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Conserved domains on  [gi|880808879|ref|WP_048661042|]
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MULTISPECIES: maltose/maltodextrin ABC transporter substrate-binding protein MalE [Vibrio]

Protein Classification

maltose/maltodextrin ABC transporter substrate-binding protein( domain architecture ID 11484205)

maltose/maltodextrin ABC transporter substrate-binding protein functions as the primary receptor for the active transport of maltose and higher maltodextrins such as maltotriose

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
1-394 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


:

Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 721.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879   1 MKNALSAVALGTIVALG-SFGANAAIEEGQLTIWVGGDKAYEGMAEVGKRFEEDTGVKVTVAFPDKLEEKFPQVAAAGDG 79
Cdd:PRK09474   3 IKKGLRTLALSALATLMfSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  80 PDMIFYAHDRFGGYAEAGLLVDIKPSKETKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNKALVPNPPKSWEEIPALD 159
Cdd:PRK09474  83 PDIIFWAHDRFGGYAQSGLLAEVTPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 160 AELKKDGKKAIMWPLRGgAYFTWPLLAADGGYAFKQTAEGYDIKDAGVATDGVQKSLGFIEKMVQDKVISADMDYSVAES 239
Cdd:PRK09474 163 KELKAKGKSAIMWNLQE-PYFTWPLIAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAEA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 240 EFVAGNVAMTINGPWGWENIKKAGVDYGVTTLPKFNGKASKPFVGVWAGGISTASPNRDLAVEFMENYLLTDEGMKSLND 319
Cdd:PRK09474 242 AFNKGETAMTINGPWAWSNIDKSGINYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNK 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 880808879 320 DKPLGAVALNSFQRQLDSDTRIAATMDNAMNGEIMPNIPQFTTFWYSMEEAIGNVVDGRQSVDQALKAAEGRMTK 394
Cdd:PRK09474 322 DKPLGAVALKSFQEELAKDPRIAATMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAKRITK 396
 
Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
1-394 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 721.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879   1 MKNALSAVALGTIVALG-SFGANAAIEEGQLTIWVGGDKAYEGMAEVGKRFEEDTGVKVTVAFPDKLEEKFPQVAAAGDG 79
Cdd:PRK09474   3 IKKGLRTLALSALATLMfSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  80 PDMIFYAHDRFGGYAEAGLLVDIKPSKETKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNKALVPNPPKSWEEIPALD 159
Cdd:PRK09474  83 PDIIFWAHDRFGGYAQSGLLAEVTPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 160 AELKKDGKKAIMWPLRGgAYFTWPLLAADGGYAFKQTAEGYDIKDAGVATDGVQKSLGFIEKMVQDKVISADMDYSVAES 239
Cdd:PRK09474 163 KELKAKGKSAIMWNLQE-PYFTWPLIAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAEA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 240 EFVAGNVAMTINGPWGWENIKKAGVDYGVTTLPKFNGKASKPFVGVWAGGISTASPNRDLAVEFMENYLLTDEGMKSLND 319
Cdd:PRK09474 242 AFNKGETAMTINGPWAWSNIDKSGINYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNK 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 880808879 320 DKPLGAVALNSFQRQLDSDTRIAATMDNAMNGEIMPNIPQFTTFWYSMEEAIGNVVDGRQSVDQALKAAEGRMTK 394
Cdd:PRK09474 322 DKPLGAVALKSFQEELAKDPRIAATMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAKRITK 396
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 28-392 4.68e-179

The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold; This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. 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: 270374 [Multi-domain]  Cd Length: 364  Bit Score: 502.51  E-value: 4.68e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  28 GQLTIWVGGDKAYEGMAEVGKRFEEDTGVKVTVAFPDKLEEKFPQVAAAGDGPDMIFYAHDRFGGYAEAGLLVDIKPSKE 107
Cdd:cd13656    1 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 108 TKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNKALVPNPPKSWEEIPALDAELKKDGKKAIMWPLRGgAYFTWPLLAA 187
Cdd:cd13656   81 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQE-PYFTWPLIAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 188 DGGYAFKQTAEGYDIKDAGVATDGVQKSLGFIEKMVQDKVISADMDYSVAESEFVAGNVAMTINGPWGWENIKKAGVDYG 267
Cdd:cd13656  160 DGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 268 VTTLPKFNGKASKPFVGVWAGGISTASPNRDLAVEFMENYLLTDEGMKSLNDDKPLGAVALNSFQRQLDSDTRIAATMDN 347
Cdd:cd13656  240 VTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMEN 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 880808879 348 AMNGEIMPNIPQFTTFWYSMEEAIGNVVDGRQSVDQALKAAEGRM 392
Cdd:cd13656  320 AQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTRI 364
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-394 2.73e-126

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 370.05  E-value: 2.73e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879   1 MKN-ALSAVALGTIVALG----------SFGANAAIEEGQLTIWVGGDKAyEGMAEVGKRFEEDTGVKVTVAFP--DKLE 67
Cdd:COG2182    1 MKRrLLAALALALALALAlaacgsgsssSGSSSAAGAGGTLTVWVDDDEA-EALEEAAAAFEEEPGIKVKVVEVpwDDLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  68 EKFPQVAAAGDGPDMIFYAHDRFGGYAEAGLLVDIKPSKETKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNKALVP- 146
Cdd:COG2182   80 EKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKa 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 147 NPPKSWEEIPALDAELKKDGKKAIMWPLrGGAYFTWPLLAADGGYAFKQTAEgyDIKDAGVATDGVQKSLGFIEKMVQDK 226
Cdd:COG2182  160 EPPKTWDELIAAAKKLTAAGKYGLAYDA-GDAYYFYPFLAAFGGYLFGKDGD--DPKDVGLNSPGAVAALEYLKDLIKDG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 227 VISADMDYSVAESEFVAGNVAMTINGPWGWENIKKA-GVDYGVTTLPKF-NGKASKPFVGVWAGGISTASPNRDLAVEFM 304
Cdd:COG2182  237 VLPADADYDAADALFAEGKAAMIINGPWAAADLKKAlGIDYGVAPLPTLaGGKPAKPFVGVKGFGVSAYSKNKEAAQEFA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 305 eNYLLTDEGMKSLNDDKPLgAVALNSFQRQLD--SDTRIAATMDNAMNGEIMPNIPQFTTFWYSMEEAIGNVVDGRQSVD 382
Cdd:COG2182  317 -EYLTSPEAQKALFEATGR-IPANKAAAEDAEvkADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPA 394

                        410
                 ....*....|..
gi 880808879 383 QALKAAEGRMTK 394
Cdd:COG2182  395 EALDAAQKQIEA 406
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 45-315 6.16e-27

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 108.26  E-value: 6.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879   45 EVGKRFEEDTGVKVTV--AFPDKLEEKFPQVAAAGDGPD--MIFYAHDRFGGYAEAGLLVDIKPSKETKeGIVDFAwDAV 120
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVepQASNDLQAKLLAAAAAGNAPDldVVWIAADQLATLAEAGLLADLSDVDNLD-DLPDAL-DAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  121 SYEGKTIAYPVAVES-VSLIYNKALVP---NPPKSWEEIPALDAELKkdGKKAIMWPlrggayftwpllaADGGYAFKQT 196
Cdd:pfam13416  79 GYDGKLYGVPYAASTpTVLYYNKDLLKkagEDPKTWDELLAAAAKLK--GKTGLTDP-------------ATGWLLWALL 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  197 AEGYDIKDAGVATDGVQKSLGFIEKMVQDKVISADmdYSVAESEFVAGNVAMTINGPWGWENIKKAGVDYGVtTLPKfng 276
Cdd:pfam13416 144 ADGVDLTDDGKGVEALDEALAYLKKLKDNGKVYNT--GADAVQLFANGEVAMTVNGTWAAAAAKKAGKKLGA-VVPK--- 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 880808879  277 kaSKPFVGVWAGGISTASPNRDL-AVEFMeNYLLTDEGMK 315
Cdd:pfam13416 218 --DGSFLGGKGLVVPAGAKDPRLaALDFI-KFLTSPENQA 254
 
Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
1-394 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 721.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879   1 MKNALSAVALGTIVALG-SFGANAAIEEGQLTIWVGGDKAYEGMAEVGKRFEEDTGVKVTVAFPDKLEEKFPQVAAAGDG 79
Cdd:PRK09474   3 IKKGLRTLALSALATLMfSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  80 PDMIFYAHDRFGGYAEAGLLVDIKPSKETKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNKALVPNPPKSWEEIPALD 159
Cdd:PRK09474  83 PDIIFWAHDRFGGYAQSGLLAEVTPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 160 AELKKDGKKAIMWPLRGgAYFTWPLLAADGGYAFKQTAEGYDIKDAGVATDGVQKSLGFIEKMVQDKVISADMDYSVAES 239
Cdd:PRK09474 163 KELKAKGKSAIMWNLQE-PYFTWPLIAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAEA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 240 EFVAGNVAMTINGPWGWENIKKAGVDYGVTTLPKFNGKASKPFVGVWAGGISTASPNRDLAVEFMENYLLTDEGMKSLND 319
Cdd:PRK09474 242 AFNKGETAMTINGPWAWSNIDKSGINYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNK 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 880808879 320 DKPLGAVALNSFQRQLDSDTRIAATMDNAMNGEIMPNIPQFTTFWYSMEEAIGNVVDGRQSVDQALKAAEGRMTK 394
Cdd:PRK09474 322 DKPLGAVALKSFQEELAKDPRIAATMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVDAALDDAAKRITK 396
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 28-392 4.68e-179

The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold; This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. 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: 270374 [Multi-domain]  Cd Length: 364  Bit Score: 502.51  E-value: 4.68e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  28 GQLTIWVGGDKAYEGMAEVGKRFEEDTGVKVTVAFPDKLEEKFPQVAAAGDGPDMIFYAHDRFGGYAEAGLLVDIKPSKE 107
Cdd:cd13656    1 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 108 TKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNKALVPNPPKSWEEIPALDAELKKDGKKAIMWPLRGgAYFTWPLLAA 187
Cdd:cd13656   81 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQE-PYFTWPLIAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 188 DGGYAFKQTAEGYDIKDAGVATDGVQKSLGFIEKMVQDKVISADMDYSVAESEFVAGNVAMTINGPWGWENIKKAGVDYG 267
Cdd:cd13656  160 DGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 268 VTTLPKFNGKASKPFVGVWAGGISTASPNRDLAVEFMENYLLTDEGMKSLNDDKPLGAVALNSFQRQLDSDTRIAATMDN 347
Cdd:cd13656  240 VTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMEN 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 880808879 348 AMNGEIMPNIPQFTTFWYSMEEAIGNVVDGRQSVDQALKAAEGRM 392
Cdd:cd13656  320 AQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTRI 364
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-394 2.73e-126

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 370.05  E-value: 2.73e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879   1 MKN-ALSAVALGTIVALG----------SFGANAAIEEGQLTIWVGGDKAyEGMAEVGKRFEEDTGVKVTVAFP--DKLE 67
Cdd:COG2182    1 MKRrLLAALALALALALAlaacgsgsssSGSSSAAGAGGTLTVWVDDDEA-EALEEAAAAFEEEPGIKVKVVEVpwDDLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  68 EKFPQVAAAGDGPDMIFYAHDRFGGYAEAGLLVDIKPSKETKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNKALVP- 146
Cdd:COG2182   80 EKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKa 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 147 NPPKSWEEIPALDAELKKDGKKAIMWPLrGGAYFTWPLLAADGGYAFKQTAEgyDIKDAGVATDGVQKSLGFIEKMVQDK 226
Cdd:COG2182  160 EPPKTWDELIAAAKKLTAAGKYGLAYDA-GDAYYFYPFLAAFGGYLFGKDGD--DPKDVGLNSPGAVAALEYLKDLIKDG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 227 VISADMDYSVAESEFVAGNVAMTINGPWGWENIKKA-GVDYGVTTLPKF-NGKASKPFVGVWAGGISTASPNRDLAVEFM 304
Cdd:COG2182  237 VLPADADYDAADALFAEGKAAMIINGPWAAADLKKAlGIDYGVAPLPTLaGGKPAKPFVGVKGFGVSAYSKNKEAAQEFA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 305 eNYLLTDEGMKSLNDDKPLgAVALNSFQRQLD--SDTRIAATMDNAMNGEIMPNIPQFTTFWYSMEEAIGNVVDGRQSVD 382
Cdd:COG2182  317 -EYLTSPEAQKALFEATGR-IPANKAAAEDAEvkADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPA 394

                        410
                 ....*....|..
gi 880808879 383 QALKAAEGRMTK 394
Cdd:COG2182  395 EALDAAQKQIEA 406
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 30-392 9.15e-104

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


Pssm-ID: 270304 [Multi-domain]  Cd Length: 367  Bit Score: 311.15  E-value: 9.15e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  30 LTIWVGGDKAYEGMAEVGKRFEEDTGVKVTVAFPD--KLEEKFPQVAAAGDGPDMIFYAHDRFGGYAEAGLLVDIKPSKE 107
Cdd:cd13586    2 ITVWTDEDGELEYLKELAEEFEKKYGIKVEVVYVDsgDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 108 TKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNKALVPNPPKSWEEIPALDA--ELKKDGKKAIMWPLrGGAYFTWPLL 185
Cdd:cd13586   82 VKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPEPPKTWEELIALAKkfNDKAGGKYGFAYDQ-TNPYFSYPFL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 186 AADGGYAFKQTaeGYDIKDAGVATDGVQKSLGFIEKMV-QDKVISADMDYSVAESEFVAGNVAMTINGPWGWENIKKAGV 264
Cdd:cd13586  161 AAFGGYVFGEN--GGDPTDIGLNNEGAVKGLKFIKDLKkKYKVLPPDLDYDIADALFKEGKAAMIINGPWDLADYKDAGI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 265 DYGVTTLPKF-NGKASKPFVGVWAGGISTASPNRDLAVEFMEnYLLTDEGMKSLNDDK---PLGAVALNsfQRQLDSDTR 340
Cdd:cd13586  239 NFGVAPLPTLpGGKQAAPFVGVQGAFVSAYSKNKEAAVEFAE-YLTSDEAQLLLFEKTgriPALKDALN--DAAVKNDPL 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 880808879 341 IAATMDNAMNGEIMPNIPQFTTFWYSMEEAIGNVVDGRQSVDQALKAAEGRM 392
Cdd:cd13586  316 VKAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEEAAKDAVAAI 367
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 30-392 3.02e-92

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


Pssm-ID: 270240 [Multi-domain]  Cd Length: 368  Bit Score: 281.61  E-value: 3.02e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  30 LTIWVGGDKA-YEGMAEVGKRFEEDT-GVKVTVAFPDK--LEEKFPQVAAAGDGPDMIFYAHDRFGGYAEAGLLVDIKPS 105
Cdd:cd13522    2 ITVWHQYDTGeNQAVNELIAKFEKAYpGITVEVTYQDTeaRRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 106 KETKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNKALVP-NPPKSWEEIPALDAELKKDGKKAIMWPLrGGAYFTWPL 184
Cdd:cd13522   82 VSKSGKYAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVPkNPPKTWQELIALAQGLKAKNVWGLVYNQ-NEPYFFAAW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 185 LAADGGYAFKqtaEGYDIKDAGVATDGVQKSLGFIEKMV-QDKVISADMDYSVAESEFVAGNVAMTINGPWGWENI-KKA 262
Cdd:cd13522  161 IGGFGGQVFK---ANNGKNNPTLDTPGAVEALQFLVDLKsKYKIMPPETDYSIADALFKAGKAAMIINGPWDLGDYrQAL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 263 GVDYGVTTLPKF-NGKASKPFVGVWAGGISTASPNRDLAVEFMENYLLTDEGMksLNDDKPLGAVALNSFQRQLDSDTRI 341
Cdd:cd13522  238 KINLGVAPLPTFsGTKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQL--VLFDDAGDIPANLQAYESPAVQNKP 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 880808879 342 A--ATMDNAMNGEIMPNIPQFTTFWYSMEEAIGNVVDGRQSVDQALKAAEGRM 392
Cdd:cd13522  316 AqkASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQQEA 368
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 29-393 6.78e-80

The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold; This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. 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: 270376 [Multi-domain]  Cd Length: 372  Bit Score: 250.09  E-value: 6.78e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  29 QLTIWVGGDKAYEGMAEVGKRFEEDTGVKVTVAFPDKLE--EKFPQVAAAGDGPDMIFYAHDRFGGYAEAGLLVDIKPSK 106
Cdd:cd13658    1 QLTVWVDEDKKMAFIKKIAKQYTKKTGVKVKLVEVDQLDqlEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 107 ETKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNKALVPNPPKSWEEIPALDAEL-KKDGKKAIMWPLRGGAYFTWPLL 185
Cdd:cd13658   81 DKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKDLtKEKGKQYGFLADATNFYYSYGLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 186 AADGGYAFKQTAEGYDIKDAGVATDGVQKSLGFIEKMVQDKVISADMDYSVAESEFVAGNVAMTINGPWGWENIKKAGVD 265
Cdd:cd13658  161 AGNGGYIFKKNGSDLDINDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAVIDGPWAIQEYQEAGVN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 266 YGVTTLPKF-NGKASKPFVGVWAGGISTASPNRDLAVEFMEnYLLTDEGMKSLNDDK---PLGAVALNSFQRQldSDTRI 341
Cdd:cd13658  241 YGVAPLPTLpNGKPMAPFLGVKGWYLSAYSKHKEWAQKFME-FLTSKENLKKRYDETneiPPRKDVRSDPEIK--NNPLT 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 880808879 342 AATMDNAMNGEIMPNIPQFTTFWYSMEEAIGNVVDGRQSVDQALKAAEGRMT 393
Cdd:cd13658  318 SAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKTPKQALNDAVNDIK 369
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 30-388 3.54e-61

The periplasmic binding component of ABC transport system specific for maltodextrin; This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . 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: 270375 [Multi-domain]  Cd Length: 368  Bit Score: 201.45  E-value: 3.54e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  30 LTIWVGGDKAYE-GMAEVGKRFEEDTGV-KVTVAF--PDKLEEKFPQVAAAGDGPDMIFYAHDRFGGYAEAGLLVDI--K 103
Cdd:cd13657    2 ITIWHALTGAEEdALQQIIDEFEAKYPVpNVKVPFekKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPIsdY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 104 PSKETKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNKALVPNPPKSWEEIPALDAELKK--DGKKAIMWPLrGGAYFT 181
Cdd:cd13657   82 LSEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQPPETTDELLAIMKDHTDpaAGSYGLAYQV-SDAYFV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 182 WPLLAADGGYAFKQTAEgydikDAGVATDGVQKSLGFIEKMVQdKVISADMDYSVAESEFVAGNVAMTINGPWGWENIKK 261
Cdd:cd13657  161 SAWIFGFGGYYFDDETD-----KPGLDTPETIKGIQFLKDFSW-PYMPSDPSYNTQTSLFNEGKAAMIINGPWFIGGIKA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 262 AGVDYGVTTLPKFNG-KASKPFVGVWAGGIST--ASPNRDLAVEFMEnYLLTDEGMKSLNDDkpLGAVALNS---FQRQL 335
Cdd:cd13657  235 AGIDLGVAPLPTVDGtNPPRPYSGVEGIYVTKyaERKNKEAALDFAK-FFTTAEASKILADE--NGYVPAATnayDDAEV 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 880808879 336 DSDTRIAATMDNAMNGEIMPNIPQFTTFWYSMEEAIGNVVDGRQSVDQALKAA 388
Cdd:cd13657  312 AADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQEALAAA 364
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-318 6.26e-49

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 169.45  E-value: 6.26e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879   1 MKNALSAVALGTIVAL-----GSFGANAAIEEGQLTIWVGGDKAYEGMAEVGKRFEEDT-GVKVTVAFP--DKLEEKFPQ 72
Cdd:COG1653    1 MRRLALALAAALALALaacggGGSGAAAAAGKVTLTVWHTGGGEAAALEALIKEFEAEHpGIKVEVESVpyDDYRTKLLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  73 VAAAGDGPDMIFYAHDRFGGYAEAGLLVDIKP----SKETKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNKALVP-- 146
Cdd:COG1653   81 ALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDllddDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEka 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 147 --NPPKSWEEIPALDAELK-KDGKKAIMWPLRGGAYFTwPLLAADGGYAFKQTaegydiKDAGVATDGVQKSLGFIEKMV 223
Cdd:COG1653  161 glDPPKTWDELLAAAKKLKaKDGVYGFALGGKDGAAWL-DLLLSAGGDLYDED------GKPAFDSPEAVEALEFLKDLV 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 224 QDKVI---SADMDYSVAESEFVAGNVAMTINGPWGWENIKKA--GVDYGVTTLPKFN-GKASKPFVGVWAGGISTASPNR 297
Cdd:COG1653  234 KDGYVppgALGTDWDDARAAFASGKAAMMINGSWALGALKDAapDFDVGVAPLPGGPgGKKPASVLGGSGLAIPKGSKNP 313

                        330       340
                 ....*....|....*....|.
gi 880808879 298 DLAVEFMEnYLLTDEGMKSLN 318
Cdd:COG1653  314 EAAWKFLK-FLTSPEAQAKWD 333
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 30-389 2.10e-47

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: 166.04  E-value: 2.10e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  30 LTIWVGGDKAY-EGMAEVGKRFEE-DTGVKVTVAFP--DKLEEKFPQVAAAGDGPDMIFYAHDRFGGYAEAGLLVDIKP- 104
Cdd:cd13585    2 LTFWDWGQPAEtAALKKLIDAFEKeNPGVKVEVVPVpyDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDDy 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 105 --SKETKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNKAL------VPNPPKSWEEIPALDAELK--KDGKKAIMWPL 174
Cdd:cd13585   82 ieKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLfdkagpGPKPPWTWDELLEAAKKLTdkKGGQYGFALRG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 175 RGGAYFTW-PLLAADGGYAFKQtaegyDIKDAGVATDGVQKSLGFIEKMVQDKVI--SADMDYSVAESEFVAGNVAMTIN 251
Cdd:cd13585  162 GSGGQTQWyPFLWSNGGDLLDE-----DDGKATLNSPEAVEALQFYVDLYKDGVApsSATTGGDEAVDLFASGKVAMMID 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 252 GPWGWENIK--KAGVDYGVTTLPKFNGKASKPFVGVWAGGISTASPNRDLAVEFMEnYLLTDEGMKSL--NDDKPLGAVA 327
Cdd:cd13585  237 GPWALGTLKdsKVKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIK-FLTSKENQLKLggAAGPAALAAA 315

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 880808879 328 LNSFQRQLDSDTRIAATMDNAMNGEIMPNIPQFTTFWYS-MEEAIGNVVDG--RQSVDQALKAAE 389
Cdd:cd13585  316 AASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPiLSEALQEALLGalGKSPEEALKEAA 380
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 29-389 5.55e-43

The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold; This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270451 [Multi-domain]  Cd Length: 385  Bit Score: 153.99  E-value: 5.55e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  29 QLTIWVGGD----KAYEGMAevgKRF-EEDTGVKVTVAFP---DKLEEKFPQVAAAGDGPDMIFYAHDRFGGYAEAGLLV 100
Cdd:cd14748    1 EITFWHGMSgpdgKALEELV---DEFnKSHPDIKVKAVYQgsyDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 101 DIKP----SKETKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNKAL-------VPNPPKSWEEI----PALDAELKKD 165
Cdd:cd14748   78 PLDDyidkDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLfeeagldPEKPPKTWDELeeaaKKLKDKGGKT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 166 GKKAIMWPLRGGAYFTWPLLAADGGYAFKQtaegyDIKDAGVATDGVQKSLGFIEKMVQDKVISADMDYSVAESEFVAGN 245
Cdd:cd14748  158 GRYGFALPPGDGGWTFQALLWQNGGDLLDE-----DGGKVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFISGK 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 246 VAMTINGPWGWENIKK--AGVDYGVTTLPKFNGKASKPFVGVWAGGISTASP-NRDLAVEFMEnYLLTDEGMKSLNDDK- 321
Cdd:cd14748  233 VAMTINGTWSLAGIRDkgAGFEYGVAPLPAGKGKKGATPAGGASLVIPKGSSkKKEAAWEFIK-FLTSPENQAKWAKATg 311

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 880808879 322 --PLGAVALNSFQRQLDSDTRIAATMDNAMNG-EIMPNIPQFTTFWYSMEEAIGNVVDGRQSVDQALKAAE 389
Cdd:cd14748  312 ylPVRKSAAEDPEEFLAENPNYKVAVDQLDYAkPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQ 382
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 30-394 1.72e-32

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


Pssm-ID: 270450 [Multi-domain]  Cd Length: 386  Bit Score: 125.89  E-value: 1.72e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  30 LTIWV-GGDKAYEGMAEVGKRFEEDT-GVKVTV------AFPDKLEEKfpqvAAAGDGPDMIFYAHDRFGGYAEAGLLVD 101
Cdd:cd14747    2 LTVWAmGNSAEAELLKELADEFEKENpGIEVKVqvlpwgDAHTKITTA----AASGDGPDVVQLGNTWVAEFAAMGALED 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 102 IKPSKETKEGIVDF---AWDAVSYEGKTIAYPVAVESVSLIYNK-----ALVPNPPKSWEEI-PALDAELKKDGKK-AIM 171
Cdd:cd14747   78 LTPYLEDLGGDKDLfpgLVDTGTVDGKYYGVPWYADTRALFYRTdllkkAGGDEAPKTWDELeAAAKKIKADGPDVsGFA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 172 WPLRGGAYFTW-PLLAADGGYAFKQtaegyDIKDAGVATDGVQKSLGFIEKMVQDKVISAD--MDYSVAESEFVAGNVAM 248
Cdd:cd14747  158 IPGKNDVWHNAlPFVWGAGGDLATK-----DKWKATLDSPEAVAGLEFYTSLYQKGLSPKStlENSADVEQAFANGKVAM 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 249 TINGPWGWENIKKAGVD----YGVTTLPKFNGKASKPFVG--VWAggISTASPNRDLAVEFMEnYLLTDEGMKSLNDDKP 322
Cdd:cd14747  233 IISGPWEIGAIREAGPDlagkWGVAPLPGGPGGGSPSFAGgsNLA--VFKGSKNKDLAWKFIE-FLSSPENQAAYAKATG 309

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 880808879 323 LG-----AVALNSFQrqldSDTRIAATMDNAMNGEIMPNIPQFTTFWYSMEEAIGNVVDG-RQSVDQALKAAEGRMTK 394
Cdd:cd14747  310 MLpantsAWDDPSLA----NDPLLAVFAEQLKTGKATPATPEWGEIEAELVLVLEEVWIGvGADVEDALDKAAAEINE 383
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 30-390 6.63e-31

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: 121.72  E-value: 6.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  30 LTIW--VGGDKAYEGMAEVGKRFEE---DTGVKVTVAFPDKLEEKFPQVAAAGDGPD-MIFYAHDRFGGYAEAGLLVDIK 103
Cdd:cd14749    2 ITYWqyFTGDTKKKYMDELIADFEKenpNIKVKVVVFPYDNYKTKLKTAVAAGEGPDvFNLWPGGWLAEFVKAGLLLPLT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 104 P---SKETKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNK-----ALVPNPPKSWEEIPALDAELKKDGKKAIMWPLR 175
Cdd:cd14749   82 DyldPNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKdlfeeAGGVKPPKTWDELIEAAKKDKFKAKGQTGFGLL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 176 GGA-----YFTWPLLAADGGYAFKQTAEGYDIKD-AGVATdgvqksLGFIEKMVQDKVISADM---DYSVAESEFVAGNV 246
Cdd:cd14749  162 LGAqgghwYFQYLVRQAGGGPLSDDGSGKATFNDpAFVQA------LQKLQDLVKAGAFQEGFegiDYDDAGQAFAQGKA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 247 AMTINGPWGWENIK--KAGVDYGVTTLPKFNGKA--SKPFVGVWAGGISTASPNRDLAVEFMeNYLLTDEGMK-SLNDDK 321
Cdd:cd14749  236 AMNIGGSWDLGAIKagEPGGKIGVFPFPTVGKGAqtSTIGGSDWAIAISANGKKKEAAVKFL-KYLTSPEVMKqYLEDVG 314

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 880808879 322 PLGAVALNSFQRQLDSDTRIAatMDNAMNGE------IMPNIPQFTTFWY-SMEEAIGNVVDGRQSVDQALKAAEG 390
Cdd:cd14749  315 LLPAKEVVAKDEDPDPVAILG--PFADVLNAagstpfLDEYWPAAAQVHKdAVQKLLTGKIDPEQVVKQAQSAAAK 388
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 45-315 6.16e-27

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 108.26  E-value: 6.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879   45 EVGKRFEEDTGVKVTV--AFPDKLEEKFPQVAAAGDGPD--MIFYAHDRFGGYAEAGLLVDIKPSKETKeGIVDFAwDAV 120
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVepQASNDLQAKLLAAAAAGNAPDldVVWIAADQLATLAEAGLLADLSDVDNLD-DLPDAL-DAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  121 SYEGKTIAYPVAVES-VSLIYNKALVP---NPPKSWEEIPALDAELKkdGKKAIMWPlrggayftwpllaADGGYAFKQT 196
Cdd:pfam13416  79 GYDGKLYGVPYAASTpTVLYYNKDLLKkagEDPKTWDELLAAAAKLK--GKTGLTDP-------------ATGWLLWALL 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  197 AEGYDIKDAGVATDGVQKSLGFIEKMVQDKVISADmdYSVAESEFVAGNVAMTINGPWGWENIKKAGVDYGVtTLPKfng 276
Cdd:pfam13416 144 ADGVDLTDDGKGVEALDEALAYLKKLKDNGKVYNT--GADAVQLFANGEVAMTVNGTWAAAAAKKAGKKLGA-VVPK--- 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 880808879  277 kaSKPFVGVWAGGISTASPNRDL-AVEFMeNYLLTDEGMK 315
Cdd:pfam13416 218 --DGSFLGGKGLVVPAGAKDPRLaALDFI-KFLTSPENQA 254
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 38-315 8.39e-25

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: 102.88  E-value: 8.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879   38 KAYEGMAEVGKRFEED-TGVKVTVAFP--DKLEEKFPQVAAAGDGP-DMIFYAHDRFGGYAEAGLLVDIKPSKETkegiv 113
Cdd:pfam01547   5 TEAAALQALVKEFEKEhPGIKVEVESVgsGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVAN----- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  114 dfawDAVSYEGKTIAYPVAVESVSLIYNKALVPN----PPKSWEEIPALDAELKKDGKKAIMWP----LRGGAYFTWPLL 185
Cdd:pfam01547  80 ----YLVLGVPKLYGVPLAAETLGLIYNKDLFKKagldPPKTWDELLEAAKKLKEKGKSPGGAGggdaSGTLGYFTLALL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  186 AADGGYAFKQTAEGYDIKDAGVATDGVQKSLGFI-EKMVQDKVISADMDYSVAESEFVAGNVAMTINGPWGW-------- 256
Cdd:pfam01547 156 ASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVlLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAAlaankvkl 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 880808879  257 -----ENIKKAGVDYGVTTLPKFNGKAskpfVGVWAGGISTASPNRDLAVEFMeNYLLTDEGMK 315
Cdd:pfam01547 236 kvafaAPAPDPKGDVGYAPLPAGKGGK----GGGYGLAIPKGSKNKEAAKKFL-DFLTSPEAQA 294
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 30-389 7.44e-24

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold; This group represents 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 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: 270453 [Multi-domain]  Cd Length: 385  Bit Score: 101.60  E-value: 7.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  30 LTIWVGGD-KAYEGMAEVGKRFEEDT-GVKVTV----AFPDKLEEKFPQVAAAGDGpDMIFYAHDRF--GGYAEAGLLVD 101
Cdd:cd14750    2 ITFAAGSDgQEGELLKKAIAAFEKKHpDIKVEIeelpASSDDQRQQLVTALAAGSS-APDVLGLDVIwiPEFAEAGWLLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 102 IKPS--KETKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNKALVP----NPPKSWEEIpaLDAELKKDGKKAIMWPL- 174
Cdd:cd14750   81 LTEYlkEEEDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEkygpEPPKTWDEL--LEAAKKRKAGEPGIWGYv 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 175 -RGGAYFT-----WPLLAADGGYAFKQTAEgydikDAGVATDGVQKSLGFIEKMVQDKVISADMD-YSVAES--EFVAGN 245
Cdd:cd14750  159 fQGKQYEGlvcnfLELLWSNGGDIFDDDSG-----KVTVDSPEALEALQFLRDLIGEGISPKGVLtYGEEEAraAFQAGK 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 246 VAMTINGPWGWENIKKAGVDY----GVTTLPKFNGKASKPFVGVWAGGISTASPNRDLAVEFMEnYLLTDEGMKSLnddk 321
Cdd:cd14750  234 AAFMRNWPYAYALLQGPESAVagkvGVAPLPAGPGGGSASTLGGWNLAISANSKHKEAAWEFVK-FLTSPEVQKRR---- 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 880808879 322 pLGAVALNSFQRQLDSDTRIAATM---DNAM----NGEIMPNIPQFTTFWYSMEEAIGNVVDGRQSVDQALKAAE 389
Cdd:cd14750  309 -AINGGLPPTRRALYDDPEVLEAYpflPALLealeNAVPRPVTPKYPEVSTAIQIALSAALSGQATPEEALKQAQ 382
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 43-389 1.06e-21

The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold; This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. 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: 270454 [Multi-domain]  Cd Length: 376  Bit Score: 95.52  E-value: 1.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  43 MAEVGKRFE-EDTGVKVT-VAFP-DKLEEKFPQVAAAGDGPDMIFYAHDRFGGYAEAGLL--VDIKPSKETKEGIVDFAW 117
Cdd:cd14751   16 YEKLIPAFEkEYPKIKVKaVRVPfDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLqpLDGTPAFDDIVDYLPGPM 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 118 DAVSYEGKTIAYPVAVESVSLIYNKALVPN----PPKSWEEIPAL-DAELKKDGKKAIMWPLRGGaYFTWPLLAADGG-Y 191
Cdd:cd14751   96 ETNRYNGHYYGVPQVTNTLALFYNKRLLEEagteVPKTMDELVAAaKAIKKKKGRYGLYISGDGP-YWLLPFLWSFGGdL 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 192 AFKQTAEGYdikdagVATDGVQKSLGFIEKMVQDKVISADMD--YSVAESEFVAGNVAMTINGPWGWENIK-----KAGV 264
Cdd:cd14751  175 TDEKKATGY------LNSPESVRALETIVDLYDEGAITPCASggYPNMQDGFKSGRYAMIVNGPWAYADILggkefKDPD 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 265 DYGVTTLPKFNGKASKPfVGVWAGGISTASPNRDLAVEFMEnYLLTDEGMKSLNddKPLGAVALNSfqrqldSDTRIAAT 344
Cdd:cd14751  249 NLGIAPVPAGPGGSGSP-VGGEDLVIFKGSKNKDAAWKFVK-FMSSAEAQALTA--AKLGLLPTRT------SAYESPEV 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 880808879 345 MDNAMNGEIM---------PNIPQFTTFWYSMEEAIGNVVDGRQSVDQALKAAE 389
Cdd:cd14751  319 ANNPMVAAFKpaletavprPPIPEWGELFEPLTLAFAKVLRGEKSPREALDEAA 372
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
2-312 5.04e-17

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 81.50  E-value: 5.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879   2 KNALSAVALGTIVALGSFGANAAiEEGQLTIWVGGDkaYEGmAEVGKRFEEDTGVKVTVAFPDKLEEKFPQVAAAGDGPD 81
Cdd:COG0687    4 RSLLGLAAAALAAALAGGAPAAA-AEGTLNVYNWGG--YID-PDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAGGSGYD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  82 MIFYAHDRFGGYAEAGLLVDIKPSK-ETKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNKALVPNPPKSWEEIpaLDA 160
Cdd:COG0687   80 VVVPSDYFVARLIKAGLLQPLDKSKlPNLANLDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEPPTSWADL--WDP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 161 ELKkdGKkaIMwpLRGGAYFTWPLLAADGGYAFKQTAEGyDIKDAgvatdgvqkslgfIEKMVQ--DKVISADMDYSVAE 238
Cdd:COG0687  158 EYK--GK--VA--LLDDPREVLGAALLYLGYDPNSTDPA-DLDAA-------------FELLIElkPNVRAFWSDGAEYI 217

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 880808879 239 SEFVAGNVAMTINGPWGWENIKKAGVDYGVTTlPKFNGKAskpFVGVWAggISTASPNRDLAVEFMeNYLLTDE 312
Cdd:COG0687  218 QLLASGEVDLAVGWSGDALALRAEGPPIAYVI-PKEGALL---WFDNMA--IPKGAPNPDLAYAFI-NFMLSPE 284
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 29-377 2.62e-16

The periplasmic binding component of ABC tansport system specific for an unknown oligosaccharide; possess the type 2 periplasmic binidng fold; This group represents an uncharacterized periplasmic-binding protein of an ATP-binding cassette transporter predicted to be involved in uptake of an unknown oligosaccharide molecule. 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: 270373 [Multi-domain]  Cd Length: 363  Bit Score: 79.70  E-value: 2.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  29 QLTIWVGGDKAyEGMAEVGKRFEE---DTGVKVT---VAFPDKLEEKFPQVAAAgdgPDMIFYAHDRFGGYAEAGLLVDI 102
Cdd:cd13655    1 TLTVWGPQEDQ-EWLKEMVDAFKEkhpEWKITITigvVGEADAKDEVLKDPSAA---ADVFAFANDQLGELVDAGAIYPL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 103 KPSKE--TKEGIVDFAWDAVSYEGKTIAYPVAVESVSLIYNKA-LVPNPPKSWEEIPAldaeLKKDGKKAIMWPLRGGAY 179
Cdd:cd13655   77 TGSAVdkIKNTNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSkLTEDDVKSLDTMLA----KAPDAKGKVSFDLSNSWY 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 180 FtWPLLAADGGYAFkqTAEGYDIKDAGVATDGVQKSLGFIEKMVQDKVISADMDySVAESEFVAGNVAMTINGPWGWENI 259
Cdd:cd13655  153 L-YAFFFGAGCKLF--GNNGGDTAGCDFNNEKGVAVTNYLVDLVANPKFVNDAD-GDAISGLKDGTLGAGVSGPWDAANL 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 260 KKA-GVDYGVTTLP--KFNGKAS--KPFVGVWAGGISTASPNRDLAVEFMEnYLLTDEGMKSLNDDKPLGAVALNSF-QR 333
Cdd:cd13655  229 KKAlGDNYAVAKLPtyTLGGKDVqmKSFAGYKAIGVNSNTKNPEAAMALAD-YLTNEESQLTRFEKRGIGPTNKEAAeSD 307

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 880808879 334 QLDSDTRIAATMDNAMNGEI-MPNIPQFTTFWYSMEEAIGNVVDG 377
Cdd:cd13655  308 AVKADPAAKALIAQSNEASVvQPKLPKMSNFWTPAEAFGKGIVDG 352
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 48-318 2.85e-11

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 2.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  48 KRFEEDTGVKVTVAF--PDKLEEKFPQVAAAGDGPDMIF-YAHDRFGGYAEAGLLVDI-----KPSKETKEGIVDFAWDA 119
Cdd:cd13580   26 KYLEEKTNIDVKVKWvpDSSYDEKLNLALASGDLPDIVVvNDPQLSITLVKQGALWDLtdyldKYYPNLKKIIEQEGWDS 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 120 VSYEGKTIAYPVAVESVS---LIYNKALVPN----PPKSWEEIPA-LDAELKKD--------------GKKAIMWPLRG- 176
Cdd:cd13580  106 ASVDGKIYGIPRKRPLIGrngLWIRKDWLDKlgleVPKTLDELYEvAKAFTEKDpdgngkkdtygltdTKDLIGSGFTGl 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 177 ----GAYFTWPLLAADGGYAFkqtaegydikdaGVATDGVQKSLGFIEKMVQDKVISAD---MDYSVAESEFVAGNVAM- 248
Cdd:cd13580  186 fgafGAPPNNWWKDEDGKLVP------------GSIQPEMKEALKFLKKLYKEGLIDPEfavNDGTKANEKFISGKAGIf 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 249 --TINGPWGWENIKKAGV---DYG-VTTLPKFNGKaskpfVGVWAGG-------ISTASPNRDLAVEFMeNYLLTDEGMK 315
Cdd:cd13580  254 vgNWWDPAWPQASLKKNDpdaEWVaVPIPSGPDGK-----YGVWAESgvngffvIPKKSKKPEAILKLL-DFLSDPEVQK 327


                 ...
gi 880808879 316 SLN 318
Cdd:cd13580  328 LLD 330
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 45-309 1.15e-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: 59.17  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  45 EVGKRFEEDTGVKVTVAFPDKLEEKFPQVAAAGDGP-DMIFYAHDRFGGYAEAGLLVDIKPSKETKEGIVDFAWDAVSY- 122
Cdd:cd13590   14 EVLKAFEKETGVKVNYDTYDSNEEMLAKLRAGGGSGyDLVVPSDYMVERLIKQGLLEPLDHSKLPNLKNLDPQFLNPPYd 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 123 EGKTIAYPVAVESVSLIYNKALVPNPPKSWEEiPALDAELKkdGKKAIM-WPLrggAYFTWPLLAAdgGYAFKQTAEGyD 201
Cdd:cd13590   94 PGNRYSVPYQWGTTGIAYNKDKVKEPPTSWDL-DLWDPALK--GRIAMLdDAR---EVLGAALLAL--GYSPNTTDPA-E 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 202 IKDAGvatdgvqkslgfiEKMVQDKVISADMDYSVAESEFVAGNV--AMTINGPWGWENIKKAGVDYgvtTLPkfngkas 279
Cdd:cd13590  165 LAAAA-------------ELLIKQKPNVRAFDSDSYVQDLASGEIwlAQAWSGDALQANRENPNLKF---VIP------- 221

                        250       260       270
                 ....*....|....*....|....*....|..
gi 880808879 280 KPFVGVWAGG--ISTASPNRDLAVEFMeNYLL 309
Cdd:cd13590  222 KEGGLLWVDNmaIPKGAPNPELAHAFI-NFLL 252
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 48-315 1.16e-09

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 58.79  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  48 KRFEEDTGVKVTVAFPDKLEEkFPQVAAAGDGP--DMIFYAH-DRFGGYAEAGLLVDIKPskETKEGIVDFAWDAVSYeg 124
Cdd:COG1840    3 EAFEKKTGIKVNVVRGGSGEL-LARLKAEGGNPpaDVVWSGDaDALEQLANEGLLQPYKS--PELDAIPAEFRDPDGY-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 125 ktiAYPVAVESVSLIYNKALVP--NPPKSWEEIpaLDAELKkdGKKAIMWPLRGGAYFTWpLLAAdggyafkqtaegydi 202
Cdd:COG1840   78 ---WFGFSVRARVIVYNTDLLKelGVPKSWEDL--LDPEYK--GKIAMADPSSSGTGYLL-VAAL--------------- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 203 kdagVATDGVQKSLGFIEKMVQDKVISADMDYSVAESeFVAGNVAMTINGPWGWENIKKAGVDYGVtTLPKFNGkaskpF 282
Cdd:COG1840  135 ----LQAFGEEKGWEWLKGLAANGARVTGSSSAVAKA-VASGEVAIGIVNSYYALRAKAKGAPVEV-VFPEDGT-----L 203

                        250       260       270
                 ....*....|....*....|....*....|...
gi 880808879 283 VGVWAGGISTASPNRDLAVEFMEnYLLTDEGMK 315
Cdd:COG1840  204 VNPSGAAILKGAPNPEAAKLFID-FLLSDEGQE 235
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 29-312 2.01e-08

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: 54.92  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  29 QLTIWVGGDKAYEGMAE-VGKRFEEDTGVKVTVAFPDKLEEKfPQVAAAGDGP--DMIFYAHDRFGGYAEAGLLVDIKPS 105
Cdd:cd13589    1 TLVVATWGGSYEDAQRKaVIEPFEKETGIKVVYDTGTSADRL-AKLQAQAGNPqwDVVDLDDGDAARAIAEGLLEPLDYS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 106 KETKEGIVDFawDAVSYEGKTIAYPVAveSVSLIYNKALVPNPPKSWeeiPALDAELKKD-GKKAIMWplRGGAYFTWPL 184
Cdd:cd13589   80 KIPNAAKDKA--PAALKTGYGVGYTLY--STGIAYNTDKFKEPPTSW---WLADFWDVGKfPGPRILN--TSGLALLEAA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 185 LAADGGyafkqtaegydikdaGVATDGVQKSLGFIEKMVQDKVISADmdySVAESE--FVAGNVAMTINGPWGWENIKKA 262
Cdd:cd13589  151 LLADGV---------------DPYPLDVDRAFAKLKELKPNVVTWWT---SGAQLAqlLQSGEVDMAPAWNGRAQALIDA 212

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 880808879 263 GVDYGVTtlpkFNGKASKPFVGVWAggISTASPNRDLAVEFMeNYLLTDE 312
Cdd:cd13589  213 GAPVAFV----WPKEGAILGPDTLA--IVKGAPNKELAMKFI-NFALSPE 255
TbpA COG4143
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ...
 1-163 1.52e-06

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


Pssm-ID: 443315 [Multi-domain]  Cd Length: 343  Bit Score: 49.46  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879   1 MK--NALSAVALGTIVALGSFGANAAIEEGQLTIWvggdkAYEGMA-------EVGKRFEEDTGVKVT-VAFPDKLEEkF 70
Cdd:COG4143    1 MKrrTFLLAAALALALALAGCSGAAAAAKPTLTVY-----TYDSFAsewgpgpWLKAAFEAECGCTLEfVAPGDGGEL-L 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  71 PQVAAAGDGP--DMIFYAHDRFGGYAEAGLLVDIKPSKETKEGIVDFAWDavsyeGKTIAYPVAVESVSLIYNKALVPNP 148
Cdd:COG4143   75 NRLRLEGANPkaDVVLGLDNNLLARALDTGLFAPHGVDALDALALPLAWD-----PDDRFVPYDYGYFAFVYDKTKLLNP 149

                        170
                 ....*....|....*
gi 880808879 149 PKSWEEIPALDAELK 163
Cdd:COG4143  150 PESLEDLVDPEYKDK 164
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 50-152 2.57e-06

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: 48.45  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  50 FEEDTGVKVTVAFPDKLEEKFPQVAAAGDGPDMIFYAHDRFGGYAEAGLLVDIKPSK--ETKEGIVDFAW-DAVSYEGKT 126
Cdd:cd13588   19 FEEATGCKVVVKFFGSEDEMVAKLRSGGGDYDVVTPSGDALLRLIAAGLVQPIDTSKipNYANIDPRLRNlPWLTVDGKV 98

                         90       100
                 ....*....|....*....|....*.
gi 880808879 127 IAYPVAVESVSLIYNKALVPNPPKSW 152
Cdd:cd13588   99 YGVPYDWGANGLAYNTKKVKTPPTSW 124
PBP2_PotD_PotF_like_3 cd13664
TThe periplasmic substrate-binding component of an uncharacterized active transport system ...
 45-163 1.61e-04

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


Pssm-ID: 270382 [Multi-domain]  Cd Length: 315  Bit Score: 43.12  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  45 EVGKRFEEDTGVKVTVAFPDKLEEKFPQVAAAGDGPDMIFYAHDRFGGYAEAGLLVDIKPSKETKEGIVDFAWDAVSY-E 123
Cdd:cd13664   14 ELLDKFEKETGIKVTLDTYDSNETLLAKLKAGGQGYDVVVPSDSFVPILIKEGLLEPLDKSQLTNYDNIDPRWRKPDFdP 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 880808879 124 GKTIAYPVAVESVSLIYNKALVPNPPKSWEEIPALDAELK 163
Cdd:cd13664   94 GNEYSIPWQWGTTGFAVDTAVYDGDIDDYSVIFQPPEELK 133
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 46-313 6.20e-04

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This family represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria and related proteins. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. In Sphingomonas sp. A1, the transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins AlgQ1 and AlgQ2. Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270239 [Multi-domain]  Cd Length: 483  Bit Score: 41.67  E-value: 6.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  46 VGKRFEEDTGVK-VTVAFPDKL-EEKFPQVAAAGDGPDMIF--YAHDRFGGYAEAGLLVDIKP---------SKETKEGI 112
Cdd:cd13521   22 VAKEIEKLTNVKlEIVAVTAATsQQKLNLMLASGDLPDIVGadYLKDKFIAYGMEGAFLPLSKyidqypnlkAFFKQHPD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 113 VDFAWdaVSYEGKT--IAY--PVAVESVSLIYNKALVPN----PPKSWEEIPAL-----DAELKKDGKK-AIMWPLRGGA 178
Cdd:cd13521  102 VLRAS--TASDGKIylIPYepPKDVPNQGYFIRKDWLDKlnlkTPKTLDELYNVlkafkEKDPNGNGKAdEIPFIDRDPL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879 179 YFTWPLLAADGGY-AFKQTAEGYDIKDAGV----ATDGVQKSLGFIEKMVQDKVISADM---DYSVAESEFVAGNVAMTI 250
Cdd:cd13521  180 YGAFRLINSWGARsAGGSTDSDWYEDNGKFkhpfASEEYKDGMKYMNKLYTEGLIDKESftqKDDQAEQKFSNGKLGGFT 259

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 880808879 251 NGPWGWENIKKAGVD-----YGVTTLPK--------FNGKASKPFVGVWAggISTASPNRDLAVEFMeNYLLTDEG 313
Cdd:cd13521  260 HNWFASDNLFTAQLGkekpmYILLPIAPagnvkgrrEEDSPGYTGPDGVA--ISKKAKNPVAALKFF-DWLASEEG 332
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
 30-181 6.72e-04

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: 41.13  E-value: 6.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  30 LTIWVGGDKAYEGmaEVGKRFEEDTGVKVTvAFPDKLEEKFPQVAAAGDGP--DmIFYAHD--RFGGYAEAGLLVDIKPS 105
Cdd:cd13518    2 LVVYTASDRDFAE--PVLKAFEEKTGIKVK-AVYDGTGELANRLIAEKNNPqaD-VFWGGEiiALEALKEEGLLEPYTPK 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 880808879 106 KETKEGIVDfaWDAVSYegktiAYPVAVESVSLIYNKALVPNP--PKSWEEIpaLDAELKkdGKKAIMWPLRGGAYFT 181
Cdd:cd13518   78 VIEAIPADY--RDPDGY-----WVGFAARARVFIYNTDKLKEPdlPKSWDDL--LDPKWK--GKIVYPTPLRSGTGLT 144
PBP2_TpPotD_like cd13662
The periplasmic substrate-binding component of an ABC-type polyamine transport system from ...
 48-152 2.43e-03

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


Pssm-ID: 270380  Cd Length: 312  Bit Score: 39.42  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  48 KRFEEDTGVKVTVAFPDKLEEKFPQVAAAGDGPDMIFYAHDRFGGYAEAGLLVDIKPSK--ETKEGIVDFAWDAVSY-EG 124
Cdd:cd13662   17 EDFEKETGIRVVYDYYASNEEMYAKLKIGGGGYDIVSPSGDYVSIMKKEGLLEKLDKSKlpNVKEEKDNLMEASKIYdPG 96

                         90       100
                 ....*....|....*....|....*...
gi 880808879 125 KTIAYPVAVESVSLIYNKALVPNPPKSW 152
Cdd:cd13662   97 LEYSVPYMFGATGIAVNKKIVKNYFRKW 124
PBP2_polyamine_2 cd13587
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 44-148 3.61e-03

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: 38.95  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  44 AEVGKRFEEDTGVKVTVAFPDKLEEKFPQV-AAAGDGPDMIFYAHDRFGGYAEAGLLVDIKPSKETKEGIVDFAWDAVS- 121
Cdd:cd13587   13 EDLLEKFENETGIKVQVTTSNNNEEMISKLrATGGGGFDLAQPSQRIAPNYEEFGLYQPIDESKIKVAQFPPSLLESTKl 92

                         90       100       110
                 ....*....|....*....|....*....|
gi 880808879 122 ---YEGKTIAYPVAVESVSLIYNKALVPNP 148
Cdd:cd13587   93 gttINGKRYAVPFDWGTEGLTVNSTKAPDV 122
PBP2_polyamines cd13523
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 50-173 4.44e-03

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: 38.57  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808879  50 FEEDTGVKVTVAFPDKLEEKFPQVAAAGDGP-DMIFYAHDRFGGYAEAGLLV--DIKPSKETKEGIVDFAWDAV-SYEGK 125
Cdd:cd13523   19 FEKETGIKVVVDTAANSERMIKKLSAGGSGGfDLVTPSDSYTSRQLGVGLMQpiDKSLLPSWATLDPHLTLAAVlTVPGK 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 880808879 126 TIAYPVAVESVSLIYNKALVPNPPKSWEEIpaLDAELKKDGKKAIMWP 173
Cdd:cd13523   99 KYGVPYQWGATGLVYNTDKVKAPPKSYAAD--LDDPKYKGRVSFSDIP 144
PBP2_AlgQ_like_3 cd13582
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 46-100 5.83e-03

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270300 [Multi-domain]  Cd Length: 504  Bit Score: 38.84  E-value: 5.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 880808879  46 VGKRFEEDTGVKVTVAFP-DKLEEKFPQVAAAGDGPDMIfYAHDRFGGYAEAGLLV 100
Cdd:cd13582   22 VAKKITELTGVTLEIEYLvGGEKQKIGLMIASGDLPDLI-YAKGDTDKLIEAGALV 76
 
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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