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Conserved domains on  [gi|1905088589|ref|WP_188211058|]
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MULTISPECIES: thiamine ABC transporter substrate-binding protein [Neisseria]

Protein Classification

type 2 periplasmic-binding domain-containing protein( domain architecture ID 229383)

type 2 periplasmic-binding protein (PBP2) is typically comprised of two globular subdomains connected by a flexible hinge; it binds its ligand in the cleft between these domains in a manner resembling a Venus flytrap; similar to the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Periplasmic_Binding_Protein_Type_2 super family cl21456
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 20-327 1.07e-142

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically 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 origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. 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. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


The actual alignment was detected with superfamily member TIGR01254:

Pssm-ID: 473866 [Multi-domain]  Cd Length: 304  Bit Score: 405.40  E-value: 1.07e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  20 QTEVRLAAHKSFSLPKGVIARFERENNA----KVSVIQAGNANEMLNKLILSRANPIADAVYGLDNANIGKAREMGVLAD 95
Cdd:TIGR01254   1 QPVVTVYTYDSFAADWGLGPVVEKAFEAdcncKVKFVALEDAGELLNRLRLEGKNPKADVVLGLDNNLLEAASKTGLLAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  96 EQPKSLPVSVG--LPS--VLAVDYGYVTLNYDKKWFAEKklplPKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMANIGS 171
Cdd:TIGR01254  81 SGVALDKVNVPggWNNatFLPFDYGYVAFVYDKNKLQNP----PQSLKELVEPEQDLLVIYQDPRTSSPGLGLLLWMQSV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 172 MGEAGAFKWWAQMRQNGVKVAKGWSEAYYTdfsHNGGAYPLVVGYAASPAAEVYFSKgkysEPPTGNLFLKGGVFRQVEG 251
Cdd:TIGR01254 157 YGEDDAPQAWKQLRKKTVTVTKGWSEAYGT---FLGGEYDLVLSYATSPAYHVLFEK----KDNYAALNFSEGHYLQVEG 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1905088589 252 AAVLKGAKQPELAAKLVQWLQSGEVQRAVSSEMWVYPAVKNTPLPEVFRFAQAPTHTdSPSRADINAKQRGWVGRW 327
Cdd:TIGR01254 230 AARLKGAKQPELADKFVQFLLSPAVQNAIPTGNWMYPVVNGTLLPGFFKLTQQPTTT-APTPAEVTAQRQAWISEW 304
 
Name Accession Description Interval E-value
sfuA TIGR01254
ABC transporter periplasmic binding protein, thiB subfamily; The model describes thiamine ABC ...
 20-327 1.07e-142

ABC transporter periplasmic binding protein, thiB subfamily; The model describes thiamine ABC transporter, periplasmic protein in bacteria and archae. The protein belongs to the larger ABC transport system. It consists of at least three components: the thiamine binding periplasmic protein; an inner membrane permease; an ATP-binding subunit. It has been experimentally demonstrated that the mutants in the various steps in the de novo synthesis of the thiamine and the biologically active form, namely thiamine pyrophosphate can be exogenously supplemented with thiamine, thiamine monophosphate (TMP) or thiamine pyrophosphate (TPP). [Transport and binding proteins, Other]


Pssm-ID: 130321 [Multi-domain]  Cd Length: 304  Bit Score: 405.40  E-value: 1.07e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  20 QTEVRLAAHKSFSLPKGVIARFERENNA----KVSVIQAGNANEMLNKLILSRANPIADAVYGLDNANIGKAREMGVLAD 95
Cdd:TIGR01254   1 QPVVTVYTYDSFAADWGLGPVVEKAFEAdcncKVKFVALEDAGELLNRLRLEGKNPKADVVLGLDNNLLEAASKTGLLAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  96 EQPKSLPVSVG--LPS--VLAVDYGYVTLNYDKKWFAEKklplPKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMANIGS 171
Cdd:TIGR01254  81 SGVALDKVNVPggWNNatFLPFDYGYVAFVYDKNKLQNP----PQSLKELVEPEQDLLVIYQDPRTSSPGLGLLLWMQSV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 172 MGEAGAFKWWAQMRQNGVKVAKGWSEAYYTdfsHNGGAYPLVVGYAASPAAEVYFSKgkysEPPTGNLFLKGGVFRQVEG 251
Cdd:TIGR01254 157 YGEDDAPQAWKQLRKKTVTVTKGWSEAYGT---FLGGEYDLVLSYATSPAYHVLFEK----KDNYAALNFSEGHYLQVEG 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1905088589 252 AAVLKGAKQPELAAKLVQWLQSGEVQRAVSSEMWVYPAVKNTPLPEVFRFAQAPTHTdSPSRADINAKQRGWVGRW 327
Cdd:TIGR01254 230 AARLKGAKQPELADKFVQFLLSPAVQNAIPTGNWMYPVVNGTLLPGFFKLTQQPTTT-APTPAEVTAQRQAWISEW 304
TbpA COG4143
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ...
 1-333 1.05e-126

ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and metabolism];


Pssm-ID: 443315 [Multi-domain]  Cd Length: 343  Bit Score: 366.09  E-value: 1.05e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589   1 MKRKIWLLP-----LLSVSAYM----QAQTEVRLAAHKSF----SLPKGVIARFERENNAKVSVIQAGNANEMLNKLILS 67
Cdd:COG4143     1 MKRRTFLLAaalalALALAGCSgaaaAAKPTLTVYTYDSFasewGPGPWLKAAFEAECGCTLEFVAPGDGGELLNRLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  68 RANPIADAVYGLDNANIGKAREMGVLADEQPKSLP-VSVGL-----PSVLAVDYGYVTLNYDKKWFaekkLPLPKTLQDL 141
Cdd:COG4143    81 GANPKADVVLGLDNNLLARALDTGLFAPHGVDALDaLALPLawdpdDRFVPYDYGYFAFVYDKTKL----LNPPESLEDL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 142 TRPEYKNLLVTPSPATSSPGLSFLMANIGSMGEAGAFKWWAQMRQNGVKVAKGWSEAyYTDFShnGGAYPLVVGYAASPA 221
Cdd:COG4143   157 VDPEYKDKLVVQDPRTSTPGLAFLLWTIAAYGEDGALDYWQKLADNGVTVTKGWSEA-YGLFL--KGEAPMVLSYSTSPA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 222 AEVYFSkgkYSEPPTGNLFLKGGVFRQVEGAAVLKGAKQPELAAKLVQWLQSGEVQRAVSSEMWVYPAVKNTPLPEVF-R 300
Cdd:COG4143   234 YHVIAE---GDKDRYAAALFDEGHYRQVEGAGVLAGAKNPELARKFLDFLLSPEFQAEIPTRNWMYPAVEDVELPEAFdE 310

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1905088589 301 FAQAPTHTDSPSRADINAKQRGWVGRWIKTVLK 333
Cdd:COG4143   311 YAPVPEKPLTFDPDEIAANRDAWIDEWQRAVSG 343
PBP2_TbpA cd13545
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ...
 22-291 1.25e-110

Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding fold superfamily; Thiamin-binding protein TbpA is the periplasmic component of ABC-type transporter in E. coli, while the transmembrane permease and ATPase are ThiP and ThiQ, respectively. Thiamin (vitamin B1) is an essential confactor in all living systems that most prokaryotes, plants, and fungi can synthesized thiamin. However, in vertebrates, thiamine cannot be synthesized and must therefore be obtained through dietary absorption. In addition to thiamin biosynthesis, most organisms can import thiamin using specific transporters. After binding thiamine with high affinity, TbpA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The thiamine-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270263 [Multi-domain]  Cd Length: 269  Bit Score: 322.71  E-value: 1.25e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  22 EVRLAAHKSF----SLPKGVIARFERENNAKVSVIQAGNANEMLNKLILSRANPIADAVYGLDNANIGKAREMGVLADEQ 97
Cdd:cd13545     1 TLTVYTYDSFvgewGPGPEVKAEFEKETGCKVEFVKPGDAGELLNRLILEKNNPRADVVLGLDNNLLSRALKEGLFEPYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  98 PKSL------PVSVGLPSVLAVDYGYVTLNYDKKWFAEKklplPKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMANIGS 171
Cdd:cd13545    81 SPALdvvpevPVFDPEDRLIPYDYGYLAFNYDKKKFKEP----PLSLEDLTAPEYKGLIVVQDPRTSSPGLGFLLWTIAV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 172 MGEAGAFKWWAQMRQNGVKVAKGWSEAYYTDFShngGAYPLVVGYAASPAAEVYFskgKYSEPPTGNLFLKGGvFRQVEG 251
Cdd:cd13545   157 FGEEGYLEYWKKLKANGVTVTPGWSEAYGLFTT---GEAPMVVSYATSPAYHVYY---EKDLRYTAVIFPEGH-YRQVEG 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1905088589 252 AAVLKGAKQPELAAKLVQWLQSGEVQRAVSSEMWVYPAVK 291
Cdd:cd13545   230 AGILKGAKNPELAKKFVDFLLSPEFQEVIPETNWMFPVNK 269
SBP_bac_6 pfam13343
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 70-297 1.39e-19

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


Pssm-ID: 463852 [Multi-domain]  Cd Length: 247  Bit Score: 86.26  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  70 NPIADAVYG-----LDNANIGKAREMGVLADEQPKSLP------VSVGLP----SVLAVDYGYVTLNYDKKWFaeKKLPL 134
Cdd:pfam13343   1 DPLPDIILSagdlfFDKRFLEKFIEEGLFQPLDSANLPnvpkdfDDEGLRdpdgYYTPYGVGPLVIAYNKERL--GGRPV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 135 PKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMANIGSMGEAGAFKWWAQMRQNGVKVakgWSEAYYTDFSHNGGAYPLVV 214
Cdd:pfam13343  79 PRSWADLLDPEYKGKVALPGPNVGDLFNALLLALYKDFGEDGVRKLARNLKANLHPA---QMVKAAGRLESGEPAVYLMP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 215 GYAASPAAEvyfskgkySEPPTGNLFLKGGVFRQVEGAAVLKGAKqpELAAKLVQWLQSGEVQRAVSSEMWVYPAVKNTP 294
Cdd:pfam13343 156 YFFADILPR--------KKKNVEVVWPEDGALVSPIFMLVKKGKK--ELADPLIDFLLSPEVQAILAKAGLVFPVVLNPA 225


                  ...
gi 1905088589 295 LPE 297
Cdd:pfam13343 226 VDN 228
PRK15046 PRK15046
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
 35-331 1.27e-14

2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional


Pssm-ID: 237887 [Multi-domain]  Cd Length: 349  Bit Score: 73.57  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  35 KGVIARFERENNAKVSVIQAGNAnEMLNKLILSRANPIADAVYGLDnANIGKAREMGVLADEQP---KSLPvsvglPSVL 111
Cdd:PRK15046   50 QDVFPAFTKATGIKVNYVEAGSG-EVVNRAAKEKSNPQADVLVTLP-PFIQQAAAEGLLQPYSSvnaKAVP-----AIAK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 112 AVDYGYVTL--NYDKkwFA---EKKLPLPKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMANIGSMGEAGAFKWWAQMRQ 186
Cdd:PRK15046  123 DADGTYAPFvnNYLS--FIynpKVLKTAPATWADLLDPKFKGKLQYSTPGQAGDGTAVLLLTFHLMGKDKAFDYLAKLQA 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 187 N-----------GVKVAKGwsEAY---------YTDFSHNGgayplvvgyaasPAAEVYFSKGKYSEPPTgnlflkggvF 246
Cdd:PRK15046  201 NnvgpskstgklTPLVSKG--EIYvangdlqmnLAQAEHGG------------PNVKIFFPAKDGGERST---------F 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 247 RQVEGAAVLKGAKQPELAAKLVQWLQSGEVQRAVSSEMWVYPAVKNTPLP----EVFRFAQAPTHTDSPSRADINAKQRG 322
Cdd:PRK15046  258 ALPYVIGLVKGAPNSENGKKLIDFLLSKEAQTKVSDMAWGIPVRTDVPPSdkngEAVKAALEGVKLWPPDWDDVMAKLDA 337


                  ....*....
gi 1905088589 323 WVGRWIKTV 331
Cdd:PRK15046  338 DIARWKKAT 346
 
Name Accession Description Interval E-value
sfuA TIGR01254
ABC transporter periplasmic binding protein, thiB subfamily; The model describes thiamine ABC ...
 20-327 1.07e-142

ABC transporter periplasmic binding protein, thiB subfamily; The model describes thiamine ABC transporter, periplasmic protein in bacteria and archae. The protein belongs to the larger ABC transport system. It consists of at least three components: the thiamine binding periplasmic protein; an inner membrane permease; an ATP-binding subunit. It has been experimentally demonstrated that the mutants in the various steps in the de novo synthesis of the thiamine and the biologically active form, namely thiamine pyrophosphate can be exogenously supplemented with thiamine, thiamine monophosphate (TMP) or thiamine pyrophosphate (TPP). [Transport and binding proteins, Other]


Pssm-ID: 130321 [Multi-domain]  Cd Length: 304  Bit Score: 405.40  E-value: 1.07e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  20 QTEVRLAAHKSFSLPKGVIARFERENNA----KVSVIQAGNANEMLNKLILSRANPIADAVYGLDNANIGKAREMGVLAD 95
Cdd:TIGR01254   1 QPVVTVYTYDSFAADWGLGPVVEKAFEAdcncKVKFVALEDAGELLNRLRLEGKNPKADVVLGLDNNLLEAASKTGLLAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  96 EQPKSLPVSVG--LPS--VLAVDYGYVTLNYDKKWFAEKklplPKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMANIGS 171
Cdd:TIGR01254  81 SGVALDKVNVPggWNNatFLPFDYGYVAFVYDKNKLQNP----PQSLKELVEPEQDLLVIYQDPRTSSPGLGLLLWMQSV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 172 MGEAGAFKWWAQMRQNGVKVAKGWSEAYYTdfsHNGGAYPLVVGYAASPAAEVYFSKgkysEPPTGNLFLKGGVFRQVEG 251
Cdd:TIGR01254 157 YGEDDAPQAWKQLRKKTVTVTKGWSEAYGT---FLGGEYDLVLSYATSPAYHVLFEK----KDNYAALNFSEGHYLQVEG 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1905088589 252 AAVLKGAKQPELAAKLVQWLQSGEVQRAVSSEMWVYPAVKNTPLPEVFRFAQAPTHTdSPSRADINAKQRGWVGRW 327
Cdd:TIGR01254 230 AARLKGAKQPELADKFVQFLLSPAVQNAIPTGNWMYPVVNGTLLPGFFKLTQQPTTT-APTPAEVTAQRQAWISEW 304
TbpA COG4143
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ...
 1-333 1.05e-126

ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and metabolism];


Pssm-ID: 443315 [Multi-domain]  Cd Length: 343  Bit Score: 366.09  E-value: 1.05e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589   1 MKRKIWLLP-----LLSVSAYM----QAQTEVRLAAHKSF----SLPKGVIARFERENNAKVSVIQAGNANEMLNKLILS 67
Cdd:COG4143     1 MKRRTFLLAaalalALALAGCSgaaaAAKPTLTVYTYDSFasewGPGPWLKAAFEAECGCTLEFVAPGDGGELLNRLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  68 RANPIADAVYGLDNANIGKAREMGVLADEQPKSLP-VSVGL-----PSVLAVDYGYVTLNYDKKWFaekkLPLPKTLQDL 141
Cdd:COG4143    81 GANPKADVVLGLDNNLLARALDTGLFAPHGVDALDaLALPLawdpdDRFVPYDYGYFAFVYDKTKL----LNPPESLEDL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 142 TRPEYKNLLVTPSPATSSPGLSFLMANIGSMGEAGAFKWWAQMRQNGVKVAKGWSEAyYTDFShnGGAYPLVVGYAASPA 221
Cdd:COG4143   157 VDPEYKDKLVVQDPRTSTPGLAFLLWTIAAYGEDGALDYWQKLADNGVTVTKGWSEA-YGLFL--KGEAPMVLSYSTSPA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 222 AEVYFSkgkYSEPPTGNLFLKGGVFRQVEGAAVLKGAKQPELAAKLVQWLQSGEVQRAVSSEMWVYPAVKNTPLPEVF-R 300
Cdd:COG4143   234 YHVIAE---GDKDRYAAALFDEGHYRQVEGAGVLAGAKNPELARKFLDFLLSPEFQAEIPTRNWMYPAVEDVELPEAFdE 310

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1905088589 301 FAQAPTHTDSPSRADINAKQRGWVGRWIKTVLK 333
Cdd:COG4143   311 YAPVPEKPLTFDPDEIAANRDAWIDEWQRAVSG 343
PBP2_TbpA cd13545
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ...
 22-291 1.25e-110

Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding fold superfamily; Thiamin-binding protein TbpA is the periplasmic component of ABC-type transporter in E. coli, while the transmembrane permease and ATPase are ThiP and ThiQ, respectively. Thiamin (vitamin B1) is an essential confactor in all living systems that most prokaryotes, plants, and fungi can synthesized thiamin. However, in vertebrates, thiamine cannot be synthesized and must therefore be obtained through dietary absorption. In addition to thiamin biosynthesis, most organisms can import thiamin using specific transporters. After binding thiamine with high affinity, TbpA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The thiamine-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270263 [Multi-domain]  Cd Length: 269  Bit Score: 322.71  E-value: 1.25e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  22 EVRLAAHKSF----SLPKGVIARFERENNAKVSVIQAGNANEMLNKLILSRANPIADAVYGLDNANIGKAREMGVLADEQ 97
Cdd:cd13545     1 TLTVYTYDSFvgewGPGPEVKAEFEKETGCKVEFVKPGDAGELLNRLILEKNNPRADVVLGLDNNLLSRALKEGLFEPYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  98 PKSL------PVSVGLPSVLAVDYGYVTLNYDKKWFAEKklplPKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMANIGS 171
Cdd:cd13545    81 SPALdvvpevPVFDPEDRLIPYDYGYLAFNYDKKKFKEP----PLSLEDLTAPEYKGLIVVQDPRTSSPGLGFLLWTIAV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 172 MGEAGAFKWWAQMRQNGVKVAKGWSEAYYTDFShngGAYPLVVGYAASPAAEVYFskgKYSEPPTGNLFLKGGvFRQVEG 251
Cdd:cd13545   157 FGEEGYLEYWKKLKANGVTVTPGWSEAYGLFTT---GEAPMVVSYATSPAYHVYY---EKDLRYTAVIFPEGH-YRQVEG 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1905088589 252 AAVLKGAKQPELAAKLVQWLQSGEVQRAVSSEMWVYPAVK 291
Cdd:cd13545   230 AGILKGAKNPELAKKFVDFLLSPEFQEVIPETNWMFPVNK 269
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
 26-288 1.02e-48

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: 164.01  E-value: 1.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  26 AAHKSFSLPkgVIARFERENNAKVSVIQAGnANEMLNKLILSRANPIADAVYGLDNANIGKAREMGVLAdeqPKSLPVSV 105
Cdd:cd13518     7 ASDRDFAEP--VLKAFEEKTGIKVKAVYDG-TGELANRLIAEKNNPQADVFWGGEIIALEALKEEGLLE---PYTPKVIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 106 GLPSVL--------AVDYGYVTLNYDKKwfAEKKLPLPKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMANIGSMGEAGA 177
Cdd:cd13518    81 AIPADYrdpdgywvGFAARARVFIYNTD--KLKEPDLPKSWDDLLDPKWKGKIVYPTPLRSGTGLTHVAALLQLMGEEKG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 178 FKWWAQMRQNGVKVAKGWSEAYYTDFShngGAYPLVVGYAASPAAEVYfsKGkysePPTGNLFLKGGVFRQVEGAAVLKG 257
Cdd:cd13518   159 GWYLLKLLANNGKPVAGNSDAYDLVAK---GEVAVGLTDTYYAARAAA--KG----EPVEIVYPDQGALVIPEGVALLKG 229

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1905088589 258 AKQPELAAKLVQWLQSGEVQRAVSSEMWVYP 288
Cdd:cd13518   230 APNPEAAKKFIDFLLSPEGQKALAAANAQLP 260
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 37-331 3.22e-37

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 134.68  E-value: 3.22e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  37 VIARFERENNAKVSVIQAGnANEMLNKLILSRANPIADAVYGLDNANIGKAREMGVLADEQPKSLPvsvGLPSVL----- 111
Cdd:COG1840     1 LLEAFEKKTGIKVNVVRGG-SGELLARLKAEGGNPPADVVWSGDADALEQLANEGLLQPYKSPELD---AIPAEFrdpdg 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 112 ---AVDYGYVTLNYDKKWFaeKKLPLPKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMANIGSMGEAGAFKWWAQMRQNG 188
Cdd:COG1840    77 ywfGFSVRARVIVYNTDLL--KELGVPKSWEDLLDPEYKGKIAMADPSSSGTGYLLVAALLQAFGEEKGWEWLKGLAANG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 189 VKVakgwseayytdFSHNGGAYPLV------VGYAASPAAEVYFSKGkysePPTGNLFLKGGVFRQVEGAAVLKGAKQPE 262
Cdd:COG1840   155 ARV-----------TGSSSAVAKAVasgevaIGIVNSYYALRAKAKG----APVEVVFPEDGTLVNPSGAAILKGAPNPE 219

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 263 LAAKLVQWLQSGEVQRAVSSEMWVYPAVKNTPLPEVF-RFAQAPTHTDSpsrADINAKQRGWVGRWIKTV 331
Cdd:COG1840   220 AAKLFIDFLLSDEGQELLAEEGYEYPVRPDVEPPEGLpPLGELKLIDDD---DKAAENREELLELWDEAV 286
PBP2_Fbp_like_1 cd13544
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ...
 37-299 4.96e-24

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: 99.60  E-value: 4.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  37 VIARFERENNAKVSVIQAGnANEMLNKLILSRANPIADAVYGLDNANIGKAREMGVLA---------------DEQPKSL 101
Cdd:cd13544    16 ILEAFKKDTGIKVEFVRLS-TGEALARLEAEKGNPQADVWFGGTADAHIQAKKEGLLEpykspnadkipakfkDPDGYWT 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 102 PVSVGlpsVLAVdygyvtlNYDKKWFAEKKLPLPKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMANIGSMGEAGAFKWW 181
Cdd:cd13544    95 GIYLG---PLGF-------GVNTDELKEKGLPVPKSWEDLLNPEYKGEIVMPNPASSGTAYTFLASLIQLMGEDEAWEYL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 182 AQMRQNgVkvakgwseAYYTdfsHNGGAYPLVVG---YAASPAAEVYFSKGKYSEPPTGNLFLKGGVFRQVEGAAVLKGA 258
Cdd:cd13544   165 KKLNKN-V--------GQYT---KSGSAPAKLVAsgeAAIGISFLHDALKLKEQGYPIKIIFPKEGTGYEIEAVAIIKGA 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1905088589 259 KQPELAAKLVQWLQSGEVQ---RAVSSemWVYPAVKNTPLPEVF 299
Cdd:cd13544   233 KNPEAAKAFIDWALSKEAQellAKVGS--YAIPTNPDAKPPEIA 274
SBP_bac_6 pfam13343
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 70-297 1.39e-19

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


Pssm-ID: 463852 [Multi-domain]  Cd Length: 247  Bit Score: 86.26  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  70 NPIADAVYG-----LDNANIGKAREMGVLADEQPKSLP------VSVGLP----SVLAVDYGYVTLNYDKKWFaeKKLPL 134
Cdd:pfam13343   1 DPLPDIILSagdlfFDKRFLEKFIEEGLFQPLDSANLPnvpkdfDDEGLRdpdgYYTPYGVGPLVIAYNKERL--GGRPV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 135 PKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMANIGSMGEAGAFKWWAQMRQNGVKVakgWSEAYYTDFSHNGGAYPLVV 214
Cdd:pfam13343  79 PRSWADLLDPEYKGKVALPGPNVGDLFNALLLALYKDFGEDGVRKLARNLKANLHPA---QMVKAAGRLESGEPAVYLMP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 215 GYAASPAAEvyfskgkySEPPTGNLFLKGGVFRQVEGAAVLKGAKqpELAAKLVQWLQSGEVQRAVSSEMWVYPAVKNTP 294
Cdd:pfam13343 156 YFFADILPR--------KKKNVEVVWPEDGALVSPIFMLVKKGKK--ELADPLIDFLLSPEVQAILAKAGLVFPVVLNPA 225


                  ...
gi 1905088589 295 LPE 297
Cdd:pfam13343 226 VDN 228
PBP2_BitB cd13546
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ...
 37-284 1.50e-19

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: 86.54  E-value: 1.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  37 VIARFERENNAKVSVIQAGnANEMLNKLILSRANPIADAVYGLDNANIGKAREM-----GVLADEQPKSL--------PV 103
Cdd:cd13546    16 IIKEFEEKPGIKVEVVTGG-TGELLARIKAEADNPQADVMWGGGIETLEAYKDLfepyeSPEAAAIPDAYkspeglwtGF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 104 SVgLPSVLAVdygyvtlNYDkkwfAEKKLPLPKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMANIGSMGEAGAFkwWAQ 183
Cdd:cd13546    95 SV-LPVVLMV-------NTD----LVKNIGAPKGWKDLLDPKWKGKIAFADPNKSGSAYTILYTILKLYGGAWEY--IEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 184 MRQNGVKVAKGWSEAYYtdfSHNGGAYPLVVGYAAspAAEVYFSKGKysepPTGNLFLKGGVFRQVEGAAVLKGAKQPEL 263
Cdd:cd13546   161 LLDNLGVILSSSSAVYK---AVADGEYAVGLTYED--AAYKYVAGGA----PVKIVYPKEGTTAVPDGVAIVKGAKNPEN 231

                         250       260
                  ....*....|....*....|.
gi 1905088589 264 AAKLVQWLQSGEVQRAVSSEM 284
Cdd:cd13546   232 AKKFIDFLLSKEVQEILVETL 252
PBP2_AEPn_like cd13548
Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member ...
 32-331 9.60e-19

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: 85.31  E-value: 9.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  32 SLPKGVIARFERENNAKVSVIQAGNAnEMLNKLILSRANPIADAVYGLDnANIGKAREMGVLADEQPKSLPVSVGLPsvl 111
Cdd:cd13548    12 SWYRDEFAAFTKATGITVNYVEAGSG-EVVERAAKEKSNPQADVLVTLP-PFIQQAAQMGLLQPYQSDAAKNPAIIK--- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 112 AVDYGYVTL--NYDKKWFAEKKLP-LPKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMANIGSMGEAGAFKWWAQMRQN- 187
Cdd:cd13548    87 AEDGTYAPLvnNYFSFIYNSAVLKnAPKTFADLLDPKYKGKIQYSTPGQAGDGMAVLLLTTHLMGSDAAFAYLAKLQQNn 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 188 ----------GVKVAKGWSEAYYTDFSHNggaypLVVGYAASPAAEVYFSKGKYSEPPTgnlflkggvFRQVEGAAVLKG 257
Cdd:cd13548   167 vgpsastgklTALVSKGEISVANGDLQMN-----LAQMEHANPNKKIFWPAKAGGQRST---------FALPYGIGLVKG 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1905088589 258 AKQPELAAKLVQWLQSGEVQRAVSSEMWVYPAVKNTPLP----EVFRFAQAPTHTDSPSRADINAKQRGWVGRWIKTV 331
Cdd:cd13548   233 APNADNGKKLIDFLLSKEAQSKVPDMAWGMPVRTDVTPSgkngEAAKAAIAGVKIWPPNWDQVLSKLPADIKRWKKAT 310
PBP2_Fbp_like_2 cd13547
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 32-288 6.73e-18

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: 81.89  E-value: 6.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  32 SLPKGVIAR----FEREN-NAKVSVIQAGnANEMLNKLI--LSRANPIADAVYGLDNANIGKAREMGVLADEQPkslpvs 104
Cdd:cd13547     7 SMPEDLANAlveaFEKKYpGVKVEVFRAG-TGKLMAKLAaeAEAGNPQADVLWVADPPTAEALKKEGLLLPYKS------ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 105 vglPSVLAVDYGYVtlNYDKKWFAEK-------------KLPLPKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMANIGS 171
Cdd:cd13547    80 ---PEADAIPAPFY--DKDGYYYGTRlsamgiayntdkvPEEAPKSWADLTKPKYKGQIVMPDPLYSGAALDLVAALADK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 172 MGEagAFKWWAQMRQNGVKVAKGWSEAyytdfsHNG---GAYPLVVGyaaspaAEVYFSKGKYSEPPTGNLFLKGGVFRQ 248
Cdd:cd13547   155 YGL--GWEYFEKLKENGVKVEGGNGQV------LDAvasGERPAGVG------VDYNALRAKEKGSPLEVIYPEEGTVVI 220

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1905088589 249 VEGAAVLKGAKQPELAAKLVQWLQSGEVQRAVsSEMWVYP 288
Cdd:cd13547   221 PSPIAILKGSKNPEAAKAFVDFLLSPEGQELV-ADAGLLP 259
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-292 6.74e-17

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 80.34  E-value: 6.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589   1 MKRKIWL--------LPLLSVSAYMQAQTEVRLAAHkSFSLPKGVIARFERENNAKVSVIQAGNANEMLNKLILSraNPI 72
Cdd:COG0687     1 MSRRSLLglaaaalaAALAGGAPAAAAEGTLNVYNW-GGYIDPDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAG--GSG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  73 ADaVYGLDNANIGKAREMGVLA-------------DEQPKSLPVSVGLPSVLAVDYGYVTLNYDKKWFAEKklplPKTLQ 139
Cdd:COG0687    78 YD-VVVPSDYFVARLIKAGLLQpldksklpnlanlDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEP----PTSWA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 140 DLTRPEYKNLLVTPSPATSSPGLSFLMA--NIGSMGEAG---AFKWWAQMRQNgvkVAKGWS--EAYYTDFShNGGAypl 212
Cdd:COG0687   153 DLWDPEYKGKVALLDDPREVLGAALLYLgyDPNSTDPADldaAFELLIELKPN---VRAFWSdgAEYIQLLA-SGEV--- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 213 VVGYAASPAAEVYFSKGkysePPTGNLFLKGGVFRQVEGAAVLKGAKQPELAAKLVQWLQSGEVQRAVSSEMWVYPAVKN 292
Cdd:COG0687   226 DLAVGWSGDALALRAEG----PPIAYVIPKEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKA 301
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 35-288 1.25e-16

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: 78.42  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  35 KGVIARFERENNAKVsVIQAGNANEMLNKLILSRANPIADAVYgLDNANIGKAREMGVLADEQPKSLPVS--VGLPSVLA 112
Cdd:cd13589    17 KAVIEPFEKETGIKV-VYDTGTSADRLAKLQAQAGNPQWDVVD-LDDGDAARAIAEGLLEPLDYSKIPNAakDKAPAALK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 113 VDYG------YVTLNYDKKWFAEkklplPKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMANI---GSMGEAG---AFKW 180
Cdd:cd13589    95 TGYGvgytlySTGIAYNTDKFKE-----PPTSWWLADFWDVGKFPGPRILNTSGLALLEAALLadgVDPYPLDvdrAFAK 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 181 WAQMRQNGVKVAKGWSEAYyTDFShNGGAyplVVGYAASPAAEVYFSKGkysePPTGNLFLKGGVFRQVEGAAVLKGAKQ 260
Cdd:cd13589   170 LKELKPNVVTWWTSGAQLA-QLLQ-SGEV---DMAPAWNGRAQALIDAG----APVAFVWPKEGAILGPDTLAIVKGAPN 240

                         250       260
                  ....*....|....*....|....*...
gi 1905088589 261 PELAAKLVQWLQSGEVQRAVSSEMWVYP 288
Cdd:cd13589   241 KELAMKFINFALSPEVQAALAEALGYGP 268
PRK15046 PRK15046
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
 35-331 1.27e-14

2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional


Pssm-ID: 237887 [Multi-domain]  Cd Length: 349  Bit Score: 73.57  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  35 KGVIARFERENNAKVSVIQAGNAnEMLNKLILSRANPIADAVYGLDnANIGKAREMGVLADEQP---KSLPvsvglPSVL 111
Cdd:PRK15046   50 QDVFPAFTKATGIKVNYVEAGSG-EVVNRAAKEKSNPQADVLVTLP-PFIQQAAAEGLLQPYSSvnaKAVP-----AIAK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 112 AVDYGYVTL--NYDKkwFA---EKKLPLPKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMANIGSMGEAGAFKWWAQMRQ 186
Cdd:PRK15046  123 DADGTYAPFvnNYLS--FIynpKVLKTAPATWADLLDPKFKGKLQYSTPGQAGDGTAVLLLTFHLMGKDKAFDYLAKLQA 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 187 N-----------GVKVAKGwsEAY---------YTDFSHNGgayplvvgyaasPAAEVYFSKGKYSEPPTgnlflkggvF 246
Cdd:PRK15046  201 NnvgpskstgklTPLVSKG--EIYvangdlqmnLAQAEHGG------------PNVKIFFPAKDGGERST---------F 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 247 RQVEGAAVLKGAKQPELAAKLVQWLQSGEVQRAVSSEMWVYPAVKNTPLP----EVFRFAQAPTHTDSPSRADINAKQRG 322
Cdd:PRK15046  258 ALPYVIGLVKGAPNSENGKKLIDFLLSKEAQTKVSDMAWGIPVRTDVPPSdkngEAVKAALEGVKLWPPDWDDVMAKLDA 337


                  ....*....
gi 1905088589 323 WVGRWIKTV 331
Cdd:PRK15046  338 DIARWKKAT 346
PBP2_Fbp cd13543
Substrate binding domain of ferric iron transporter, a member of the type 2 periplasmic ...
 32-297 5.07e-14

Substrate binding domain of 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 protein (Fbp) has high affinities 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: 270261 [Multi-domain]  Cd Length: 306  Bit Score: 71.57  E-value: 5.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  32 SLPKGVIARFERENNAKVSVIQAGNAnEMLNKLILSRANPIADAVYGLDNANIGKAREMGVLAD------EQPKSLPVS- 104
Cdd:cd13543    11 SLVDPLVEAFEQETGIKVELRYGDTA-ELANQLVEEGDASPADVFYAEDAGALGALADAGLLAPlpedtlTQVPPRFRSp 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 105 ----VGLPSVLAVdygyvtLNYDKKWFAEKklPLPKTLQDLTRPEYKNLL-VTPspaTSSPGLSFLMANIGSMGEAGAFK 179
Cdd:cd13543    90 dgdwVGVSGRARV------VVYNTDKLSED--DLPKSVLDLAKPEWKGRVgWAP---TNGSFQAFVTAMRVLEGEEATRE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 180 WWAQMRQNGVKVAKGWS---EA-------------YYTDFSHNGGAyplvvgyAASPAAEVYFSKGKyseppTGNLFLkg 243
Cdd:cd13543   159 WLKGLKANGPKAYAKNSavvEAvnrgevdaglinhYYWFRLRAEQG-------EDAPVALHYFKNGD-----PGALVN-- 224

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1905088589 244 gvfrqVEGAAVLKGAKQPELAAKLVQWLQSGEVQRAVSSEMWVYPAVKNTPLPE 297
Cdd:cd13543   225 -----VSGAGVLKTSKNQAEAQKFLAFLLSKEGQEFLATANFEYPLVAGVASPP 273
PBP2_Fbp_like_4 cd13550
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 37-288 8.28e-14

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: 270268 [Multi-domain]  Cd Length: 265  Bit Score: 70.25  E-value: 8.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  37 VIARFERENNAKVsVIQAGNANEMLNKLILSRANPIADAVYGLDNANIGKAREMGVLADEQPKSlPVSVGLPSvLAVDYG 116
Cdd:cd13550    16 VLEKFRADTGVEV-ALKHGSNSAIANQLIEEQSNPQADVFISNDVGALGKLSENGVLQPYTPAG-PELIPADG-RAEDNT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 117 YVTLN-------YDKKWFAEKKLPlpKTLQDLTRPEYKNLLVTPSPATSSpglsfLMANIGSM----GEAGAFKWWAQMR 185
Cdd:cd13550    93 WVALTararvimYNKDLIPEEELP--KSIEDLTDPKWKGQVAAANSTNGS-----MQGQVSAMrqllGDEKTEEWIKGLM 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 186 QNGVKVAKGwseayYTDFSHNGGA----YPLVVGYaaspaaevYFSKGKYSEPPTGNLFL-----KGGVFRQVEGAAVLK 256
Cdd:cd13550   166 ANEVTFLGG-----HTDVRKAVGAgefkLGLVNHY--------YYHLQLAEGSPVGVIYPdqgegQMGVVTNAAGVGLVK 232

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1905088589 257 GAKQPELAAKLVQWLQSGEVQRAVSSEMWVYP 288
Cdd:cd13550   233 GGPNPTNAQAFLDFLLLPENQRIFAEENYEYP 264
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 37-299 6.23e-13

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 67.82  E-value: 6.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  37 VIARFERENNAKVSVIQAGnANEMLNKLILSRA--NPIADAVYGLDNANIGKAREMGVLAD--------EQPKSLPVSVG 106
Cdd:pfam13416   2 LAKAFEKKTGVTVEVEPQA-SNDLQAKLLAAAAagNAPDLDVVWIAADQLATLAEAGLLADlsdvdnldDLPDALDAAGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 107 LPSVLAVDYGYVT---LNYDKKWFAEKKLPlPKTLQDLT--RPEYKNLLVTPSPATSSpGLSFLMANIGSMGEAG----- 176
Cdd:pfam13416  81 DGKLYGVPYAASTptvLYYNKDLLKKAGED-PKTWDELLaaAAKLKGKTGLTDPATGW-LLWALLADGVDLTDDGkgvea 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 177 ---AFKWWAQMRQNGvKVAKGWSEAyyTDFSHNGgaypLVVGYAASPAAEVYFSKGKysePPTGNLFLKGGVFRQVEGAA 253
Cdd:pfam13416 159 ldeALAYLKKLKDNG-KVYNTGADA--VQLFANG----EVAMTVNGTWAAAAAKKAG---KKLGAVVPKDGSFLGGKGLV 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1905088589 254 VLKGAKQPELAA-KLVQWLQSGEVQRAVSSEMWVYPAVKNTPLPEVF 299
Cdd:pfam13416 229 VPAGAKDPRLAAlDFIKFLTSPENQAALAEDTGYIPANKSAALSDEV 275
PBP2_FutA1_ilke cd13542
Substrate binding domain of ferric iron-binding protein, a member of the type 2 periplasmic ...
 22-298 1.20e-12

Substrate binding domain of ferric iron-binding protein, a member of the type 2 periplasmic binding fold superfamily; FutA1 is the periplasmic component of an ABC-type iron transporter and serves as the primary receptor in Synerchosystis species. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria and is critical for survival of these pathogens within the host. After binding iron with high affinity, FutA1 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: 270260 [Multi-domain]  Cd Length: 314  Bit Score: 67.36  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  22 EVRLAAHKSFSLPKGVIARFERENNAKVSVIQAgNANEMLNKLILSRANPIADAVYGLDNANIGKAREMGVLADEQPKSL 101
Cdd:cd13542     1 EVNVYSSRHYNTDKPLYKAFEKETGIKVNVVFA-SADELLERLKAEGANSPADVLLTVDAGRLWEAKEAGLLQPVTSEKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 102 PVSVglPSVLAVDygyvtlnyDKKWFA------------EKKLPLP-KTLQDLTRPEYK-NLLVTPSpaTSSPGLSFLMA 167
Cdd:cd13542    80 ESNV--PANLRDP--------DGNWFGltkrarvivynkDKVNPEElSTYEDLADPKWKgKVCMRSS--SNSYNQSLVAS 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 168 NIGSMGEAGAFKWWAQMRQNGVKVAKGWSEAYYTDFSHNGGAYPLVVGYaaspaaevYFSKGKYSEPPT--------GNL 239
Cdd:cd13542   148 MIAHDGEKETKEWLQGWVNNLAREPQGGDRDQAKAIAAGICDVGIANSY--------YLGRMLNSEDPEekevaepvGVF 219

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1905088589 240 FL---KGGVFRQVEGAAVLKGAKQPELAAKLVQWLQSGEVQRAVSSEMWVYPAVKNTPLPEV 298
Cdd:cd13542   220 FPnqdNRGTHVNISGIGVTKYAKNKENAIKFLEFLVSEPAQKLYAGGNYEYPVNPGVELSEL 281
PBP2_Fbp_like_5 cd13551
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 48-288 4.67e-09

Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270269 [Multi-domain]  Cd Length: 267  Bit Score: 56.26  E-value: 4.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  48 KVSVIQAGNAnEMLNKLILSRANPIADAVYGLDNANIGKAREMGVLADEQPKSLPVsvgLPSVLAVDYGYVT-------- 119
Cdd:cd13551    27 NIKIVNGGGG-DLANRLIAEKNNPVADVVFGLNAVSFERLKKQGLLVPYTPSWAGE---IPSALSDGDGYYYplvqqpiv 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 120 LNYDKKWFAEKklPLPKTLQDLTRPEYKNLLVTPSPATSSPGL---SFLMANIGSMGEAGAF-KWWAQMRQ---NGVKVA 192
Cdd:cd13551   103 LAYNPDTMTDP--DAPKSWTDLAKPKYKGKYEVPGLLGGTGQAilaGILVRYLDPKGEYGVSdEGWQVLEDyfaNGYPAQ 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 193 KGwsEAYYTDFSHNGGAYPLVVGYAASPAAEVYFSKGKYSEPptgnlflKGGVFRQVEGAAVLKGAKQPELAAKLVQWLQ 272
Cdd:cd13551   181 EG--TDFYAPFADGQVPIGYLWSSGLAGIQKQYGVEFKIVDP-------EIGVPFVTEQVGIVKGTKKEAEAKAFIDWFG 251

                         250
                  ....*....|....*.
gi 1905088589 273 SGEVQRAVSSEMWVYP 288
Cdd:cd13551   252 SAEIQAEFAKKFGSIP 267
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 35-281 7.42e-08

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 53.51  E-value: 7.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  35 KGVIARFEREN-NAKVSVIQAGNaNEMLNKLILSRANPIADAVYGLDNANIGKAREMGVLAD----EQPKSLPVSVGLPS 109
Cdd:COG1653    49 EALIKEFEAEHpGIKVEVESVPY-DDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPlddlLDDDGLDKDDFLPG 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 110 VLA------------VDYGYVTLNYDKKWFAEKKLPLPKTLQD-------LTRPEYKNLLVTPSpATSSPGLSFLMANIG 170
Cdd:COG1653   128 ALDagtydgklygvpFNTDTLGLYYNKDLFEKAGLDPPKTWDEllaaakkLKAKDGVYGFALGG-KDGAAWLDLLLSAGG 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 171 SM----GEAG--------AFKWWAQMRQNGVkVAKGWSEAYYTD-----------FSHNGgayPLVVGYAASPAAEVYFs 227
Cdd:COG1653   207 DLydedGKPAfdspeaveALEFLKDLVKDGY-VPPGALGTDWDDaraafasgkaaMMING---SWALGALKDAAPDFDV- 281

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1905088589 228 kgKYSEPPTGNLFLKGGVFRQVEGAAVLKGAKQPELAAKLVQWLQSGEVQRAVS 281
Cdd:COG1653   282 --GVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQAKWD 333
PBP2_Fbp_like_6 cd13552
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 37-288 1.01e-07

Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270270 [Multi-domain]  Cd Length: 266  Bit Score: 52.46  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  37 VIARFERENNAKVSVIQAGnANEMLNKLILSRANPIADAVYGLDNANIGKAREMGVLADEQPkslpvSVGlpSVLAVDYG 116
Cdd:cd13552    16 VEDAFEEKTGVEVEWLNMG-SQELLDRVRAEKENPQADVWWGGPSQLFMQLKEEGLLEPTEP-----SWA--EKVAAEFK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 117 yvtlNYDKKWFAEKKLP--------------LPKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMANIgsmgeagafkwwA 182
Cdd:cd13552    88 ----DADGYWYGTIQTPevimyntellseeeAPKDWDDLLDPKWKDKIIIRNPLASGTMRTIFAALI------------Q 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 183 QMRQNGVKVAKGWseAYYTDFSHNggayplVVGYAASPA----------AEVYFS----------KGKYsepPTGNLFLK 242
Cdd:cd13552   152 RELKGTGSLDAGY--AWLKKLDAN------TKEYAASPTmlylkigrgeAAISLWnlndvldqreNNKM---PFGFIDPA 220

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1905088589 243 GGVFRQVEGAAVLKGAKQPELAAKLVQWLQSGEVQRAVSSEMWVYP 288
Cdd:cd13552   221 SGAPVITDGIALIKGAPHPEAAKAFYEFVGSAEIQALLAEKFNRMP 266
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 37-279 6.46e-07

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


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 49.57  E-value: 6.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  37 VIARFERENNAKVsVIQAGNANEMLNKLilsRANPIADAVYGLDNANIGKAREMGVLADEQPKSLpvsVGLPSVLAVDYG 116
Cdd:pfam13531  15 LAAAFEAETGVKV-VVSYGGSGKLAKQI---ANGAPADVFISADSAWLDKLAAAGLVVPGSRVPL---AYSPLVIAVPKG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 117 yvtlNYDKkwfaekklplPKTLQDLTRPEYKnlLVTPSPATSSPGLSFLMAnigsmgeAGAFKWWAQMRQNGVKVAKGwS 196
Cdd:pfam13531  88 ----NPKD----------ISGLADLLKPGVR--LAVADPKTAPSGRAALEL-------LEKAGLLKALEKKVVVLGEN-V 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 197 EAYYTDFShnGGAYPLVVGYAASPAAEVYFSKGKYSEPPtgnlflKGGVFRQVEGAAVLKGAKQPELAAKLVQWLQSGEV 276
Cdd:pfam13531 144 RQALTAVA--SGEADAGIVYLSEALFPENGPGLEVVPLP------EDLNLPLDYPAAVLKKAAHPEAARAFLDFLLSPEA 215


                  ...
gi 1905088589 277 QRA 279
Cdd:pfam13531 216 QAI 218
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 35-277 6.47e-07

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: 50.11  E-value: 6.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  35 KGVIARFEREN-NAKVSVIQAGNANEMLNKLILSRANPIADAVYGLDNANIGKAREMGVLADEQP---KSLPVSVGLPSV 110
Cdd:pfam01547  11 QALVKEFEKEHpGIKVEVESVGSGSLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDyvaNYLVLGVPKLYG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 111 LAVDYGYVTLNYDKKWFAEKKLPLPKTLQDLTRPEYKNLLVTPSPATSSPGLS------FLMANIGSMGEAGAFKWWAQM 184
Cdd:pfam01547  91 VPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAGGGDAsgtlgyFTLALLASLGGPLFDKDGGGL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 185 RQNGVKVAKGWSEAYYTDFSHNGGAYPLVVGYAASPAAEVYFSKGK---------------------YSEPPTGNLFLKG 243
Cdd:pfam01547 171 DNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKaamgivgpwaalaankvklkvAFAAPAPDPKGDV 250

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1905088589 244 GVF---------RQVEGAAVLKGAKQPELAAKLVQWLQSGEVQ 277
Cdd:pfam01547 251 GYAplpagkggkGGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQ 293
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 35-294 2.74e-06

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: 48.56  E-value: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  35 KGVIARFEREN-NAKVSVIQAGNANeMLNKLILS-RANPIADAVYgLDNANIGKAREMGVLADEQP--KSLPVSVGLPSV 110
Cdd:cd13585    17 KKLIDAFEKENpGVKVEVVPVPYDD-YWTKLTTAaAAGTAPDVFY-VDGPWVPEFASNGALLDLDDyiEKDGLDDDFPPG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 111 LAVDYGY-------------VTLNYDKKWFAEKKLPL--PKTLQDL---------TRPEYKNLLVTPSPATSSPGLSFLM 166
Cdd:cd13585    95 LLDAGTYdgklyglpfdadtLVLFYNKDLFDKAGPGPkpPWTWDELleaakkltdKKGGQYGFALRGGSGGQTQWYPFLW 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 167 ANIGSM-----GEAG--------AFKWWAQMRQNGV--KVAKGWSEAYYTDFShNGGAYPLVVGYAASPAAEVYFSKGKY 231
Cdd:cd13585   175 SNGGDLldeddGKATlnspeaveALQFYVDLYKDGVapSSATTGGDEAVDLFA-SGKVAMMIDGPWALGTLKDSKVKFKW 253

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1905088589 232 --SEPPTGNLFLKGGVFrQVEGAAVLKGAKQPELAAKLVQWLQSGEVQRAVSSEMWVYPAVKNTP 294
Cdd:cd13585   254 gvAPLPAGPGGKRASVL-GGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAA 317
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
37-291 8.71e-06

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 46.87  E-value: 8.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  37 VIARFERENNAKVSVIQAGNAnEMLNKLILS-RANPIADAVYGlDNANIGKAREMGVLADEQPKSLPVSVGLPSVLA--- 112
Cdd:COG2182    56 AAAAFEEEPGIKVKVVEVPWD-DLREKLTTAaPAGKGPDVFVG-AHDWLGELAEAGLLAPLDDDLADKDDFLPAALDavt 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 113 VD---YGY------VTLNYDKKWFAEKKlplPKTLQDL-------TRPEYKNLLV-TPSPATSSPglsFLMAN------- 168
Cdd:COG2182   134 YDgklYGVpyavetLALYYNKDLVKAEP---PKTWDELiaaakklTAAGKYGLAYdAGDAYYFYP---FLAAFggylfgk 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589 169 ---------IGSMGEAGAFKWWAQMRQNGVkVAKGWSEAYYTD-FshNGGAYPLVVG--YAASPAAEVY----------- 225
Cdd:COG2182   208 dgddpkdvgLNSPGAVAALEYLKDLIKDGV-LPADADYDAADAlF--AEGKAAMIINgpWAAADLKKALgidygvaplpt 284

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1905088589 226 FSKGKYSEPPTGnlflkggvfrqVEGAAVLKGAKQPELAAKLVQWLQSGEVQRAVSSEMWVYPAVK 291
Cdd:COG2182   285 LAGGKPAKPFVG-----------VKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALFEATGRIPANK 339
PBP2_Fbp_like_3 cd13549
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 56-193 2.90e-05

Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270267 [Multi-domain]  Cd Length: 263  Bit Score: 44.75  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905088589  56 NANEMLNKLILSRANPIADAVY-GLDNAniGKAREMGVLADEQPKSLPVsvgLPSVL--------AVDYGYVTLNYDKKw 126
Cdd:cd13549    35 NSGQALAALIAERARPVADVAYyGVAFG--IQAVAQGVVQPYKPAHWDE---IPEGLkdpdgkwfAIHSGTLGFIVNVD- 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1905088589 127 fAEKKLPLPKTLQDLTRPEYKNLLVTPSPATSSPGLSFLMA----NIGSMGEAG-AFKWWAQMRQNGVKVAK 193
Cdd:cd13549   109 -ALGGKPVPKSWADLLKPEYKGMVGYLDPRSAFVGYVGAVAvnqaMGGSLDNFGpGIDYFKKLHKNGPIVPK 179
 
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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