|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10682 |
PRK10682 |
putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional |
1-370 |
0e+00 |
|
putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional
Pssm-ID: 182645 [Multi-domain] Cd Length: 370 Bit Score: 798.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 1 MTAFGKKWLTGLVTGALMAVSAGSLAAEQKTLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFD 80
Cdd:PRK10682 1 MTALNKKWLSGLVAGALMAVSVGTLAAEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 81 LVVPSASFLERQLAAGVFQPLDKSKLPNWKNLDPEVLKLVAKHDPENKYAMPYLWATTGIGYNVDKVKAVLGKDAPVDSW 160
Cdd:PRK10682 81 LVVPSASFLERQLTAGVFQPLDKSKLPNWKNLDPELLKLVAKHDPDNKYAMPYMWATTGIGYNVDKVKAVLGEDAPVDSW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 161 DLVLKPENLEKLKSCGVSFLDAPEEIFATVLNYLGKDPNSSKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICV 240
Cdd:PRK10682 161 DLVLKPENLEKLKSCGVSFLDAPEEIFATVLNYLGKDPNSTKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 241 AIGWAGDVWQAANRAKEAKNGVNVSYFIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDVIAKISDQVFYANGNKA 320
Cdd:PRK10682 241 AIGWAGDVWQASNRAKEAKNGVNVSYSIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPDVIAHISDHVFYANANKA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2276266925 321 STPLVSETIRNNPAIYPPADVFAKLFTLKVQDPKIDRVRTRAWTKVKSGK 370
Cdd:PRK10682 321 ATPLVSAEVRDNPGIYPPADVRAKLFTLKVQDPKIDRVRTRAWTKVKSGK 370
|
|
| PBP2_PotF |
cd13659 |
The periplasmic substrate-binding component of an ABC putrescine transport system and related ... |
31-363 |
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: 562.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNWK 110
Cdd:cd13659 1 TLNVYNWSDYIAPDTLEDFEKETGIKVVYDTYDSNEELEAKLLAGGSGYDLVVPSANFLGRQIKAGALQKLDKSKLPNWK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 111 NLDPEVLKLVAKHDPENKYAMPYLWATTGIGYNVDKVKAVLGKDAPvDSWDLVLKPENLEKLKSCGVSFLDAPEEIFATV 190
Cdd:cd13659 81 NLDPLLLKLLAAVDPGNRYAVPYMWGTTGIAYNVDKVKAALGDDLP-DSWDLVFDPENLSKLKSCGVSVLDSPEEVFPAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 191 LNYLGKDPNSSKADDYtGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQAANRAKEAKNGVNVSYFIPK 270
Cdd:cd13659 160 LNYLGLDPNSTDPEDI-KAAEDLLKKVRPYVRYFHSSKYINDLANGEICVAIGWSGDAVQAAQRAKEAGNGVTLEYVIPK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 271 EGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDVIAKISDQVFYANGNKASTPLVSETIRNNPAIYPPADVFAKLFTLKV 350
Cdd:cd13659 239 EGANLWFDMFAIPADAKNPDNAYRFINYLMRPEVIAKISNYVNYANANKAATPLVDEAIKDDPAIYPPEEVLKKLYALPP 318
|
330
....*....|...
gi 2276266925 351 QDPKIDRVRTRAW 363
Cdd:cd13659 319 LSAKVQRALTRAW 331
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
6-367 |
3.79e-148 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 422.40 E-value: 3.79e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 6 KKWLTGLVTGALMAVSAG--SLAAEQKTLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVV 83
Cdd:COG0687 3 RRSLLGLAAAALAAALAGgaPAAAAEGTLNVYNWGGYIDPDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAGGSGYDVVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 84 PSASFLERQLAAGVFQPLDKSKLPNWKNLDPEVLKLvaKHDPENKYAMPYLWATTGIGYNVDKVKavlgkdAPVDSWDLV 163
Cdd:COG0687 83 PSDYFVARLIKAGLLQPLDKSKLPNLANLDPRFKDP--PFDPGNVYGVPYTWGTTGIAYNTDKVK------EPPTSWADL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 164 LKPENLEKlkscgVSFLDAPEEIFATVLNYLGKDPNSSKADDYTgPATDLLLKLRPNIRYFHSS--QYINDLANGDICVA 241
Cdd:COG0687 155 WDPEYKGK-----VALLDDPREVLGAALLYLGYDPNSTDPADLD-AAFELLIELKPNVRAFWSDgaEYIQLLASGEVDLA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 242 IGWAGDVWQAANRakeaknGVNVSYFIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDVIAKISDQVFYANGNKAS 321
Cdd:COG0687 229 VGWSGDALALRAE------GPPIAYVIPKEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAA 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2276266925 322 TPLVSETIRNNPAIYPPADVFAKLFTLKVQDPKIDRVRTRAWTKVK 367
Cdd:COG0687 303 RELLPPELAANPAIYPPEEVLDKLEFWNPLPPENRELYTRRWTEIK 348
|
|
| PBP2_PotD_PotF_like |
cd13590 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
31-363 |
9.17e-126 |
|
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: 364.25 E-value: 9.17e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGS-TGFDLVVPSASFLERQLAAGVFQPLDKSKLPNW 109
Cdd:cd13590 1 ELNIYNWSDYIDPEVLKAFEKETGVKVNYDTYDSNEEMLAKLRAGGgSGYDLVVPSDYMVERLIKQGLLEPLDHSKLPNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 110 KNLDPEVLKLvaKHDPENKYAMPYLWATTGIGYNVDKVKAvlgkdaPVDSWDLVLKPENLeklkSCGVSFLDAPEEIFAT 189
Cdd:cd13590 81 KNLDPQFLNP--PYDPGNRYSVPYQWGTTGIAYNKDKVKE------PPTSWDLDLWDPAL----KGRIAMLDDAREVLGA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 190 VLNYLGKDPNSSKADDyTGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQAANRAKeakngvNVSYFIP 269
Cdd:cd13590 149 ALLALGYSPNTTDPAE-LAAAAELLIKQKPNVRAFDSDSYVQDLASGEIWLAQAWSGDALQANRENP------NLKFVIP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 270 KEGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDVIAKISDQVFYANGNKASTPLVSETIRNNPAIYPPADVFAKLFTLK 349
Cdd:cd13590 222 KEGGLLWVDNMAIPKGAPNPELAHAFINFLLDPEVAAKNAEYIGYATPNKAALELLPPELLDNPALYPPIEPLAKLLTFK 301
|
330
....*....|....
gi 2276266925 350 VQDPKIDRVRTRAW 363
Cdd:cd13590 302 DVDGEALELYDRIW 315
|
|
| PBP2_polyamines |
cd13523 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
31-311 |
4.61e-114 |
|
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: 332.86 E-value: 4.61e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMA-GSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNW 109
Cdd:cd13523 1 TVVIYTWGGYLPQDIIDPFEKETGIKVVVDTAANSERMIKKLSAgGSGGFDLVTPSDSYTSRQLGVGLMQPIDKSLLPSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 110 KNLDPEVLKLVAKHDPENKYAMPYLWATTGIGYNVDKVKAVLgkdapvDSWdlvlKPENLEKLKSCGVSFLDAPEEIFAT 189
Cdd:cd13523 81 ATLDPHLTLAAVLTVPGKKYGVPYQWGATGLVYNTDKVKAPP------KSY----AADLDDPKYKGRVSFSDIPRETFAM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 190 VLNYLGKDPNSSKADDYTGPATDLLLKLRPNIRYFHS--SQYINDLANGDICVAIGWAGDVWQAANRakeaknGVNVSYF 267
Cdd:cd13523 151 ALANLGADGNEELYPDFTDAAAALLKELKPNVKKYWSnaSQPANLLLNGEVVLAMAWLGSGFKLKQA------GAPIEFV 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2276266925 268 IPKEGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDVIAKISDQ 311
Cdd:cd13523 225 VPKEGAVGWLDTFAVPANAPNKDGAYKLLNALLRPKVAAAVAAT 268
|
|
| PBP2_PotD_PotF_like_3 |
cd13664 |
TThe periplasmic substrate-binding component of an uncharacterized active transport system ... |
31-363 |
1.38e-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: 241.49 E-value: 1.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNWK 110
Cdd:cd13664 1 ELNLYNWTDYTSPELLDKFEKETGIKVTLDTYDSNETLLAKLKAGGQGYDVVVPSDSFVPILIKEGLLEPLDKSQLTNYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 111 NLDPEVLKLVAkhDPENKYAMPYLWATTGIGYNVDKVkavlgkDAPVDSWDLVLKPENLEKLKscgVSFLDAPEEIFATV 190
Cdd:cd13664 81 NIDPRWRKPDF--DPGNEYSIPWQWGTTGFAVDTAVY------DGDIDDYSVIFQPPEELKGK---IAMVDSMNEVVNAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 191 LNYLGKDPNSSKADDYTgPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGdvwqAANRAKEAKNgvNVSYFIPK 270
Cdd:cd13664 150 IYYLGGPICTTDPKLMR-KVRDLLLEQKPHVKAYDSDGIVERMASGDVAAHVDWNG----ASLRARRQNP--SLAYAYPK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 271 EGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDVIAKISDQVFYANGNKASTPLVSETIRNNPAIYPPADVFAKLFTLKV 350
Cdd:cd13664 223 EGVLIWSDNLVIPKGAPNYENARTFLNFIMEPENAALQSNFAGYANAITGAEKFMDDPLKDAPALEIPPPEGSRLKFSTL 302
|
330
....*....|...
gi 2276266925 351 QDPKIDRVRTRAW 363
Cdd:cd13664 303 CPPKAEKLQSRIW 315
|
|
| PBP2_PotD_PotF_like_2 |
cd13663 |
The periplasmic substrate-binding component of an uncharacterized active transport system ... |
31-367 |
1.65e-70 |
|
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: 223.32 E-value: 1.65e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNWK 110
Cdd:cd13663 1 TLKVYNWGEYIDPDLIDDFEKETGIKVNYETFDSNEEMYTKIKTGGTSYDVIVPSDYMIEKLIKEDLLQPLDYSKLPNVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 111 ---NLDPEVLKLvaKHDPENKYAMPYLWATTGIGYNVDKVkavlgKDAPVDSWDLVLKPENLEKlkscgVSFLDAPEEIF 187
Cdd:cd13663 81 kniNIQPDLLNL--AFDPINEYSVPYFWGTLGIVYNKTKV-----SLEELSWWNILWNKKYKGK-----ILMYDSPRDAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 188 ATVLNYLGKDPNSSKaDDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDvwqaANRAKEaKNgVNVSYF 267
Cdd:cd13663 149 MVALKALGYSLNTTN-PDEIEEAKDWLIKQKPNVKAFVVDEIKDLMINGNADIAVTYSGD----AAYAME-EN-ENLDYV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 268 IPKEGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDVIAKISDQVFYANGNKASTPLVSE--TIRNNPAIYPPADVFAKL 345
Cdd:cd13663 222 IPKEGSNLWFDNWVIPKNAKNVDLAYKFINFLLRPDNALKNAEYVGYSTPNAAAEELLPEeeSIKDDKIFYPDEDIYKKC 301
|
330 340
....*....|....*....|..
gi 2276266925 346 FTLKVQDPKIDRVRTRAWTKVK 367
Cdd:cd13663 302 EVFKYLGGDAKKEYNDLWLEVK 323
|
|
| PBP2_PotD |
cd13660 |
The periplasmic substrate-binding component of an active spermidine-preferential transport ... |
31-340 |
3.73e-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: 217.07 E-value: 3.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKL-MAGSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNW 109
Cdd:cd13660 1 TLNFYNWSEYVPPELLEQFTKETGIKVILSTYESNETMYAKVkLYKDGAYDLVVPSTYYVDKMRKEGLIQKIDKSKITNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 110 KNLDPEVLKlvAKHDPENKYAMPYLWATTGIGYNVDkvkaVLGKDApVDSWDLVLKPENLEKLkscgvSFLDAPEEIFAT 189
Cdd:cd13660 81 SNIDPDFLN--QPFDPNNDYSIPYIWGATALAVNGD----AVDGKS-VTSWADLWKPEYKGKL-----LLTDDAREVFQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 190 VLNYLGKDPNSSKADDYTGpATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQAANRAKeakngvNVSYFIP 269
Cdd:cd13660 149 ALRKLGYSGNTKDPEEIEA-AFEELKKLMPNVAAFDSDNPANPYMEGEVALGMIWNGSAFVARQANK------PIHVVWP 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2276266925 270 KEGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDVIAKISDQVFYANGNKASTPLVSETIRNNPAIYPPAD 340
Cdd:cd13660 222 KEGGIFWMDSFAIPANAKNKEGALKFINFLLRPDVSKQIAETIGYPTPNLKARKLLSPEVANNKIVYPSAE 292
|
|
| potD |
PRK09501 |
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed |
6-344 |
6.60e-68 |
|
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed
Pssm-ID: 181913 [Multi-domain] Cd Length: 348 Bit Score: 217.48 E-value: 6.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 6 KKWLTGLVTGALMAVSAGSLAA-EQKTLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTG-FDLVV 83
Cdd:PRK09501 2 KKWSRHLLAAGALALGMSAAHAdDNNTLYFYNWTEYVPPGLLEQFTKETGIKVIYSTYESNETMYAKLKTYKDGaYDLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 84 PSASFLERQLAAGVFQPLDKSKLPNWKNLDPEVLKlvAKHDPENKYAMPYLWATTGIGYNVDKVKAvlgkdAPVDSWDLV 163
Cdd:PRK09501 82 PSTYYVDKMRKEGMIQKIDKSKLTNFSNLDPDMLN--KPFDPNNDYSIPYIWGATAIGVNSDAIDP-----KSVTSWADL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 164 LKPENLEKLkscgvSFLDAPEEIFATVLNYLGKDPNSSKADDYTGpATDLLLKLRPNIRYFHSSQYINDLANGDICVAIG 243
Cdd:PRK09501 155 WKPEYKGSL-----LLTDDAREVFQMALRKLGYSGNTTDPKEIEA-AYNELKKLMPNVAAFNSDNPANPYMEGEVNLGMI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 244 WAGDVWQAanraKEAKNGVNVSYfiPKEGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDVIAKISDQVFYANGNKASTP 323
Cdd:PRK09501 229 WNGSAFVA----RQAGTPIDVVW--PKEGGIFWMDSLAIPANAKNKEGALKLINFLLRPDVAKQVAETIGYPTPNLAARK 302
|
330 340
....*....|....*....|.
gi 2276266925 324 LVSETIRNNPAIYPPADVFAK 344
Cdd:PRK09501 303 LLSPEVANDKSLYPDAETIKK 323
|
|
| PBP2_TpPotD_like |
cd13662 |
The periplasmic substrate-binding component of an ABC-type polyamine transport system from ... |
31-336 |
2.08e-60 |
|
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: 196.97 E-value: 2.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNWK 110
Cdd:cd13662 1 VLYIYNWTYYIPDKVIEDFEKETGIRVVYDYYASNEEMYAKLKIGGGGYDIVSPSGDYVSIMKKEGLLEKLDKSKLPNVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 111 NLDPEVLKLVAKHDPENKYAMPYLWATTGIGYNVDKVkavlgKDAPVDsWDLVLKpenlEKLKScGVSFLDAPEEIFATV 190
Cdd:cd13662 81 EEKDNLMEASKIYDPGLEYSVPYMFGATGIAVNKKIV-----KNYFRK-WSIFLR----EDLAG-RMTMLDDMREVIGAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 191 LNYLGKdPNSSKADDYTGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQAANRAKEAkngvNVSYFIPK 270
Cdd:cd13662 150 LAYLGY-PVDSKDIEQLEEAKEVILSWKKNLAKFDSNSYGKGFASGDFWVVHGYAEDVFYEVPEEEEE----KFDFFIPE 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2276266925 271 EGA-LAFFDVFAMPADAKNKDEAYQFLNYLMRPDVIAKISDQVfyanGNKASTPLVSETIRNNPAIY 336
Cdd:cd13662 225 GAAsMMYIDSFVIPKGSKHKDNAYKFINFILRPENYAEILDVL----GNPSIIKEAEKKSQKKPIIY 287
|
|
| PBP2_polyamine_1 |
cd13588 |
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
31-318 |
1.08e-59 |
|
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: 194.05 E-value: 1.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMAGSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNWK 110
Cdd:cd13588 1 ELNVLTWPGYADPDWVTAFEEATGCKVVVKFFGSEDEMVAKLRSGGGDYDVVTPSGDALLRLIAAGLVQPIDTSKIPNYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 111 NLDPEvLKLVAKHDPENK-YAMPYLWATTGIGYNVDKVKAvlgkdAPVDSWDLVLKPENLEKlkscgVSFLDAPEEIFAT 189
Cdd:cd13588 81 NIDPR-LRNLPWLTVDGKvYGVPYDWGANGLAYNTKKVKT-----PPTSWLALLWDPKYKGR-----VAARDDPIDAIAD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 190 VLNYLGKDPNSSKADDYTGPATDLLLKLRPNIR-YFHSS-QYINDLANGDICVAIGWAGdvwqAANRAKeaKNGVNVSYF 267
Cdd:cd13588 150 AALYLGQDPPFNLTDEQLDAVKAKLREQRPLVRkYWSDGaELVQLFANGEVVAATAWSG----QVNALQ--KAGKPVAYV 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2276266925 268 IPKEGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDVIAKISDQVFYANGN 318
Cdd:cd13588 224 IPKEGATGWVDTWMILKDAKNPDCAYKWLNYMLSPKVQAAVAEWTGYAPSN 274
|
|
| PBP2_polyamine_RpCGA009 |
cd13589 |
The periplasmic-binding component of an uncharacterized ABC transport system from ... |
49-315 |
1.08e-38 |
|
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: 138.90 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 49 FEKETGIKVVYDVFDSNEVLeGKLMA--GSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNWKNLDPevlklvaKHDPE 126
Cdd:cd13589 23 FEKETGIKVVYDTGTSADRL-AKLQAqaGNPQWDVVDLDDGDAARAIAEGLLEPLDYSKIPNAAKDKA-------PAALK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 127 NKYAMPYLWATTGIGYNVDKVKAvlgkdaPVDSWDLvLKPENLEKLKSCGVSFLDAPEEIFAtVLNYLGKDPNSSKADdy 206
Cdd:cd13589 95 TGYGVGYTLYSTGIAYNTDKFKE------PPTSWWL-ADFWDVGKFPGPRILNTSGLALLEA-ALLADGVDPYPLDVD-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 207 tgPATDLLLKLRPNIRYFHSS--QYINDLANGDICVAIGWAGDVWQAAnrakeaKNGVNVSYFIPKEGALAFFDVFAMPA 284
Cdd:cd13589 165 --RAFAKLKELKPNVVTWWTSgaQLAQLLQSGEVDMAPAWNGRAQALI------DAGAPVAFVWPKEGAILGPDTLAIVK 236
|
250 260 270
....*....|....*....|....*....|.
gi 2276266925 285 DAKNKDEAYQFLNYLMRPDVIAKISDQVFYA 315
Cdd:cd13589 237 GAPNKELAMKFINFALSPEVQAALAEALGYG 267
|
|
| PBP2_polyamine_2 |
cd13587 |
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
31-310 |
3.80e-37 |
|
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: 135.64 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 31 TLHVYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKLMA-GSTGFDLVVPSASFLERQLAAGVFQPLDKSKLpNW 109
Cdd:cd13587 1 TLRILTWAGYAPEDLLEKFENETGIKVQVTTSNNNEEMISKLRAtGGGGFDLAQPSQRIAPNYEEFGLYQPIDESKI-KV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 110 KNLDP---EVLKLVAKHDPEnKYAMPYLWATTGIGYNVDKVKAVLGkDAPVDSWDlvlkPENLEKlkscgVSFldAPEEI 186
Cdd:cd13587 80 AQFPPsllESTKLGTTINGK-RYAVPFDWGTEGLTVNSTKAPDVSG-FSYGDLWA----PEYAGK-----VAY--RLKSP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 187 FATVLNYL---GKDPnSSKADDYTGPAT---------DLLLKLRPNIRYF--HSSQYINDLANGDICVAIGWAGDVWqaa 252
Cdd:cd13587 147 LTGLGLYAdatGEDP-FNRYLDYKDEAKyqkildqvlQFLIERKANVKAYwnNADEALAAFRSGGCVIGQTWDSTGL--- 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2276266925 253 nraKEAKNGVNVSYFIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDVIAKISD 310
Cdd:cd13587 223 ---KLNRENPPIDYGAPKEGALGWIDTFAIPAKAENVDQAYAFINFMLRPEIAAMFTN 277
|
|
| AfuA |
COG1840 |
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
45-314 |
2.78e-23 |
|
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 98.08 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 45 TVANFEKETGIKVVYDVFDSNEVLEgKLMA--GSTGFDLV-VPSASFLERQLAAGVFQPLdksKLPNWKNLDPEVlklva 121
Cdd:COG1840 1 LLEAFEKKTGIKVNVVRGGSGELLA-RLKAegGNPPADVVwSGDADALEQLANEGLLQPY---KSPELDAIPAEF----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 122 kHDPENKYAMPYLWATtGIGYNVDKVKAvlgKDAPvDSWDLVLKPENLEKLKSCGVSFLDAPEEIFATVLNYLGKDPnss 201
Cdd:COG1840 72 -RDPDGYWFGFSVRAR-VIVYNTDLLKE---LGVP-KSWEDLLDPEYKGKIAMADPSSSGTGYLLVAALLQAFGEEK--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 202 kaddytgpATDLLLKLRPNIRYF--HSSQYINDLANGDICVAIGWAGDVwqaanrAKEAKNGVNVSYFIPKEGALAFFDV 279
Cdd:COG1840 143 --------GWEWLKGLAANGARVtgSSSAVAKAVASGEVAIGIVNSYYA------LRAKAKGAPVEVVFPEDGTLVNPSG 208
|
250 260 270
....*....|....*....|....*....|....*
gi 2276266925 280 FAMPADAKNKDEAYQFLNYLMRPDVIAKISDQVFY 314
Cdd:COG1840 209 AAILKGAPNPEAAKLFIDFLLSDEGQELLAEEGYE 243
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
46-335 |
4.96e-23 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 97.09 E-value: 4.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 46 VANFEKETGIKVVYDVFDSNEvLEGKLM----AGSTG-FDLVVPSASFLERQLAAGVFQPLDKskLPNWKNLDPEVLKLV 120
Cdd:pfam13416 3 AKAFEKKTGVTVEVEPQASND-LQAKLLaaaaAGNAPdLDVVWIAADQLATLAEAGLLADLSD--VDNLDDLPDALDAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 121 AKhdpENKYAMPYLW-ATTGIGYNVDKVKAvlgKDAPVDSWDLVLkpENLEKLKSCgVSFLDAPEEIFATVLNYLGKDPN 199
Cdd:pfam13416 80 YD---GKLYGVPYAAsTPTVLYYNKDLLKK---AGEDPKTWDELL--AAAAKLKGK-TGLTDPATGWLLWALLADGVDLT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 200 -SSKADDYTGPATDLLLKLRPNIRYF-HSSQYINDLANGDICVAIGWAGDVwqaanrAKEAKNGVNVSYFIPKEGALAFF 277
Cdd:pfam13416 151 dDGKGVEALDEALAYLKKLKDNGKVYnTGADAVQLFANGEVAMTVNGTWAA------AAAKKAGKKLGAVVPKDGSFLGG 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2276266925 278 DVFAMPADAKNKDE-AYQFLNYLMRPDVIAKISDQVFYANGNKASTPlvSETIRNNPAI 335
Cdd:pfam13416 225 KGLVVPAGAKDPRLaALDFIKFLTSPENQAALAEDTGYIPANKSAAL--SDEVKADPAL 281
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
6-309 |
1.12e-20 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 92.03 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 6 KKWLTGLVTGALMAVSA-------GSLAAEQKTLHVYNWSDYIAP---DTVANFEKET-GIKVVYDVFDSNEVLEgKL-- 72
Cdd:COG1653 2 RRLALALAAALALALAAcggggsgAAAAAGKVTLTVWHTGGGEAAaleALIKEFEAEHpGIKVEVESVPYDDYRT-KLlt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 73 -MAGSTGFDLVVPSASFLERQLAAGVFQPLD---KSKLPNWKNLDPEVLKLVAkhdPENK-YAMPYLWATTGIGYNVDKV 147
Cdd:COG1653 81 aLAAGNAPDVVQVDSGWLAEFAAAGALVPLDdllDDDGLDKDDFLPGALDAGT---YDGKlYGVPFNTDTLGLYYNKDLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 148 KAvLGKDAPvDSWDLVLkpENLEKLKS----CGVSFLDAPEEIFATVLNYLGKDP-NSSKADDYTGPAT----DLLLKLR 218
Cdd:COG1653 158 EK-AGLDPP-KTWDELL--AAAKKLKAkdgvYGFALGGKDGAAWLDLLLSAGGDLyDEDGKPAFDSPEAvealEFLKDLV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 219 ------PNIRYFHSSQYINDLANGDicVAIGWAGDvWQAANrAKEAKNGVNVSYF-IP------KEGALAFFDVFAMPAD 285
Cdd:COG1653 234 kdgyvpPGALGTDWDDARAAFASGK--AAMMINGS-WALGA-LKDAAPDFDVGVApLPggpggkKPASVLGGSGLAIPKG 309
|
330 340
....*....|....*....|....
gi 2276266925 286 AKNKDEAYQFLNYLMRPDVIAKIS 309
Cdd:COG1653 310 SKNPEAAWKFLKFLTSPEAQAKWD 333
|
|
| PBP2_PotD_PotF_like_1 |
cd13661 |
The periplasmic substrate-binding component of an uncharacterized active transport system ... |
129-344 |
3.52e-20 |
|
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: 89.78 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 129 YAMPYLWATTGIGYNVDKVKAvLGKDaPVDSWDLvLKPEnlekLKScGVSFLDAPEEIFATVLNYLGKDPNSSkaddyTG 208
Cdd:cd13661 81 WAVPYRWGTTVIAYRKDKLKK-LGWD-PIDWSDL-WRPE----LAG-RIAMVDSPREVIGLVLKKLGASYNTA-----EV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 209 PATD-----LLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVWQAANRAKeakngvNVSYFIPKEGALAFFDVFAMP 283
Cdd:cd13661 148 PGGRealeeRLAALRRQVKLYSSNNYLQALLLGDVWVAVGWSQDIIPLARRYS------NLAVVIPRSGTSLWADLWVIP 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2276266925 284 ADAKNKDEA-------YQFLNYLMRPDVIAKISDQVFYANG---NKASTPLVSETIR------NNPAIYPPADVFAK 344
Cdd:cd13661 222 AGSDFGGRVrgpspllSQWIDFCLQPARATQFAQLSFGGASpliLDGPSLTPPEATRklkldtNLVLGLPPDEILAK 298
|
|
| SBP_bac_6 |
pfam13343 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
80-340 |
3.42e-15 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 463852 [Multi-domain] Cd Length: 247 Bit Score: 74.32 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 80 DLVVP------SASFLERQLAAGVFQPLDKSKLPNW-KNLDPEVLKlvakhDPENKYAMpYLWATTGIGYNVDKVKavlG 152
Cdd:pfam13343 5 DIILSagdlffDKRFLEKFIEEGLFQPLDSANLPNVpKDFDDEGLR-----DPDGYYTP-YGVGPLVIAYNKERLG---G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 153 KDAPVdSWDLVLKPEnlekLKSCGVSFLDAPEEIFATVLNYLGKDPNSSkaddytgPATDLLLKLRPNIRYFHSSQYIND 232
Cdd:pfam13343 76 RPVPR-SWADLLDPE----YKGKVALPGPNVGDLFNALLLALYKDFGED-------GVRKLARNLKANLHPAQMVKAAGR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 233 LANGD--ICVAIGWAGDVWQAanrakeakNGVNVSYFIPKEGALAFFDVFAMPADakNKDEAYQFLNYLMRPDVIAKISD 310
Cdd:pfam13343 144 LESGEpaVYLMPYFFADILPR--------KKKNVEVVWPEDGALVSPIFMLVKKG--KKELADPLIDFLLSPEVQAILAK 213
|
250 260 270
....*....|....*....|....*....|..
gi 2276266925 311 Q--VFYANGNKAstpLVSETIRNNPAIYPPAD 340
Cdd:pfam13343 214 AglVFPVVLNPA---VDNPLPEGAPFKWLGWD 242
|
|
| PBP2_Fbp_like_1 |
cd13544 |
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ... |
46-315 |
4.11e-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: 71.86 E-value: 4.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 46 VANFEKETGIKVVYdVFDSNEVLEGKLMA--GSTGFDLVV--PSASFLerQLAA-GVFQPLdksKLPNWKNLDPEVlklv 120
Cdd:cd13544 17 LEAFKKDTGIKVEF-VRLSTGEALARLEAekGNPQADVWFggTADAHI--QAKKeGLLEPY---KSPNADKIPAKF---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 121 akHDPENKYAMPYLWaTTGIGYNVDKVKAvLGKDAPvDSWDLVLKPEnlekLK---------SCGVSFLdapeeIFATVL 191
Cdd:cd13544 87 --KDPDGYWTGIYLG-PLGFGVNTDELKE-KGLPVP-KSWEDLLNPE----YKgeivmpnpaSSGTAYT-----FLASLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 192 NYLGKDpnssKADDYtgpatdlLLKLRPNIRYFHSSQY--INDLANGDICVAIGWAGDVwqaanrAKEAKNGVNVSYFIP 269
Cdd:cd13544 153 QLMGED----EAWEY-------LKKLNKNVGQYTKSGSapAKLVASGEAAIGISFLHDA------LKLKEQGYPIKIIFP 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2276266925 270 KEGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDVIAKISDQVFYA 315
Cdd:cd13544 216 KEGTGYEIEAVAIIKGAKNPEAAKAFIDWALSKEAQELLAKVGSYA 261
|
|
| PBP2_Fbp_like_2 |
cd13547 |
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
31-311 |
6.13e-12 |
|
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: 64.94 E-value: 6.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 31 TLHVYNwSDY--IAPDTVANFEKE-TGIKVvyDVFDSNEvleGKLM--------AGSTGFDLV-VPSASFLERQLAAGVF 98
Cdd:cd13547 1 KLVVYT-SMPedLANALVEAFEKKyPGVKV--EVFRAGT---GKLMaklaaeaeAGNPQADVLwVADPPTAEALKKEGLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 99 QPLDksklpnwknlDPEVLKLVAKHDPENKYAMPYLWATTGIGYNVDKVkavlGKDAPVDSWDLvLKPEnleklkscgvs 178
Cdd:cd13547 75 LPYK----------SPEADAIPAPFYDKDGYYYGTRLSAMGIAYNTDKV----PEEAPKSWADL-TKPK----------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 179 fldapeeifatvlnYLGK----DPNsskaddYTGPATDLL--LKLRPNIR--YFH------------SSQYINDLANGDI 238
Cdd:cd13547 129 --------------YKGQivmpDPL------YSGAALDLVaaLADKYGLGweYFEklkengvkveggNGQVLDAVASGER 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2276266925 239 CVAIGwagdVWQAANRAKEAKNGVNVSYfiPKEGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDVIAKISDQ 311
Cdd:cd13547 189 PAGVG----VDYNALRAKEKGSPLEVIY--PEEGTVVIPSPIAILKGSKNPEAAKAFVDFLLSPEGQELVADA 255
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
46-304 |
2.91e-11 |
|
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: 63.59 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 46 VANFEKE-TGIKVVYDVFDSNEV---LEGKLMAGSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPNWKNLDPEVlklva 121
Cdd:pfam01547 14 VKEFEKEhPGIKVEVESVGSGSLaqkLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYLVLGVPKL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 122 khdpenkYAMPYLWATTGIGYNVDKVKAVlgKDAPVDSWDLVLKPenLEKLKSCGVSFLDAP------------EEIFAT 189
Cdd:pfam01547 89 -------YGVPLAAETLGLIYNKDLFKKA--GLDPPKTWDELLEA--AKKLKEKGKSPGGAGggdasgtlgyftLALLAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 190 VLNYLGKDPNSSKADDYTGPATDLLLKLR-----------PNIRYFHSSQYINDLANGDICVAIGWAGDV-------WQA 251
Cdd:pfam01547 158 LGGPLFDKDGGGLDNPEAVDAITYYVDLYakvlllkklknPGVAGADGREALALFEQGKAAMGIVGPWAAlaankvkLKV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2276266925 252 ANRAKEAKNGVNVSYFIPKEGALAFF--DVFAMPADAKNKDEAYQFLNYLMRPDV 304
Cdd:pfam01547 238 AFAAPAPDPKGDVGYAPLPAGKGGKGggYGLAIPKGSKNKEAAKKFLDFLTSPEA 292
|
|
| PBP2_Fe3_thiamine_like |
cd13518 |
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ... |
31-304 |
4.18e-10 |
|
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: 59.62 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 31 TLHVYNWSDYIAPDTVAN-FEKETGIKVVYdVFDSNEVLEGKLMA--GSTGFDLVVPSA-SFLERQLAAGVFQPLDkskl 106
Cdd:cd13518 1 ELVVYTASDRDFAEPVLKaFEEKTGIKVKA-VYDGTGELANRLIAekNNPQADVFWGGEiIALEALKEEGLLEPYT---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 107 PNWKNLDPEVLKlvakhDPENKYaMPYLWATTGIGYNVDKVKavlGKDAPVDSWDLvLKPENLEKLKSCGVSFLDAPEEI 186
Cdd:cd13518 76 PKVIEAIPADYR-----DPDGYW-VGFAARARVFIYNTDKLK---EPDLPKSWDDL-LDPKWKGKIVYPTPLRSGTGLTH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 187 FATVLNYLGKDpnssKADDYtgpatdLLLKLRPNIRYFHSSQYINDL-ANGDICVAIGWAGDVwqaanrAKEAKNGVNVS 265
Cdd:cd13518 146 VAALLQLMGEE----KGGWY------LLKLLANNGKPVAGNSDAYDLvAKGEVAVGLTDTYYA------ARAAAKGEPVE 209
|
250 260 270
....*....|....*....|....*....|....*....
gi 2276266925 266 YFIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDV 304
Cdd:cd13518 210 IVYPDQGALVIPEGVALLKGAPNPEAAKKFIDFLLSPEG 248
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
46-355 |
2.85e-09 |
|
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: 58.19 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 46 VANFEKE-TGIKVVYDVFDSNEVLEgKLM---AGSTGFDLVVPSASFLERQLAAGVFQPLDK--SKLPNWKNLDPEVLKL 119
Cdd:cd13585 20 IDAFEKEnPGVKVEVVPVPYDDYWT-KLTtaaAAGTAPDVFYVDGPWVPEFASNGALLDLDDyiEKDGLDDDFPPGLLDA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 120 VAKhdpENK-YAMPYLWATTGIGYNVDKVKAVLGKDAPVDSWDLVL---KPENLEKLKSCGVSFlDAPEEIFATVLNYL- 194
Cdd:cd13585 99 GTY---DGKlYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLeaaKKLTDKKGGQYGFAL-RGGSGGQTQWYPFLw 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 195 ---GK--DPNSSKADdYTGPAT--------DLLL-KLRPNIRYFHSSQYINDLANGDicVAIGWAGDVWQAANRAKEAKN 260
Cdd:cd13585 175 sngGDllDEDDGKAT-LNSPEAvealqfyvDLYKdGVAPSSATTGGDEAVDLFASGK--VAMMIDGPWALGTLKDSKVKF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 261 GVNVSYF----IPKEGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDVIAKISDQVFYANGNKASTPLVSETIRNNPAIY 336
Cdd:cd13585 252 KWGVAPLpagpGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAASAAAPDAKPALALA 331
|
330
....*....|....*....
gi 2276266925 337 PPADVFAKLFTLKVQDPKI 355
Cdd:cd13585 332 AAADALAAAVPPPVPPPWP 350
|
|
| PBP2_Fbp_like_3 |
cd13549 |
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
37-300 |
3.65e-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: 270267 [Multi-domain] Cd Length: 263 Bit Score: 57.08 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 37 WSDYIApdTVANFEKETGIKVVYDVFDSNEVLeGKLMA--GSTGFDLVVPSASFLERQLAAGVFQPLdksKLPNWKNLdP 114
Cdd:cd13549 11 WADWGT--QLKAFKKRTGIQIPYDNKNSGQAL-AALIAerARPVADVAYYGVAFGIQAVAQGVVQPY---KPAHWDEI-P 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 115 EVLKlvakhDPENKYAMPYlwaTTGIGYNVDkVKAVLGKDAPvDSWDLVLKPENLEKlkscgVSFLDAPEEIFATVLNYL 194
Cdd:cd13549 84 EGLK-----DPDGKWFAIH---SGTLGFIVN-VDALGGKPVP-KSWADLLKPEYKGM-----VGYLDPRSAFVGYVGAVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 195 GKDPNSSKADDYtGPATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDvwqaANRAKEaKNGVNVSYFIPKEGAL 274
Cdd:cd13549 149 VNQAMGGSLDNF-GPGIDYFKKLHKNGPIVPKQTAYARVLSGEIPILIDYDFN----AYRAKY-TDKANVAFVIPKEGSV 222
|
250 260
....*....|....*....|....*.
gi 2276266925 275 AFFDVFAMPADAKNKDEAYQFLNYLM 300
Cdd:cd13549 223 VVPYVMSLVKNAPNPNNGKKVLDFIM 248
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
6-308 |
5.96e-09 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 57.27 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 6 KKWLTGLVTGALMAVS------------AGSLAAEQKTLHVYNWSDYIAP--DTVANFEKETGIKVVYDVFDSNEVLEGK 71
Cdd:COG2182 3 RRLLAALALALALALAlaacgsgssssgSSSAAGAGGTLTVWVDDDEAEAleEAAAAFEEEPGIKVKVVEVPWDDLREKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 72 LMAGSTGF--DLVVPSASFLERQLAAGVFQPLDKSkLPNWKNLDPEVLKLVaKHDPENkYAMPYLWATTGIGYNVDKVKA 149
Cdd:COG2182 83 TTAAPAGKgpDVFVGAHDWLGELAEAGLLAPLDDD-LADKDDFLPAALDAV-TYDGKL-YGVPYAVETLALYYNKDLVKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 150 vlgkDAPVdSWDLVLkpENLEKLKSCGVSFL--DAPEEIFATVL------NYLGKDPNSSKADDYTGPAT----DLLLKL 217
Cdd:COG2182 160 ----EPPK-TWDELI--AAAKKLTAAGKYGLayDAGDAYYFYPFlaafggYLFGKDGDDPKDVGLNSPGAvaalEYLKDL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 218 RPNiRYFHSS----QYINDLANGDICVAIGWAgdvWQAANrAKEAKnGVNVSYF-IPK----EGALAFFDV--FAMPADA 286
Cdd:COG2182 233 IKD-GVLPADadydAADALFAEGKAAMIINGP---WAAAD-LKKAL-GIDYGVApLPTlaggKPAKPFVGVkgFGVSAYS 306
|
330 340
....*....|....*....|..
gi 2276266925 287 KNKDEAYQFLNYLMRPDVIAKI 308
Cdd:COG2182 307 KNKEAAQEFAEYLTSPEAQKAL 328
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
46-367 |
6.83e-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: 57.00 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 46 VANFEKET-GIKVVYDVF---DSNEVLEgKLMAGSTGFDLV-VPSASFLERQLAAGVFQPLDKsKLPNWKNLDPEVLKLV 120
Cdd:cd14749 21 IADFEKENpNIKVKVVVFpydNYKTKLK-TAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPLTD-YLDPNGVDKRFLPGLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 121 AKHDPENK-YAMPYLWATTGIGYNVDKVKAVLGKDAPvDSWDLVLkpENLEKLKS-------CGVSFLDAPEEIFATVLN 192
Cdd:cd14749 99 DAVTFNGKvYGIPFAARALALFYNKDLFEEAGGVKPP-KTWDELI--EAAKKDKFkakgqtgFGLLLGAQGGHWYFQYLV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 193 Y-LGKDPnssKADDYTGPAT--------------DLLLK--LRPNIRYFHSSQYINDLANGDICVAIGwaGDvWQAANrA 255
Cdd:cd14749 176 RqAGGGP---LSDDGSGKATfndpafvqalqklqDLVKAgaFQEGFEGIDYDDAGQAFAQGKAAMNIG--GS-WDLGA-I 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 256 KEAKNGVNVSYF-IP--KEGAL-----AFFDVFAMPADAKNKDEAYQFLNYLMRPDViAKISDQVfyaNGNKASTPLVSE 327
Cdd:cd14749 249 KAGEPGGKIGVFpFPtvGKGAQtstigGSDWAIAISANGKKKEAAVKFLKYLTSPEV-MKQYLED---VGLLPAKEVVAK 324
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2276266925 328 TIRN-NPAIYPPadvFAKLFTLKVQDPKIDRVRTRAWTKVK 367
Cdd:cd14749 325 DEDPdPVAILGP---FADVLNAAGSTPFLDEYWPAAAQVHK 362
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
46-333 |
3.74e-08 |
|
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: 54.61 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 46 VANFEKE-TGIKVVYDVFDSNEVLEGKLMA---GSTGFDLVVPSASFLERQLAAGVFQPLD---KSKLPNWKNLDPEVLK 118
Cdd:cd14748 20 VDEFNKShPDIKVKAVYQGSYDDTLTKLLAalaAGTAPDVAQVDASWVAQLADSGALEPLDdyiDKDGVDDDDFYPAALD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 119 LVAKHDpeNKYAMPYLWATTGIGYNVD--KvKAVLGKDAPVDSWDLV------LKPENLEKLKSCGVSFLDAPEEIFATV 190
Cdd:cd14748 100 AGTYDG--KLYGLPFDTSTPVLYYNKDlfE-EAGLDPEKPPKTWDELeeaakkLKDKGGKTGRYGFALPPGDGGWTFQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 191 LNYLGK---DPNSSKADdYTGPA--------TDLLLKlRPNIRYFHSSQYINDLANGDICVAIGWagdVWQAANrAKEAK 259
Cdd:cd14748 177 LWQNGGdllDEDGGKVT-FNSPEgvealeflVDLVGK-DGVSPLNDWGDAQDAFISGKVAMTING---TWSLAG-IRDKG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 260 NGVNVSY-FIP-----KEGALAFFDVFAMPAD-AKNKDEAYQFLNYLMRPDVIAKISDQVFYANGNKASTPLVSETIRNN 332
Cdd:cd14748 251 AGFEYGVaPLPagkgkKGATPAGGASLVIPKGsSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRKSAAEDPEEFLAEN 330
|
.
gi 2276266925 333 P 333
Cdd:cd14748 331 P 331
|
|
| YnjB |
COG4134 |
ABC-type uncharacterized transport system YnjBCD, periplasmic component [General function ... |
6-313 |
1.57e-05 |
|
ABC-type uncharacterized transport system YnjBCD, periplasmic component [General function prediction only];
Pssm-ID: 443309 [Multi-domain] Cd Length: 401 Bit Score: 46.39 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 6 KKWLTGLVTGALMAVSAGSL-----------AAEQKTLHVYNW------SDYIAPDTVANFEKETGIKVVY-DVFDSNEV 67
Cdd:COG4134 2 RRLALALALLALLLAACSAAlaaadwqaieaEARGQTVYFNAWggdpniNDYIDDWVAPQLKERYGITLEHvKLADTADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 68 LE--------GKLMAGStgFDLVV----PSASFLERQLAAGVFqpldKSKLPNWKNLDPEvlKLVAKHD---PENKYAMP 132
Cdd:COG4134 82 VNrvlaekqaGKDDGGS--VDLIWingeNFAAMKEAGLLFGPF----AEKLPNWAYVDTE--KPTVTTDfgvPVDGYEAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 133 YLWATTGIGYNVDKVKAVlgkdapvdswdlvlkPENLEKLKS-----------------CGVSFLdapEEIFATVLNY-- 193
Cdd:COG4134 154 WGMAQLVFIYDSARVPNP---------------PRSLAELLEwakanpgrftypappdfTGSTFL---KQALYELTGDpd 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 194 -LGKDPNSSKADDYTGPATDLLLKLRPNI----RYFHSS--QYINDLANGDICVAIgwagdVWQAANRAKEAKNGV---N 263
Cdd:COG4134 216 aLQQPVDEAKFAKVTAPLWAYLDELHPYLwrqgKTYPASnaALDQLLADGEIDMAM-----SFNPAEASSAIANGElppT 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2276266925 264 VSYFIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDV-IAKISDQVF 313
Cdd:COG4134 291 VRTFVFDGGTIGNTHFLAIPFNAPNKAGAMVVANFLLSPEAqARKADPAVW 341
|
|
| PBP2_TbpA |
cd13545 |
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ... |
31-309 |
2.12e-04 |
|
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: 42.67 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 31 TLHVY-----NWSDYIAPDTVANFEKETGIKV-VYDVFDSNEVLE-GKLMAGSTGFDLVVP-SASFLERQLAAGVFQPLD 102
Cdd:cd13545 1 TLTVYtydsfVGEWGPGPEVKAEFEKETGCKVeFVKPGDAGELLNrLILEKNNPRADVVLGlDNNLLSRALKEGLFEPYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 103 KsklpnwKNLDPevlKLVAKHDPENKYAMPYLWATTGIGYNVDKVkavlgKDAPVDSWDLvLKPENLEKL-------KSC 175
Cdd:cd13545 81 S------PALDV---VPEVPVFDPEDRLIPYDYGYLAFNYDKKKF-----KEPPLSLEDL-TAPEYKGLIvvqdprtSSP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 176 GVSFLdapeeiFATVlnylgkdpNSSKADDYtgpatdlllklrpniryfhsSQYINDLANGDICVAIGWaGDVWQ----- 250
Cdd:cd13545 146 GLGFL------LWTI--------AVFGEEGY--------------------LEYWKKLKANGVTVTPGW-SEAYGlfttg 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2276266925 251 --------AANRAKEAKNGVNVSY--FIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDVIAKIS 309
Cdd:cd13545 191 eapmvvsyATSPAYHVYYEKDLRYtaVIFPEGHYRQVEGAGILKGAKNPELAKKFVDFLLSPEFQEVIP 259
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
46-303 |
2.20e-04 |
|
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: 42.69 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 46 VANFEKET-GIKVVYDVF---DSNEVLEGKLmAGSTGFDLVvpsasflerQL---------AAGVFQPLDkSKLPNWKNL 112
Cdd:cd14747 20 ADEFEKENpGIEVKVQVLpwgDAHTKITTAA-ASGDGPDVV---------QLgntwvaefaAMGALEDLT-PYLEDLGGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 113 DPEVLKLVAKHDPENK-YAMPYLWATTGIGYNVDKVKAVLGKDAP--VDSWDLVLKPENLEKLKSCGVSF---LDAPEEI 186
Cdd:cd14747 89 KDLFPGLVDTGTVDGKyYGVPWYADTRALFYRTDLLKKAGGDEAPktWDELEAAAKKIKADGPDVSGFAIpgkNDVWHNA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 187 FATVL----NYLGKDPNSSKADD---------YTGPATDLL-LKLRPNiryfHSSQYINDLANGDICVAIGWAGDVWQAA 252
Cdd:cd14747 169 LPFVWgaggDLATKDKWKATLDSpeavaglefYTSLYQKGLsPKSTLE----NSADVEQAFANGKVAMIISGPWEIGAIR 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2276266925 253 NRAKEAKNGVNVSYF--IPKEGALAFF--DVFAMPADAKNKDEAYQFLNYLMRPD 303
Cdd:cd14747 245 EAGPDLAGKWGVAPLpgGPGGGSPSFAggSNLAVFKGSKNKDLAWKFIEFLSSPE 299
|
|
| Lipoprotein_8 |
pfam02030 |
Hypothetical lipoprotein (MG045 family); This family includes hypothetical lipoproteins, the ... |
6-299 |
6.48e-04 |
|
Hypothetical lipoprotein (MG045 family); This family includes hypothetical lipoproteins, the amino terminal part of this protein is related to pfam01547, a family of solute binding proteins. This suggests this family also has a solute binding function.
Pssm-ID: 307931 [Multi-domain] Cd Length: 493 Bit Score: 41.48 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 6 KKWLTGLVTGALMAVSAGSLAAEQKTLHVYNWSDYIAPdtVANFEKETGIKVVYDVFDSNEVLEgKLMAGSTgFDLVVPS 85
Cdd:pfam02030 2 KKQLKYLFIFAGITFSPILTACSSSKFVVANFESYMSP--LLLERAKRKRPLTFLTYPNNEKLI-NGFANNT-YDVAVAS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 86 ASFLERQLAAGVFQPLDKSKLpNWKNLDPEVLKLVAKHDPEN----------------------KYAMPYLWATTGIGYN 143
Cdd:pfam02030 78 AYAVSELAKNGLLKPIDWAKF-NLKKENNQSITVNNIEDAKKlftkqiwaisnaykdgkndellEWMVPYFLQDLVFVYR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 144 VDKVKAVLGKDApvdSWDLVLK-----PENLEKLKscgVSFLDAPEEIF--ATVLNYLGKD------PNSSKADdYTGPA 210
Cdd:pfam02030 157 GEKIPELEKKDV---YWSDVIKaivrhKDRFNKNR---LIAIDDARTIFslANIVQLENKNniidvnPKELKTN-YFLNV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 211 TDLLLKL---RPNIRYF----HSSQYINDLANGDICVAIGWAGDVWQAAN--------RAKEAKNGVNVSYFIPKEGALA 275
Cdd:pfam02030 230 YESFSYLglkLNNLSNMfvnsDSNIVINELAMGRRQGGIVYNGDAVYAALggdlrdeaDENMKPTGDNFHIVQPKDSPVA 309
|
330 340
....*....|....*....|....
gi 2276266925 276 FFDVFAMPADAKNKDEAYQFLNYL 299
Cdd:pfam02030 310 LDFLIINSQQKQFEQAAHEYINEL 333
|
|
| PBP2_BitB |
cd13546 |
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ... |
31-304 |
8.50e-04 |
|
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: 40.70 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 31 TLHVY--NWSDYIAPdTVANFEKETGIKVvydvfdsnevlegKLMAGSTGfDLvvpsasfLERqLAAGVFQPL------- 101
Cdd:cd13546 1 TLVVYspNSEEIIEP-IIKEFEEKPGIKV-------------EVVTGGTG-EL-------LAR-IKAEADNPQadvmwgg 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 102 DKSKLPNWKNL-----DPEVLKL-VAKHDPENKYAmPYLWATTGIGYNVDkvkaVLGKDAPVDSWDLVLKPenleKLKsc 175
Cdd:cd13546 58 GIETLEAYKDLfepyeSPEAAAIpDAYKSPEGLWT-GFSVLPVVLMVNTD----LVKNIGAPKGWKDLLDP----KWK-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 176 gvsfldapeeifatvlnylGK----DPNSSKA---------DDYtGPATDLLLKLRPN--IRYFHSSQYINDLANGDICV 240
Cdd:cd13546 127 -------------------GKiafaDPNKSGSaytilytilKLY-GGAWEYIEKLLDNlgVILSSSSAVYKAVADGEYAV 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2276266925 241 AIGWAgdvwqaANRAKEAKNGVNVSYFIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDV 304
Cdd:cd13546 187 GLTYE------DAAYKYVAGGAPVKIVYPKEGTTAVPDGVAIVKGAKNPENAKKFIDFLLSKEV 244
|
|
| PBP2_Fbp_like_6 |
cd13552 |
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
44-314 |
1.36e-03 |
|
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: 270270 [Multi-domain] Cd Length: 266 Bit Score: 40.13 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 44 DTVAN-FEKETGIKVVYDVFDSNEVLE----------GKLMAGStgfdlvvPSASFLERQlAAGVFQPLDksklPNWKN- 111
Cdd:cd13552 14 EYVEDaFEEKTGVEVEWLNMGSQELLDrvraekenpqADVWWGG-------PSQLFMQLK-EEGLLEPTE----PSWAEk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 112 LDPEVlklvakHDPENKYAMPYLWATTgIGYNVDKVKAvlgKDAPVDsWDLVLKPENLEKLKSCGVSFLDAPEEIFATVL 191
Cdd:cd13552 82 VAAEF------KDADGYWYGTIQTPEV-IMYNTELLSE---EEAPKD-WDDLLDPKWKDKIIIRNPLASGTMRTIFAALI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 192 NYlgkdpnSSKADDYTGPATDLLLKLRPNI-RYFHS-SQYINDLANGDICVAIGWAGDVWQAANrakeaKNGVNVSYFIP 269
Cdd:cd13552 151 QR------ELKGTGSLDAGYAWLKKLDANTkEYAASpTMLYLKIGRGEAAISLWNLNDVLDQRE-----NNKMPFGFIDP 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2276266925 270 KEGALAFFDVFAMPADAKNKDEAYQFLNYLMRPDvIAKISDQVFY 314
Cdd:cd13552 220 ASGAPVITDGIALIKGAPHPEAAKAFYEFVGSAE-IQALLAEKFN 263
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
37-343 |
2.80e-03 |
|
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: 39.20 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 37 WSDYIAPDTVAN-----FEKETGIKVVYdVFDSNEVLEGKLMA---GSTGFDLVVPSASFLERQLAAGVFQPLDKSKLPN 108
Cdd:cd13586 5 WTDEDGELEYLKelaeeFEKKYGIKVEV-VYVDSGDTREKFITagpAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLAVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 109 WKNLDPEVLKLVAKHdpeNKYAMPYLWATTGIGYNVDKVKavlgkdAPVDSWDLVL---KPENLEKLKSCGVSFlDAPEE 185
Cdd:cd13586 84 IKNLPVALAAVTYNG---KLYGVPVSVETIALFYNKDLVP------EPPKTWEELIalaKKFNDKAGGKYGFAY-DQTNP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 186 IFATVL------NYLGKDPnsskaDDYTGPATD---------LLLKLRPNIRYFHSSqyindlANGDICVAIGWAGDV-- 248
Cdd:cd13586 154 YFSYPFlaafggYVFGENG-----GDPTDIGLNnegavkglkFIKDLKKKYKVLPPD------LDYDIADALFKEGKAam 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276266925 249 -----WQAANrAKEAknGVNvsyF----IPK----EGALAFFDV--FAMPADAKNKDEAYQFLNYLMRPDVIAKISDQVF 313
Cdd:cd13586 223 iingpWDLAD-YKDA--GIN---FgvapLPTlpggKQAAPFVGVqgAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTG 296
|
330 340 350
....*....|....*....|....*....|
gi 2276266925 314 YANGNKAStpLVSETIRNNPAIYPPADVFA 343
Cdd:cd13586 297 RIPALKDA--LNDAAVKNDPLVKAFAEQAQ 324
|
|
| |
