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Conserved domains on  [gi|2674824722|ref|WP_331825134|]
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thiamine ABC transporter substrate-binding protein [Deinococcus sp. YIM 134068]

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 ...
 19-335 2.25e-139

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: 397.31  E-value: 2.25e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  19 QTTLTVITHDSFDVDKQLVAGFEKANEA----RVRFVRGGDAGELLNRLILTRRAPVADVVYGLDNSLLARARQAGILEA 94
Cdd:TIGR01254   1 QPVVTVYTYDSFAADWGLGPVVEKAFEAdcncKVKFVALEDAGELLNRLRLEGKNPKADVVLGLDNNLLEAASKTGLLAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  95 YRsPALARVPAAYRLDEKgLLNTVNYGFVALNYDRAALARTglplPKTLDDLKKPEYARLTVVSSPATSSPGLAFLLATV 174
Cdd:TIGR01254  81 SG-VALDKVNVPGGWNNA-TFLPFDYGYVAFVYDKNKLQNP----PQSLKELVEPEQDLLVIYQDPRTSSPGLGLLLWMQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 175 NHYGEAGAWTWWREARLSGLKVTRGWSDAYnkeFSKNGGRFPIVLSYASSPAAEVYYADgydparlpaQSPTANLLLPGS 254
Cdd:TIGR01254 155 SVYGEDDAPQAWKQLRKKTVTVTKGWSEAY---GTFLGGEYDLVLSYATSPAYHVLFEK---------KDNYAALNFSEG 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 255 TFLQLEGVGVLKGAKRPALARKFVDFMLSGGVQSDFPTRMWVYPAVTGTKLDPVFGFAQRPD-VAQVKASVTANPQRLVD 333
Cdd:TIGR01254 223 HYLQVEGAARLKGAKQPELADKFVQFLLSPAVQNAIPTGNWMYPVVNGTLLPGFFKLTQQPTtTAPTPAEVTAQRQAWIS 302


                  ..
gi 2674824722 334 AW 335
Cdd:TIGR01254 303 EW 304
 
Name Accession Description Interval E-value
sfuA TIGR01254
ABC transporter periplasmic binding protein, thiB subfamily; The model describes thiamine ABC ...
 19-335 2.25e-139

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: 397.31  E-value: 2.25e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  19 QTTLTVITHDSFDVDKQLVAGFEKANEA----RVRFVRGGDAGELLNRLILTRRAPVADVVYGLDNSLLARARQAGILEA 94
Cdd:TIGR01254   1 QPVVTVYTYDSFAADWGLGPVVEKAFEAdcncKVKFVALEDAGELLNRLRLEGKNPKADVVLGLDNNLLEAASKTGLLAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  95 YRsPALARVPAAYRLDEKgLLNTVNYGFVALNYDRAALARTglplPKTLDDLKKPEYARLTVVSSPATSSPGLAFLLATV 174
Cdd:TIGR01254  81 SG-VALDKVNVPGGWNNA-TFLPFDYGYVAFVYDKNKLQNP----PQSLKELVEPEQDLLVIYQDPRTSSPGLGLLLWMQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 175 NHYGEAGAWTWWREARLSGLKVTRGWSDAYnkeFSKNGGRFPIVLSYASSPAAEVYYADgydparlpaQSPTANLLLPGS 254
Cdd:TIGR01254 155 SVYGEDDAPQAWKQLRKKTVTVTKGWSEAY---GTFLGGEYDLVLSYATSPAYHVLFEK---------KDNYAALNFSEG 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 255 TFLQLEGVGVLKGAKRPALARKFVDFMLSGGVQSDFPTRMWVYPAVTGTKLDPVFGFAQRPD-VAQVKASVTANPQRLVD 333
Cdd:TIGR01254 223 HYLQVEGAARLKGAKQPELADKFVQFLLSPAVQNAIPTGNWMYPVVNGTLLPGFFKLTQQPTtTAPTPAEVTAQRQAWIS 302


                  ..
gi 2674824722 334 AW 335
Cdd:TIGR01254 303 EW 304
TbpA COG4143
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ...
 4-342 5.92e-121

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


Pssm-ID: 443315 [Multi-domain]  Cd Length: 343  Bit Score: 351.84  E-value: 5.92e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722   4 LILLTALALGTHATAQTTLTVITHDSFDVD----KQLVAGFEKANEARVRFVRGGDAGELLNRLILTRRAPVADVVYGLD 79
Cdd:COG4143    14 LALALAGCSGAAAAAKPTLTVYTYDSFASEwgpgPWLKAAFEAECGCTLEFVAPGDGGELLNRLRLEGANPKADVVLGLD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  80 NSLLARARQAGILEAYRSPALARVPAAYRLDEKGLLNTVNYGFVALNYDRAALartgLPLPKTLDDLKKPEYARLTVVSS 159
Cdd:COG4143    94 NNLLARALDTGLFAPHGVDALDALALPLAWDPDDRFVPYDYGYFAFVYDKTKL----LNPPESLEDLVDPEYKDKLVVQD 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 160 PATSSPGLAFLLATVNHYGEAGAWTWWREARLSGLKVTRGWSDAYNkEFSKngGRFPIVLSYASSPAAEVYYAdgydpar 239
Cdd:COG4143   170 PRTSTPGLAFLLWTIAAYGEDGALDYWQKLADNGVTVTKGWSEAYG-LFLK--GEAPMVLSYSTSPAYHVIAE------- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 240 lPAQSPTANLLLPGSTFLQLEGVGVLKGAKRPALARKFVDFMLSGGVQSDFPTRMWVYPAVTGTKLDPVFG-FAQRPDva 318
Cdd:COG4143   240 -GDKDRYAAALFDEGHYRQVEGAGVLAGAKNPELARKFLDFLLSPEFQAEIPTRNWMYPAVEDVELPEAFDeYAPVPE-- 316

                         330       340
                  ....*....|....*....|....*..
gi 2674824722 319 qvkASVTANPQRL---VDAWVTNVLRA 342
Cdd:COG4143   317 ---KPLTFDPDEIaanRDAWIDEWQRA 340
PBP2_TbpA cd13545
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ...
 21-301 7.57e-117

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: 338.89  E-value: 7.57e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  21 TLTVITHDSFDVD----KQLVAGFEKANEARVRFVRGGDAGELLNRLILTRRAPVADVVYGLDNSLLARARQAGILEAYR 96
Cdd:cd13545     1 TLTVYTYDSFVGEwgpgPEVKAEFEKETGCKVEFVKPGDAGELLNRLILEKNNPRADVVLGLDNNLLSRALKEGLFEPYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  97 SPALARVPAAYRLDEKGLLNTVNYGFVALNYDRAALARTglplPKTLDDLKKPEYARLTVVSSPATSSPGLAFLLATVNH 176
Cdd:cd13545    81 SPALDVVPEVPVFDPEDRLIPYDYGYLAFNYDKKKFKEP----PLSLEDLTAPEYKGLIVVQDPRTSSPGLGFLLWTIAV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 177 YGEAGAWTWWREARLSGLKVTRGWSDAYNKEFSkngGRFPIVLSYASSPAAEVYYAdgydparlPAQSPTANLLLPGStF 256
Cdd:cd13545   157 FGEEGYLEYWKKLKANGVTVTPGWSEAYGLFTT---GEAPMVVSYATSPAYHVYYE--------KDLRYTAVIFPEGH-Y 224

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2674824722 257 LQLEGVGVLKGAKRPALARKFVDFMLSGGVQSDFPTRMWVYPAVT 301
Cdd:cd13545   225 RQVEGAGILKGAKNPELAKKFVDFLLSPEFQEVIPETNWMFPVNK 269
SBP_bac_6 pfam13343
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 69-307 6.31e-22

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


Pssm-ID: 463852 [Multi-domain]  Cd Length: 247  Bit Score: 92.81  E-value: 6.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  69 APVADVVYG-----LDNSLLARARQAGILEAYRSPALARVPAAYRL----DEKGLLNTVNYGFVALNYDRAALArtGLPL 139
Cdd:pfam13343   1 DPLPDIILSagdlfFDKRFLEKFIEEGLFQPLDSANLPNVPKDFDDeglrDPDGYYTPYGVGPLVIAYNKERLG--GRPV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 140 PKTLDDLKKPEYARLTVVSSPATSSPGLAFLLATVNHYGEAGAWTWWREARlsglkvtRGWSDAYNKefsKNGGRFpivl 219
Cdd:pfam13343  79 PRSWADLLDPEYKGKVALPGPNVGDLFNALLLALYKDFGEDGVRKLARNLK-------ANLHPAQMV---KAAGRL---- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 220 syaSSPAAEVYYADGYDPARLPAQSPTANLLLPGS-TFLQLEGVGVLKGAKrpALARKFVDFMLSGGVQSDFPTRMWVYP 298
Cdd:pfam13343 145 ---ESGEPAVYLMPYFFADILPRKKKNVEVVWPEDgALVSPIFMLVKKGKK--ELADPLIDFLLSPEVQAILAKAGLVFP 219


                  ....*....
gi 2674824722 299 AVTGTKLDP 307
Cdd:pfam13343 220 VVLNPAVDN 228
PRK15046 PRK15046
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
 2-301 1.29e-20

2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional


Pssm-ID: 237887 [Multi-domain]  Cd Length: 349  Bit Score: 91.29  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722   2 RRLILLTALALGTHATAQT----TLTVITHDSF-DVDKQLVAGFEKANEARVRFVRGGdAGELLNRLILTRRAPVADVVY 76
Cdd:PRK15046   13 MKLAAAAAAAAFGGGAAPAwaadAVTVYSADGLeDWYQDVFPAFTKATGIKVNYVEAG-SGEVVNRAAKEKSNPQADVLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  77 GLDnSLLARARQAGILEAYRSPALARVPAAYRlDEKGLLNTVNYGFVALNYDRAALartgLPLPKTLDDLKKPEYARLTV 156
Cdd:PRK15046   92 TLP-PFIQQAAAEGLLQPYSSVNAKAVPAIAK-DADGTYAPFVNNYLSFIYNPKVL----KTAPATWADLLDPKFKGKLQ 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 157 VSSPATSSPGLAFLLATVNHYGEAGAWTWWreARLSglkvtrgwsdAYNKEFSKNGGRFPIVLSyasspAAEVYYADG-- 234
Cdd:PRK15046  166 YSTPGQAGDGTAVLLLTFHLMGKDKAFDYL--AKLQ----------ANNVGPSKSTGKLTPLVS-----KGEIYVANGdl 228

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674824722 235 -YDPARLPAQSPTANLLLPG------STFLQLEGVGVLKGAKRPALARKFVDFMLSGGVQSDFPTRMWVYPAVT 301
Cdd:PRK15046  229 qMNLAQAEHGGPNVKIFFPAkdggerSTFALPYVIGLVKGAPNSENGKKLIDFLLSKEAQTKVSDMAWGIPVRT 302
 
Name Accession Description Interval E-value
sfuA TIGR01254
ABC transporter periplasmic binding protein, thiB subfamily; The model describes thiamine ABC ...
 19-335 2.25e-139

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: 397.31  E-value: 2.25e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  19 QTTLTVITHDSFDVDKQLVAGFEKANEA----RVRFVRGGDAGELLNRLILTRRAPVADVVYGLDNSLLARARQAGILEA 94
Cdd:TIGR01254   1 QPVVTVYTYDSFAADWGLGPVVEKAFEAdcncKVKFVALEDAGELLNRLRLEGKNPKADVVLGLDNNLLEAASKTGLLAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  95 YRsPALARVPAAYRLDEKgLLNTVNYGFVALNYDRAALARTglplPKTLDDLKKPEYARLTVVSSPATSSPGLAFLLATV 174
Cdd:TIGR01254  81 SG-VALDKVNVPGGWNNA-TFLPFDYGYVAFVYDKNKLQNP----PQSLKELVEPEQDLLVIYQDPRTSSPGLGLLLWMQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 175 NHYGEAGAWTWWREARLSGLKVTRGWSDAYnkeFSKNGGRFPIVLSYASSPAAEVYYADgydparlpaQSPTANLLLPGS 254
Cdd:TIGR01254 155 SVYGEDDAPQAWKQLRKKTVTVTKGWSEAY---GTFLGGEYDLVLSYATSPAYHVLFEK---------KDNYAALNFSEG 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 255 TFLQLEGVGVLKGAKRPALARKFVDFMLSGGVQSDFPTRMWVYPAVTGTKLDPVFGFAQRPD-VAQVKASVTANPQRLVD 333
Cdd:TIGR01254 223 HYLQVEGAARLKGAKQPELADKFVQFLLSPAVQNAIPTGNWMYPVVNGTLLPGFFKLTQQPTtTAPTPAEVTAQRQAWIS 302


                  ..
gi 2674824722 334 AW 335
Cdd:TIGR01254 303 EW 304
TbpA COG4143
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ...
 4-342 5.92e-121

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


Pssm-ID: 443315 [Multi-domain]  Cd Length: 343  Bit Score: 351.84  E-value: 5.92e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722   4 LILLTALALGTHATAQTTLTVITHDSFDVD----KQLVAGFEKANEARVRFVRGGDAGELLNRLILTRRAPVADVVYGLD 79
Cdd:COG4143    14 LALALAGCSGAAAAAKPTLTVYTYDSFASEwgpgPWLKAAFEAECGCTLEFVAPGDGGELLNRLRLEGANPKADVVLGLD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  80 NSLLARARQAGILEAYRSPALARVPAAYRLDEKGLLNTVNYGFVALNYDRAALartgLPLPKTLDDLKKPEYARLTVVSS 159
Cdd:COG4143    94 NNLLARALDTGLFAPHGVDALDALALPLAWDPDDRFVPYDYGYFAFVYDKTKL----LNPPESLEDLVDPEYKDKLVVQD 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 160 PATSSPGLAFLLATVNHYGEAGAWTWWREARLSGLKVTRGWSDAYNkEFSKngGRFPIVLSYASSPAAEVYYAdgydpar 239
Cdd:COG4143   170 PRTSTPGLAFLLWTIAAYGEDGALDYWQKLADNGVTVTKGWSEAYG-LFLK--GEAPMVLSYSTSPAYHVIAE------- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 240 lPAQSPTANLLLPGSTFLQLEGVGVLKGAKRPALARKFVDFMLSGGVQSDFPTRMWVYPAVTGTKLDPVFG-FAQRPDva 318
Cdd:COG4143   240 -GDKDRYAAALFDEGHYRQVEGAGVLAGAKNPELARKFLDFLLSPEFQAEIPTRNWMYPAVEDVELPEAFDeYAPVPE-- 316

                         330       340
                  ....*....|....*....|....*..
gi 2674824722 319 qvkASVTANPQRL---VDAWVTNVLRA 342
Cdd:COG4143   317 ---KPLTFDPDEIaanRDAWIDEWQRA 340
PBP2_TbpA cd13545
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ...
 21-301 7.57e-117

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: 338.89  E-value: 7.57e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  21 TLTVITHDSFDVD----KQLVAGFEKANEARVRFVRGGDAGELLNRLILTRRAPVADVVYGLDNSLLARARQAGILEAYR 96
Cdd:cd13545     1 TLTVYTYDSFVGEwgpgPEVKAEFEKETGCKVEFVKPGDAGELLNRLILEKNNPRADVVLGLDNNLLSRALKEGLFEPYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  97 SPALARVPAAYRLDEKGLLNTVNYGFVALNYDRAALARTglplPKTLDDLKKPEYARLTVVSSPATSSPGLAFLLATVNH 176
Cdd:cd13545    81 SPALDVVPEVPVFDPEDRLIPYDYGYLAFNYDKKKFKEP----PLSLEDLTAPEYKGLIVVQDPRTSSPGLGFLLWTIAV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 177 YGEAGAWTWWREARLSGLKVTRGWSDAYNKEFSkngGRFPIVLSYASSPAAEVYYAdgydparlPAQSPTANLLLPGStF 256
Cdd:cd13545   157 FGEEGYLEYWKKLKANGVTVTPGWSEAYGLFTT---GEAPMVVSYATSPAYHVYYE--------KDLRYTAVIFPEGH-Y 224

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2674824722 257 LQLEGVGVLKGAKRPALARKFVDFMLSGGVQSDFPTRMWVYPAVT 301
Cdd:cd13545   225 RQVEGAGILKGAKNPELAKKFVDFLLSPEFQEVIPETNWMFPVNK 269
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
 21-298 8.97e-51

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: 169.40  E-value: 8.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  21 TLTVITHDSFDVDKQLVAGFEKANEARVRFVRGGdAGELLNRLILTRRAPVADVVYGLDNSLLARARQAGILEAYRSPAL 100
Cdd:cd13518     1 ELVVYTASDRDFAEPVLKAFEEKTGIKVKAVYDG-TGELANRLIAEKNNPQADVFWGGEIIALEALKEEGLLEPYTPKVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 101 ARVPAAYRlDEKGLLntvnYGFVA----LNYDRAALArtGLPLPKTLDDLKKPEYARLTVVSSPATSSPGLAFLLATVNH 176
Cdd:cd13518    80 EAIPADYR-DPDGYW----VGFAArarvFIYNTDKLK--EPDLPKSWDDLLDPKWKGKIVYPTPLRSGTGLTHVAALLQL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 177 YGEAGAWTWWREARLSGLKVTRGWSDAYNKEFSkngGRFPIVLSYASSPAAEVYYADGYDPArLPAQsptanlllpgSTF 256
Cdd:cd13518   153 MGEEKGGWYLLKLLANNGKPVAGNSDAYDLVAK---GEVAVGLTDTYYAARAAAKGEPVEIV-YPDQ----------GAL 218

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2674824722 257 LQLEGVGVLKGAKRPALARKFVDFMLSGGVQSDFPTRMWVYP 298
Cdd:cd13518   219 VIPEGVALLKGAPNPEAAKKFIDFLLSPEGQKALAAANAQLP 260
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 36-339 5.58e-44

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 152.78  E-value: 5.58e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  36 LVAGFEKANEARVRFVRGGdAGELLNRLILTRRAPVADVVYGLDNSLLARARQAGILEAYRSPALARVPAAYRlDEKGLL 115
Cdd:COG1840     1 LLEAFEKKTGIKVNVVRGG-SGELLARLKAEGGNPPADVVWSGDADALEQLANEGLLQPYKSPELDAIPAEFR-DPDGYW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 116 NTVNYGFVALNYDRAALArtGLPLPKTLDDLKKPEYARLTVVSSPATSSPGLAFLLATVNHYGEAGAWTWWREARLSGLK 195
Cdd:COG1840    79 FGFSVRARVIVYNTDLLK--ELGVPKSWEDLLDPEYKGKIAMADPSSSGTGYLLVAALLQAFGEEKGWEWLKGLAANGAR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 196 VTRGWSDAYNKEFSkngGRFPIVLSYAsspaaevyyadgYDPARLPAQSPTANLLLP-GSTFLQLEGVGVLKGAKRPALA 274
Cdd:COG1840   157 VTGSSSAVAKAVAS---GEVAIGIVNS------------YYALRAKAKGAPVEVVFPeDGTLVNPSGAAILKGAPNPEAA 221

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 275 RKFVDFMLSGGVQSDFPTRMWVYPAVTGTKLDPVFgfaqrPDVAQVKA-----SVTANPQRLVDAWVTNV 339
Cdd:COG1840   222 KLFIDFLLSDEGQELLAEEGYEYPVRPDVEPPEGL-----PPLGELKLiddddKAAENREELLELWDEAV 286
PBP2_Fbp_like_1 cd13544
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ...
 34-283 1.95e-33

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: 125.02  E-value: 1.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  34 KQLVAGFEKANEARVRFVRGGdAGELLNRLILTRRAPVADVVYG--LDNSLLARARqaGILEAYRSPALARVPAAYRlDE 111
Cdd:cd13544    14 KAILEAFKKDTGIKVEFVRLS-TGEALARLEAEKGNPQADVWFGgtADAHIQAKKE--GLLEPYKSPNADKIPAKFK-DP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 112 KGLLNTVNYGFVALNYDRAALARTGLPLPKTLDDLKKPEYARLTVVSSPATSSPGLAFLLATVNHYGEAGAWTWWrearl 191
Cdd:cd13544    90 DGYWTGIYLGPLGFGVNTDELKEKGLPVPKSWEDLLNPEYKGEIVMPNPASSGTAYTFLASLIQLMGEDEAWEYL----- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 192 sglkvtrgwsDAYNK---EFSKNG---------GRFPIVLSYASspaAEVYYADGYDPARL--PAQsptanlllpGSTFl 257
Cdd:cd13544   165 ----------KKLNKnvgQYTKSGsapaklvasGEAAIGISFLH---DALKLKEQGYPIKIifPKE---------GTGY- 221

                         250       260
                  ....*....|....*....|....*.
gi 2674824722 258 QLEGVGVLKGAKRPALARKFVDFMLS 283
Cdd:cd13544   222 EIEAVAIIKGAKNPEAAKAFIDWALS 247
PBP2_BitB cd13546
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ...
 21-287 2.74e-23

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: 96.94  E-value: 2.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  21 TLTVITHDSFDVDKQLVAGFEKANEARVRFVRGGdAGELLNRLILTRRAPVADVVYGLDNSLLARARQagILEAYRSPAL 100
Cdd:cd13546     1 TLVVYSPNSEEIIEPIIKEFEEKPGIKVEVVTGG-TGELLARIKAEADNPQADVMWGGGIETLEAYKD--LFEPYESPEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 101 ARVPAAYRlDEKGLLNTVNYGFVALNYDRAALarTGLPLPKTLDDLKKPEYARLTVVSSPATSSPGLAFLLATVNHYGEA 180
Cdd:cd13546    78 AAIPDAYK-SPEGLWTGFSVLPVVLMVNTDLV--KNIGAPKGWKDLLDPKWKGKIAFADPNKSGSAYTILYTILKLYGGA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 181 gawtWWREARLSG-LKVTRGWSDAYNKEFSKngGRFPIVLSY---------ASSPAAEVYYADGydparlpaqsptanll 250
Cdd:cd13546   155 ----WEYIEKLLDnLGVILSSSSAVYKAVAD--GEYAVGLTYedaaykyvaGGAPVKIVYPKEG---------------- 212

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2674824722 251 lpgsTFLQLEGVGVLKGAKRPALARKFVDFMLSGGVQ 287
Cdd:cd13546   213 ----TTAVPDGVAIVKGAKNPENAKKFIDFLLSKEVQ 245
PBP2_Fbp_like_2 cd13547
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 21-298 1.55e-22

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: 94.98  E-value: 1.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  21 TLTVITHDSFDVDKQLVAGFEKAN-EARVRFVRGGdAGELLNRLILTRRA--PVADVVYGLDNSLLARARQAGILEAYRS 97
Cdd:cd13547     1 KLVVYTSMPEDLANALVEAFEKKYpGVKVEVFRAG-TGKLMAKLAAEAEAgnPQADVLWVADPPTAEALKKEGLLLPYKS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  98 PALARVPAAYRLDEK-----GLLNTVnygfVALNYDRaalarTGLPLPKTLDDLKKPEYARLTVVSSPATSSPGLAFLLA 172
Cdd:cd13547    80 PEADAIPAPFYDKDGyyygtRLSAMG----IAYNTDK-----VPEEAPKSWADLTKPKYKGQIVMPDPLYSGAALDLVAA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 173 TVNHYGEagAWTWWREARLSGLKVTRGWSDAYNKefsknggrfpivlsYASSPAAEVYYADgYDPARLPAQSPTANLLLP 252
Cdd:cd13547   151 LADKYGL--GWEYFEKLKENGVKVEGGNGQVLDA--------------VASGERPAGVGVD-YNALRAKEKGSPLEVIYP 213

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2674824722 253 GS-TFLQLEGVGVLKGAKRPALARKFVDFMLSGGVQSDFpTRMWVYP 298
Cdd:cd13547   214 EEgTVVIPSPIAILKGSKNPEAAKAFVDFLLSPEGQELV-ADAGLLP 259
SBP_bac_6 pfam13343
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 69-307 6.31e-22

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


Pssm-ID: 463852 [Multi-domain]  Cd Length: 247  Bit Score: 92.81  E-value: 6.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  69 APVADVVYG-----LDNSLLARARQAGILEAYRSPALARVPAAYRL----DEKGLLNTVNYGFVALNYDRAALArtGLPL 139
Cdd:pfam13343   1 DPLPDIILSagdlfFDKRFLEKFIEEGLFQPLDSANLPNVPKDFDDeglrDPDGYYTPYGVGPLVIAYNKERLG--GRPV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 140 PKTLDDLKKPEYARLTVVSSPATSSPGLAFLLATVNHYGEAGAWTWWREARlsglkvtRGWSDAYNKefsKNGGRFpivl 219
Cdd:pfam13343  79 PRSWADLLDPEYKGKVALPGPNVGDLFNALLLALYKDFGEDGVRKLARNLK-------ANLHPAQMV---KAAGRL---- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 220 syaSSPAAEVYYADGYDPARLPAQSPTANLLLPGS-TFLQLEGVGVLKGAKrpALARKFVDFMLSGGVQSDFPTRMWVYP 298
Cdd:pfam13343 145 ---ESGEPAVYLMPYFFADILPRKKKNVEVVWPEDgALVSPIFMLVKKGKK--ELADPLIDFLLSPEVQAILAKAGLVFP 219


                  ....*....
gi 2674824722 299 AVTGTKLDP 307
Cdd:pfam13343 220 VVLNPAVDN 228
PRK15046 PRK15046
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
 2-301 1.29e-20

2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional


Pssm-ID: 237887 [Multi-domain]  Cd Length: 349  Bit Score: 91.29  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722   2 RRLILLTALALGTHATAQT----TLTVITHDSF-DVDKQLVAGFEKANEARVRFVRGGdAGELLNRLILTRRAPVADVVY 76
Cdd:PRK15046   13 MKLAAAAAAAAFGGGAAPAwaadAVTVYSADGLeDWYQDVFPAFTKATGIKVNYVEAG-SGEVVNRAAKEKSNPQADVLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  77 GLDnSLLARARQAGILEAYRSPALARVPAAYRlDEKGLLNTVNYGFVALNYDRAALartgLPLPKTLDDLKKPEYARLTV 156
Cdd:PRK15046   92 TLP-PFIQQAAAEGLLQPYSSVNAKAVPAIAK-DADGTYAPFVNNYLSFIYNPKVL----KTAPATWADLLDPKFKGKLQ 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 157 VSSPATSSPGLAFLLATVNHYGEAGAWTWWreARLSglkvtrgwsdAYNKEFSKNGGRFPIVLSyasspAAEVYYADG-- 234
Cdd:PRK15046  166 YSTPGQAGDGTAVLLLTFHLMGKDKAFDYL--AKLQ----------ANNVGPSKSTGKLTPLVS-----KGEIYVANGdl 228

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674824722 235 -YDPARLPAQSPTANLLLPG------STFLQLEGVGVLKGAKRPALARKFVDFMLSGGVQSDFPTRMWVYPAVT 301
Cdd:PRK15046  229 qMNLAQAEHGGPNVKIFFPAkdggerSTFALPYVIGLVKGAPNSENGKKLIDFLLSKEAQTKVSDMAWGIPVRT 302
PBP2_AEPn_like cd13548
Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member ...
 38-321 4.08e-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: 86.46  E-value: 4.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  38 AGFEKANEARVRFVRGGdAGELLNRLILTRRAPVADVVYGLDnSLLARARQAGILEAYRSPAlARVPAAYRlDEKGLLNT 117
Cdd:cd13548    19 AAFTKATGITVNYVEAG-SGEVVERAAKEKSNPQADVLVTLP-PFIQQAAQMGLLQPYQSDA-AKNPAIIK-AEDGTYAP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 118 VNYGFVALNYDRAALARTglplPKTLDDLKKPEYARLTVVSSPATSSPGLAFLLATVNHYGEAGAWTWWreARLSglkvt 197
Cdd:cd13548    95 LVNNYFSFIYNSAVLKNA----PKTFADLLDPKYKGKIQYSTPGQAGDGMAVLLLTTHLMGSDAAFAYL--AKLQ----- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 198 rgwsdAYNKEFSKNGGRFPIVLSyasspAAEVYYADG---YDPARLPAQSPTANLLLPG------STFLQLEGVGVLKGA 268
Cdd:cd13548   164 -----QNNVGPSASTGKLTALVS-----KGEISVANGdlqMNLAQMEHANPNKKIFWPAkaggqrSTFALPYGIGLVKGA 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2674824722 269 KRPALARKFVDFMLSGGVQSDFPTRMWVYPAVTGTKLDPVFGFAQRPDVAQVK 321
Cdd:cd13548   234 PNADNGKKLIDFLLSKEAQSKVPDMAWGMPVRTDVTPSGKNGEAAKAAIAGVK 286
PBP2_Fbp cd13543
Substrate binding domain of ferric iron transporter, a member of the type 2 periplasmic ...
 21-307 2.03e-17

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: 81.58  E-value: 2.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  21 TLTVITHDSFDVDKQLVAGFEKANEARVRfVRGGDAGELLNRLILTRRAPVADVVYGLDNSLLARARQAGILEAYRSPAL 100
Cdd:cd13543     1 ELTVYSGRHESLVDPLVEAFEQETGIKVE-LRYGDTAELANQLVEEGDASPADVFYAEDAGALGALADAGLLAPLPEDTL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 101 ARVPAAYRLDEK------GLLNTVNYgfvalNYDRAALArtglPLPKTLDDLKKPEYaRLTVVSSPATSSpGLAFLLATV 174
Cdd:cd13543    80 TQVPPRFRSPDGdwvgvsGRARVVVY-----NTDKLSED----DLPKSVLDLAKPEW-KGRVGWAPTNGS-FQAFVTAMR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 175 NHYGEAGAWTWwrearLSGLKVTRGwsdaynKEFSKNGgrfPIVLSYAsspAAEV-------YYADGyDPARLPAQSPTA 247
Cdd:cd13543   149 VLEGEEATREW-----LKGLKANGP------KAYAKNS---AVVEAVN---RGEVdaglinhYYWFR-LRAEQGEDAPVA 210

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674824722 248 NLLL----PGStFLQLEGVGVLKGAKRPALARKFVDFMLSGGVQSDFPTRMWVYPAVTGTKLDP 307
Cdd:cd13543   211 LHYFkngdPGA-LVNVSGAGVLKTSKNQAEAQKFLAFLLSKEGQEFLATANFEYPLVAGVASPP 273
PBP2_Fbp_like_5 cd13551
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 38-298 8.20e-17

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: 78.98  E-value: 8.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  38 AGFEkanearVRFVrGGDAGELLNRLILTRRAPVADVVYGLDNSLLARARQAGILEAYRSPALARVPAAYRlDEKGLLNT 117
Cdd:cd13551    24 AGFN------IKIV-NGGGGDLANRLIAEKNNPVADVVFGLNAVSFERLKKQGLLVPYTPSWAGEIPSALS-DGDGYYYP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 118 VNYGFVALNYDRAALarTGLPLPKTLDDLKKPEYARLTVVSSPATSSPGLA---FLLATVNHYGEAGawtwwrearLSGl 194
Cdd:cd13551    96 LVQQPIVLAYNPDTM--TDPDAPKSWTDLAKPKYKGKYEVPGLLGGTGQAIlagILVRYLDPKGEYG---------VSD- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 195 kvtRGWSDAynKEFSKNG---------------GRFPIVLSYASSPAAevyYADGYDparlpaqsPTANLLLP--GSTFL 257
Cdd:cd13551   164 ---EGWQVL--EDYFANGypaqegtdfyapfadGQVPIGYLWSSGLAG---IQKQYG--------VEFKIVDPeiGVPFV 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2674824722 258 QlEGVGVLKGAKRPALARKFVDFMLSGGVQSDFPTRMWVYP 298
Cdd:cd13551   228 T-EQVGIVKGTKKEAEAKAFIDWFGSAEIQAEFAKKFGSIP 267
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
2-328 3.28e-15

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 75.33  E-value: 3.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722   2 RRLILLTALAL-------GTHATAQTTLTVIThDSFDVDKQLVAGFEKANEARVRFVRGGDAGELLNRLILtrRAPVADV 74
Cdd:COG0687     4 RSLLGLAAAALaaalaggAPAAAAEGTLNVYN-WGGYIDPDVLEPFEKETGIKVVYDTYDSNEEMLAKLRA--GGSGYDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  75 VYgLDNSLLARARQAGILEAY---RSPALARVPAAYR--LDEKGLLNTVNY--GFVALNYDRAALARTglplPKTLDDLK 147
Cdd:COG0687    81 VV-PSDYFVARLIKAGLLQPLdksKLPNLANLDPRFKdpPFDPGNVYGVPYtwGTTGIAYNTDKVKEP----PTSWADLW 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 148 KPEYA-RLTVVSSPATsSPGLAFLLATVNHYGE-----AGAWTWWREARlsglkvtrgwsdaynkefsknggrfPIVLSY 221
Cdd:COG0687   156 DPEYKgKVALLDDPRE-VLGAALLYLGYDPNSTdpadlDAAFELLIELK-------------------------PNVRAF 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 222 ASSPAA--------EVYYADGYDPARLPAQS--PTANLLLPGS-TFLQLEGVGVLKGAKRPALARKFVDFMLSGGVQSDF 290
Cdd:COG0687   210 WSDGAEyiqllasgEVDLAVGWSGDALALRAegPPIAYVIPKEgALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAAL 289

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2674824722 291 PTRMWVYPAVTGTK--LDPVF--GFAQRPDVAQVKASVTANP 328
Cdd:COG0687   290 AEYVGYAPPNKAARelLPPELaaNPAIYPPEEVLDKLEFWNP 331
PBP2_FutA1_ilke cd13542
Substrate binding domain of ferric iron-binding protein, a member of the type 2 periplasmic ...
 21-308 4.15e-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: 66.20  E-value: 4.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  21 TLTVITHDSFDVDKQLVAGFEKANEARVRFVRgGDAGELLNRLILTRRAPVADVVYGLDNSLLARARQAGILEAYRSPAL 100
Cdd:cd13542     1 EVNVYSSRHYNTDKPLYKAFEKETGIKVNVVF-ASADELLERLKAEGANSPADVLLTVDAGRLWEAKEAGLLQPVTSEKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 101 -ARVPAAYRLDEKGLlntvnYGFValNYDRAALARTGLPLP---KTLDDLKKPEYA-RLTVVSSpaTSSPGLAFLLATVN 175
Cdd:cd13542    80 eSNVPANLRDPDGNW-----FGLT--KRARVIVYNKDKVNPeelSTYEDLADPKWKgKVCMRSS--SNSYNQSLVASMIA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 176 HYGEAGAWTWwrearlsglkvTRGWSDAYNKEFSKN-----------GGRFPIVLSYasspaaevYYA---DGYDPARLP 241
Cdd:cd13542   151 HDGEKETKEW-----------LQGWVNNLAREPQGGdrdqakaiaagICDVGIANSY--------YLGrmlNSEDPEEKE 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674824722 242 AQSPtANLLLP----GSTFLQLEGVGVLKGAKRPALARKFVDFMLSGGVQSDFPTRMWVYPAVTGTKLDPV 308
Cdd:cd13542   212 VAEP-VGVFFPnqdnRGTHVNISGIGVTKYAKNKENAIKFLEFLVSEPAQKLYAGGNYEYPVNPGVELSEL 281
PBP2_Fbp_like_6 cd13552
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 26-298 2.40e-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: 270270 [Multi-domain]  Cd Length: 266  Bit Score: 63.24  E-value: 2.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  26 THDSfDVDKQLVAGFEKANEARVRFVRGGdAGELLNRLILTRRAPVADVVYGLDNSLLARARQAGILEAYRSPALARVPA 105
Cdd:cd13552     7 THGK-EMLEYVEDAFEEKTGVEVEWLNMG-SQELLDRVRAEKENPQADVWWGGPSQLFMQLKEEGLLEPTEPSWAEKVAA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 106 AYRlDEKGLLNTVNYGFVALNYDRAALarTGLPLPKTLDDLKKPEYARLTVVSSPATSSPGLAFLLATVNHYGEAG---- 181
Cdd:cd13552    85 EFK-DADGYWYGTIQTPEVIMYNTELL--SEEEAPKDWDDLLDPKWKDKIIIRNPLASGTMRTIFAALIQRELKGTgsld 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 182 -AWTWwrearLSGLkvtrgwsDAYNKEFSKNG-------GRFPIVLSYASSPAAevyyADGYDPARLPAQsptanLLLPG 253
Cdd:cd13552   162 aGYAW-----LKKL-------DANTKEYAASPtmlylkiGRGEAAISLWNLNDV----LDQRENNKMPFG-----FIDPA 220

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2674824722 254 STFLQL-EGVGVLKGAKRPALARKFVDFMLSGGVQSDFPTRMWVYP 298
Cdd:cd13552   221 SGAPVItDGIALIKGAPHPEAAKAFYEFVGSAEIQALLAEKFNRMP 266
PBP2_Fbp_like_3 cd13549
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 56-283 3.07e-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: 270267 [Multi-domain]  Cd Length: 263  Bit Score: 62.85  E-value: 3.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  56 AGELLNRLILTRRAPVADVVYGLDNSLLaRARQAGILEAYRSPALARVPAAYRlDEKGLLNTVNYGFVALNYDRAALArt 135
Cdd:cd13549    36 SGQALAALIAERARPVADVAYYGVAFGI-QAVAQGVVQPYKPAHWDEIPEGLK-DPDGKWFAIHSGTLGFIVNVDALG-- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 136 GLPLPKTLDDLKKPEYARLTVVSSPatSSPGLAFLLATVNHYGEAGAWTWWREARLsglkvtrgwsdaYNKEFSKNGGRF 215
Cdd:cd13549   112 GKPVPKSWADLLKPEYKGMVGYLDP--RSAFVGYVGAVAVNQAMGGSLDNFGPGID------------YFKKLHKNGPIV 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674824722 216 PIVLSYASSPAAEV-----YYADGYDpARLPAQSPTANLLLPGSTFLQLEGVGVLKGAKRPALARKFVDFMLS 283
Cdd:cd13549   178 PKQTAYARVLSGEIpilidYDFNAYR-AKYTDKANVAFVIPKEGSVVVPYVMSLVKNAPNPNNGKKVLDFIMS 249
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 40-298 1.64e-10

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: 60.70  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  40 FEKANEARVRFVRGGDAgELLNRLILTRRAPVADVVYgLDNSLLARARQAGILE-----AYRSPALARVPAAYRlDEKGL 114
Cdd:cd13589    23 FEKETGIKVVYDTGTSA-DRLAKLQAQAGNPQWDVVD-LDDGDAARAIAEGLLEpldysKIPNAAKDKAPAALK-TGYGV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 115 LNTVN-YGFValnYDRAALartglPLPKTLDDLKKPEYARLTVVSSPATSSPGLAF----LLATVNHYGE--AGAWtwwr 187
Cdd:cd13589   100 GYTLYsTGIA---YNTDKF-----KEPPTSWWLADFWDVGKFPGPRILNTSGLALLeaalLADGVDPYPLdvDRAF---- 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 188 eARLSGLKvtrgwsdaynkefsknggrfPIVLSYASSPAA--------EVYYADGYD--PARLPAQSPTANLLLPGS-TF 256
Cdd:cd13589   168 -AKLKELK--------------------PNVVTWWTSGAQlaqllqsgEVDMAPAWNgrAQALIDAGAPVAFVWPKEgAI 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2674824722 257 LQLEGVGVLKGAKRPALARKFVDFMLSGGVQSDFPTRMWVYP 298
Cdd:cd13589   227 LGPDTLAIVKGAPNKELAMKFINFALSPEVQAALAEALGYGP 268
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-304 8.27e-10

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 59.29  E-value: 8.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722   1 MRRLILLTALAL-------------GTHATAQTTLTVITHDSFDVD--KQLVAGFEKAN---EARVRFVRGGDAGELLNR 62
Cdd:COG1653     1 MRRLALALAAALalalaacggggsgAAAAAGKVTLTVWHTGGGEAAalEALIKEFEAEHpgiKVEVESVPYDDYRTKLLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  63 LILTRRAPvaDVVYgLDNSLLARARQAGILEAyrspaLARVPAAYRLDEK----GLLNTVNYG-----------FVALNY 127
Cdd:COG1653    81 ALAAGNAP--DVVQ-VDSGWLAEFAAAGALVP-----LDDLLDDDGLDKDdflpGALDAGTYDgklygvpfntdTLGLYY 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 128 DRAALARTGLPLPKTLDDLKkpEYAR-LT-------VVSSPATSSPGLAFLLA----TVNHYGEAG--------AWTWWR 187
Cdd:COG1653   153 NKDLFEKAGLDPPKTWDELL--AAAKkLKakdgvygFALGGKDGAAWLDLLLSaggdLYDEDGKPAfdspeaveALEFLK 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 188 EARLSGL----KVTRGWSDAYNkEFSKngGRFPIVL--SYASSPAAEVYYADGYDPARLPAQSPTAnlllPGSTFLQLEG 261
Cdd:COG1653   231 DLVKDGYvppgALGTDWDDARA-AFAS--GKAAMMIngSWALGALKDAAPDFDVGVAPLPGGPGGK----KPASVLGGSG 303

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2674824722 262 VGVLKGAKRPALARKFVDFMLSGGVQSDFPTrmwVYPAVTGTK 304
Cdd:COG1653   304 LAIPKGSKNPEAAWKFLKFLTSPEAQAKWDA---LQAVLLGQK 343
PBP2_Fbp_like_4 cd13550
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 54-298 5.85e-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: 270268 [Multi-domain]  Cd Length: 265  Bit Score: 56.00  E-value: 5.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  54 GDAGELLNRLILTRRAPVADVVYGLDNSLLARARQAGILEAYRSPALARVPAAYRLDEKgllntvnyGFVALN-YDRAAL 132
Cdd:cd13550    33 GSNSAIANQLIEEQSNPQADVFISNDVGALGKLSENGVLQPYTPAGPELIPADGRAEDN--------TWVALTaRARVIM 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 133 ARTGL----PLPKTLDDLKKPEYArlTVVSSPATSSPGLAFLLATVNH-YGEAGAWTWWREARLSGLKVTRGWSDAyNKE 207
Cdd:cd13550   105 YNKDLipeeELPKSIEDLTDPKWK--GQVAAANSTNGSMQGQVSAMRQlLGDEKTEEWIKGLMANEVTFLGGHTDV-RKA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 208 FSKNGGRFPIVLSY-------ASSPAAEVYYADGYDPArlpaqsptanlllpgSTFLQLEGVGVLKGAKRPALARKFVDF 280
Cdd:cd13550   182 VGAGEFKLGLVNHYyyhlqlaEGSPVGVIYPDQGEGQM---------------GVVTNAAGVGLVKGGPNPTNAQAFLDF 246

                         250
                  ....*....|....*...
gi 2674824722 281 MLSGGVQSDFPTRMWVYP 298
Cdd:cd13550   247 LLLPENQRIFAEENYEYP 264
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 34-287 7.20e-06

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: 47.03  E-value: 7.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  34 KQLVAGFEKAN---EARVRFVrGGDAGELLNRLILTRRAPVADVVYGlDNSLLARARQAGILEAYRSPAlarVPAAYRLD 110
Cdd:pfam01547  11 QALVKEFEKEHpgiKVEVESV-GSGSLAQKLTTAIAAGDGPADVFAS-DNDWIAELAKAGLLLPLDDYV---ANYLVLGV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 111 EKGLLNTVNYGFVALNYDRAALARTGLPLPKTLDDL----KKPEYARLTVVSSPATSSPGLAFLLATvNHYGEAGAWTWW 186
Cdd:pfam01547  86 PKLYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELleaaKKLKEKGKSPGGAGGGDASGTLGYFTL-ALLASLGGPLFD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 187 REARLSGLKVTRGWSDAYNKEFSK------------------------NGGRFPIVLSYASSPAAEVYYADGYDPA---- 238
Cdd:pfam01547 165 KDGGGLDNPEAVDAITYYVDLYAKvlllkklknpgvagadgrealalfEQGKAAMGIVGPWAALAANKVKLKVAFAapap 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2674824722 239 RLPAQSPTANLLLPGSTFLQLEGVGVLKGAKRPALARKFVDFMLSGGVQ 287
Cdd:pfam01547 245 DPKGDVGYAPLPAGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQ 293
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 34-283 1.04e-04

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


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 43.02  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  34 KQLVAGFEKANEARVRfVRGGDAGELLNRLILTRRApvaDVVYGLDNSLLARARQAGILEAYRSPALARVPAAyrldekg 113
Cdd:pfam13531  13 RELAAAFEAETGVKVV-VSYGGSGKLAKQIANGAPA---DVFISADSAWLDKLAAAGLVVPGSRVPLAYSPLV------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 114 llntvnygfvalnydraALARTGLPL-PKTLDDLKKPEYaRLtVVSSPATSSPGLAFLLAtvnhygeAGAWTWWREARLS 192
Cdd:pfam13531  82 -----------------IAVPKGNPKdISGLADLLKPGV-RL-AVADPKTAPSGRAALEL-------LEKAGLLKALEKK 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 193 GLKvtrgwsdaynkeFSKNGGRfpiVLSYASSPAAE---VYYADGYDPARLPaqsPTANLLLPGSTFLQLE-GVGVLKGA 268
Cdd:pfam13531 136 VVV------------LGENVRQ---ALTAVASGEADagiVYLSEALFPENGP---GLEVVPLPEDLNLPLDyPAAVLKKA 197

                         250
                  ....*....|....*
gi 2674824722 269 KRPALARKFVDFMLS 283
Cdd:pfam13531 198 AHPEAARAFLDFLLS 212
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 32-301 3.21e-03

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: 38.82  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722  32 VDKQLVAGFEKANEARVRFVRGGDAGELLNRLiltrRAP--VADVVYgLDNSLLARARQAGILEAY---RSPALARVPAA 106
Cdd:cd13588    11 ADPDWVTAFEEATGCKVVVKFFGSEDEMVAKL----RSGggDYDVVT-PSGDALLRLIAAGLVQPIdtsKIPNYANIDPR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 107 YRldeKGLLNTVN---------YGFVALNYDRAALARtglPLPKTLDDLKKPEYA-RLTVVSSPATSsPGLAFLLATVNH 176
Cdd:cd13588    86 LR---NLPWLTVDgkvygvpydWGANGLAYNTKKVKT---PPTSWLALLWDPKYKgRVAARDDPIDA-IADAALYLGQDP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674824722 177 YGE------AGAWTWWREARlsGLkVTRGWSDA--YNKEFSKNGgrfpIVLSYASSPAAEVYYADGYDPA-RLPAQSPTA 247
Cdd:cd13588   159 PFNltdeqlDAVKAKLREQR--PL-VRKYWSDGaeLVQLFANGE----VVAATAWSGQVNALQKAGKPVAyVIPKEGATG 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2674824722 248 nlllpgstflQLEGVGVLKGAKRPALARKFVDFMLSGGVQSDFPtrMWVYPAVT 301
Cdd:cd13588   232 ----------WVDTWMILKDAKNPDCAYKWLNYMLSPKVQAAVA--EWTGYAPS 273
 
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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