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Conserved domains on  [gi|1819641189|ref|WP_165313351|]
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PotD/PotF family extracellular solute-binding protein [Vibrio ziniensis]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 11430824)

ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of one or more from a variety of substrates including polyamines

CATH:  3.40.190.10
Gene Ontology:  GO:0140359|GO:0042626|GO:0055052|GO:0019808|GO:0015846|GO:0042597
PubMed:  26517916|24638992|25750732|11421274|8336670|11741199
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
7-342 2.91e-137

Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];


:

Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 393.51  E-value: 2.91e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189   7 GLVLAATIGSAQVSAEMQTLNVYAWGGYLPETSLKKFEEQEGVTINYSTFENNESMYTKLKLlKGTGYDVVFASAYFIEK 86
Cdd:COG0687    12 AALAAALAGGAPAAAAEGTLNVYNWGGYIDPDVLEPFEKETGIKVVYDTYDSNEEMLAKLRA-GGSGYDVVVPSDYFVAR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  87 MGREGLLAELDHNQIPNMKDALPALLGQAHDPKNKYSLPYIFGVTGMSYNSSVLPEGVTHWAELWDKKYAQQVMLIDDIR 166
Cdd:COG0687    91 LIKAGLLQPLDKSKLPNLANLDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEPPTSWADLWDPEYKGKVALLDDPR 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 167 DVFGMALKLNGYSINTKNEKEIEKAYQSLVALKDNVLLYNSDAPHV--PYVSGEASVGMQWNGNAYQGQADMPELKFVFP 244
Cdd:COG0687   171 EVLGAALLYLGYDPNSTDPADLDAAFELLIELKPNVRAFWSDGAEYiqLLASGEVDLAVGWSGDALALRAEGPPIAYVIP 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 245 KEGSVLWMDNFTIPSGSEHKALAHKFINFMYQADNQAEIVNSLGYASATTTGRALLPEELRNNTTIFPTDEDIANGEFIN 324
Cdd:COG0687   251 KEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAARELLPPELAANPAIYPPEEVLDKLEFWN 330

                         330
                  ....*....|....*...
gi 1819641189 325 DVGPEALAIYEKYWQRLR 342
Cdd:COG0687   331 PLPPENRELYTRRWTEIK 348
 
Name Accession Description Interval E-value
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
7-342 2.91e-137

Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 393.51  E-value: 2.91e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189   7 GLVLAATIGSAQVSAEMQTLNVYAWGGYLPETSLKKFEEQEGVTINYSTFENNESMYTKLKLlKGTGYDVVFASAYFIEK 86
Cdd:COG0687    12 AALAAALAGGAPAAAAEGTLNVYNWGGYIDPDVLEPFEKETGIKVVYDTYDSNEEMLAKLRA-GGSGYDVVVPSDYFVAR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  87 MGREGLLAELDHNQIPNMKDALPALLGQAHDPKNKYSLPYIFGVTGMSYNSSVLPEGVTHWAELWDKKYAQQVMLIDDIR 166
Cdd:COG0687    91 LIKAGLLQPLDKSKLPNLANLDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEPPTSWADLWDPEYKGKVALLDDPR 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 167 DVFGMALKLNGYSINTKNEKEIEKAYQSLVALKDNVLLYNSDAPHV--PYVSGEASVGMQWNGNAYQGQADMPELKFVFP 244
Cdd:COG0687   171 EVLGAALLYLGYDPNSTDPADLDAAFELLIELKPNVRAFWSDGAEYiqLLASGEVDLAVGWSGDALALRAEGPPIAYVIP 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 245 KEGSVLWMDNFTIPSGSEHKALAHKFINFMYQADNQAEIVNSLGYASATTTGRALLPEELRNNTTIFPTDEDIANGEFIN 324
Cdd:COG0687   251 KEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAARELLPPELAANPAIYPPEEVLDKLEFWN 330

                         330
                  ....*....|....*...
gi 1819641189 325 DVGPEALAIYEKYWQRLR 342
Cdd:COG0687   331 PLPPENRELYTRRWTEIK 348
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 25-338 8.45e-133

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: 380.81  E-value: 8.45e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  25 TLNVYAWGGYLPETSLKKFEEQEGVTINYSTFENNESMYTKLKLLKGTGYDVVFASAYFIEKMGREGLLAELDHNQIPNM 104
Cdd:cd13590     1 ELNIYNWSDYIDPEVLKAFEKETGVKVNYDTYDSNEEMLAKLRAGGGSGYDLVVPSDYMVERLIKQGLLEPLDHSKLPNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 105 KDALPALLGQAHDPKNKYSLPYIFGVTGMSYNSSVLPEGVTHWAE-LWDKKYAQQVMLIDDIRDVFGMALKLNGYSINTK 183
Cdd:cd13590    81 KNLDPQFLNPPYDPGNRYSVPYQWGTTGIAYNKDKVKEPPTSWDLdLWDPALKGRIAMLDDAREVLGAALLALGYSPNTT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 184 NEKEIEKAYQSLVALKDNVLLYNSDAPHVPYVSGEASVGMQWNGNAYQGQADMPELKFVFPKEGSVLWMDNFTIPSGSEH 263
Cdd:cd13590   161 DPAELAAAAELLIKQKPNVRAFDSDSYVQDLASGEIWLAQAWSGDALQANRENPNLKFVIPKEGGLLWVDNMAIPKGAPN 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819641189 264 KALAHKFINFMYQADNQAEIVNSLGYASATTTGRALLPEELRNNTTIFPTDEDIANGEFINDVGPEALAIYEKYW 338
Cdd:cd13590   241 PELAHAFINFLLDPEVAAKNAEYIGYATPNKAALELLPPELLDNPALYPPIEPLAKLLTFKDVDGEALELYDRIW 315
potD PRK09501
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed
 9-342 1.80e-105

spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed


Pssm-ID: 181913 [Multi-domain]  Cd Length: 348  Bit Score: 313.01  E-value: 1.80e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189   9 VLAATIGSAQvSAEMQTLNVYAWGGYLPETSLKKFEEQEGVTINYSTFENNESMYTKLKLLKGTGYDVVFASAYFIEKMG 88
Cdd:PRK09501   13 ALALGMSAAH-ADDNNTLYFYNWTEYVPPGLLEQFTKETGIKVIYSTYESNETMYAKLKTYKDGAYDLVVPSTYYVDKMR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  89 REGLLAELDHNQIPNMKDALPALLGQAHDPKNKYSLPYIFGVTGMSYNSSVL-PEGVTHWAELWDKKYAQQVMLIDDIRD 167
Cdd:PRK09501   92 KEGMIQKIDKSKLTNFSNLDPDMLNKPFDPNNDYSIPYIWGATAIGVNSDAIdPKSVTSWADLWKPEYKGSLLLTDDARE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 168 VFGMALKLNGYSINTKNEKEIEKAYQSLVALKDNVLLYNSDAPHVPYVSGEASVGMQWNGNAYQG-QADMPeLKFVFPKE 246
Cdd:PRK09501  172 VFQMALRKLGYSGNTTDPKEIEAAYNELKKLMPNVAAFNSDNPANPYMEGEVNLGMIWNGSAFVArQAGTP-IDVVWPKE 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 247 GSVLWMDNFTIPSGSEHKALAHKFINFMYQADNQAEIVNSLGYASATTTGRALLPEELRNNTTIFPTDEDIANGEFINDV 326
Cdd:PRK09501  251 GGIFWMDSLAIPANAKNKEGALKLINFLLRPDVAKQVAETIGYPTPNLAARKLLSPEVANDKSLYPDAETIKKGEWQNDV 330

                         330
                  ....*....|....*.
gi 1819641189 327 GpEALAIYEKYWQRLR 342
Cdd:PRK09501  331 G-AASSIYEEYYQKLK 345
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 41-307 1.67e-31

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 119.82  E-value: 1.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  41 KKFEEQEGVTINYSTFENNESMyTKLKLL----KGTGYDVVFASAYFIEKMGREGLLAELDHnqIPNMKDALPALLGQAH 116
Cdd:pfam13416   4 KAFEKKTGVTVEVEPQASNDLQ-AKLLAAaaagNAPDLDVVWIAADQLATLAEAGLLADLSD--VDNLDDLPDALDAAGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 117 DPKNkYSLPY-IFGVTGMSYNSSVLPE---GVTHWAELWD--KKYAQQVMLIDDIRDVFGMALKLNGYSIN--TKNEKEI 188
Cdd:pfam13416  81 DGKL-YGVPYaASTPTVLYYNKDLLKKageDPKTWDELLAaaAKLKGKTGLTDPATGWLLWALLADGVDLTddGKGVEAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 189 EKAYQSLVALKDNVLLYNSDA-PHVPYVSGEASVGMQWNGNAYQGQADMPELKFVFPKEGSVLWMDNFTIPSGSEHKAL- 266
Cdd:pfam13416 160 DEALAYLKKLKDNGKVYNTGAdAVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVPKDGSFLGGKGLVVPAGAKDPRLa 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1819641189 267 AHKFINFMYQADNQAEIVNSLGYASATTTgrALLPEELRNN 307
Cdd:pfam13416 240 ALDFIKFLTSPENQAALAEDTGYIPANKS--AALSDEVKAD 278
 
Name Accession Description Interval E-value
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
7-342 2.91e-137

Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 393.51  E-value: 2.91e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189   7 GLVLAATIGSAQVSAEMQTLNVYAWGGYLPETSLKKFEEQEGVTINYSTFENNESMYTKLKLlKGTGYDVVFASAYFIEK 86
Cdd:COG0687    12 AALAAALAGGAPAAAAEGTLNVYNWGGYIDPDVLEPFEKETGIKVVYDTYDSNEEMLAKLRA-GGSGYDVVVPSDYFVAR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  87 MGREGLLAELDHNQIPNMKDALPALLGQAHDPKNKYSLPYIFGVTGMSYNSSVLPEGVTHWAELWDKKYAQQVMLIDDIR 166
Cdd:COG0687    91 LIKAGLLQPLDKSKLPNLANLDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEPPTSWADLWDPEYKGKVALLDDPR 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 167 DVFGMALKLNGYSINTKNEKEIEKAYQSLVALKDNVLLYNSDAPHV--PYVSGEASVGMQWNGNAYQGQADMPELKFVFP 244
Cdd:COG0687   171 EVLGAALLYLGYDPNSTDPADLDAAFELLIELKPNVRAFWSDGAEYiqLLASGEVDLAVGWSGDALALRAEGPPIAYVIP 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 245 KEGSVLWMDNFTIPSGSEHKALAHKFINFMYQADNQAEIVNSLGYASATTTGRALLPEELRNNTTIFPTDEDIANGEFIN 324
Cdd:COG0687   251 KEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAARELLPPELAANPAIYPPEEVLDKLEFWN 330

                         330
                  ....*....|....*...
gi 1819641189 325 DVGPEALAIYEKYWQRLR 342
Cdd:COG0687   331 PLPPENRELYTRRWTEIK 348
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 25-338 8.45e-133

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: 380.81  E-value: 8.45e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  25 TLNVYAWGGYLPETSLKKFEEQEGVTINYSTFENNESMYTKLKLLKGTGYDVVFASAYFIEKMGREGLLAELDHNQIPNM 104
Cdd:cd13590     1 ELNIYNWSDYIDPEVLKAFEKETGVKVNYDTYDSNEEMLAKLRAGGGSGYDLVVPSDYMVERLIKQGLLEPLDHSKLPNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 105 KDALPALLGQAHDPKNKYSLPYIFGVTGMSYNSSVLPEGVTHWAE-LWDKKYAQQVMLIDDIRDVFGMALKLNGYSINTK 183
Cdd:cd13590    81 KNLDPQFLNPPYDPGNRYSVPYQWGTTGIAYNKDKVKEPPTSWDLdLWDPALKGRIAMLDDAREVLGAALLALGYSPNTT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 184 NEKEIEKAYQSLVALKDNVLLYNSDAPHVPYVSGEASVGMQWNGNAYQGQADMPELKFVFPKEGSVLWMDNFTIPSGSEH 263
Cdd:cd13590   161 DPAELAAAAELLIKQKPNVRAFDSDSYVQDLASGEIWLAQAWSGDALQANRENPNLKFVIPKEGGLLWVDNMAIPKGAPN 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819641189 264 KALAHKFINFMYQADNQAEIVNSLGYASATTTGRALLPEELRNNTTIFPTDEDIANGEFINDVGPEALAIYEKYW 338
Cdd:cd13590   241 PELAHAFINFLLDPEVAAKNAEYIGYATPNKAALELLPPELLDNPALYPPIEPLAKLLTFKDVDGEALELYDRIW 315
PBP2_PotD cd13660
The periplasmic substrate-binding component of an active spermidine-preferential transport ...
 25-339 2.56e-109

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: 321.45  E-value: 2.56e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  25 TLNVYAWGGYLPETSLKKFEEQEGVTINYSTFENNESMYTKLKLLKGTGYDVVFASAYFIEKMGREGLLAELDHNQIPNM 104
Cdd:cd13660     1 TLNFYNWSEYVPPELLEQFTKETGIKVILSTYESNETMYAKVKLYKDGAYDLVVPSTYYVDKMRKEGLIQKIDKSKITNF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 105 KDALPALLGQAHDPKNKYSLPYIFGVTGMSYNSSVL-PEGVTHWAELWDKKYAQQVMLIDDIRDVFGMALKLNGYSINTK 183
Cdd:cd13660    81 SNIDPDFLNQPFDPNNDYSIPYIWGATALAVNGDAVdGKSVTSWADLWKPEYKGKLLLTDDAREVFQMALRKLGYSGNTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 184 NEKEIEKAYQSLVALKDNVLLYNSDAPHVPYVSGEASVGMQWNGNAYQGQADMPELKFVFPKEGSVLWMDNFTIPSGSEH 263
Cdd:cd13660   161 DPEEIEAAFEELKKLMPNVAAFDSDNPANPYMEGEVALGMIWNGSAFVARQANKPIHVVWPKEGGIFWMDSFAIPANAKN 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819641189 264 KALAHKFINFMYQADNQAEIVNSLGYASATTTGRALLPEELRNNTTIFPTDEDIANGEFINDVGpEALAIYEKYWQ 339
Cdd:cd13660   241 KEGALKFINFLLRPDVSKQIAETIGYPTPNLKARKLLSPEVANNKIVYPSAETIKNGEFQNDVG-AASLIYEEYYQ 315
potD PRK09501
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed
 9-342 1.80e-105

spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed


Pssm-ID: 181913 [Multi-domain]  Cd Length: 348  Bit Score: 313.01  E-value: 1.80e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189   9 VLAATIGSAQvSAEMQTLNVYAWGGYLPETSLKKFEEQEGVTINYSTFENNESMYTKLKLLKGTGYDVVFASAYFIEKMG 88
Cdd:PRK09501   13 ALALGMSAAH-ADDNNTLYFYNWTEYVPPGLLEQFTKETGIKVIYSTYESNETMYAKLKTYKDGAYDLVVPSTYYVDKMR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  89 REGLLAELDHNQIPNMKDALPALLGQAHDPKNKYSLPYIFGVTGMSYNSSVL-PEGVTHWAELWDKKYAQQVMLIDDIRD 167
Cdd:PRK09501   92 KEGMIQKIDKSKLTNFSNLDPDMLNKPFDPNNDYSIPYIWGATAIGVNSDAIdPKSVTSWADLWKPEYKGSLLLTDDARE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 168 VFGMALKLNGYSINTKNEKEIEKAYQSLVALKDNVLLYNSDAPHVPYVSGEASVGMQWNGNAYQG-QADMPeLKFVFPKE 246
Cdd:PRK09501  172 VFQMALRKLGYSGNTTDPKEIEAAYNELKKLMPNVAAFNSDNPANPYMEGEVNLGMIWNGSAFVArQAGTP-IDVVWPKE 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 247 GSVLWMDNFTIPSGSEHKALAHKFINFMYQADNQAEIVNSLGYASATTTGRALLPEELRNNTTIFPTDEDIANGEFINDV 326
Cdd:PRK09501  251 GGIFWMDSLAIPANAKNKEGALKLINFLLRPDVAKQVAETIGYPTPNLAARKLLSPEVANDKSLYPDAETIKKGEWQNDV 330

                         330
                  ....*....|....*.
gi 1819641189 327 GpEALAIYEKYWQRLR 342
Cdd:PRK09501  331 G-AASSIYEEYYQKLK 345
PBP2_PotD_PotF_like_2 cd13663
The periplasmic substrate-binding component of an uncharacterized active transport system ...
 25-342 7.00e-87

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: 264.54  E-value: 7.00e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  25 TLNVYAWGGYLPETSLKKFEEQEGVTINYSTFENNESMYTKLKLlKGTGYDVVFASAYFIEKMGREGLLAELDHNQIPNM 104
Cdd:cd13663     1 TLKVYNWGEYIDPDLIDDFEKETGIKVNYETFDSNEEMYTKIKT-GGTSYDVIVPSDYMIEKLIKEDLLQPLDYSKLPNV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 105 K---DALPALLGQAHDPKNKYSLPYIFGVTGMSYNSSVLPEGVTHWAE-LWDKKYAQQVMLIDDIRDVFGMALKLNGYSI 180
Cdd:cd13663    80 DkniNIQPDLLNLAFDPINEYSVPYFWGTLGIVYNKTKVSLEELSWWNiLWNKKYKGKILMYDSPRDAFMVALKALGYSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 181 NTKNEKEIEKAYQSLVALKDNVLLYNSDAPHVPYVSGEASVGMQWNGNAYQGQADMPELKFVFPKEGSVLWMDNFTIPSG 260
Cdd:cd13663   160 NTTNPDEIEEAKDWLIKQKPNVKAFVVDEIKDLMINGNADIAVTYSGDAAYAMEENENLDYVIPKEGSNLWFDNWVIPKN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 261 SEHKALAHKFINFMYQADNQAEIVNSLGYASATTTGRALLPEEL--RNNTTIFPTDEDIANGEFINDVGPEALAIYEKYW 338
Cdd:cd13663   240 AKNVDLAYKFINFLLRPDNALKNAEYVGYSTPNAAAEELLPEEEsiKDDKIFYPDEDIYKKCEVFKYLGGDAKKEYNDLW 319


                  ....
gi 1819641189 339 QRLR 342
Cdd:cd13663   320 LEVK 323
PBP2_PotD_PotF_like_3 cd13664
TThe periplasmic substrate-binding component of an uncharacterized active transport system ...
 25-338 4.16e-79

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: 244.19  E-value: 4.16e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  25 TLNVYAWGGYLPETSLKKFEEQEGVTINYSTFENNESMYTKLKLlKGTGYDVVFASAYFIEKMGREGLLAELDHNQIPNM 104
Cdd:cd13664     1 ELNLYNWTDYTSPELLDKFEKETGIKVTLDTYDSNETLLAKLKA-GGQGYDVVVPSDSFVPILIKEGLLEPLDKSQLTNY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 105 KDALPALLGQAHDPKNKYSLPYIFGVTGMSYNSSVLPEGVTHWAELWD--KKYAQQVMLIDDIRDVFGMALKLNGYSINT 182
Cdd:cd13664    80 DNIDPRWRKPDFDPGNEYSIPWQWGTTGFAVDTAVYDGDIDDYSVIFQppEELKGKIAMVDSMNEVVNAAIYYLGGPICT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 183 KNEKEIEKAYQSLVALKDNVLLYNSDAPHVPYVSGEASVGMQWNGNAYQGQADMPELKFVFPKEGSVLWMDNFTIPSGSE 262
Cdd:cd13664   160 TDPKLMRKVRDLLLEQKPHVKAYDSDGIVERMASGDVAAHVDWNGASLRARRQNPSLAYAYPKEGVLIWSDNLVIPKGAP 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819641189 263 HKALAHKFINFMYQADNQAEIVNSLGYASATTTGRALLPEELRNNTTIFPTDEDIANGEFINDVGPEALAIYEKYW 338
Cdd:cd13664   240 NYENARTFLNFIMEPENAALQSNFAGYANAITGAEKFMDDPLKDAPALEIPPPEGSRLKFSTLCPPKAEKLQSRIW 315
PBP2_TpPotD_like cd13662
The periplasmic substrate-binding component of an ABC-type polyamine transport system from ...
 25-338 6.14e-76

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: 236.26  E-value: 6.14e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  25 TLNVYAWGGYLPETSLKKFEEQEGVTINYSTFENNESMYTKLKLlKGTGYDVVFASAYFIEKMGREGLLAELDHNQIPNM 104
Cdd:cd13662     1 VLYIYNWTYYIPDKVIEDFEKETGIRVVYDYYASNEEMYAKLKI-GGGGYDIVSPSGDYVSIMKKEGLLEKLDKSKLPNV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 105 KDALPALLG--QAHDPKNKYSLPYIFGVTGMSYNSSVLPEGVTHWAELWDKKYAQQVMLIDDIRDVFGMALKLNGYSINT 182
Cdd:cd13662    80 KEEKDNLMEasKIYDPGLEYSVPYMFGATGIAVNKKIVKNYFRKWSIFLREDLAGRMTMLDDMREVIGAALAYLGYPVDS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 183 KNEKEIEKAYQSLVALKDNVLLYNSDAPHVPYVSGEASVGMQWNGNAYQGQADMPELKFVF---PKEGSVLWMDNFTIPS 259
Cdd:cd13662   160 KDIEQLEEAKEVILSWKKNLAKFDSNSYGKGFASGDFWVVHGYAEDVFYEVPEEEEEKFDFfipEGAASMMYIDSFVIPK 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819641189 260 GSEHKALAHKFINFMYQADNQAEIVNSLGYASATTTGRALLPEElrnntTIFPTDEDIANGEFINDVGpEALAIYEKYW 338
Cdd:cd13662   240 GSKHKDNAYKFINFILRPENYAEILDVLGNPSIIKEAEKKSQKK-----PIIYAEEDLKNSKLPGDVG-DALELQNKIW 312
PBP2_PotF cd13659
The periplasmic substrate-binding component of an ABC putrescine transport system and related ...
 25-338 2.24e-71

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: 224.90  E-value: 2.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  25 TLNVYAWGGYLPETSLKKFEEQEGVTINYSTFENNESMYTKLkLLKGTGYDVVFASAYFIEKMGREGLLAELDHNQIPNM 104
Cdd:cd13659     1 TLNVYNWSDYIAPDTLEDFEKETGIKVVYDTYDSNEELEAKL-LAGGSGYDLVVPSANFLGRQIKAGALQKLDKSKLPNW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 105 KDALPALLG--QAHDPKNKYSLPYIFGVTGMSYN----SSVLPEG-VTHWAELWDKKYAQQ-----VMLIDDIRDVFGMA 172
Cdd:cd13659    80 KNLDPLLLKllAAVDPGNRYAVPYMWGTTGIAYNvdkvKAALGDDlPDSWDLVFDPENLSKlkscgVSVLDSPEEVFPAA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 173 LKLNGYSINTKNEKEIEKAYQSLVALKDNVLLYNSDAPHVPYVSGEASVGMQWNGNAYQGQA------DMPELKFVFPKE 246
Cdd:cd13659   160 LNYLGLDPNSTDPEDIKAAEDLLKKVRPYVRYFHSSKYINDLANGEICVAIGWSGDAVQAAQrakeagNGVTLEYVIPKE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 247 GSVLWMDNFTIPSGSEHKALAHKFINFMYQADNQAEIVNSLGYASATTTGRALLPEELRNNTTIFPTDEDIANGEFINDV 326
Cdd:cd13659   240 GANLWFDMFAIPADAKNPDNAYRFINYLMRPEVIAKISNYVNYANANKAATPLVDEAIKDDPAIYPPEEVLKKLYALPPL 319

                         330
                  ....*....|..
gi 1819641189 327 GPEALAIYEKYW 338
Cdd:cd13659   320 SAKVQRALTRAW 331
PBP2_polyamines cd13523
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 25-285 2.63e-64

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: 204.59  E-value: 2.63e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  25 TLNVYAWGGYLPETSLKKFEEQEGVTINYSTFENNESMYTKLKLLKGTGYDVVFASAYFIEKMGREGLLAELDHNQIPNM 104
Cdd:cd13523     1 TVVIYTWGGYLPQDIIDPFEKETGIKVVVDTAANSERMIKKLSAGGSGGFDLVTPSDSYTSRQLGVGLMQPIDKSLLPSW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 105 K--DALPALLGQAHDPKNKYSLPYIFGVTGMSYNSS-VLPEGVTHWAELWDKKYAQQVMLIDDIRDVFGMALKLNGYSIN 181
Cdd:cd13523    81 AtlDPHLTLAAVLTVPGKKYGVPYQWGATGLVYNTDkVKAPPKSYAADLDDPKYKGRVSFSDIPRETFAMALANLGADGN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 182 -TKNEKEIEKAYQSLVALKDNVLLYNSDA--PHVPYVSGEASVGMQWNGNAYQGQADMPELKFVFPKEGSVLWMDNFTIP 258
Cdd:cd13523   161 eELYPDFTDAAAALLKELKPNVKKYWSNAsqPANLLLNGEVVLAMAWLGSGFKLKQAGAPIEFVVPKEGAVGWLDTFAVP 240

                         250       260
                  ....*....|....*....|....*..
gi 1819641189 259 SGSEHKALAHKFINFMYQADNQAEIVN 285
Cdd:cd13523   241 ANAPNKDGAYKLLNALLRPKVAAAVAA 267
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 25-298 1.61e-57

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: 187.50  E-value: 1.61e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  25 TLNVYAWGGYLPETSLKKFEEQEGVTINYSTFENNESMYTKLKLLKGtGYDVVFASAYFIEKMGREGLLAELDHNQIPNM 104
Cdd:cd13588     1 ELNVLTWPGYADPDWVTAFEEATGCKVVVKFFGSEDEMVAKLRSGGG-DYDVVTPSGDALLRLIAAGLVQPIDTSKIPNY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 105 KDALPALLGQAHDPKNK--YSLPYIFGVTGMSYNSSVLP-EGVTHWAELWDKKYAQQVMLIDDIRDVFGMALKLNGYSIN 181
Cdd:cd13588    80 ANIDPRLRNLPWLTVDGkvYGVPYDWGANGLAYNTKKVKtPPTSWLALLWDPKYKGRVAARDDPIDAIADAALYLGQDPP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 182 TKN-EKEIEKAYQSLVALKDNVLLYNSDAPHVP--YVSGEASVGMQWNGNAYQGQADMPELKFVFPKEGSVLWMDNFTIP 258
Cdd:cd13588   160 FNLtDEQLDAVKAKLREQRPLVRKYWSDGAELVqlFANGEVVAATAWSGQVNALQKAGKPVAYVIPKEGATGWVDTWMIL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1819641189 259 SGSEHKALAHKFINFMYQADNQAEIVNSLGYASATTTGRA 298
Cdd:cd13588   240 KDAKNPDCAYKWLNYMLSPKVQAAVAEWTGYAPSNPEACA 279
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 25-290 1.07e-51

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: 172.41  E-value: 1.07e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  25 TLNVYAWGGY----LPETSLKKFEEQEGVTINYSTfENNESMYTKLKLLKGT-GYDVVFASAYFIEKMGREGLLAELDHN 99
Cdd:cd13589     1 TLVVATWGGSyedaQRKAVIEPFEKETGIKVVYDT-GTSADRLAKLQAQAGNpQWDVVDLDDGDAARAIAEGLLEPLDYS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 100 QIPNM-KDALPALLgqahdpKNKYSLPYIFGVTGMSYNSSVLPEGVTHWAeLWDKKYAQQV----MLIDDIRDVFGMALK 174
Cdd:cd13589    80 KIPNAaKDKAPAAL------KTGYGVGYTLYSTGIAYNTDKFKEPPTSWW-LADFWDVGKFpgprILNTSGLALLEAALL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 175 LNGYSINTKNekeIEKAYQSLVALKDNVLLYNSDAPHVP--YVSGEASVGMQWNGNAYQGQADMPELKFVFPKEGSVLWM 252
Cdd:cd13589   153 ADGVDPYPLD---VDRAFAKLKELKPNVVTWWTSGAQLAqlLQSGEVDMAPAWNGRAQALIDAGAPVAFVWPKEGAILGP 229

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1819641189 253 DNFTIPSGSEHKALAHKFINFMYQADNQAEIVNSLGYA 290
Cdd:cd13589   230 DTLAIVKGAPNKELAMKFINFALSPEVQAALAEALGYG 267
PRK10682 PRK10682
putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional
 5-313 1.21e-45

putrescine transporter subunit: periplasmic-binding component of ABC superfamily; Provisional


Pssm-ID: 182645 [Multi-domain]  Cd Length: 370  Bit Score: 159.63  E-value: 1.21e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189   5 IKGLVLAATIGSaqVSAEMQTLNVYAWGGYLPETSLKKFEEQEGVTINYSTFENNESMYTKLkLLKGTGYDVVFASAYFI 84
Cdd:PRK10682   13 VAGALMAVSVGT--LAAEQKTLHIYNWSDYIAPDTVANFEKETGIKVVYDVFDSNEVLEGKL-MAGSTGFDLVVPSASFL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  85 EKMGREGLLAELDHNQIPNMKDALPALLG--QAHDPKNKYSLPYIFGVTGMSYN----SSVLPEG--VTHW-----AELW 151
Cdd:PRK10682   90 ERQLTAGVFQPLDKSKLPNWKNLDPELLKlvAKHDPDNKYAMPYMWATTGIGYNvdkvKAVLGEDapVDSWdlvlkPENL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 152 DKKYAQQVMLIDDIRDVFGMALKLNGYSINTKNEKEIEK-AYQSLVALKDNVLLYNSDAPHVPYVSGEASVGMQWNGNAY 230
Cdd:PRK10682  170 EKLKSCGVSFLDAPEEIFATVLNYLGKDPNSTKADDYTGpATDLLLKLRPNIRYFHSSQYINDLANGDICVAIGWAGDVW 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 231 QGQADMPELK------FVFPKEGSVLWMDNFTIPSGSEHKALAHKFINFMYQADNQAEIVNSLGYASATTTGRALLPEEL 304
Cdd:PRK10682  250 QASNRAKEAKngvnvsYSIPKEGALAFFDVFAMPADAKNKDEAYQFLNYLLRPDVIAHISDHVFYANANKAATPLVSAEV 329


                  ....*....
gi 1819641189 305 RNNTTIFPT 313
Cdd:PRK10682  330 RDNPGIYPP 338
PBP2_polyamine_2 cd13587
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 25-292 2.79e-43

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: 151.05  E-value: 2.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  25 TLNVYAWGGYLPETSLKKFEEQEGVTINYSTFENNESMYTKLKLLKGTGYDVVFASAYFIEKMGREGLLAELDHNQI--- 101
Cdd:cd13587     1 TLRILTWAGYAPEDLLEKFENETGIKVQVTTSNNNEEMISKLRATGGGGFDLAQPSQRIAPNYEEFGLYQPIDESKIkva 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 102 ---PNMKDALPalLGQAHDPKnKYSLPYIFGVTGMSYNSSVLP-EGVTHWAELWDKKYAQQV------MLIDDIRDVFGM 171
Cdd:cd13587    81 qfpPSLLESTK--LGTTINGK-RYAVPFDWGTEGLTVNSTKAPdVSGFSYGDLWAPEYAGKVayrlksPLTGLGLYADAT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 172 ALKLNGYSINTKNEKEIEKAY----QSLVALKDNVLLY--NSDAPHVPYVSGEASVGMQWNGNAYQGQADMPELKFVFPK 245
Cdd:cd13587   158 GEDPFNRYLDYKDEAKYQKILdqvlQFLIERKANVKAYwnNADEALAAFRSGGCVIGQTWDSTGLKLNRENPPIDYGAPK 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1819641189 246 EGSVLWMDNFTIPSGSEHKALAHKFINFMYQADNQAEIVNSLGYASA 292
Cdd:cd13587   238 EGALGWIDTFAIPAKAENVDQAYAFINFMLRPEIAAMFTNATGYNTA 284
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 41-307 1.67e-31

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 119.82  E-value: 1.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  41 KKFEEQEGVTINYSTFENNESMyTKLKLL----KGTGYDVVFASAYFIEKMGREGLLAELDHnqIPNMKDALPALLGQAH 116
Cdd:pfam13416   4 KAFEKKTGVTVEVEPQASNDLQ-AKLLAAaaagNAPDLDVVWIAADQLATLAEAGLLADLSD--VDNLDDLPDALDAAGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 117 DPKNkYSLPY-IFGVTGMSYNSSVLPE---GVTHWAELWD--KKYAQQVMLIDDIRDVFGMALKLNGYSIN--TKNEKEI 188
Cdd:pfam13416  81 DGKL-YGVPYaASTPTVLYYNKDLLKKageDPKTWDELLAaaAKLKGKTGLTDPATGWLLWALLADGVDLTddGKGVEAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 189 EKAYQSLVALKDNVLLYNSDA-PHVPYVSGEASVGMQWNGNAYQGQADMPELKFVFPKEGSVLWMDNFTIPSGSEHKAL- 266
Cdd:pfam13416 160 DEALAYLKKLKDNGKVYNTGAdAVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVPKDGSFLGGKGLVVPAGAKDPRLa 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1819641189 267 AHKFINFMYQADNQAEIVNSLGYASATTTgrALLPEELRNN 307
Cdd:pfam13416 240 ALDFIKFLTSPENQAALAEDTGYIPANKS--AALSDEVKAD 278
PBP2_PotD_PotF_like_1 cd13661
The periplasmic substrate-binding component of an uncharacterized active transport system ...
 25-340 8.90e-24

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: 99.41  E-value: 8.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  25 TLNVYAWGGYLPETSLKKFEEQEGVTInystfennesmytKLKLLKGTGYDVVFASayfiekmgregLLAELDHNQIPNM 104
Cdd:cd13661     1 PLQIVALRGSIPPQWLNEFQQSQGKRV-------------KLSLEFRGQLADLFKE-----------LQDWSKNGKATSK 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 105 KDALPAL-------LGQAHDPKNKYSLPYIFGVTGMSYNSSVLPEGV---THWAELWDKKYAQQVMLIDDIRDVFGMALK 174
Cdd:cd13661    57 SAPAADLvtlgdswLGRAIARGQIWAVPYRWGTTVIAYRKDKLKKLGwdpIDWSDLWRPELAGRIAMVDSPREVIGLVLK 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 175 LNGYSINT-KNEKEIEKAYQSLVALKDNVLLYNSDAPHVPYVSGEASVGMQWNGNAYQGQADMPELKFVFPKEGSVLWMD 253
Cdd:cd13661   137 KLGASYNTaEVPGGREALEERLAALRRQVKLYSSNNYLQALLLGDVWVAVGWSQDIIPLARRYSNLAVVIPRSGTSLWAD 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 254 NFTIPSGSEHKA-------LAHKFINFMYQADNQAEIVN-SLGYASA-TTTGRALLPEELR-------NNTTIFPTDEDI 317
Cdd:cd13661   217 LWVIPAGSDFGGrvrgpspLLSQWIDFCLQPARATQFAQlSFGGASPlILDGPSLTPPEATrklkldtNLVLGLPPDEIL 296

                         330       340
                  ....*....|....*....|...
gi 1819641189 318 ANGEFINDVGPEALAIYEKYWQR 340
Cdd:cd13661   297 AKSEFLLPLSEATLAQYRALWQT 319
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 40-321 2.27e-22

ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 95.00  E-value: 2.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  40 LKKFEEQEGVTINYsTFENNESMYTKLKLLKG-TGYDVVFAS-AYFIEKMGREGLLAELDhnqiPNMKDALPAllgQAHD 117
Cdd:COG1840     2 LEAFEKKTGIKVNV-VRGGSGELLARLKAEGGnPPADVVWSGdADALEQLANEGLLQPYK----SPELDAIPA---EFRD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 118 PKNKYSLPYIfGVTGMSYNSSVLPEG--VTHWAELWDKKYAQQVMLIDDIRDVFGMAL-----KLNGYsintknekeiEK 190
Cdd:COG1840    74 PDGYWFGFSV-RARVIVYNTDLLKELgvPKSWEDLLDPEYKGKIAMADPSSSGTGYLLvaallQAFGE----------EK 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 191 AYQSLVALKDNV-LLYNSDAPHVPYV-SGEASVGMQWNGNAYQGQADMPELKFVFPKEGSVLWMDNFTIPSGSEHKALAH 268
Cdd:COG1840   143 GWEWLKGLAANGaRVTGSSSAVAKAVaSGEVAIGIVNSYYALRAKAKGAPVEVVFPEDGTLVNPSGAAILKGAPNPEAAK 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1819641189 269 KFINFMYQADNQaEIVNSLGYASATTTGrALLPEELRNNTTIFPTDEDIANGE 321
Cdd:COG1840   223 LFIDFLLSDEGQ-ELLAEEGYEYPVRPD-VEPPEGLPPLGELKLIDDDDKAAE 273
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-283 2.96e-22

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 95.88  E-value: 2.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189   1 MKTFIKGLVLAATI---------GSAQVSAEMQTLNVYAWGGYLPET---SLKKFEEQ-EGVTINYSTFENNEsMYTKLK 67
Cdd:COG1653     1 MRRLALALAAALALalaacggggSGAAAAAGKVTLTVWHTGGGEAAAleaLIKEFEAEhPGIKVEVESVPYDD-YRTKLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  68 --LLKGTGYDVVFASAYFIEKMGREGLLAELDH---NQIPNMKDALPALLgQAHDPKNK-YSLPYIFGVTGMSYNSSVLP 141
Cdd:COG1653    80 taLAAGNAPDVVQVDSGWLAEFAAAGALVPLDDlldDDGLDKDDFLPGAL-DAGTYDGKlYGVPFNTDTLGLYYNKDLFE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 142 E-GVTH---WAELwdKKYAQQvmlIDDIRDVFGMALKLNGYSI---------------NTK---NEKEIEKAYQSLVALK 199
Cdd:COG1653   159 KaGLDPpktWDEL--LAAAKK---LKAKDGVYGFALGGKDGAAwldlllsaggdlydeDGKpafDSPEAVEALEFLKDLV 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 200 D------NVLLYNSDAPHVPYVSGEAsvGMQWNGNAYQG--QADMPELKF-VFP--------KEGSVLWMDNFTIPSGSE 262
Cdd:COG1653   234 KdgyvppGALGTDWDDARAAFASGKA--AMMINGSWALGalKDAAPDFDVgVAPlpggpggkKPASVLGGSGLAIPKGSK 311

                         330       340
                  ....*....|....*....|.
gi 1819641189 263 HKALAHKFINFMYQADNQAEI 283
Cdd:COG1653   312 NPEAAWKFLKFLTSPEAQAKW 332
SBP_bac_6 pfam13343
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 78-319 8.64e-19

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 463852 [Multi-domain]  Cd Length: 247  Bit Score: 84.33  E-value: 8.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  78 FASAYFIEKMGREGLLAELDHNQIPNMKDALPALlgQAHDPKNKYSlPYIFGVTGMSYNSSVLPEGV--THWAELWDKKY 155
Cdd:pfam13343  14 FFDKRFLEKFIEEGLFQPLDSANLPNVPKDFDDE--GLRDPDGYYT-PYGVGPLVIAYNKERLGGRPvpRSWADLLDPEY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 156 AQQVMLIDDIRDVFGMALKLNGYSinTKNEKEIEKAyqsLVALKDNVLLYNSDAPHVPYVSGEA--SVGMQWNGNAYQGQ 233
Cdd:pfam13343  91 KGKVALPGPNVGDLFNALLLALYK--DFGEDGVRKL---ARNLKANLHPAQMVKAAGRLESGEPavYLMPYFFADILPRK 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 234 ADmpELKFVFPKEGSVLWMDNFTIPSGseHKALAHKFINFMYQADNQAeIVNSLGYASATTTGRALLPEELRNNTTIFPT 313
Cdd:pfam13343 166 KK--NVEVVWPEDGALVSPIFMLVKKG--KKELADPLIDFLLSPEVQA-ILAKAGLVFPVVLNPAVDNPLPEGAPFKWLG 240


                  ....*.
gi 1819641189 314 DEDIAN 319
Cdd:pfam13343 241 WDYIRK 246
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 25-339 1.53e-14

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: 73.98  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  25 TLNVYAWGGYLPETSLKK----FEEQE-GVTINYsTFENNESMYTKLK--LLKGTGYDVVFASAYFIEKMGREGLLAELD 97
Cdd:cd13585     1 TLTFWDWGQPAETAALKKlidaFEKENpGVKVEV-VPVPYDDYWTKLTtaAAAGTAPDVFYVDGPWVPEFASNGALLDLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  98 H--NQIPNMKDALPALLGQAHDPKNKYSLPYIFGVTGMSYNSSVL------PEGVTHWAELWDkkYAQQvmLIDDIRDVF 169
Cdd:cd13585    80 DyiEKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFdkagpgPKPPWTWDELLE--AAKK--LTDKKGGQY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 170 GMALKLNGYSI------------------NTK---NEKEIEKAYQSLVAL-KDNV----LLYNSDAPHVPYVSGEasVGM 223
Cdd:cd13585   156 GFALRGGSGGQtqwypflwsnggdlldedDGKatlNSPEAVEALQFYVDLyKDGVapssATTGGDEAVDLFASGK--VAM 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 224 QWNGNAYQGQADMPELKF-----VFP-----KEGSVLWMDNFTIPSGSEHKALAHKFINFMYQADNQAEIVNSLG--YAS 291
Cdd:cd13585   234 MIDGPWALGTLKDSKVKFkwgvaPLPagpggKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGpaALA 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1819641189 292 ATTTGRALLPEELRNNTTIFPTDEDIANGEFINDVGPEALAIYEKYWQ 339
Cdd:cd13585   314 AAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQ 361
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 40-294 5.24e-13

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: 69.24  E-value: 5.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  40 LKKF-EEQEGVTINYSTFENNESMYTKLK--LLKGTGYDVVFASAYFIEKMGREGLLAELD---HNQIPNMKDALPALLG 113
Cdd:cd14748    20 VDEFnKSHPDIKVKAVYQGSYDDTLTKLLaaLAAGTAPDVAQVDASWVAQLADSGALEPLDdyiDKDGVDDDDFYPAALD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 114 QAHDPKNKYSLPYIFGVTGMSYNSSVL------PEGV-THWAELwdKKYAQQVMLIDDIRDVFGMALKLNGYSI------ 180
Cdd:cd14748   100 AGTYDGKLYGLPFDTSTPVLYYNKDLFeeagldPEKPpKTWDEL--EEAAKKLKDKGGKTGRYGFALPPGDGGWtfqall 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 181 -----------NTK---NEKEIEKAYQSLVAL--KDNVLLYNS-DAPHVPYVSGEasVGMQWNGNAYQGQADMPELKFVF 243
Cdd:cd14748   178 wqnggdlldedGGKvtfNSPEGVEALEFLVDLvgKDGVSPLNDwGDAQDAFISGK--VAMTINGTWSLAGIRDKGAGFEY 255

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819641189 244 ----------PKEGSVLWMDNFTIPSG-SEHKALAHKFINFMYQADNQAEIVNSLGYASATT 294
Cdd:cd14748   256 gvaplpagkgKKGATPAGGASLVIPKGsSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRK 317
PBP2_Fbp_like_2 cd13547
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 75-285 2.44e-11

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: 63.01  E-value: 2.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  75 DVVF-ASAYFIEKMGREGLLAEldhNQIPNMKDALPALlgqahDPKNKYSLPYIFGVTGMSYNS-SVLPEGVTHWAELWD 152
Cdd:cd13547    55 DVLWvADPPTAEALKKEGLLLP---YKSPEADAIPAPF-----YDKDGYYYGTRLSAMGIAYNTdKVPEEAPKSWADLTK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 153 KKYAQQVMLIDDIRDvfGMALKLNGYSINTKNEKE--IEKayqslvaLKDNVLLYNSDAPHV--PYVSGEASVGMQWNGN 228
Cdd:cd13547   127 PKYKGQIVMPDPLYS--GAALDLVAALADKYGLGWeyFEK-------LKENGVKVEGGNGQVldAVASGERPAGVGVDYN 197

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819641189 229 AYQGQADMPELKFVFPKEGSVLwmdnftIPS------GSEHKALAHKFINFMYQADNQAEIVN 285
Cdd:cd13547   198 ALRAKEKGSPLEVIYPEEGTVV------IPSpiailkGSKNPEAAKAFVDFLLSPEGQELVAD 254
PBP2_Fbp_like_1 cd13544
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ...
 25-338 3.99e-11

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: 63.00  E-value: 3.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  25 TLNVYawgGYLPETSLKK----FEEQEGVTINYSTFENNESMyTKLKLLKG-TGYDVVF--ASAYFIEkMGREGLLAELD 97
Cdd:cd13544     1 ELTVY---TSLEEEEAKAileaFKKDTGIKVEFVRLSTGEAL-ARLEAEKGnPQADVWFggTADAHIQ-AKKEGLLEPYK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  98 hnqIPNMKDALPallgQAHDPKNKYSLPYIfGVTGMSYNSSVLPE-GV---THWAELWDKKYAQQVMliddirdvfgMAl 173
Cdd:cd13544    76 ---SPNADKIPA----KFKDPDGYWTGIYL-GPLGFGVNTDELKEkGLpvpKSWEDLLNPEYKGEIV----------MP- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 174 klN------GYS-----INTKNEkeiEKAYQSLVALKDNVLLY--NSDAPHVPYVSGEASVGMQWNGNAYQGQADMPELK 240
Cdd:cd13544   137 --NpassgtAYTflaslIQLMGE---DEAWEYLKKLNKNVGQYtkSGSAPAKLVASGEAAIGISFLHDALKLKEQGYPIK 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 241 FVFPKEGSVLWMDNFTIPSGSEHKALAHKFINFMYQADNQAEIVNSLGYAsatttgrallpeelrnnttiFPTDEDIANG 320
Cdd:cd13544   212 IIFPKEGTGYEIEAVAIIKGAKNPEAAKAFIDWALSKEAQELLAKVGSYA--------------------IPTNPDAKPP 271

                         330
                  ....*....|....*...
gi 1819641189 321 EFINDVGPEALAIYEKYW 338
Cdd:cd13544   272 EIAPDLKKDKLIKYDFEW 289
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 40-281 2.62e-10

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: 60.51  E-value: 2.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  40 LKKFEEQE-GVTINYSTFENNeSMYTKLKLLKGTG---YDVVFASAYFIEKMGREGLLAELDHNQIPNMKDALPALlgqa 115
Cdd:pfam01547  14 VKEFEKEHpGIKVEVESVGSG-SLAQKLTTAIAAGdgpADVFASDNDWIAELAKAGLLLPLDDYVANYLVLGVPKL---- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 116 hdpknkYSLPYIFGVTGMSYNSSVLPE-GVTH---WAEL-----------------------WDKKYAQQVMLIDDIRDV 168
Cdd:pfam01547  89 ------YGVPLAAETLGLIYNKDLFKKaGLDPpktWDELleaakklkekgkspggagggdasGTLGYFTLALLASLGGPL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 169 FGMALKL--NGYSINTKNEKEIEKAYQSLVALKDNVLLYNSDAPHV--PYVSGEASVGMQWNGNAYQGQADMPELKFVFP 244
Cdd:pfam01547 163 FDKDGGGldNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREAlaLFEQGKAAMGIVGPWAALAANKVKLKVAFAAP 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1819641189 245 KE---------------GSVLWMDNFTIPSGSEHKALAHKFINFMYQADNQA 281
Cdd:pfam01547 243 APdpkgdvgyaplpagkGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQA 294
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
 25-288 1.02e-09

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: 58.47  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  25 TLNVYAWGGYLP-ETSLKKFEEQEGVTINYSTFENNEsMYTKLKLLKG-TGYDVVFASAYF-IEKMGREGLLAeldhnqi 101
Cdd:cd13518     1 ELVVYTASDRDFaEPVLKAFEEKTGIKVKAVYDGTGE-LANRLIAEKNnPQADVFWGGEIIaLEALKEEGLLE------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 102 PNMKDALPALLGQAHDPKNKYSlPYIFGVTGMSYNSSVL--PEGVTHWAELWDKKYAQQVMLIDdiRDVFGMALKLNGYS 179
Cdd:cd13518    73 PYTPKVIEAIPADYRDPDGYWV-GFAARARVFIYNTDKLkePDLPKSWDDLLDPKWKGKIVYPT--PLRSGTGLTHVAAL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 180 INTKNEKEIEKAYQSLvaLKDNVLLY--NSDAPHVpYVSGEASVGMQWNGNAYQGQADMPELKFVFPKEGSVLWMDNFTI 257
Cdd:cd13518   150 LQLMGEEKGGWYLLKL--LANNGKPVagNSDAYDL-VAKGEVAVGLTDTYYAARAAAKGEPVEIVYPDQGALVIPEGVAL 226

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1819641189 258 PSGSEHKALAHKFINFMYQADNQAEIVNSLG 288
Cdd:cd13518   227 LKGAPNPEAAKKFIDFLLSPEGQKALAAANA 257
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
7-295 2.82e-08

Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 54.96  E-value: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189   7 GLVLAA------TIGSAQVSAEMQTLNVYAWGGYLP--ETSLKKFEEQEGVTINYSTFENNEsMYTKLKLLK--GTGYDV 76
Cdd:COG2182    16 ALALAAcgsgssSSGSSSAAGAGGTLTVWVDDDEAEalEEAAAAFEEEPGIKVKVVEVPWDD-LREKLTTAApaGKGPDV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  77 VFASAYFIEKMGREGLLAELDhNQIPNMKDALPALLGQA-HDPKNkYSLPYIFGVTGMSYNSSVLPEGV-THWAEL--WD 152
Cdd:COG2182    95 FVGAHDWLGELAEAGLLAPLD-DDLADKDDFLPAALDAVtYDGKL-YGVPYAVETLALYYNKDLVKAEPpKTWDELiaAA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 153 KKYAQQvmliddirDVFGMALKL-NGYSI--------------NTKNEKEI-------EKAYQSLVALKDNVLLYNS--- 207
Cdd:COG2182   173 KKLTAA--------GKYGLAYDAgDAYYFypflaafggylfgkDGDDPKDVglnspgaVAALEYLKDLIKDGVLPADady 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 208 DAPHVPYVSGEASVGMQ--WNGNAYQ-------GQADMPELK-------FVfpkeGSVLWMdnftIPSGSEHKALAHKFI 271
Cdd:COG2182   245 DAADALFAEGKAAMIINgpWAAADLKkalgidyGVAPLPTLAggkpakpFV----GVKGFG----VSAYSKNKEAAQEFA 316

                         330       340
                  ....*....|....*....|....
gi 1819641189 272 NFMYQADNQAEIVNSLGYASATTT 295
Cdd:COG2182   317 EYLTSPEAQKALFEATGRIPANKA 340
PBP2_BitB cd13546
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ...
 115-287 1.36e-07

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: 51.87  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 115 AHDPKNKYsLPYIFGVTGMSYNSSVLPEG--VTHWAELWDKKYAQQVMLIDDIRDVFGMALKLNGYSINTKNEKEIEKAY 192
Cdd:cd13546    84 YKSPEGLW-TGFSVLPVVLMVNTDLVKNIgaPKGWKDLLDPKWKGKIAFADPNKSGSAYTILYTILKLYGGAWEYIEKLL 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 193 QSLValkdnVLLYNSDAPHVPYVSGEASVGMQWNGNAYQGQADMPELKFVFPKEGSVLWMDNFTIPSGSEHKALAHKFIN 272
Cdd:cd13546   163 DNLG-----VILSSSSAVYKAVADGEYAVGLTYEDAAYKYVAGGAPVKIVYPKEGTTAVPDGVAIVKGAKNPENAKKFID 237

                         170
                  ....*....|....*
gi 1819641189 273 FMYQADNQAEIVNSL 287
Cdd:cd13546   238 FLLSKEVQEILVETL 252
PBP2_AEPn_like cd13548
Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member ...
 37-283 3.20e-07

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: 51.41  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  37 ETSLKKFEEQEGVTINYSTFENNESMYTKLKLLKGTGYDVVFASAYFIEKMGREGLLAELDHNQIPNmkdalPAllgQAH 116
Cdd:cd13548    15 RDEFAAFTKATGITVNYVEAGSGEVVERAAKEKSNPQADVLVTLPPFIQQAAQMGLLQPYQSDAAKN-----PA---IIK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 117 DPKNKYSlPYIFGVTGMSYNSSVLPEGVTHWAELWDKKYAQQVMLIDDIRDVFGMALKLNGYSINTKnekeiEKAYQSLV 196
Cdd:cd13548    87 AEDGTYA-PLVNNYFSFIYNSAVLKNAPKTFADLLDPKYKGKIQYSTPGQAGDGMAVLLLTTHLMGS-----DAAFAYLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 197 ALKDNVLLYNSDAPHV-PYVS-GEASVGmqwNGNAYQGQADMPELKFVFPkegsVLWMDN-------FTIP------SGS 261
Cdd:cd13548   161 KLQQNNVGPSASTGKLtALVSkGEISVA---NGDLQMNLAQMEHANPNKK----IFWPAKaggqrstFALPygiglvKGA 233

                         250       260
                  ....*....|....*....|..
gi 1819641189 262 EHKALAHKFINFMYQADNQAEI 283
Cdd:cd13548   234 PNADNGKKLIDFLLSKEAQSKV 255
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 25-292 1.12e-06

The periplasmic-binding component of ABC transport systems specific for maltose and related oligosaccharides; possess type 2 periplasmic binding fold; This family represents the periplasmic binding component of ABC transport systems involved in uptake of oligosaccharides including maltose, trehalose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270240 [Multi-domain]  Cd Length: 368  Bit Score: 49.72  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  25 TLNVYAWGGYLPE----TSLKKFEEQ-EGVTIN--YSTFENNESMYTKLKLlKGTGYDVVFASAYFIEKMGREGLLAELD 97
Cdd:cd13522     1 TITVWHQYDTGENqavnELIAKFEKAyPGITVEvtYQDTEARRQFFSTAAA-GGKGPDVVFGPSDSLGPFAAAGLLAPLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  98 HNQIPNMKDALPALLGQAHDPKNkYSLPYIFGVTGMSYNSSVLPEGV-THWAELwdKKYAQQVMLIDDIRDVF------- 169
Cdd:cd13522    80 EYVSKSGKYAPNTIAAMKLNGKL-YGVPVSVGAHLMYYNKKLVPKNPpKTWQEL--IALAQGLKAKNVWGLVYnqnepyf 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 170 ---------GMALKLNGYSIN-TKNEKEIEKAYQSLVALKDNVLLYNSDAPHVP----YVSGEAsvGMQWNG----NAYQ 231
Cdd:cd13522   157 faawiggfgGQVFKANNGKNNpTLDTPGAVEALQFLVDLKSKYKIMPPETDYSIadalFKAGKA--AMIINGpwdlGDYR 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1819641189 232 -------GQADMP---ELKFVFPKEGSVLWMdnftIPSGSEHKALAHKFINFMYQADNQAEIVNSLGYASA 292
Cdd:cd13522   235 qalkinlGVAPLPtfsGTKHAAPFVGGKGFG----INKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDIPA 301
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 40-310 1.23e-06

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: 49.60  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  40 LKKFEEQEGVTINYsTFENNESMYTKLKLLKGTGY--DVVFASAYFIEKMGREGLLAELDhNQIPNMKDALP-ALLGQAH 116
Cdd:cd13586    19 AEEFEKKYGIKVEV-VYVDSGDTREKFITAGPAGKgpDVFFGPHDWLGELAAAGLLAPIP-EYLAVKIKNLPvALAAVTY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 117 DPKNkYSLPYIFGVTGMSYNSSVLPEGVTHWAEL--WDKKYAQQVmliddiRDVFGMALKL-NGY--------------- 178
Cdd:cd13586    97 NGKL-YGVPVSVETIALFYNKDLVPEPPKTWEELiaLAKKFNDKA------GGKYGFAYDQtNPYfsypflaafggyvfg 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 179 -------SINTKNEKEIeKAYQSLVALKDNV-LLY---NSDAPHVPYVSGEAsvGMQ----WNGNAYQ------GQADMP 237
Cdd:cd13586   170 enggdptDIGLNNEGAV-KGLKFIKDLKKKYkVLPpdlDYDIADALFKEGKA--AMIingpWDLADYKdaginfGVAPLP 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 238 ELK-------FVfpkeGSVLWMdnftIPSGSEHKALAHKFINFMYQADNQAEIVNSLGYASATTtgRALLPEELRNNTTI 310
Cdd:cd13586   247 TLPggkqaapFV----GVQGAF----VSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALK--DALNDAAVKNDPLV 316
PRK15046 PRK15046
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
 7-283 6.76e-06

2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional


Pssm-ID: 237887 [Multi-domain]  Cd Length: 349  Bit Score: 47.37  E-value: 6.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189   7 GLVLAATIGSAQVSAEMQTlnVYAWGGY--LPETSLKKFEEQEGVTINYSTFENNEsMYTKLKLLKG-TGYDVVFASAYF 83
Cdd:PRK15046   20 AAAAFGGGAAPAWAADAVT--VYSADGLedWYQDVFPAFTKATGIKVNYVEAGSGE-VVNRAAKEKSnPQADVLVTLPPF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  84 IEKMGREGLLAeldhNQIPNMKDALPAllgQAHDPKNKYSlPYIFGVTGMSYNSSVLPEGVTHWAELWDKKYAQQVMLID 163
Cdd:PRK15046   97 IQQAAAEGLLQ----PYSSVNAKAVPA---IAKDADGTYA-PFVNNYLSFIYNPKVLKTAPATWADLLDPKFKGKLQYST 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 164 DIRDVFGMALKLNGYSINTKnekeiEKAYQSLVALKDNVLLYNSDAPHV-PYVS-GEASVGmqwNG----NAYQGQADMP 237
Cdd:PRK15046  169 PGQAGDGTAVLLLTFHLMGK-----DKAFDYLAKLQANNVGPSKSTGKLtPLVSkGEIYVA---NGdlqmNLAQAEHGGP 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1819641189 238 ELKFVFPKEGsvlwmD----NFTIP------SGSEHKALAHKFINFMYQADNQAEI 283
Cdd:PRK15046  241 NVKIFFPAKD-----GgersTFALPyviglvKGAPNSENGKKLIDFLLSKEAQTKV 291
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 25-322 7.54e-05

Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270450 [Multi-domain]  Cd Length: 386  Bit Score: 44.23  E-value: 7.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  25 TLNVYAWGGYLPETSLKK----FEEQ-EGVTINYsTFENNESMYTKLK--LLKGTGYDVV---------FASAyfiekmg 88
Cdd:cd14747     1 TLTVWAMGNSAEAELLKEladeFEKEnPGIEVKV-QVLPWGDAHTKITtaAASGDGPDVVqlgntwvaeFAAM------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  89 reGLLAELD--HNQIPNMKDALPALLGQAHDPKNKYSLPYIFGVTGMSYNSSVLPE-GVTHWAELWDKKYAQQVMLIDDI 165
Cdd:cd14747    73 --GALEDLTpyLEDLGGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKaGGDEAPKTWDELEAAAKKIKADG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 166 RDVFGMALKL--------------NGYSINTK-------NEKEIEKA---YQSLVALKDNVLLYNSDAPHVPYVSGEASV 221
Cdd:cd14747   151 PDVSGFAIPGkndvwhnalpfvwgAGGDLATKdkwkatlDSPEAVAGlefYTSLYQKGLSPKSTLENSADVEQAFANGKV 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 222 GM----QWNGNAYQGQADMPELKF-VFP-----KEGSVLWM--DNFTIPSGSEHKALAHKFINFMYQADNQAEIVNSLGY 289
Cdd:cd14747   231 AMiisgPWEIGAIREAGPDLAGKWgVAPlpggpGGGSPSFAggSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGM 310

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1819641189 290 ASATTTgrALLPEELRNNTTIFPTDEDIANGEF 322
Cdd:cd14747   311 LPANTS--AWDDPSLANDPLLAVFAEQLKTGKA 341
PBP2_Fbp_like_5 cd13551
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 178-288 1.78e-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: 270269 [Multi-domain]  Cd Length: 267  Bit Score: 39.31  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 178 YSINTKNEKEIEKAYQSLVALKDNVLLYnsdaphVPYVSGEASVGMQWNGNAYQGQADMP-ELKFVFPKEGSVLWMDNFT 256
Cdd:cd13551   159 YGVSDEGWQVLEDYFANGYPAQEGTDFY------APFADGQVPIGYLWSSGLAGIQKQYGvEFKIVDPEIGVPFVTEQVG 232

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1819641189 257 IPSGSEHKALAHKFINFMYQADNQAEIVNSLG 288
Cdd:cd13551   233 IVKGTKKEAEAKAFIDWFGSAEIQAEFAKKFG 264
Lipoprotein_8 pfam02030
Hypothetical lipoprotein (MG045 family); This family includes hypothetical lipoproteins, the ...
 34-229 5.07e-03

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: 38.40  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189  34 YLPETSLKKFEEQEGVTinYSTFENNESMytkLKLLKGTGYDVVFASAYFIEKMGREGLLAELD------------HNQI 101
Cdd:pfam02030  36 YMSPLLLERAKRKRPLT--FLTYPNNEKL---INGFANNTYDVAVASAYAVSELAKNGLLKPIDwakfnlkkennqSITV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 102 PNMKDA-------LPALLGQAHDPKN----KYSLPYIFGVTGMSYNSSVLPE---GVTHWAELW-------DKKYAQQVM 160
Cdd:pfam02030 111 NNIEDAkklftkqIWAISNAYKDGKNdellEWMVPYFLQDLVFVYRGEKIPElekKDVYWSDVIkaivrhkDRFNKNRLI 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819641189 161 LIDDIRDVFGMALKLNGYSINTK---NEKE--------IEKAYQSLVALKDNV--LLYNSDAPHV--PYVSGEASVGMQW 225
Cdd:pfam02030 191 AIDDARTIFSLANIVQLENKNNIidvNPKElktnyflnVYESFSYLGLKLNNLsnMFVNSDSNIVinELAMGRRQGGIVY 270


                  ....
gi 1819641189 226 NGNA 229
Cdd:pfam02030 271 NGDA 274
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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