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Conserved domains on  [gi|773064230|gb|AJY42131|]
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bacterial extracellular solute-binding family protein [Burkholderia sp. 2002721687]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 11447308)

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

Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
PubMed:  26517916|24638992|25750732|26517916
SCOP:  3000083
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 36-330 3.51e-58

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 194.11  E-value: 3.51e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  36 GNQRATWQAVFDQFHKANPDIDLKVSYVGEEAYKVQMSGWLAT-DPPDVLSWNNGeRLAYFAKRGLIEDLSADWQKNGW- 113
Cdd:COG1653   42 GGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAgNAPDVVQVDSG-WLAEFAAAGALVPLDDLLDDDGLd 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 114 -NDTYAAVKQSSTYGGKLYSLPLGYDAYGLFYRKDLFEKAGIhGEPADWAQFLDACRKLRA-AGIAPIAVAARDAWTLAA 191
Cdd:COG1653  121 kDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGL-DPPKTWDELLAAAKKLKAkDGVYGFALGGKDGAAWLD 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 192 WFDYldlriNGYAFHQKlmAGDVAYTDPRVRAVYAAWKKLIDDKYFIDNALSYDVDSLSPLIVNGQAAMTLMGTWYSAGL 271
Cdd:COG1653  200 LLLS-----AGGDLYDE--DGKPAFDSPEAVEALEFLKDLVKDGYVPPGALGTDWDDARAAFASGKAAMMINGSWALGAL 272

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 272 LSATRN-PISFFRFPVLDASVPLAEDGPVNVLIVPAKARNKTDARRLLAFMGQPAINGEF 330
Cdd:COG1653  273 KDAAPDfDVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQAKW 332
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 36-330 3.51e-58

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 194.11  E-value: 3.51e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  36 GNQRATWQAVFDQFHKANPDIDLKVSYVGEEAYKVQMSGWLAT-DPPDVLSWNNGeRLAYFAKRGLIEDLSADWQKNGW- 113
Cdd:COG1653   42 GGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAgNAPDVVQVDSG-WLAEFAAAGALVPLDDLLDDDGLd 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 114 -NDTYAAVKQSSTYGGKLYSLPLGYDAYGLFYRKDLFEKAGIhGEPADWAQFLDACRKLRA-AGIAPIAVAARDAWTLAA 191
Cdd:COG1653  121 kDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGL-DPPKTWDELLAAAKKLKAkDGVYGFALGGKDGAAWLD 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 192 WFDYldlriNGYAFHQKlmAGDVAYTDPRVRAVYAAWKKLIDDKYFIDNALSYDVDSLSPLIVNGQAAMTLMGTWYSAGL 271
Cdd:COG1653  200 LLLS-----AGGDLYDE--DGKPAFDSPEAVEALEFLKDLVKDGYVPPGALGTDWDDARAAFASGKAAMMINGSWALGAL 272

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 272 LSATRN-PISFFRFPVLDASVPLAEDGPVNVLIVPAKARNKTDARRLLAFMGQPAINGEF 330
Cdd:COG1653  273 KDAAPDfDVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQAKW 332
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 37-404 5.86e-45

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: 159.85  E-value: 5.86e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  37 NQRATWQAVFDQFHKANPDIDLKVSYVGEEAYKVQMSGWLAT-DPPDVLSWNNGERLAYFAKRGLIEDLSADWQKNGWND 115
Cdd:cd14749   12 TKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAgEGPDVFNLWPGGWLAEFVKAGLLLPLTDYLDPNGVDK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 116 TY-AAVKQSSTYGGKLYSLPLGYDAYGLFYRKDLFEKAGIHGEPADWAQFLDACRKLRAAGIAPIAVAARDAWTLAAWFD 194
Cdd:cd14749   92 RFlPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGVKPPKTWDELIEAAKKDKFKAKGQTGFGLLLGAQGGHWYF 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 195 YLDLRINGYAFHQKLMAGDVAYTDPrvrAVYAAWKKLID---DKYFIDNALSYDVDSLSPLIVNGQAAMTLMGTWYSAGL 271
Cdd:cd14749  172 QYLVRQAGGGPLSDDGSGKATFNDP---AFVQALQKLQDlvkAGAFQEGFEGIDYDDAGQAFAQGKAAMNIGGSWDLGAI 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 272 LSAT-RNPISFFRFPVLDAS-VPLAEDGPVNVLIVPAKARNKTDARRLLAFMGQPAINGEFAKGMGQLPSNN---KAPEP 346
Cdd:cd14749  249 KAGEpGGKIGVFPFPTVGKGaQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQYLEDVGLLPAKEvvaKDEDP 328

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 773064230 347 QDPISKIGFRTFAATPGGIAqFYDRDMTKEmADEGMKAMQQFLSDPTQLDAILQRLEQ 404
Cdd:cd14749  329 DPVAILGPFADVLNAAGSTP-FLDEYWPAA-AQVHKDAVQKLLTGKIDPEQVVKQAQS 384
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 33-325 6.95e-32

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: 122.52  E-value: 6.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230   33 AARGNQRATWQAVFDQFHKANPDIDLKVSYVGEEAYKVQMSGWLATD--PPDVLsWNNGERLAYFAKRGLIEDLSADWQK 110
Cdd:pfam01547   1 AASLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGdgPADVF-ASDNDWIAELAKAGLLLPLDDYVAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  111 NGWNDTyaavkqsstygGKLYSLPLGYDAYGLFYRKDLFEKAGIhGEPADWAQFLDACRKLRAAGIAPIAVAARDAW-TL 189
Cdd:pfam01547  80 YLVLGV-----------PKLYGVPLAAETLGLIYNKDLFKKAGL-DPPKTWDELLEAAKKLKEKGKSPGGAGGGDASgTL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  190 AAWFDYLDLRINGYAFHQKLMAGD-VAYTDPRVRAVYAAWKKLIDDKYFIDNALSYDVDSLSPLIVNGQAAMTLMGTWY- 267
Cdd:pfam01547 148 GYFTLALLASLGGPLFDKDGGGLDnPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAa 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 773064230  268 ----SAGLLSATRNPISFFRFPVLDASVPLAEDGPVNV--LIVPAKARNKTDARRLLAFMGQPA 325
Cdd:pfam01547 228 laanKVKLKVAFAAPAPDPKGDVGYAPLPAGKGGKGGGygLAIPKGSKNKEAAKKFLDFLTSPE 291
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
79-266 1.14e-05

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 47.31  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  79 DPPDVLSWNNgERLAYFAKRGLIEDL--SADWQKNGWNDTYAAVkqssTYGGKLYSLPLGYDAYGLFYRKDLFEKAgihg 156
Cdd:PRK09474  81 DGPDIIFWAH-DRFGGYAQSGLLAEVtpSKAFKDKLVPFTWDAV----RYNGKLIGYPIAVEALSLIYNKDLVPTP---- 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 157 ePADWAQFLDACRKLRAAGIAPIavaardAWTLA-AWFDYLDLRING-YAFhqKLMAG-----DVAYTDPRVRAVYAAWK 229
Cdd:PRK09474 152 -PKTWEEIPALDKELKAKGKSAI------MWNLQePYFTWPLIAADGgYAF--KFENGgydvkDVGVNNAGAKAGLQFLV 222

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 773064230 230 KLIDDKYfidnaLSYDVD-SLSPLIVN-GQAAMTLMGTW 266
Cdd:PRK09474 223 DLVKNKH-----MNADTDySIAEAAFNkGETAMTINGPW 256
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 36-330 3.51e-58

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 194.11  E-value: 3.51e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  36 GNQRATWQAVFDQFHKANPDIDLKVSYVGEEAYKVQMSGWLAT-DPPDVLSWNNGeRLAYFAKRGLIEDLSADWQKNGW- 113
Cdd:COG1653   42 GGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAgNAPDVVQVDSG-WLAEFAAAGALVPLDDLLDDDGLd 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 114 -NDTYAAVKQSSTYGGKLYSLPLGYDAYGLFYRKDLFEKAGIhGEPADWAQFLDACRKLRA-AGIAPIAVAARDAWTLAA 191
Cdd:COG1653  121 kDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGL-DPPKTWDELLAAAKKLKAkDGVYGFALGGKDGAAWLD 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 192 WFDYldlriNGYAFHQKlmAGDVAYTDPRVRAVYAAWKKLIDDKYFIDNALSYDVDSLSPLIVNGQAAMTLMGTWYSAGL 271
Cdd:COG1653  200 LLLS-----AGGDLYDE--DGKPAFDSPEAVEALEFLKDLVKDGYVPPGALGTDWDDARAAFASGKAAMMINGSWALGAL 272

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 272 LSATRN-PISFFRFPVLDASVPLAEDGPVNVLIVPAKARNKTDARRLLAFMGQPAINGEF 330
Cdd:COG1653  273 KDAAPDfDVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQAKW 332
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 37-404 5.86e-45

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: 159.85  E-value: 5.86e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  37 NQRATWQAVFDQFHKANPDIDLKVSYVGEEAYKVQMSGWLAT-DPPDVLSWNNGERLAYFAKRGLIEDLSADWQKNGWND 115
Cdd:cd14749   12 TKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAgEGPDVFNLWPGGWLAEFVKAGLLLPLTDYLDPNGVDK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 116 TY-AAVKQSSTYGGKLYSLPLGYDAYGLFYRKDLFEKAGIHGEPADWAQFLDACRKLRAAGIAPIAVAARDAWTLAAWFD 194
Cdd:cd14749   92 RFlPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGVKPPKTWDELIEAAKKDKFKAKGQTGFGLLLGAQGGHWYF 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 195 YLDLRINGYAFHQKLMAGDVAYTDPrvrAVYAAWKKLID---DKYFIDNALSYDVDSLSPLIVNGQAAMTLMGTWYSAGL 271
Cdd:cd14749  172 QYLVRQAGGGPLSDDGSGKATFNDP---AFVQALQKLQDlvkAGAFQEGFEGIDYDDAGQAFAQGKAAMNIGGSWDLGAI 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 272 LSAT-RNPISFFRFPVLDAS-VPLAEDGPVNVLIVPAKARNKTDARRLLAFMGQPAINGEFAKGMGQLPSNN---KAPEP 346
Cdd:cd14749  249 KAGEpGGKIGVFPFPTVGKGaQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQYLEDVGLLPAKEvvaKDEDP 328

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 773064230 347 QDPISKIGFRTFAATPGGIAqFYDRDMTKEmADEGMKAMQQFLSDPTQLDAILQRLEQ 404
Cdd:cd14749  329 DPVAILGPFADVLNAAGSTP-FLDEYWPAA-AQVHKDAVQKLLTGKIDPEQVVKQAQS 384
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 36-387 2.04e-36

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: 137.04  E-value: 2.04e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  36 GNQRATWQAVFDQFHKANPDIDLKVSYVG---EEAYKVQMSgwLAT-DPPDVLsWNNGERLAYFAKRGLIEDLS--ADWQ 109
Cdd:cd14748   10 GPDGKALEELVDEFNKSHPDIKVKAVYQGsydDTLTKLLAA--LAAgTAPDVA-QVDASWVAQLADSGALEPLDdyIDKD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 110 KNGWNDTYAAVKQSSTYGGKLYSLPLGYDAYGLFYRKDLFEKAGIHGE--PADWAQFLDACRKLRAAG----IAPIAVAA 183
Cdd:cd14748   87 GVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEkpPKTWDELEEAAKKLKDKGgktgRYGFALPP 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 184 RDA-WTLAAWFdyldlringYAFHQKLM---AGDVAYTDPRVRAVYAAWKKLIDDKYFIDNALSYDVDSlspLIVNGQAA 259
Cdd:cd14748  167 GDGgWTFQALL---------WQNGGDLLdedGGKVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQD---AFISGKVA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 260 MTLMGTWYSAGLLSATrnpisfFRFPVLDASVPLAEDGPV------NVLIVPAKARNKTD-ARRLLAFMGQPAINGEFAK 332
Cdd:cd14748  235 MTINGTWSLAGIRDKG------AGFEYGVAPLPAGKGKKGatpaggASLVIPKGSSKKKEaAWEFIKFLTSPENQAKWAK 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 773064230 333 GMGQLPSNNKAPEP------QDPISKI-----GFRTFAATPGGIAQFYDRDMTKEM---------ADEGMKAMQQ 387
Cdd:cd14748  309 ATGYLPVRKSAAEDpeeflaENPNYKVavdqlDYAKPWGPPVPNGAEIRDELNEALeaallgkktPEEALKEAQE 383
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 36-352 5.31e-36

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: 136.00  E-value: 5.31e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  36 GNQRATWQAVFDQFHKANPDIDLKVSYVGEEAYKVQMS-GWLATDPPDVLsWNNGERLAYFAKRGLIEDLS---ADWQKN 111
Cdd:cd13585   10 PAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTtAAAAGTAPDVF-YVDGPWVPEFASNGALLDLDdyiEKDGLD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 112 GwnDTYAAVKQSSTYGGKLYSLPLGYDAYGLFYRKDLFEKAGIHGE-PADWAQFLDACRKLRAAGIAPIAVAARDAWTLA 190
Cdd:cd13585   89 D--DFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKpPWTWDELLEAAKKLTDKKGGQYGFALRGGSGGQ 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 191 AWFDYLdLRINGyAFHQKLMAGDVAYTDPRVRAVYAAWKKLIDDKYfIDNALSYDVDSLSPLIVNGQAAMTLMGTWYSAG 270
Cdd:cd13585  167 TQWYPF-LWSNG-GDLLDEDDGKATLNSPEAVEALQFYVDLYKDGV-APSSATTGGDEAVDLFASGKVAMMIDGPWALGT 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 271 LlsatRNPISFFRFPVldASVPLAEDGPVNVLI------VPAKARNKTDARRLLAFMGQPAINGEFAKGMGQLPSNNKAP 344
Cdd:cd13585  244 L----KDSKVKFKWGV--APLPAGPGGKRASVLggwglaISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAA 317


                 ....*...
gi 773064230 345 EPQDPISK 352
Cdd:cd13585  318 SAAAPDAK 325
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
29-343 1.48e-33

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 129.68  E-value: 1.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  29 KVNVAARGNQRATWQAVFDQFHKAnPDIDLKVSYVGEEAYKVQMS-GWLATDPPDVLSWNNgERLAYFAKRGLIEDLSAD 107
Cdd:COG2182   40 TLTVWVDDDEAEALEEAAAAFEEE-PGIKVKVVEVPWDDLREKLTtAAPAGKGPDVFVGAH-DWLGELAEAGLLAPLDDD 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 108 WQKngWNDTYAAVKQSSTYGGKLYSLPLGYDAYGLFYRKDLFEKAgihgEPADWAQFLDACRKLRAAGIAPIAVAARDAW 187
Cdd:COG2182  118 LAD--KDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKAE----PPKTWDELIAAAKKLTAAGKYGLAYDAGDAY 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 188 TLAAWFdyldLRINGYAFHQKLM-AGDVAYTDPRVRAVYAAWKKLIDDKYFiDNALSYDVdsLSPLIVNGQAAMTLMGTW 266
Cdd:COG2182  192 YFYPFL----AAFGGYLFGKDGDdPKDVGLNSPGAVAALEYLKDLIKDGVL-PADADYDA--ADALFAEGKAAMIINGPW 264

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 773064230 267 YSAGLLSATRNPISFFRFPVLDASVPLAEDGPVNVLIVPAKARNKTDARRLLAFMGQPAINGEFAKGMGQLPSNNKA 343
Cdd:COG2182  265 AAADLKKALGIDYGVAPLPTLAGGKPAKPFVGVKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAA 341
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 33-325 6.95e-32

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: 122.52  E-value: 6.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230   33 AARGNQRATWQAVFDQFHKANPDIDLKVSYVGEEAYKVQMSGWLATD--PPDVLsWNNGERLAYFAKRGLIEDLSADWQK 110
Cdd:pfam01547   1 AASLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGdgPADVF-ASDNDWIAELAKAGLLLPLDDYVAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  111 NGWNDTyaavkqsstygGKLYSLPLGYDAYGLFYRKDLFEKAGIhGEPADWAQFLDACRKLRAAGIAPIAVAARDAW-TL 189
Cdd:pfam01547  80 YLVLGV-----------PKLYGVPLAAETLGLIYNKDLFKKAGL-DPPKTWDELLEAAKKLKEKGKSPGGAGGGDASgTL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  190 AAWFDYLDLRINGYAFHQKLMAGD-VAYTDPRVRAVYAAWKKLIDDKYFIDNALSYDVDSLSPLIVNGQAAMTLMGTWY- 267
Cdd:pfam01547 148 GYFTLALLASLGGPLFDKDGGGLDnPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAa 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 773064230  268 ----SAGLLSATRNPISFFRFPVLDASVPLAEDGPVNV--LIVPAKARNKTDARRLLAFMGQPA 325
Cdd:pfam01547 228 laanKVKLKVAFAAPAPDPKGDVGYAPLPAGKGGKGGGygLAIPKGSKNKEAAKKFLDFLTSPE 291
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 43-361 4.58e-27

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: 111.25  E-value: 4.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  43 QAVFDQFHKANPDIDLKVSYVGEEAY--KVQMSgwLAT-DPPDVL----SWnngerLAYFAKRGLIEDLSADWQKNGWND 115
Cdd:cd14747   17 KELADEFEKENPGIEVKVQVLPWGDAhtKITTA--AASgDGPDVVqlgnTW-----VAEFAAMGALEDLTPYLEDLGGDK 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 116 TYAA-VKQSSTYGGKLYSLPLGYDAYGLFYRKDLFEKAGIHGEPADWAQFLDACRKLRAAG--IAPIAVAAR-DAW-TLA 190
Cdd:cd14747   90 DLFPgLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGDEAPKTWDELEAAAKKIKADGpdVSGFAIPGKnDVWhNAL 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 191 AWfdyldLRINGyafhqklmaGDVA--------YTDPRVRAVYAAWKKLIDDKYfIDNALSYDVDSLSPLIVNGQAAMTL 262
Cdd:cd14747  170 PF-----VWGAG---------GDLAtkdkwkatLDSPEAVAGLEFYTSLYQKGL-SPKSTLENSADVEQAFANGKVAMII 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 263 MGTWYSAGLLSATRNP---ISFFRFPVLDASVPLAEDGPVNvLIVPAKARNKTDARRLLAFMGQPAINGEFAKGMGQLPS 339
Cdd:cd14747  235 SGPWEIGAIREAGPDLagkWGVAPLPGGPGGGSPSFAGGSN-LAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGMLPA 313

                        330       340
                 ....*....|....*....|..
gi 773064230 340 NNKAPEPQDPISKIGFRTFAAT 361
Cdd:cd14747  314 NTSAWDDPSLANDPLLAVFAEQ 335
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 32-340 2.66e-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: 103.14  E-value: 2.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  32 VAARGNQRATWQAVFDQFHKANPDIDLKVSYVGEEA--YKVQMSGWLA--TDPPDVLS----WnngerLAYFAKRGLIED 103
Cdd:cd14750    6 AGSDGQEGELLKKAIAAFEKKHPDIKVEIEELPASSddQRQQLVTALAagSSAPDVLGldviW-----IPEFAEAGWLLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 104 LSADWQKNGWNDTYAAVKQSSTYGGKLYSLPLGYDAYGLFYRKDLFEKAGIhGEPADWAQFLDACRKLRAA--GIAPIAV 181
Cdd:cd14750   81 LTEYLKEEEDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYGP-EPPKTWDELLEAAKKRKAGepGIWGYVF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 182 AARDAWTLAAWFDYLDLRINGYAFHQKlmAGDVAYTDPRVRAVYAAWKKLIDDKYFIDNALSYDVDSLSPLIVNGQAAMt 261
Cdd:cd14750  160 QGKQYEGLVCNFLELLWSNGGDIFDDD--SGKVTVDSPEALEALQFLRDLIGEGISPKGVLTYGEEEARAAFQAGKAAF- 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 262 lMGTW-YSAGLLSATRNPIsFFRFPVldasVPL-AEDGPVNV-------LIVPAKARNKTDARRLLAFMGQPAINGEFAK 332
Cdd:cd14750  237 -MRNWpYAYALLQGPESAV-AGKVGV----APLpAGPGGGSAstlggwnLAISANSKHKEAAWEFVKFLTSPEVQKRRAI 310


                 ....*...
gi 773064230 333 GMGQLPSN 340
Cdd:cd14750  311 NGGLPPTR 318
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 44-348 2.70e-20

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 90.16  E-value: 2.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230   44 AVFDQFHKANpDIDLKVSYVGEEAYKVQMSGWLATD--PPDVLSWNNGERLAYFAKRGLIEDLSADWQKNGWNDTYAAVk 121
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGnaPDLDVVWIAADQLATLAEAGLLADLSDVDNLDDLPDALDAA- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  122 qssTYGGKLYSLPLGYDA-YGLFYRKDLFEKAGihGEPADWAQFLDACRKLraagiapiavAARDAWTLAAWFDYldlri 200
Cdd:pfam13416  79 ---GYDGKLYGVPYAASTpTVLYYNKDLLKKAG--EDPKTWDELLAAAAKL----------KGKTGLTDPATGWL----- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  201 ngyafHQKLMAGDVAYTDPRVR-----AVYAAWKKLIDDKYFIDNalsyDVDSLSPLIvNGQAAMTLMGTWYSAGLLSAT 275
Cdd:pfam13416 139 -----LWALLADGVDLTDDGKGvealdEALAYLKKLKDNGKVYNT----GADAVQLFA-NGEVAMTVNGTWAAAAAKKAG 208

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 773064230  276 RNpisffrfpvLDASVPlaEDGPV---NVLIVPAKARNK-TDARRLLAFMGQPAINGEFAKGMGQLPSNNKAPEPQD 348
Cdd:pfam13416 209 KK---------LGAVVP--KDGSFlggKGLVVPAGAKDPrLAALDFIKFLTSPENQAALAEDTGYIPANKSAALSDE 274
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 42-405 3.73e-17

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: 82.46  E-value: 3.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  42 WQAVFDQFHKANPDIDLKVSY-VGEEAYKVQMSGWLATDPPDVLSWNNgERLAYFAKRGLIEDLSADWQKNGWN--DTYA 118
Cdd:cd13522   16 VNELIAKFEKAYPGITVEVTYqDTEARRQFFSTAAAGGKGPDVVFGPS-DSLGPFAAAGLLAPLDEYVSKSGKYapNTIA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 119 AVKqsstYGGKLYSLPLGYDAYGLFYRKDLFEKAgihgEPADWAQFLDACRKLRAAGIAPIAVAARDAWTLAAWFDyldl 198
Cdd:cd13522   95 AMK----LNGKLYGVPVSVGAHLMYYNKKLVPKN----PPKTWQELIALAQGLKAKNVWGLVYNQNEPYFFAAWIG---- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 199 RINGYAFHQKLMAGDVAYTDPRVRAVYAAWKKLIdDKYFIDNALSYD--VDSlspLIVNGQAAMTLMGTWYSAGLLSATR 276
Cdd:cd13522  163 GFGGQVFKANNGKNNPTLDTPGAVEALQFLVDLK-SKYKIMPPETDYsiADA---LFKAGKAAMIINGPWDLGDYRQALK 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 277 NPISFFRFPVLDASVPLAEDGPVNVLIVPAKARNKTDARRLLAFMGQPAINGEFAKGMGQLPSNNKApEPQDPI-SKIGF 355
Cdd:cd13522  239 INLGVAPLPTFSGTKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDIPANLQA-YESPAVqNKPAQ 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 773064230 356 RTFAAtpggIAQfYDRDM--TKEMA---DEGMKAMQQFLSDPTQLDAILQRLEQT 405
Cdd:cd13522  318 KASAE----QAA-YGVPMpnIPEMRavwDAFRIAVNSVLAGKVTPEAAAKDAQQE 367
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 40-345 1.80e-15

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: 77.42  E-value: 1.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  40 ATWQAVFDQFHKANPDIDLK---VSYVG-EEAYKVQMSGwlaTDPPDVL----SWnngerLAYFAKRGLIEDLSADWQKN 111
Cdd:cd14751   14 VLYEKLIPAFEKEYPKIKVKavrVPFDGlHNQIKTAAAG---GQAPDVMradiAW-----VPEFAKLGYLQPLDGTPAFD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 112 GWNDTYAAVKQSSTYGGKLYSLPLGYDAYGLFYRKDLFEKAGIhGEPADWAQFLDACRK-LRAAGIAPIAVAARDAWTLA 190
Cdd:cd14751   86 DIVDYLPGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGT-EVPKTMDELVAAAKAiKKKKGRYGLYISGDGPYWLL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 191 AWFdyldlringYAFhqklmAGDvaYTDPRVRAVY-------AAWKKLID--DKYFIDNALSYDVDSLSPLIVNGQAAMT 261
Cdd:cd14751  165 PFL---------WSF-----GGD--LTDEKKATGYlnspesvRALETIVDlyDEGAITPCASGGYPNMQDGFKSGRYAMI 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 262 LMGTWYSAGLLSATRnpisFFR-FPVLDASVPLAEDGPVNV-----LIVPAKARNKTDARRLLAFMGQPAINGEFAKGMG 335
Cdd:cd14751  229 VNGPWAYADILGGKE----FKDpDNLGIAPVPAGPGGSGSPvggedLVIFKGSKNKDAAWKFVKFMSSAEAQALTAAKLG 304

                        330
                 ....*....|
gi 773064230 336 QLPSNNKAPE 345
Cdd:cd14751  305 LLPTRTSAYE 314
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 33-343 3.83e-12

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: 67.02  E-value: 3.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  33 AARGNQRATWQAVFDQFHKANPDIDLKVSYVGEEAYKVQMSgwlATDP----PDVLSWNNgERLAYFAKRGLIEDLSADW 108
Cdd:cd13657    7 ALTGAEEDALQQIIDEFEAKYPVPNVKVPFEKKPDLQNKLL---TAIPagegPDLFIWAH-DWIGQFAEAGLLVPISDYL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 109 QKNGWNDTYAAVKQSSTYGGKLYSLPLGYDAYGLFYRKDLFEKAgihgePADWAQFLDACRKL--RAAGIAPIAVAARDA 186
Cdd:cd13657   83 SEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQP-----PETTDELLAIMKDHtdPAAGSYGLAYQVSDA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 187 WTLAAWFDYLdlriNGYAFHQKlmAGDVAYTDPRVRAVYAAWKKLIDDkyFIDNALSYdvDSLSPLIVNGQAAMTLMGTW 266
Cdd:cd13657  158 YFVSAWIFGF----GGYYFDDE--TDKPGLDTPETIKGIQFLKDFSWP--YMPSDPSY--NTQTSLFNEGKAAMIINGPW 227

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 773064230 267 YSAGLLSATRNpISFFRFPVLDASVPLAEDGPVNVLIV--PAKARNKTDARRLLAFMGQPAINGEFAKGMGQLPSNNKA 343
Cdd:cd13657  228 FIGGIKAAGID-LGVAPLPTVDGTNPPRPYSGVEGIYVtkYAERKNKEAALDFAKFFTTAEASKILADENGYVPAATNA 305
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
43-349 3.98e-09

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 57.61  E-value: 3.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  43 QAVFDQFHKANpDIDLKVSYVG--EEAY-KVQMSGwlatDPPDVLSwNNGERLAYFAKRGLIEDLsaDWQK-NGWNDTYA 118
Cdd:COG0687   42 PDVLEPFEKET-GIKVVYDTYDsnEEMLaKLRAGG----SGYDVVV-PSDYFVARLIKAGLLQPL--DKSKlPNLANLDP 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 119 AVKQSSTYGGKLYSLPLGYDAYGLFYRKDLFEKagihgEPADWAQFLDAcrklRAAGiaPIAV--AARDAWTLAawfdyl 196
Cdd:COG0687  114 RFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKE-----PPTSWADLWDP----EYKG--KVALldDPREVLGAA------ 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 197 dLRINGYafhqklmagDVAYTDP----RVRAVYAAWKKLIddkyfidNALSYDVDSLSPLIVNGQAAMTLMgtWYSAGLL 272
Cdd:COG0687  177 -LLYLGY---------DPNSTDPadldAAFELLIELKPNV-------RAFWSDGAEYIQLLASGEVDLAVG--WSGDALA 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 273 SATRNPisffrfPVlDASVPlaEDGP---VNVLIVPAKARNKTDARRLLAFMGQPAINGEFAKGMGQLPSNNKAPEPQDP 349
Cdd:COG0687  238 LRAEGP------PI-AYVIP--KEGAllwFDNMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAARELLPP 308
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 36-343 4.37e-09

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: 57.69  E-value: 4.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  36 GNQRATWQAVFDQFHKANpDIDLKVSYVGEEAYKVQMS-GWLATDPPDVLSWNNgERLAYFAKRGLIEDLS-ADWQKNGW 113
Cdd:cd13586    9 DGELEYLKELAEEFEKKY-GIKVEVVYVDSGDTREKFItAGPAGKGPDVFFGPH-DWLGELAAAGLLAPIPeYLAVKIKN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 114 NDT-YAAVkqssTYGGKLYSLPLGYDAYGLFYRKDLFEKAgihgePADWAQFLDACRK--LRAAGIAPIAVAARDAWTLA 190
Cdd:cd13586   87 LPVaLAAV----TYNGKLYGVPVSVETIALFYNKDLVPEP-----PKTWEELIALAKKfnDKAGGKYGFAYDQTNPYFSY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 191 AWFDYLDlrinGYAFHQKlmagDVAYTDPRV-RAVYAAWKKLIDDKYFIDNALSYDVDS--LSPLIVNGQAAMTLMGTWY 267
Cdd:cd13586  158 PFLAAFG----GYVFGEN----GGDPTDIGLnNEGAVKGLKFIKDLKKKYKVLPPDLDYdiADALFKEGKAAMIINGPWD 229

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 773064230 268 SAGLLSATRNpisfF---RFPVLDASVPLAEDGPVNVLIVPAKARNKTDARRLLAFMGQPAINGEFAKGMGQLPSNNKA 343
Cdd:cd13586  230 LADYKDAGIN----FgvaPLPTLPGGKQAAPFVGVQGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALKDA 304
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 51-174 9.25e-09

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: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 56.98  E-value: 9.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  51 KANPDIDLKVSYVGEEAYKVQMSGWLAT-DPPDVLSWNNGERLAYFAKRGLIEDLS----------ADWQKNGWNDTYAA 119
Cdd:cd13583   27 EEKTNVKFKRTPIPSSDYETKRSLLIASgDAPDIIPVLYPGEENEFVASGALLPISdyldympnykKYVEKWGLGKELAT 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 773064230 120 VKQSStygGKLYSLP-LGYDA---YGLFYRKDLFEKAGIHgEPADWAQFLDACRKLRAA 174
Cdd:cd13583  107 GRQSD---GKYYSLPgLHEDPgvqYSFLYRKDIFEKAGIK-IPTTWDEFYAALKKLKEK 161
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 81-363 1.88e-08

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: 55.95  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  81 PDVLSWNNgERLAYFAKRGLIEDLSAD-WQKNGWNDTyaAVKQSsTYGGKLYSLPLGYDAYGLFYRKDLFEKAgihgePA 159
Cdd:cd13658   54 PDVMVAPH-DRIGSAVLQGLLSPIKLSkDKKKGFTDQ--ALKAL-TYDGKLYGLPAAVETLALYYNKDLVKNA-----PK 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 160 DWAQFLDACRKLraagiapiavAARDAWTLAAWFDYLDLRIN--------GYAFHQK---LMAGDVAYTDPR-VRAVYAA 227
Cdd:cd13658  125 TFDELEALAKDL----------TKEKGKQYGFLADATNFYYSygllagngGYIFKKNgsdLDINDIGLNSPGaVKAVKFL 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 228 wKKLIDDKYFIDNALSydvDSLSPLIVNGQAAMTLMGTWYSAGLLSATRN----PIsffrfPVLDASVPLAEDGPVNVLI 303
Cdd:cd13658  195 -KKWYTEGYLPKGMTG---DVIQGLFKEGKAAAVIDGPWAIQEYQEAGVNygvaPL-----PTLPNGKPMAPFLGVKGWY 265

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 773064230 304 VPAKARNKTDARRLLAFMGQPAINGEFAKGMGQLPSN----NKAPEPQDPISK---IGFRTFAATPG 363
Cdd:cd13658  266 LSAYSKHKEWAQKFMEFLTSKENLKKRYDETNEIPPRkdvrSDPEIKNNPLTSafaKQASRAVPMPN 332
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 43-343 1.87e-06

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: 49.15  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  43 QAVFDQFHKANpDIDLKVSYV--GEEAY-KVQMSGWLATD---PPDVLswnngerLAYFAKRGLIEDLSADWQKNgWNDT 116
Cdd:cd13590   13 PEVLKAFEKET-GVKVNYDTYdsNEEMLaKLRAGGGSGYDlvvPSDYM-------VERLIKQGLLEPLDHSKLPN-LKNL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 117 YAAVKQSSTYGGKLYSLPLGYDAYGLFYRKDLFEkagihGEPADWAQFLDAcrklrAAGIAPIAV--AARDAWTLAawfd 194
Cdd:cd13590   84 DPQFLNPPYDPGNRYSVPYQWGTTGIAYNKDKVK-----EPPTSWDLDLWD-----PALKGRIAMldDAREVLGAA---- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 195 yldLRINGYafhqklmagDVAYTDPRVRAvyAAWKKLIDDKyfiDNALSYDVDSLSPLIVNGQAAMTLMgtwYSAGLLSA 274
Cdd:cd13590  150 ---LLALGY---------SPNTTDPAELA--AAAELLIKQK---PNVRAFDSDSYVQDLASGEIWLAQA---WSGDALQA 209

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 773064230 275 TRnpisffRFPVLDASVPlAEDGPVNV--LIVPAKARNKTDARRLLAFMGQPAINGEFAKGMGQLPSNNKA 343
Cdd:cd13590  210 NR------ENPNLKFVIP-KEGGLLWVdnMAIPKGAPNPELAHAFINFLLDPEVAAKNAEYIGYATPNKAA 273
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
79-266 1.14e-05

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 47.31  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  79 DPPDVLSWNNgERLAYFAKRGLIEDL--SADWQKNGWNDTYAAVkqssTYGGKLYSLPLGYDAYGLFYRKDLFEKAgihg 156
Cdd:PRK09474  81 DGPDIIFWAH-DRFGGYAQSGLLAEVtpSKAFKDKLVPFTWDAV----RYNGKLIGYPIAVEALSLIYNKDLVPTP---- 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 157 ePADWAQFLDACRKLRAAGIAPIavaardAWTLA-AWFDYLDLRING-YAFhqKLMAG-----DVAYTDPRVRAVYAAWK 229
Cdd:PRK09474 152 -PKTWEEIPALDKELKAKGKSAI------MWNLQePYFTWPLIAADGgYAF--KFENGgydvkDVGVNNAGAKAGLQFLV 222

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 773064230 230 KLIDDKYfidnaLSYDVD-SLSPLIVN-GQAAMTLMGTW 266
Cdd:PRK09474 223 DLVKNKH-----MNADTDySIAEAAFNkGETAMTINGPW 256
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 56-154 4.62e-05

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: 45.40  E-value: 4.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  56 IDLKVSYVGEEAYKVQMSGWLAT-DPPDVLSWNNGERLAYFAKRGLIEDLSADWQKNGwnDTYAAV-----KQSSTYGGK 129
Cdd:cd13580   34 IDVKVKWVPDSSYDEKLNLALASgDLPDIVVVNDPQLSITLVKQGALWDLTDYLDKYY--PNLKKIieqegWDSASVDGK 111

                         90       100
                 ....*....|....*....|....*...
gi 773064230 130 LYSLPLGYDAY---GLFYRKDLFEKAGI 154
Cdd:cd13580  112 IYGIPRKRPLIgrnGLWIRKDWLDKLGL 139
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 79-266 9.03e-05

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: 44.12  E-value: 9.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  79 DPPDVLSWNNgERLAYFAKRGLIEDLSAD--WQKNGWNDTYAAVKqsstYGGKLYSLPLGYDAYGLFYRKDLfekagIHG 156
Cdd:cd13656   51 DGPDIIFWAH-DRFGGYAQSGLLAEITPDkaFQDKLYPFTWDAVR----YNGKLIAYPIAVEALSLIYNKDL-----LPN 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 157 EPADWAQFLDACRKLRAAGIAPIAVAARD---AWTLAAwfdyldlRINGYAF---HQKLMAGDVAYTDPRVRAVYAAWKK 230
Cdd:cd13656  121 PPKTWEEIPALDKELKAKGKSALMFNLQEpyfTWPLIA-------ADGGYAFkyeNGKYDIKDVGVDNAGAKAGLTFLVD 193

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 773064230 231 LIDDKYFIDNAlSYDVdsLSPLIVNGQAAMTLMGTW 266
Cdd:cd13656  194 LIKNKHMNADT-DYSI--AEAAFNKGETAMTINGPW 226
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 37-338 3.75e-04

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: 41.83  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  37 NQRATWQAVFDQFHKANPdIDLK-VSYVGEEAY-KVQMSgwlATDPP-DVLsWNNGERLAYFAKRGLIEDLsaDWQKNGw 113
Cdd:cd13589   11 YEDAQRKAVIEPFEKETG-IKVVyDTGTSADRLaKLQAQ---AGNPQwDVV-DLDDGDAARAIAEGLLEPL--DYSKIP- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 114 NDTYAAVKQSStygGKLYSLPLGYDAYGLFYRKDLFEKAGihgEPADWAQFLDAcrklraAGIAPIAVAARDAWTLAAWF 193
Cdd:cd13589   83 NAAKDKAPAAL---KTGYGVGYTLYSTGIAYNTDKFKEPP---TSWWLADFWDV------GKFPGPRILNTSGLALLEAA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 194 dyldLRINGyafhqklmaGDVAYTDprVRAVYAAWKKLIDDKYFIDNALSydvdSLSPLIVNGQAAMTlMGTWYSAGLLS 273
Cdd:cd13589  151 ----LLADG---------VDPYPLD--VDRAFAKLKELKPNVVTWWTSGA----QLAQLLQSGEVDMA-PAWNGRAQALI 210

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 773064230 274 ATRNPISFfrfpVLDASVPLAEdgpVNVLIVPAKARNKTDARRLLAFMGQPAINGEFAKGMGQLP 338
Cdd:cd13589  211 DAGAPVAF----VWPKEGAILG---PDTLAIVKGAPNKELAMKFINFALSPEVQAALAEALGYGP 268
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
128-177 1.01e-03

sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 40.94  E-value: 1.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 773064230 128 GKLYSLPLGYDAYGLFYRKDLFEKAGIHGE--PADWAQFLDACRKLRAAGIA 177
Cdd:PRK10974 135 GHLLSQPFNSSTPVLYYNKDAFKKAGLDPEqpPKTWQDLAAYAAKLRAAGMK 186
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 37-149 1.38e-03

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: 40.41  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  37 NQRATWQAVFDQFHKANPDIDLKVSY--VGEEAYKVQmsgwLATDP---PDVLSWNNGErLAYFAKRGLIEDLSADWQKN 111
Cdd:cd13655    9 EDQEWLKEMVDAFKEKHPEWKITITIgvVGEADAKDE----VLKDPsaaADVFAFANDQ-LGELVDAGAIYPLTGSAVDK 83

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 773064230 112 GWNDTYAAVKQSSTYGGKLYSLPLGYDAYGLFYRKDLF 149
Cdd:cd13655   84 IKNTNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKL 121
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 45-348 4.64e-03

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 38.76  E-value: 4.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230  45 VFDQFHKANpdiDLKVSYV----GEEAYKVQMSGwlATDPPDVLSWNNGERLAYFAKRGLIEDLSADWqkngWNDTYAAV 120
Cdd:COG1840    1 LLEAFEKKT---GIKVNVVrggsGELLARLKAEG--GNPPADVVWSGDADALEQLANEGLLQPYKSPE----LDAIPAEF 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 121 KqsstyGGKLYSLPLGYDAYGLFYRKDLFEKAGIhgePADWAQFLDAcrKLRAA-GIAPIAVAArDAWTLAAWFDYLDLR 199
Cdd:COG1840   72 R-----DPDGYWFGFSVRARVIVYNTDLLKELGV---PKSWEDLLDP--EYKGKiAMADPSSSG-TGYLLVAALLQAFGE 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 773064230 200 INGYAFHQKLMAGDVAYTDpRVRAVYAAwkkliddkyfidnalsydvdslsplIVNGQAAMTLMGTWYSAGLLsATRNPI 279
Cdd:COG1840  141 EKGWEWLKGLAANGARVTG-SSSAVAKA-------------------------VASGEVAIGIVNSYYALRAK-AKGAPV 193

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 773064230 280 SFFrFPvldasvplaEDG-PVNV--LIVPAKARNKTDARRLLAFMGQPAINGEFAKGMGQLPSNNKAPEPQD 348
Cdd:COG1840  194 EVV-FP---------EDGtLVNPsgAAILKGAPNPEAAKLFIDFLLSDEGQELLAEEGYEYPVRPDVEPPEG 255
 
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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