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Conserved domains on  [gi|504340041|ref|WP_014527143|]
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putative 2-aminoethylphosphonate ABC transporter substrate-binding protein [Sinorhizobium meliloti]

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 ...
9-337 0e+00

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 TIGR03261:

Pssm-ID: 473866 [Multi-domain]  Cd Length: 334  Bit Score: 529.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041    9 GAGTALILASSAAYAETELTVYTSIEAVDLDRYKETFKKAHPDIKINWVRDSTGVMTAKLLAEKDNPQADVVWGVAATSL 88
Cdd:TIGR03261   6 FIMTSLFFSACNSKANTELTVYTAIEDELIAKYKDAFEKVNPDIKINWVRDSTGIITAKLLAEKNNPQADVVWGLAASSL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041   89 LLLKSEGMLEPYSPKNVEALDPRFVDGDKPPSWVGMDAYVAALCYNTVEAGKLGLTPPTSWKDLTKPEYKGHVVMPNPNS 168
Cdd:TIGR03261  86 ALLDKEGMLKPYKPKGLDALNPKFRDAKNPPHWVGMDAWMAAICFNTVEAKKKGLPKPTSWEDLTKPEYKGHIVMPNPAS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  169 SGTGFLDVSAWLQTFGEEEAWSFMDALHENIAAYTHSGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSEGSG 248
Cdd:TIGR03261 166 SGTGFLDVSAWLQMMGEDKGWDYMDKLHKNIAVYTHSGSKPCKLAGMGEFPIGISMAYRALKEKKKGAPIDVVFPKEGLG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  249 WEAEATAIIAGTANLEAAKTLVDWSISKEANEMYNVGYAVVAYPGVAKPIENLPDDVADKMIKNDFEWAANNRARILKEW 328
Cdd:TIGR03261 246 WDIEATAIIKGSKNNDAAKKLVDWSISDEAMELYAKNYAVVATPGVAKPDAGFPKNVEDLLIKNDFVWAAANRDKILEEW 325

                  ....*....
gi 504340041  329 QKRYDAKSE 337
Cdd:TIGR03261 326 SKRYGAKAE 334
 
Name Accession Description Interval E-value
phnS2 TIGR03261
putative 2-aminoethylphosphonate ABC transporter, periplasmic 2-aminoethylphosphonate-binding ...
9-337 0e+00

putative 2-aminoethylphosphonate ABC transporter, periplasmic 2-aminoethylphosphonate-binding protein; This ABC transporter extracellular solute-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274494 [Multi-domain]  Cd Length: 334  Bit Score: 529.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041    9 GAGTALILASSAAYAETELTVYTSIEAVDLDRYKETFKKAHPDIKINWVRDSTGVMTAKLLAEKDNPQADVVWGVAATSL 88
Cdd:TIGR03261   6 FIMTSLFFSACNSKANTELTVYTAIEDELIAKYKDAFEKVNPDIKINWVRDSTGIITAKLLAEKNNPQADVVWGLAASSL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041   89 LLLKSEGMLEPYSPKNVEALDPRFVDGDKPPSWVGMDAYVAALCYNTVEAGKLGLTPPTSWKDLTKPEYKGHVVMPNPNS 168
Cdd:TIGR03261  86 ALLDKEGMLKPYKPKGLDALNPKFRDAKNPPHWVGMDAWMAAICFNTVEAKKKGLPKPTSWEDLTKPEYKGHIVMPNPAS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  169 SGTGFLDVSAWLQTFGEEEAWSFMDALHENIAAYTHSGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSEGSG 248
Cdd:TIGR03261 166 SGTGFLDVSAWLQMMGEDKGWDYMDKLHKNIAVYTHSGSKPCKLAGMGEFPIGISMAYRALKEKKKGAPIDVVFPKEGLG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  249 WEAEATAIIAGTANLEAAKTLVDWSISKEANEMYNVGYAVVAYPGVAKPIENLPDDVADKMIKNDFEWAANNRARILKEW 328
Cdd:TIGR03261 246 WDIEATAIIKGSKNNDAAKKLVDWSISDEAMELYAKNYAVVATPGVAKPDAGFPKNVEDLLIKNDFVWAAANRDKILEEW 325

                  ....*....
gi 504340041  329 QKRYDAKSE 337
Cdd:TIGR03261 326 SKRYGAKAE 334
PBP2_Fbp_like_1 cd13544
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ...
26-319 3.21e-138

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: 393.89  E-value: 3.21e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  26 ELTVYTSIEAVDLDRYKETFKKAHPdIKINWVRDSTGVMTAKLLAEKDNPQADVVWGVAATSLLLLKSEGMLEPYSPKNV 105
Cdd:cd13544    1 ELTVYTSLEEEEAKAILEAFKKDTG-IKVEFVRLSTGEALARLEAEKGNPQADVWFGGTADAHIQAKKEGLLEPYKSPNA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 106 EALDPRFVDgdKPPSWVGMDAYVAALCYNTVEAGKLGLTPPTSWKDLTKPEYKGHVVMPNPNSSGTGFLDVSAWLQTFGE 185
Cdd:cd13544   80 DKIPAKFKD--PDGYWTGIYLGPLGFGVNTDELKEKGLPVPKSWEDLLNPEYKGEIVMPNPASSGTAYTFLASLIQLMGE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 186 EEAWSFMDALHENIAAYTHSGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSEGSGWEAEATAIIAGTANLEA 265
Cdd:cd13544  158 DEAWEYLKKLNKNVGQYTKSGSAPAKLVASGEAAIGISFLHDALKLKEQGYPIKIIFPKEGTGYEIEAVAIIKGAKNPEA 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504340041 266 AKTLVDWSISKEANEMY--NVGYAVVAYPGvAKPIENLPDDVADKMIKNDFEWAAN 319
Cdd:cd13544  238 AKAFIDWALSKEAQELLakVGSYAIPTNPD-AKPPEIAPDLKKDKLIKYDFEWAGE 292
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
41-332 4.49e-97

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 289.14  E-value: 4.49e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  41 YKETFKKAHpDIKINWVRDSTGVMTAKLLAEKDNPQADVVWGVAATSLLLLKSEGMLEPYSPKNVEALDPRFVDGDKppS 120
Cdd:COG1840    1 LLEAFEKKT-GIKVNVVRGGSGELLARLKAEGGNPPADVVWSGDADALEQLANEGLLQPYKSPELDAIPAEFRDPDG--Y 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 121 WVGMDAYVAALCYNTVEAGKLGltPPTSWKDLTKPEYKGHVVMPNPNSSGTGFLDVSAWLQTFGEEEAWSFMDALHENIA 200
Cdd:COG1840   78 WFGFSVRARVIVYNTDLLKELG--VPKSWEDLLDPEYKGKIAMADPSSSGTGYLLVAALLQAFGEEKGWEWLKGLAANGA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 201 AYTHSGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSEGSGWEAEATAIIAGTANLEAAKTLVDWSISKEANE 280
Cdd:COG1840  156 RVTGSSSAVAKAVASGEVAIGIVNSYYALRAKAKGAPVEVVFPEDGTLVNPSGAAILKGAPNPEAAKLFIDFLLSDEGQE 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504340041 281 MY-NVGYAVVAYPGVAKPiENLPDDVADKMIKNDfEWAANNRARILKEWQKRY 332
Cdd:COG1840  236 LLaEEGYEYPVRPDVEPP-EGLPPLGELKLIDDD-DKAAENREELLELWDEAV 286
SBP_bac_6 pfam13343
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
91-314 6.67e-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: 6.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041   91 LKSEGMLEPYSPKNVEALDPRF-----VDGDKppSWVGMDAYVAALCYNTVEAGKLGLtpPTSWKDLTKPEYKGHVVMPN 165
Cdd:pfam13343  23 FIEEGLFQPLDSANLPNVPKDFddeglRDPDG--YYTPYGVGPLVIAYNKERLGGRPV--PRSWADLLDPEYKGKVALPG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  166 PNSSGTGFLDVSAWLQTFGEEEAWSFMDALHENIAAYThsGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSE 245
Cdd:pfam13343  99 PNVGDLFNALLLALYKDFGEDGVRKLARNLKANLHPAQ--MVKAAGRLESGEPAVYLMPYFFADILPRKKKNVEVVWPED 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504340041  246 GSgwEAEATAIIAGTANLEAAKTLVDWSISKEANEM---YNVGYAVVAYPGVAkpiENLPDDVADKMIKNDF 314
Cdd:pfam13343 177 GA--LVSPIFMLVKKGKKELADPLIDFLLSPEVQAIlakAGLVFPVVLNPAVD---NPLPEGAPFKWLGWDY 243
PRK15046 PRK15046
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
3-280 1.07e-19

2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional


Pssm-ID: 237887 [Multi-domain]  Cd Length: 349  Bit Score: 88.59  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041   3 FSKIFLGAGTALILASSAAYAETE-LTVYTsieAVDL-DRYKETFKK--AHPDIKINWVRDSTGVMTAKLLAEKDNPQAD 78
Cdd:PRK15046  12 AMKLAAAAAAAAFGGGAAPAWAADaVTVYS---ADGLeDWYQDVFPAftKATGIKVNYVEAGSGEVVNRAAKEKSNPQAD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  79 VVWGV------AAtsllllkSEGMLEPYSPKNVEALDPRFVDGDKppSWVGMDAYVAALCYNTveagKLGLTPPTSWKDL 152
Cdd:PRK15046  89 VLVTLppfiqqAA-------AEGLLQPYSSVNAKAVPAIAKDADG--TYAPFVNNYLSFIYNP----KVLKTAPATWADL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 153 TKPEYKGHVVMPNPNSSGTGFLDVSAWLQTFGEEEAWSFMDALHENIAAYTHSGSKPCKMAASGE-TVIGVSFEFPGAKA 231
Cdd:PRK15046 156 LDPKFKGKLQYSTPGQAGDGTAVLLLTFHLMGKDKAFDYLAKLQANNVGPSKSTGKLTPLVSKGEiYVANGDLQMNLAQA 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504340041 232 KTSGAPIDIIFPSEGSGweaEATAI--------IAGTANLEAAKTLVDWSISKEANE 280
Cdd:PRK15046 236 EHGGPNVKIFFPAKDGG---ERSTFalpyviglVKGAPNSENGKKLIDFLLSKEAQT 289
 
Name Accession Description Interval E-value
phnS2 TIGR03261
putative 2-aminoethylphosphonate ABC transporter, periplasmic 2-aminoethylphosphonate-binding ...
9-337 0e+00

putative 2-aminoethylphosphonate ABC transporter, periplasmic 2-aminoethylphosphonate-binding protein; This ABC transporter extracellular solute-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274494 [Multi-domain]  Cd Length: 334  Bit Score: 529.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041    9 GAGTALILASSAAYAETELTVYTSIEAVDLDRYKETFKKAHPDIKINWVRDSTGVMTAKLLAEKDNPQADVVWGVAATSL 88
Cdd:TIGR03261   6 FIMTSLFFSACNSKANTELTVYTAIEDELIAKYKDAFEKVNPDIKINWVRDSTGIITAKLLAEKNNPQADVVWGLAASSL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041   89 LLLKSEGMLEPYSPKNVEALDPRFVDGDKPPSWVGMDAYVAALCYNTVEAGKLGLTPPTSWKDLTKPEYKGHVVMPNPNS 168
Cdd:TIGR03261  86 ALLDKEGMLKPYKPKGLDALNPKFRDAKNPPHWVGMDAWMAAICFNTVEAKKKGLPKPTSWEDLTKPEYKGHIVMPNPAS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  169 SGTGFLDVSAWLQTFGEEEAWSFMDALHENIAAYTHSGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSEGSG 248
Cdd:TIGR03261 166 SGTGFLDVSAWLQMMGEDKGWDYMDKLHKNIAVYTHSGSKPCKLAGMGEFPIGISMAYRALKEKKKGAPIDVVFPKEGLG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  249 WEAEATAIIAGTANLEAAKTLVDWSISKEANEMYNVGYAVVAYPGVAKPIENLPDDVADKMIKNDFEWAANNRARILKEW 328
Cdd:TIGR03261 246 WDIEATAIIKGSKNNDAAKKLVDWSISDEAMELYAKNYAVVATPGVAKPDAGFPKNVEDLLIKNDFVWAAANRDKILEEW 325

                  ....*....
gi 504340041  329 QKRYDAKSE 337
Cdd:TIGR03261 326 SKRYGAKAE 334
PBP2_Fbp_like_1 cd13544
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ...
26-319 3.21e-138

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: 393.89  E-value: 3.21e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  26 ELTVYTSIEAVDLDRYKETFKKAHPdIKINWVRDSTGVMTAKLLAEKDNPQADVVWGVAATSLLLLKSEGMLEPYSPKNV 105
Cdd:cd13544    1 ELTVYTSLEEEEAKAILEAFKKDTG-IKVEFVRLSTGEALARLEAEKGNPQADVWFGGTADAHIQAKKEGLLEPYKSPNA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 106 EALDPRFVDgdKPPSWVGMDAYVAALCYNTVEAGKLGLTPPTSWKDLTKPEYKGHVVMPNPNSSGTGFLDVSAWLQTFGE 185
Cdd:cd13544   80 DKIPAKFKD--PDGYWTGIYLGPLGFGVNTDELKEKGLPVPKSWEDLLNPEYKGEIVMPNPASSGTAYTFLASLIQLMGE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 186 EEAWSFMDALHENIAAYTHSGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSEGSGWEAEATAIIAGTANLEA 265
Cdd:cd13544  158 DEAWEYLKKLNKNVGQYTKSGSAPAKLVASGEAAIGISFLHDALKLKEQGYPIKIIFPKEGTGYEIEAVAIIKGAKNPEA 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504340041 266 AKTLVDWSISKEANEMY--NVGYAVVAYPGvAKPIENLPDDVADKMIKNDFEWAAN 319
Cdd:cd13544  238 AKAFIDWALSKEAQELLakVGSYAIPTNPD-AKPPEIAPDLKKDKLIKYDFEWAGE 292
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
41-332 4.49e-97

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 289.14  E-value: 4.49e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  41 YKETFKKAHpDIKINWVRDSTGVMTAKLLAEKDNPQADVVWGVAATSLLLLKSEGMLEPYSPKNVEALDPRFVDGDKppS 120
Cdd:COG1840    1 LLEAFEKKT-GIKVNVVRGGSGELLARLKAEGGNPPADVVWSGDADALEQLANEGLLQPYKSPELDAIPAEFRDPDG--Y 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 121 WVGMDAYVAALCYNTVEAGKLGltPPTSWKDLTKPEYKGHVVMPNPNSSGTGFLDVSAWLQTFGEEEAWSFMDALHENIA 200
Cdd:COG1840   78 WFGFSVRARVIVYNTDLLKELG--VPKSWEDLLDPEYKGKIAMADPSSSGTGYLLVAALLQAFGEEKGWEWLKGLAANGA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 201 AYTHSGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSEGSGWEAEATAIIAGTANLEAAKTLVDWSISKEANE 280
Cdd:COG1840  156 RVTGSSSAVAKAVASGEVAIGIVNSYYALRAKAKGAPVEVVFPEDGTLVNPSGAAILKGAPNPEAAKLFIDFLLSDEGQE 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504340041 281 MY-NVGYAVVAYPGVAKPiENLPDDVADKMIKNDfEWAANNRARILKEWQKRY 332
Cdd:COG1840  236 LLaEEGYEYPVRPDVEPP-EGLPPLGELKLIDDD-DKAAENREELLELWDEAV 286
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
26-280 1.06e-73

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: 228.34  E-value: 1.06e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  26 ELTVYTSIEAVDLDRYKETFKKAhPDIKINWVRDSTGVMTAKLLAEKDNPQADVVWGVAATSLLLLKSEGMLEPYSPKNV 105
Cdd:cd13518    1 ELVVYTASDRDFAEPVLKAFEEK-TGIKVKAVYDGTGELANRLIAEKNNPQADVFWGGEIIALEALKEEGLLEPYTPKVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 106 EALDPRFVDGDKppSWVGMDAYVAALCYNTVEAGKLGLtpPTSWKDLTKPEYKGHVVMPNPNSSGTGFLDVSAWLQTFGE 185
Cdd:cd13518   80 EAIPADYRDPDG--YWVGFAARARVFIYNTDKLKEPDL--PKSWDDLLDPKWKGKIVYPTPLRSGTGLTHVAALLQLMGE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 186 EEAWSFMDALHENIAAYTHSGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSEGSGWEAEATAIIAGTANLEA 265
Cdd:cd13518  156 EKGGWYLLKLLANNGKPVAGNSDAYDLVAKGEVAVGLTDTYYAARAAAKGEPVEIVYPDQGALVIPEGVALLKGAPNPEA 235
                        250
                 ....*....|....*
gi 504340041 266 AKTLVDWSISKEANE 280
Cdd:cd13518  236 AKKFIDFLLSPEGQK 250
PBP2_Fbp_like_2 cd13547
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
27-281 6.05e-62

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: 198.22  E-value: 6.05e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  27 LTVYTSIEAVDLDRYKETFKKAHPDIKINWVRDSTGVMTAKLLAEK--DNPQADVVWGVAATSLLLLKSEGMLEPYSPKN 104
Cdd:cd13547    2 LVVYTSMPEDLANALVEAFEKKYPGVKVEVFRAGTGKLMAKLAAEAeaGNPQADVLWVADPPTAEALKKEGLLLPYKSPE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 105 VEALDPRFVDGDKppSWVGMDAYVAALCYNTveaGKLGLTPPTSWKDLTKPEYKGHVVMPNPNSSGTGFLDVSAWLQTFG 184
Cdd:cd13547   82 ADAIPAPFYDKDG--YYYGTRLSAMGIAYNT---DKVPEEAPKSWADLTKPKYKGQIVMPDPLYSGAALDLVAALADKYG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 185 eeEAWSFMDALHENIAAYTHSGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSEGSGWEAEATAIIAGTANLE 264
Cdd:cd13547  157 --LGWEYFEKLKENGVKVEGGNGQVLDAVASGERPAGVGVDYNALRAKEKGSPLEVIYPEEGTVVIPSPIAILKGSKNPE 234
                        250
                 ....*....|....*..
gi 504340041 265 AAKTLVDWSISKEANEM 281
Cdd:cd13547  235 AAKAFVDFLLSPEGQEL 251
PBP2_BitB cd13546
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ...
26-284 3.49e-59

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: 191.32  E-value: 3.49e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  26 ELTVYTSIEAVDLDRYKETFKKAhPDIKINWVRDSTGVMTAKLLAEKDNPQADVVWGVAATSLLllKSEGMLEPYSPKNV 105
Cdd:cd13546    1 TLVVYSPNSEEIIEPIIKEFEEK-PGIKVEVVTGGTGELLARIKAEADNPQADVMWGGGIETLE--AYKDLFEPYESPEA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 106 EALDPRFVDGDKppSWVGMDAYVAALCYNTVEAGKLGltPPTSWKDLTKPEYKGHVVMPNPNSSGTGFLDVSAWLQTFGE 185
Cdd:cd13546   78 AAIPDAYKSPEG--LWTGFSVLPVVLMVNTDLVKNIG--APKGWKDLLDPKWKGKIAFADPNKSGSAYTILYTILKLYGG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 186 eeAWSFMDALHENIAAYTHSGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSEGSGWEAEATAIIAGTANLEA 265
Cdd:cd13546  154 --AWEYIEKLLDNLGVILSSSSAVYKAVADGEYAVGLTYEDAAYKYVAGGAPVKIVYPKEGTTAVPDGVAIVKGAKNPEN 231
                        250
                 ....*....|....*....
gi 504340041 266 AKTLVDWSISKEANEMYNV 284
Cdd:cd13546  232 AKKFIDFLLSKEVQEILVE 250
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
8-330 4.53e-37

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 136.19  E-value: 4.53e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041   8 LGAGTALILASSAAYAETELTVYTSIEAVDlDRYKETFKKAHpDIKINW-VRDSTGVMTAKLLAekDNPQADVVWgVAAT 86
Cdd:COG0687   12 AALAAALAGGAPAAAAEGTLNVYNWGGYID-PDVLEPFEKET-GIKVVYdTYDSNEEMLAKLRA--GGSGYDVVV-PSDY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  87 SLLLLKSEGMLEPYSP---KNVEALDPRFVDGDKPP---SWVGMDAYVAALCYNTVEAGKlgltPPTSWKDLTKPEYKGH 160
Cdd:COG0687   87 FVARLIKAGLLQPLDKsklPNLANLDPRFKDPPFDPgnvYGVPYTWGTTGIAYNTDKVKE----PPTSWADLWDPEYKGK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 161 VVMPNpnsSGTGFLDVSawLQTFGE----------EEAWSFMDALHENIAAYTHSGSKPCKMAASGETVIGVSFEFPGAK 230
Cdd:COG0687  163 VALLD---DPREVLGAA--LLYLGYdpnstdpadlDAAFELLIELKPNVRAFWSDGAEYIQLLASGEVDLAVGWSGDALA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 231 AKTSGAPIDIIFPSEGSGWEAEATAIIAGTANLEAAKTLVDWSISKEANEMY--NVGYAvvayPGVAKPIENLPDDVADK 308
Cdd:COG0687  238 LRAEGPPIAYVIPKEGALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAALaeYVGYA----PPNKAARELLPPELAAN 313
                        330       340       350
                 ....*....|....*....|....*....|...
gi 504340041 309 --------MIKNDFEWAA---NNRARILKEWQK 330
Cdd:COG0687  314 paiyppeeVLDKLEFWNPlppENRELYTRRWTE 346
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
43-282 2.85e-29

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: 113.09  E-value: 2.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  43 ETFKKAHPdIKINWVRDSTGVMTAKLLAEKDNPQADVVWgVAATSLLLLKSEGMLEPYSPKNVEALDPRFV-DGDKPPSW 121
Cdd:cd13589   21 EPFEKETG-IKVVYDTGTSADRLAKLQAQAGNPQWDVVD-LDDGDAARAIAEGLLEPLDYSKIPNAAKDKApAALKTGYG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 122 VGMDAYVAALCYNTvEAGKlglTPPTSWkDLTKPEYKGHVVMPNP-NSSGTGFLDVSAWLQTFGEEE-----AWSFMDAL 195
Cdd:cd13589   99 VGYTLYSTGIAYNT-DKFK---EPPTSW-WLADFWDVGKFPGPRIlNTSGLALLEAALLADGVDPYPldvdrAFAKLKEL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 196 HENIAAYTHSGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSEGSGWEAEATAIIAGTANLEAAKTLVDWSIS 275
Cdd:cd13589  174 KPNVVTWWTSGAQLAQLLQSGEVDMAPAWNGRAQALIDAGAPVAFVWPKEGAILGPDTLAIVKGAPNKELAMKFINFALS 253

                 ....*..
gi 504340041 276 KEANEMY 282
Cdd:cd13589  254 PEVQAAL 260
TbpA COG4143
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ...
1-329 4.15e-29

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


Pssm-ID: 443315 [Multi-domain]  Cd Length: 343  Bit Score: 114.56  E-value: 4.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041   1 MPFSKIFLGAGTALILA-----SSAAYAETELTVYT--SIEAVDL--DRYKETFKKAHpDIKINWVR-DSTGVMTAKLLA 70
Cdd:COG4143    1 MKRRTFLLAAALALALAlagcsGAAAAAKPTLTVYTydSFASEWGpgPWLKAAFEAEC-GCTLEFVApGDGGELLNRLRL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  71 EKDNPQADVVWGVAATSLLLLKSEGMLEPYSPKNVEALDPRF-VDGDK---PPSWvgmdAYVAaLCYNTveaGKLgLTPP 146
Cdd:COG4143   80 EGANPKADVVLGLDNNLLARALDTGLFAPHGVDALDALALPLaWDPDDrfvPYDY----GYFA-FVYDK---TKL-LNPP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 147 TSWKDLTKPEYKGHVVMPNPNSS--GTGFLdvsAWLQ-TFGEEEAWSFMDALHENIA--------AYTH--SGSKPckMA 213
Cdd:COG4143  151 ESLEDLVDPEYKDKLVVQDPRTStpGLAFL---LWTIaAYGEDGALDYWQKLADNGVtvtkgwseAYGLflKGEAP--MV 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 214 ASGETVIGVSFEFPGAKAKTSgapidIIFPSEGSGWEAEATAIIAGTANLEAAKTLVDWSISKEANEM---YNVGYAVVa 290
Cdd:COG4143  226 LSYSTSPAYHVIAEGDKDRYA-----AALFDEGHYRQVEGAGVLAGAKNPELARKFLDFLLSPEFQAEiptRNWMYPAV- 299
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 504340041 291 yPGVAkpienLPDD------VADKMIKNDFEWAANNRARILKEWQ 329
Cdd:COG4143  300 -EDVE-----LPEAfdeyapVPEKPLTFDPDEIAANRDAWIDEWQ 338
PBP2_TbpA cd13545
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ...
26-280 6.47e-29

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: 112.39  E-value: 6.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  26 ELTVYT--SIEAVD--LDRYKETFKKAHpDIKINWVR-DSTGVMTAKLLAEKDNPQADVVWGVAATSLLLLKSEGMLEPY 100
Cdd:cd13545    1 TLTVYTydSFVGEWgpGPEVKAEFEKET-GCKVEFVKpGDAGELLNRLILEKNNPRADVVLGLDNNLLSRALKEGLFEPY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 101 SPKNVEALDPRFVDgDKPPSWVGMDAYVAALCYNTveagKLGLTPPTSWKDLTKPEYKGHVVMPNPNSSGTGFLDVSAWL 180
Cdd:cd13545   80 RSPALDVVPEVPVF-DPEDRLIPYDYGYLAFNYDK----KKFKEPPLSLEDLTAPEYKGLIVVQDPRTSSPGLGFLLWTI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 181 QTFGEEEAWSFMDALHENIAAYTHSGSKPCKMAASGETVIGVS-------FEFPGAKAKTSGapidIIFPsEGSGWEAEA 253
Cdd:cd13545  155 AVFGEEGYLEYWKKLKANGVTVTPGWSEAYGLFTTGEAPMVVSyatspayHVYYEKDLRYTA----VIFP-EGHYRQVEG 229
                        250       260
                 ....*....|....*....|....*..
gi 504340041 254 TAIIAGTANLEAAKTLVDWSISKEANE 280
Cdd:cd13545  230 AGILKGAKNPELAKKFVDFLLSPEFQE 256
PBP2_Fbp_like_5 cd13551
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
26-272 3.14e-27

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: 107.87  E-value: 3.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  26 ELTVYTSIEAVDLDRY-KETFKKAHPDIKInwVRDSTGVMTAKLLAEKDNPQADVVWGVAATSLLLLKSEGMLEPYSPKN 104
Cdd:cd13551    1 KLVVYSNSNSNGRGEWiKEQAKKAGFNIKI--VNGGGGDLANRLIAEKNNPVADVVFGLNAVSFERLKKQGLLVPYTPSW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 105 VEALDPRFVDGDK--PPSWVgmDAYVAALCYNTVEAGKlgltPPTSWKDLTKPEYKGHVVMPNpNSSGTGFLDVSAWLQT 182
Cdd:cd13551   79 AGEIPSALSDGDGyyYPLVQ--QPIVLAYNPDTMTDPD----APKSWTDLAKPKYKGKYEVPG-LLGGTGQAILAGILVR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 183 F----GE----EEAWSFMDALHENIaAYTHSGSKPCKMAASGETVIGVSF-EFPGAKAKTSGAPIDIIFPSEGSGWEAEA 253
Cdd:cd13551  152 YldpkGEygvsDEGWQVLEDYFANG-YPAQEGTDFYAPFADGQVPIGYLWsSGLAGIQKQYGVEFKIVDPEIGVPFVTEQ 230
                        250
                 ....*....|....*....
gi 504340041 254 TAIIAGTANLEAAKTLVDW 272
Cdd:cd13551  231 VGIVKGTKKEAEAKAFIDW 249
PBP2_Fbp_like_6 cd13552
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
26-281 1.47e-26

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: 106.00  E-value: 1.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  26 ELTVYTSIEAVDLDRYKETFKKAhPDIKINWVRDSTGVMTAKLLAEKDNPQADVVWGVAATSLLLLKSEGMLEPYSPKNV 105
Cdd:cd13552    1 KVVIYSTHGKEMLEYVEDAFEEK-TGVEVEWLNMGSQELLDRVRAEKENPQADVWWGGPSQLFMQLKEEGLLEPTEPSWA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 106 EALDPRFVDGDKppSWVGMDAYVAALCYNTVEagklgLTP---PTSWKDLTKPEYKGHVVMPNPNSSGTGFLDVSAWLQT 182
Cdd:cd13552   80 EKVAAEFKDADG--YWYGTIQTPEVIMYNTEL-----LSEeeaPKDWDDLLDPKWKDKIIIRNPLASGTMRTIFAALIQR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 183 FGE-----EEAWSFMDALHENIAAYTHSGSKPCKMAASGETVIGVS-FEFPGAKAKTSGAPIDIIFPSEGSGWEAEATAI 256
Cdd:cd13552  153 ELKgtgslDAGYAWLKKLDANTKEYAASPTMLYLKIGRGEAAISLWnLNDVLDQRENNKMPFGFIDPASGAPVITDGIAL 232
                        250       260
                 ....*....|....*....|....*
gi 504340041 257 IAGTANLEAAKTLVDWSISKEANEM 281
Cdd:cd13552  233 IKGAPHPEAAKAFYEFVGSAEIQAL 257
SBP_bac_6 pfam13343
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
91-314 6.67e-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: 6.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041   91 LKSEGMLEPYSPKNVEALDPRF-----VDGDKppSWVGMDAYVAALCYNTVEAGKLGLtpPTSWKDLTKPEYKGHVVMPN 165
Cdd:pfam13343  23 FIEEGLFQPLDSANLPNVPKDFddeglRDPDG--YYTPYGVGPLVIAYNKERLGGRPV--PRSWADLLDPEYKGKVALPG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  166 PNSSGTGFLDVSAWLQTFGEEEAWSFMDALHENIAAYThsGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSE 245
Cdd:pfam13343  99 PNVGDLFNALLLALYKDFGEDGVRKLARNLKANLHPAQ--MVKAAGRLESGEPAVYLMPYFFADILPRKKKNVEVVWPED 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504340041  246 GSgwEAEATAIIAGTANLEAAKTLVDWSISKEANEM---YNVGYAVVAYPGVAkpiENLPDDVADKMIKNDF 314
Cdd:pfam13343 177 GA--LVSPIFMLVKKGKKELADPLIDFLLSPEVQAIlakAGLVFPVVLNPAVD---NPLPEGAPFKWLGWDY 243
PBP2_Fbp_like_3 cd13549
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
41-286 7.87e-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: 270267 [Multi-domain]  Cd Length: 263  Bit Score: 92.90  E-value: 7.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  41 YKETFK--KAHPDIKINWVRDSTGVMTAKLLAEKDNPQADVVWgVAATSLLLLKSEGMLEPYSPKNVEALDPRFVDGDKp 118
Cdd:cd13549   14 WGTQLKafKKRTGIQIPYDNKNSGQALAALIAERARPVADVAY-YGVAFGIQAVAQGVVQPYKPAHWDEIPEGLKDPDG- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 119 pSWVGMDAYVAALCYNTVEAGklGLTPPTSWKDLTKPEYKGHVVMPNPNSSGTGFLDVSAWLQTFGEE-----EAWSFMD 193
Cdd:cd13549   92 -KWFAIHSGTLGFIVNVDALG--GKPVPKSWADLLKPEYKGMVGYLDPRSAFVGYVGAVAVNQAMGGSldnfgPGIDYFK 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 194 ALHENIAAYthSGSKPCKMAASGETVIGVSFEFPGAKAK-TSGAPIDIIFPSEGSGWEAEATAIIAGTANLEAAKTLVDW 272
Cdd:cd13549  169 KLHKNGPIV--PKQTAYARVLSGEIPILIDYDFNAYRAKyTDKANVAFVIPKEGSVVVPYVMSLVKNAPNPNNGKKVLDF 246
                        250
                 ....*....|....
gi 504340041 273 SISKEANEMYNVGY 286
Cdd:cd13549  247 IMSDKGQALWANAY 260
PBP2_Fbp_like_4 cd13550
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
26-282 6.61e-21

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: 90.67  E-value: 6.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  26 ELTVYTS-----IEAVdLDRYKETfkkahPDIKINWVRDSTGVMTAKLLAEKDNPQADVVWGVAATSLLLLKSEGMLEPY 100
Cdd:cd13550    1 ELVVYSGrnealIQPV-LEKFRAD-----TGVEVALKHGSNSAIANQLIEEQSNPQADVFISNDVGALGKLSENGVLQPY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 101 SPKNVEALDPRFVDGDKppSWVGMDAYVAALCYNT--VEAGKLgltpPTSWKDLTKPEYKGHVVMPN-PNSSGTGflDVS 177
Cdd:cd13550   75 TPAGPELIPADGRAEDN--TWVALTARARVIMYNKdlIPEEEL----PKSIEDLTDPKWKGQVAAANsTNGSMQG--QVS 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 178 AWLQTFGEEEAWSFMDALHENIAAYTHSGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSEGSGW-----EAE 252
Cdd:cd13550  147 AMRQLLGDEKTEEWIKGLMANEVTFLGGHTDVRKAVGAGEFKLGLVNHYYYHLQLAEGSPVGVIYPDQGEGQmgvvtNAA 226
                        250       260       270
                 ....*....|....*....|....*....|
gi 504340041 253 ATAIIAGTANLEAAKTLVDWSISKEANEMY 282
Cdd:cd13550  227 GVGLVKGGPNPTNAQAFLDFLLLPENQRIF 256
PRK15046 PRK15046
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
3-280 1.07e-19

2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional


Pssm-ID: 237887 [Multi-domain]  Cd Length: 349  Bit Score: 88.59  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041   3 FSKIFLGAGTALILASSAAYAETE-LTVYTsieAVDL-DRYKETFKK--AHPDIKINWVRDSTGVMTAKLLAEKDNPQAD 78
Cdd:PRK15046  12 AMKLAAAAAAAAFGGGAAPAWAADaVTVYS---ADGLeDWYQDVFPAftKATGIKVNYVEAGSGEVVNRAAKEKSNPQAD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  79 VVWGV------AAtsllllkSEGMLEPYSPKNVEALDPRFVDGDKppSWVGMDAYVAALCYNTveagKLGLTPPTSWKDL 152
Cdd:PRK15046  89 VLVTLppfiqqAA-------AEGLLQPYSSVNAKAVPAIAKDADG--TYAPFVNNYLSFIYNP----KVLKTAPATWADL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 153 TKPEYKGHVVMPNPNSSGTGFLDVSAWLQTFGEEEAWSFMDALHENIAAYTHSGSKPCKMAASGE-TVIGVSFEFPGAKA 231
Cdd:PRK15046 156 LDPKFKGKLQYSTPGQAGDGTAVLLLTFHLMGKDKAFDYLAKLQANNVGPSKSTGKLTPLVSKGEiYVANGDLQMNLAQA 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504340041 232 KTSGAPIDIIFPSEGSGweaEATAI--------IAGTANLEAAKTLVDWSISKEANE 280
Cdd:PRK15046 236 EHGGPNVKIFFPAKDGG---ERSTFalpyviglVKGAPNSENGKKLIDFLLSKEAQT 289
PBP2_Fbp cd13543
Substrate binding domain of ferric iron transporter, a member of the type 2 periplasmic ...
26-302 1.39e-18

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: 84.66  E-value: 1.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  26 ELTVYTSIEAVDLDRYKETFKKAhPDIKINWVRDSTGVMTAKLLAEKDNPQADVVWGVAATSLLLLKSEGMLEPYSPKNV 105
Cdd:cd13543    1 ELTVYSGRHESLVDPLVEAFEQE-TGIKVELRYGDTAELANQLVEEGDASPADVFYAEDAGALGALADAGLLAPLPEDTL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 106 EALDPRFVDGDKppSWVGMDAYVAALCYNTveaGKLGLT-PPTSWKDLTKPEYKGHVVMPNPNSSGTGFldVSAWLQTFG 184
Cdd:cd13543   80 TQVPPRFRSPDG--DWVGVSGRARVVVYNT---DKLSEDdLPKSVLDLAKPEWKGRVGWAPTNGSFQAF--VTAMRVLEG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 185 EEEAWSFMDALHENiAAYTHSGSKPCKMA-ASGETVIGVS-----FEFpgAKAKTSGAPIDIIFPSEGSgweAEATAIIA 258
Cdd:cd13543  153 EEATREWLKGLKAN-GPKAYAKNSAVVEAvNRGEVDAGLInhyywFRL--RAEQGEDAPVALHYFKNGD---PGALVNVS 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504340041 259 GTA------NLEAAKTLVDWSISKEANEMY---NVGYAVVayPGVAKPiENLP 302
Cdd:cd13543  227 GAGvlktskNQAEAQKFLAFLLSKEGQEFLataNFEYPLV--AGVASP-PGLP 276
sfuA TIGR01254
ABC transporter periplasmic binding protein, thiB subfamily; The model describes thiamine ABC ...
24-278 4.77e-17

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: 80.29  E-value: 4.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041   24 ETELTVYTSiEAVDLD-----RYKETFKkAHPDIKINWVR-DSTGVMTAKLLAEKDNPQADVVWGVAATSLLLLKSEGML 97
Cdd:TIGR01254   1 QPVVTVYTY-DSFAADwglgpVVEKAFE-ADCNCKVKFVAlEDAGELLNRLRLEGKNPKADVVLGLDNNLLEAASKTGLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041   98 EPYSPknveALDPRFVDGDKP-PSWVGMDAYVAALCYNTVEAGKlgltPPTSWKDLTKPEYKGHVVMPNPNSS--GTGFL 174
Cdd:TIGR01254  79 APSGV----ALDKVNVPGGWNnATFLPFDYGYVAFVYDKNKLQN----PPQSLKELVEPEQDLLVIYQDPRTSspGLGLL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  175 dvsAWLQT-FGEEEAWSFMDALHENIAAYTHSGSKPCKMAASGETVIGVSFEF-PGAKAKTSG-APIDIIFPSEGSGWEA 251
Cdd:TIGR01254 151 ---LWMQSvYGEDDAPQAWKQLRKKTVTVTKGWSEAYGTFLGGEYDLVLSYATsPAYHVLFEKkDNYAALNFSEGHYLQV 227
                         250       260
                  ....*....|....*....|....*..
gi 504340041  252 EATAIIAGTANLEAAKTLVDWSISKEA 278
Cdd:TIGR01254 228 EGAARLKGAKQPELADKFVQFLLSPAV 254
PBP2_polyamines cd13523
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
59-278 3.07e-13

The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding proteins that function as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270241 [Multi-domain]  Cd Length: 268  Bit Score: 68.62  E-value: 3.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  59 DSTGVMTAKLLAEKDnPQADVVWgVAATSLLLLKSEGMLEPYSPKNVEA---LDPR-------FVDGDK---PPSWVGMd 125
Cdd:cd13523   33 ANSERMIKKLSAGGS-GGFDLVT-PSDSYTSRQLGVGLMQPIDKSLLPSwatLDPHltlaavlTVPGKKygvPYQWGAT- 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 126 ayvaALCYNTveaGKLGLTPPTSWKDLTKPEYKGHVVMPNpnSSGTGFLDVSAWLQTFGEEE--------AWSFMDALHE 197
Cdd:cd13523  110 ----GLVYNT---DKVKAPPKSYAADLDDPKYKGRVSFSD--IPRETFAMALANLGADGNEElypdftdaAAALLKELKP 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 198 NIAAYTHSGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSEGS-GWeAEATAIIAGTANLEAAKTLVDWSISK 276
Cdd:cd13523  181 NVKKYWSNASQPANLLLNGEVVLAMAWLGSGFKLKQAGAPIEFVVPKEGAvGW-LDTFAVPANAPNKDGAYKLLNALLRP 259

                 ..
gi 504340041 277 EA 278
Cdd:cd13523  260 KV 261
PBP2_AEPn_like cd13548
Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member ...
52-278 1.15e-12

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: 67.59  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  52 IKINWVRDSTGVMTAKLLAEKDNPQADVVwgVAATSLLL-LKSEGMLEPYSPKNveALDPRFVDGDKPpSWVGMDAYVAA 130
Cdd:cd13548   27 ITVNYVEAGSGEVVERAAKEKSNPQADVL--VTLPPFIQqAAQMGLLQPYQSDA--AKNPAIIKAEDG-TYAPLVNNYFS 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 131 LCYNTveagKLGLTPPTSWKDLTKPEYKGHVVMPNPNSSGTGFLDVSAWLQTFGEEEAWSFMDALHENIAAYTHSGSKPC 210
Cdd:cd13548  102 FIYNS----AVLKNAPKTFADLLDPKYKGKIQYSTPGQAGDGMAVLLLTTHLMGSDAAFAYLAKLQQNNVGPSASTGKLT 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504340041 211 KMAASGE-TVIGVSFEFPGAKAKTSGAPIDIIFPSEGSGWEAE-----ATAIIAGTANLEAAKTLVDWSISKEA 278
Cdd:cd13548  178 ALVSKGEiSVANGDLQMNLAQMEHANPNKKIFWPAKAGGQRSTfalpyGIGLVKGAPNADNGKKLIDFLLSKEA 251
PBP2_FutA1_ilke cd13542
Substrate binding domain of ferric iron-binding protein, a member of the type 2 periplasmic ...
26-291 1.94e-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: 66.98  E-value: 1.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  26 ELTVYTSIEaVDLDR--YKEtFKKAhPDIKINWVRDSTGVMTAKLLAEKDNPQADVVWGVAATSLLLLKSEGMLEPYSPK 103
Cdd:cd13542    1 EVNVYSSRH-YNTDKplYKA-FEKE-TGIKVNVVFASADELLERLKAEGANSPADVLLTVDAGRLWEAKEAGLLQPVTSE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 104 NVEALDP-RFVDGDKppSWVGMDAYVAALCYN--TVEAGKLgltppTSWKDLTKPEYKGHVVMPNPNSSGTGFLdVSAWL 180
Cdd:cd13542   78 KLESNVPaNLRDPDG--NWFGLTKRARVIVYNkdKVNPEEL-----STYEDLADPKWKGKVCMRSSSNSYNQSL-VASMI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 181 QTFGEEEAWSFMDALHENIAA-YTHSGSKPCKMAASGETVIGVSFEFPGAKAKTS--------GAPIDIIFPSE---GSG 248
Cdd:cd13542  150 AHDGEKETKEWLQGWVNNLARePQGGDRDQAKAIAAGICDVGIANSYYLGRMLNSedpeekevAEPVGVFFPNQdnrGTH 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 504340041 249 WEAEATAIIAGTANLEAAKTLVDWSISKEANEMY---NVGYAVVAY 291
Cdd:cd13542  230 VNISGIGVTKYAKNKENAIKFLEFLVSEPAQKLYaggNYEYPVNPG 275
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
80-295 5.96e-12

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: 65.01  E-value: 5.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  80 VWGVAATSLLLLKSEGMLEPYSPKNVEA---LDPRFVDG-----DKPPSWVGMDAYVAALCYNTveagKLGLTPPTSW-K 150
Cdd:cd13588   51 VVTPSGDALLRLIAAGLVQPIDTSKIPNyanIDPRLRNLpwltvDGKVYGVPYDWGANGLAYNT----KKVKTPPTSWlA 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 151 DLTKPEYKGHVVMP-NPNSS---GTGFLDVSAWLQTFGEE--EAWSFMDALHENIAAYTHSGSKPCKMAASGETVIGVSF 224
Cdd:cd13588  127 LLWDPKYKGRVAARdDPIDAiadAALYLGQDPPFNLTDEQldAVKAKLREQRPLVRKYWSDGAELVQLFANGEVVAATAW 206
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504340041 225 EFPGAKAKTSGAPIDIIFPSEG-SGWeAEATAIIAGTANLEAAKTLVDWSISKEanemynVGYAVVAYPGVA 295
Cdd:cd13588  207 SGQVNALQKAGKPVAYVIPKEGaTGW-VDTWMILKDAKNPDCAYKWLNYMLSPK------VQAAVAEWTGYA 271
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
31-280 1.07e-11

Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.


Pssm-ID: 460248 [Multi-domain]  Cd Length: 294  Bit Score: 64.74  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041   31 TSIEAVDLDRYKETFKKAHPDIKINWVRDSTGVMTAKLLA--EKDNPQADVVWgVAATSLLLLKSEGMLEPYSPKnveaL 108
Cdd:pfam01547   3 SLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTaiAAGDGPADVFA-SDNDWIAELAKAGLLLPLDDY----V 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  109 DPRFVDGDKPPSWVGMDAYVAALCYNTVEAGKLGLTPPTSWKDLTKPEYKGH------VVMPNPNSSGTGFLDVSAWLQT 182
Cdd:pfam01547  78 ANYLVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKekgkspGGAGGGDASGTLGYFTLALLAS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  183 FGEEE------------------------AWSFMDALHENIAAYTHSGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPI 238
Cdd:pfam01547 158 LGGPLfdkdgggldnpeavdaityyvdlyAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAANKVKLKV 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 504340041  239 DIIFPSE---------------GSGWEAEATAIIAGTANLEAAKTLVDWSISKEANE 280
Cdd:pfam01547 238 AFAAPAPdpkgdvgyaplpagkGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQA 294
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
1-290 1.20e-11

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 65.07  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041   1 MPFSKIFLGAGTALILA--------SSAAYAETELTVYTSI--EAVDLDRYKETFKKAHPDIKINWVRDSTGVMTAKLLA 70
Cdd:COG1653    1 MRRLALALAAALALALAacggggsgAAAAAGKVTLTVWHTGggEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  71 E---KDNPqaDVVWgVAATSLLLLKSEGMLEPYSPknvEALDPRFVDGDKPPSWVG------------MDAYVAALCYNT 135
Cdd:COG1653   81 AlaaGNAP--DVVQ-VDSGWLAEFAAAGALVPLDD---LLDDDGLDKDDFLPGALDagtydgklygvpFNTDTLGLYYNK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 136 VEAGKLGLTPPTSWKDLTK-----PEYKGHVVMPNPNSSGTGFLDvsaWLQTFGEE----------------EAWSFMDA 194
Cdd:COG1653  155 DLFEKAGLDPPKTWDELLAaakklKAKDGVYGFALGGKDGAAWLD---LLLSAGGDlydedgkpafdspeavEALEFLKD 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 195 L------HENIAAYTHSGSKPckMAASGETVIGV--SFEFPGAKAKTSGAPIDII-FPSEGSGWEAEAT------AIIAG 259
Cdd:COG1653  232 LvkdgyvPPGALGTDWDDARA--AFASGKAAMMIngSWALGALKDAAPDFDVGVApLPGGPGGKKPASVlggsglAIPKG 309
                        330       340       350
                 ....*....|....*....|....*....|.
gi 504340041 260 TANLEAAKTLVDWSISKEANEMYNVGYAVVA 290
Cdd:COG1653  310 SKNPEAAWKFLKFLTSPEAQAKWDALQAVLL 340
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
41-282 3.25e-11

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 63.19  E-value: 3.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041   41 YKETFKKAHpDIKINWVRDSTGVMTAKLLAE---KDNPQADVVWGVAAtSLLLLKSEGMLEPYSP-KNVEALDPRFVDGD 116
Cdd:pfam13416   2 LAKAFEKKT-GVTVEVEPQASNDLQAKLLAAaaaGNAPDLDVVWIAAD-QLATLAEAGLLADLSDvDNLDDLPDALDAAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  117 KPPSWVGMdAYVA----ALCYNTVEAGKLGLtPPTSWKDLTK--PEYKGHVVMPNP-NSSGTGFLDVSAWLQT------F 183
Cdd:pfam13416  80 YDGKLYGV-PYAAstptVLYYNKDLLKKAGE-DPKTWDELLAaaAKLKGKTGLTDPaTGWLLWALLADGVDLTddgkgvE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  184 GEEEAWSFMDALHENIAAYThSGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSEGSGWEAEATAIIAGTANL 263
Cdd:pfam13416 158 ALDEALAYLKKLKDNGKVYN-TGADAVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVPKDGSFLGGKGLVVPAGAKDP 236
                         250       260
                  ....*....|....*....|
gi 504340041  264 E-AAKTLVDWSISKEANEMY 282
Cdd:pfam13416 237 RlAALDFIKFLTSPENQAAL 256
PBP2_PotD cd13660
The periplasmic substrate-binding component of an active spermidine-preferential transport ...
42-286 8.21e-10

The periplasmic substrate-binding component of an active spermidine-preferential transport system; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that serves as the primary polyamine receptor of ABC-type spermindine-preferential transport system from gram-negative bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270378 [Multi-domain]  Cd Length: 315  Bit Score: 59.13  E-value: 8.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  42 KETFKKAHPDikinwVRDSTGVMTAKLLAEKDNPQADVVwgVAATSLLLLKSEGMLEPYSPK---NVEALDPRFV----- 113
Cdd:cd13660   21 KETGIKVILS-----TYESNETMYAKVKLYKDGAYDLVV--PSTYYVDKMRKEGLIQKIDKSkitNFSNIDPDFLnqpfd 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 114 ---DGDKPPSWVGMdayvaALCYNTVEAGKLGLTpptSWKDLTKPEYKGHVVMPNPNSS--GTGFLDVSAWLQTFGEEE- 187
Cdd:cd13660   94 pnnDYSIPYIWGAT-----ALAVNGDAVDGKSVT---SWADLWKPEYKGKLLLTDDAREvfQMALRKLGYSGNTKDPEEi 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 188 --AWSFMDALHENIAAYthSGSKPCKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSEGSGWEAEATAIIAGTANLEA 265
Cdd:cd13660  166 eaAFEELKKLMPNVAAF--DSDNPANPYMEGEVALGMIWNGSAFVARQANKPIHVVWPKEGGIFWMDSFAIPANAKNKEG 243
                        250       260
                 ....*....|....*....|....*
gi 504340041 266 AKTLVDW----SISKEANEmyNVGY 286
Cdd:cd13660  244 ALKFINFllrpDVSKQIAE--TIGY 266
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
43-272 4.24e-09

The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270308 [Multi-domain]  Cd Length: 315  Bit Score: 56.86  E-value: 4.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  43 ETFKKAHpDIKINWVR-DSTGVMTAKLLAEKdNPQADVVWgVAATSLLLLKSEGMLEPYSPK---NVEALDPRFvdgdKP 118
Cdd:cd13590   17 KAFEKET-GVKVNYDTyDSNEEMLAKLRAGG-GSGYDLVV-PSDYMVERLIKQGLLEPLDHSklpNLKNLDPQF----LN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 119 PSWVGMDAY-------VAALCYNTVEAGklglTPPTSW-KDLTKPEYKGHVVMPN----------------PNSSgtgfl 174
Cdd:cd13590   90 PPYDPGNRYsvpyqwgTTGIAYNKDKVK----EPPTSWdLDLWDPALKGRIAMLDdarevlgaallalgysPNTT----- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 175 DVSAWlqtfgeEEAWSFMDALHENIAAYTHSGSKpcKMAASGETVIGVSFEFPGAKAKTSGAPIDIIFPSEGSGWEAEAT 254
Cdd:cd13590  161 DPAEL------AAAAELLIKQKPNVRAFDSDSYV--QDLASGEIWLAQAWSGDALQANRENPNLKFVIPKEGGLLWVDNM 232
                        250
                 ....*....|....*...
gi 504340041 255 AIIAGTANLEAAKTLVDW 272
Cdd:cd13590  233 AIPKGAPNPELAHAFINF 250
PBP2_polyamine_2 cd13587
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
95-282 2.01e-08

The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This family represents the periplasmic binding domain that functions as the primary polyamine receptor of an uncharacterized ABC-type transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270305 [Multi-domain]  Cd Length: 292  Bit Score: 54.75  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  95 GMLEPY--SPKNVEALDPRFVDGDKPPSWVGMDAYVAALCYNT----VEAGKLGLTPPTSWKDLTKPEYKGHVVMpNPNS 168
Cdd:cd13587   67 GLYQPIdeSKIKVAQFPPSLLESTKLGTTINGKRYAVPFDWGTegltVNSTKAPDVSGFSYGDLWAPEYAGKVAY-RLKS 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 169 SGTGF--------LDVSAWLQTFGEEEAW--------SFMDALHENIAAYTHSGSKPCKMAASGETVIGVSFEFPGAKAK 232
Cdd:cd13587  146 PLTGLglyadatgEDPFNRYLDYKDEAKYqkildqvlQFLIERKANVKAYWNNADEALAAFRSGGCVIGQTWDSTGLKLN 225
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504340041 233 TSGAPIDIIFPSEGS-GWeAEATAIIAGTANLEAAKTLVDWSISKEANEMY 282
Cdd:cd13587  226 RENPPIDYGAPKEGAlGW-IDTFAIPAKAENVDQAYAFINFMLRPEIAAMF 275
potD PRK09501
spermidine/putrescine ABC transporter periplasmic substrate-binding protein; Reviewed
1-329 3.78e-08

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


Pssm-ID: 181913 [Multi-domain]  Cd Length: 348  Bit Score: 54.15  E-value: 3.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041   1 MPFSKIFLGAGtALILASSAAYAETELTVY--TSIEAVD---LDRY-KETFKKAhpdikINWVRDSTGVMTAKLLAEKDN 74
Cdd:PRK09501   2 KKWSRHLLAAG-ALALGMSAAHADDNNTLYfyNWTEYVPpglLEQFtKETGIKV-----IYSTYESNETMYAKLKTYKDG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  75 PQaDVVwgVAATSLL-LLKSEGMLEPYSPK---NVEALDPRFVDGDKPPSWVGMDAYVAALCYNTVEAGKLGLTPPTSWK 150
Cdd:PRK09501  76 AY-DLV--VPSTYYVdKMRKEGMIQKIDKSkltNFSNLDPDMLNKPFDPNNDYSIPYIWGATAIGVNSDAIDPKSVTSWA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 151 DLTKPEYKGHVVMPNPNSS----GTGFLDVSAWLQTFGE-EEAWSFMDALHENIAAYthSGSKPCKMAASGETVIGVSFE 225
Cdd:PRK09501 153 DLWKPEYKGSLLLTDDAREvfqmALRKLGYSGNTTDPKEiEAAYNELKKLMPNVAAF--NSDNPANPYMEGEVNLGMIWN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 226 FPGAKAKTSGAPIDIIFPSEGSGWEAEATAIIAGTANLEAAKTLVDW----SISKEANEmyNVGYAVvayPGVAKPiENL 301
Cdd:PRK09501 231 GSAFVARQAGTPIDVVWPKEGGIFWMDSLAIPANAKNKEGALKLINFllrpDVAKQVAE--TIGYPT---PNLAAR-KLL 304
                        330       340
                 ....*....|....*....|....*....
gi 504340041 302 PDDVA-DKMIKNDFEWAANNrarilkEWQ 329
Cdd:PRK09501 305 SPEVAnDKSLYPDAETIKKG------EWQ 327
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
26-323 1.24e-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: 49.71  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  26 ELTVYTSIEAVDLDRYKE---TFKKAHPDIKINWVRDSTGVMTAKLLAE---KDNPqaDVVWgVAATSLLLLKSEGMLEP 99
Cdd:cd13585    1 TLTFWDWGQPAETAALKKlidAFEKENPGVKVEVVPVPYDDYWTKLTTAaaaGTAP--DVFY-VDGPWVPEFASNGALLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 100 YSPKnveaLDPRFVDGDKPPSW------------VGMDAYVAALCYNT--VEAGKLGLTPPTSWKDL---------TKPE 156
Cdd:cd13585   78 LDDY----IEKDGLDDDFPPGLldagtydgklygLPFDADTLVLFYNKdlFDKAGPGPKPPWTWDELleaakkltdKKGG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 157 YKGHVVMPNPN----------SSGTGFLDVSAWLQTFGEE---EAWSFMDALHENIAA-----YTHSGSKPckMAASGET 218
Cdd:cd13585  154 QYGFALRGGSGgqtqwypflwSNGGDLLDEDDGKATLNSPeavEALQFYVDLYKDGVApssatTGGDEAVD--LFASGKV 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 219 --VIGVSFEFPGAKAKTSGAPIDII-FPS-----EGSGWEAEATAIIAGTANLEAAKTLVDWSISKEANEMYNvGYAVVA 290
Cdd:cd13585  232 amMIDGPWALGTLKDSKVKFKWGVApLPAgpggkRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLG-GAAGPA 310
                        330       340       350
                 ....*....|....*....|....*....|...
gi 504340041 291 YPGVAKPIENLPDDVADKMIKNDFEWAANNRAR 323
Cdd:cd13585  311 ALAAAAASAAAPDAKPALALAAAADALAAAVPP 343
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
28-278 2.20e-06

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


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 48.03  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041   28 TVYTSIEAVD-LDRYKETFKKaHPDIKINWVRDSTGVMTAKLlaeKDNPQADVVWGVAATSLLLLKSEGMLEPYSPKnve 106
Cdd:pfam13531   1 TVAAAGGLAAaLRELAAAFEA-ETGVKVVVSYGGSGKLAKQI---ANGAPADVFISADSAWLDKLAAAGLVVPGSRV--- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  107 aldprfvdgdkppswvgmdayvaALCYNT-VEAGKLGL-TPPTSWKDLTKPEYKghVVMPNPNSSGTGFldvsAWLQTFg 184
Cdd:pfam13531  74 -----------------------PLAYSPlVIAVPKGNpKDISGLADLLKPGVR--LAVADPKTAPSGR----AALELL- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  185 eeEAWSFMDALHENIAAYTHSGSKPCKMAASGETVIGVSFEfPGAKAKTSGAPIDII-FPSEGSGWEAEATAIIAGTANL 263
Cdd:pfam13531 124 --EKAGLLKALEKKVVVLGENVRQALTAVASGEADAGIVYL-SEALFPENGPGLEVVpLPEDLNLPLDYPAAVLKKAAHP 200
                         250
                  ....*....|....*
gi 504340041  264 EAAKTLVDWSISKEA 278
Cdd:pfam13531 201 EAARAFLDFLLSPEA 215
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
45-311 7.03e-06

The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; possesses type 2 periplasmic binding fold; This group represents the periplasmic component of an ABC transport system XBP1 that shows preference for xylo-oligosaccharides in the order of xylotriose > xylobiose > xylotetraose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270452 [Multi-domain]  Cd Length: 388  Bit Score: 47.37  E-value: 7.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  45 FKKAHPDIKIN-----WVRDSTGVMTAklLAEKDNPqaDVVWGVAATSLLLLKSEGMLEPYSPKnveaLDPRFVDGDKPP 119
Cdd:cd14749   24 FEKENPNIKVKvvvfpYDNYKTKLKTA--VAAGEGP--DVFNLWPGGWLAEFVKAGLLLPLTDY----LDPNGVDKRFLP 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 120 SWVG------------MDAYVAALCYNT---VEAGklGLTPPTSWKDL------TKPEYKGHVVMPNPNSSGTGFLDVSA 178
Cdd:cd14749   96 GLADavtfngkvygipFAARALALFYNKdlfEEAG--GVKPPKTWDELieaakkDKFKAKGQTGFGLLLGAQGGHWYFQY 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 179 WLQTFGEEE-------AWSFMD-----------------ALHENIAAYTHSGSKPCKMAASGETVIGVSFEFPGAKAKTS 234
Cdd:cd14749  174 LVRQAGGGPlsddgsgKATFNDpafvqalqklqdlvkagAFQEGFEGIDYDDAGQAFAQGKAAMNIGGSWDLGAIKAGEP 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 235 GAPIDII-FPSEGSGWEAEAT-------AIIAGTANLEAAKTLVDWSISKEANEMYNVGYAVVAY-PGVAKPIENLPDDV 305
Cdd:cd14749  254 GGKIGVFpFPTVGKGAQTSTIggsdwaiAISANGKKKEAAVKFLKYLTSPEVMKQYLEDVGLLPAkEVVAKDEDPDPVAI 333

                 ....*.
gi 504340041 306 ADKMIK 311
Cdd:cd14749  334 LGPFAD 339
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
6-290 3.19e-03

ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, periplasmic Mo-binding protein ModA is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440489 [Multi-domain]  Cd Length: 253  Bit Score: 38.70  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041   6 IFLGAGTALILASSAAYAETELTVYT--SIEAVdLDRYKETFKKAHPDIKINWVRDSTGVMTAKLLAEKdnpQADVVWGV 83
Cdd:COG0725    6 LALLLLALLLAGASAAAAAAELTVFAaaSLKEA-LEELAAAFEKEHPGVKVELSFGGSGALARQIEQGA---PADVFISA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041  84 AATSLLLLKSEGMLEPYSPKNVealdprfvdgdkppswvgmdAYVA-ALCYNTVEAGKLgltppTSWKDLTKPEYKghVV 162
Cdd:COG0725   82 DEKYMDKLAKKGLILAGSRVVF--------------------ATNRlVLAVPKGNPADI-----SSLEDLAKPGVR--IA 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504340041 163 MPNPNSSGTGFldvsAWLQTFGEEEAWsfmDALHENIaAYTHSGSKPCKMAASGETVIGVSF--EFPGAKAKTSGAPID- 239
Cdd:COG0725  135 IGDPKTVPYGK----YAKEALEKAGLW---DALKPKL-VLGENVRQVLAYVESGEADAGIVYlsDALAAKGVLVVVELPa 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504340041 240 -----IIFPsegsgweaeaTAIIAGTANLEAAKTLVDWSISKEANEMY-NVGYAVVA 290
Cdd:COG0725  207 elyapIVYP----------AAVLKGAKNPEAAKAFLDFLLSPEAQAILeKYGFEPPK 253
 
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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