_AEPn_like |
cd13548 |
Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member ... |
43-322 |
9.45e-04 |
|
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: 40.62 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 43 DTLAKFQKETGIKVVYDVFDSNEVLE-GKLMAGSTGYDLVVPSSNFLERQSQAGIFEPldkSKIPNYKNldPEMLKlvah 121
Cdd:cd13548 16 DEFAAFTKATGITVNYVEAGSGEVVErAAKEKSNPQADVLVTLPPFIQQAAQMGLLQP---YQSDAAKN--PAIIK---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 122 nDKDNKYgIPYMMVTTGIGYNVDKVKaalgkdAPVNSWDLIFKPENLEKLKSCGVSFLDAPSEVYATVLHYLGKDpnstn 201
Cdd:cd13548 87 -AEDGTY-APLVNNYFSFIYNSAVLK------NAPKTFADLLDPKYKGKIQYSTPGQAGDGMAVLLLTTHLMGSD----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 202 aadytgAANDLLLKLRPNIRyFHSSQ--YINDLAN-GDICVAigwSGDVMQAANRAKEAKNGVNVAYA-----IPKEGAL 273
Cdd:cd13548 154 ------AAFAYLAKLQQNNV-GPSAStgKLTALVSkGEISVA---NGDLQMNLAQMEHANPNKKIFWPakaggQRSTFAL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 727179692 274 TYFdmFAMPADAKSKDAAYQFLNFLLKPDVMADISNHIYYANAVKDSTP 322
Cdd:cd13548 224 PYG--IGLVKGAPNADNGKKLIDFLLSKEAQSKVPDMAWGMPVRTDVTP 270
|
|
| PBP2_BitB |
cd13546 |
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ... |
30-303 |
2.26e-03 |
|
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: 39.16 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 30 TLHVY--NWSDYIAPdTLAKFQKETGIKVvydvfdsnevlegKLMAGSTGyDLVVPSSNflERQS-QAGIFEPLDKSKIP 106
Cdd:cd13546 1 TLVVYspNSEEIIEP-IIKEFEEKPGIKV-------------EVVTGGTG-ELLARIKA--EADNpQADVMWGGGIETLE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 107 NYKNL-----DPEMLKLVAHNDKDNKYGIPYMMVTTGIGYNVDKVKaalgKDAPVNSWDLIFKPenleKLKscgvsflda 181
Cdd:cd13546 64 AYKDLfepyeSPEAAAIPDAYKSPEGLWTGFSVLPVVLMVNTDLVK----NIGAPKGWKDLLDP----KWK--------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727179692 182 psevyatvlhylGK----DPNSTNAAdYT---------GAANDLLLKLRPN--IRYFHSSQYINDLANGDICVAIGWSgd 246
Cdd:cd13546 127 ------------GKiafaDPNKSGSA-YTilytilklyGGAWEYIEKLLDNlgVILSSSSAVYKAVADGEYAVGLTYE-- 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 727179692 247 vmqaANRAKEAKNGVNVAYAIPKEGalTYFDMFAMP--ADAKSKDAAYQFLNFLLKPDV 303
Cdd:cd13546 192 ----DAAYKYVAGGAPVKIVYPKEG--TTAVPDGVAivKGAKNPENAKKFIDFLLSKEV 244
|
|
| |
