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Conserved domains on  [gi|489612332|ref|WP_003516773|]
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MULTISPECIES: extracellular solute-binding protein [Rhizobium/Agrobacterium group]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Periplasmic_Binding_Protein_Type_2 super family cl21456
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 35-406 2.64e-72

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


The actual alignment was detected with superfamily member cd14748:

Pssm-ID: 473866 [Multi-domain]  Cd Length: 385  Bit Score: 231.41  E-value: 2.64e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  35 WIYCGDKMDPIHEKYIKEWEGKNAGWKVVPEVVGWAQ-CQDKATTLAAAGTPVAMAYVGSRTLKQFAQNDLIVPVP---- 109
Cdd:cd14748    5 WHGMSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDdTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDdyid 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 110 MTEDEKKTYYPNIVDTVTFEDTQWGVPVAFSTKALYWNKDLFKQAGLDPEVPPKTWAEEIAFAKQIK---EKTGVAGYGL 186
Cdd:cd14748   85 KDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKdkgGKTGRYGFAL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 187 PAktfDNTMHQFMHWVYTNNGKVIDGD--KITVDSPQVLAALKAYKDItpYSVEGPTAYE-QNEIRAIFLDGKVGMIQAG 263
Cdd:cd14748  165 PP---GDGGWTFQALLWQNGGDLLDEDggKVTFNSPEGVEALEFLVDL--VGKDGVSPLNdWGDAQDAFISGKVAMTING 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 264 SGAATRLQET--KINWGIATLPlGPEAKGPGTLLITDSLAIFKGTGVEEKAT-EFAKFITSPGPQGEYELQGgaGLTPLR 340
Cdd:cd14748  240 TWSLAGIRDKgaGFEYGVAPLP-AGKGKKGATPAGGASLVIPKGSSKKKEAAwEFIKFLTSPENQAKWAKAT--GYLPVR 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489612332 341 PSPKVDE--FIAKDPFWKPLIDGIAYGGPE-PLFTDYKGFQDTMIEMVQSVVTGKATPEDAAKKASAAL 406
Cdd:cd14748  317 KSAAEDPeeFLAENPNYKVAVDQLDYAKPWgPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
 
Name Accession Description Interval E-value
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 35-406 2.64e-72

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: 231.41  E-value: 2.64e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  35 WIYCGDKMDPIHEKYIKEWEGKNAGWKVVPEVVGWAQ-CQDKATTLAAAGTPVAMAYVGSRTLKQFAQNDLIVPVP---- 109
Cdd:cd14748    5 WHGMSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDdTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDdyid 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 110 MTEDEKKTYYPNIVDTVTFEDTQWGVPVAFSTKALYWNKDLFKQAGLDPEVPPKTWAEEIAFAKQIK---EKTGVAGYGL 186
Cdd:cd14748   85 KDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKdkgGKTGRYGFAL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 187 PAktfDNTMHQFMHWVYTNNGKVIDGD--KITVDSPQVLAALKAYKDItpYSVEGPTAYE-QNEIRAIFLDGKVGMIQAG 263
Cdd:cd14748  165 PP---GDGGWTFQALLWQNGGDLLDEDggKVTFNSPEGVEALEFLVDL--VGKDGVSPLNdWGDAQDAFISGKVAMTING 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 264 SGAATRLQET--KINWGIATLPlGPEAKGPGTLLITDSLAIFKGTGVEEKAT-EFAKFITSPGPQGEYELQGgaGLTPLR 340
Cdd:cd14748  240 TWSLAGIRDKgaGFEYGVAPLP-AGKGKKGATPAGGASLVIPKGSSKKKEAAwEFIKFLTSPENQAKWAKAT--GYLPVR 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489612332 341 PSPKVDE--FIAKDPFWKPLIDGIAYGGPE-PLFTDYKGFQDTMIEMVQSVVTGKATPEDAAKKASAAL 406
Cdd:cd14748  317 KSAAEDPeeFLAENPNYKVAVDQLDYAKPWgPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 8-409 5.73e-70

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 224.54  E-value: 5.73e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332   8 LALCAFAFAG-STALGTVAAHAADKEISWIYCGDKMDPIHEKYIKEWEGKNAGWKVVPEVVGWAQCQDKATTLAAAGTPV 86
Cdd:COG1653    9 AAALALALAAcGGGGSGAAAAAGKVTLTVWHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  87 AMAYVGSRTLKQFAQNDLIVP----VPMTEDEKKTYYPNIVDTVTFEDTQWGVPVAFSTKALYWNKDLFKQAGLDpevPP 162
Cdd:COG1653   89 DVVQVDSGWLAEFAAAGALVPlddlLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLD---PP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 163 KTWAEEIAFAKQIKEKTGVAGYGLPAKTFDntmhQFMHWVYTNNGKVIDGD-KITVDSPQVLAALKAYKDI--TPYSVEG 239
Cdd:COG1653  166 KTWDELLAAAKKLKAKDGVYGFALGGKDGA----AWLDLLLSAGGDLYDEDgKPAFDSPEAVEALEFLKDLvkDGYVPPG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 240 PTAYEQNEIRAIFLDGKVGMIQAGSGAATRLQET--KINWGIATLPLGPEAKGPGTLLITDSLAIFKGTGVEEKATEFAK 317
Cdd:COG1653  242 ALGTDWDDARAAFASGKAAMMINGSWALGALKDAapDFDVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAAWKFLK 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 318 FITSPGPQGEYelqggagltplrpspkvdefiakdpfwkplidgiayggpeplftdykgfqdtmiEMVQSVVTGKATPED 397
Cdd:COG1653  322 FLTSPEAQAKW------------------------------------------------------DALQAVLLGQKTPEE 347

                        410
                 ....*....|..
gi 489612332 398 AAKKASAALEQY 409
Cdd:COG1653  348 ALDAAQAAANAA 359
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 48-353 1.27e-27

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 110.57  E-value: 1.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332   48 KYIKEWEGKNaGWKVVPEVVGWAQCQDKATTLAAAGTP--VAMAYVGSRTLKQFAQNDLIVPvpMTEDEKKTYYPNIVDT 125
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNApdLDVVWIAADQLATLAEAGLLAD--LSDVDNLDDLPDALDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  126 VTFEDTQWGVPVAFSTK-ALYWNKDLFKQAGLDPevppKTWAEEIAFAKQIKEKTGVAGYGlpaktfdNTMHQFMHWVyt 204
Cdd:pfam13416  78 AGYDGKLYGVPYAASTPtVLYYNKDLLKKAGEDP----KTWDELLAAAAKLKGKTGLTDPA-------TGWLLWALLA-- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  205 nNGKVIDGD-KITVDSPQVLAALKAYKDitpysvEGPTAYEQNEIRAIFLDGKVGMIQAGSGAATRLQETKINWGIAtlp 283
Cdd:pfam13416 145 -DGVDLTDDgKGVEALDEALAYLKKLKD------NGKVYNTGADAVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAV--- 214

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489612332  284 lgpeAKGPGTLLITDSLAIFKGTGVEEKAT-EFAKFITSpgPQGEYELQGGAGLTPLRPSPKVDEFIAKDP 353
Cdd:pfam13416 215 ----VPKDGSFLGGKGLVVPAGAKDPRLAAlDFIKFLTS--PENQAALAEDTGYIPANKSAALSDEVKADP 279
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
136-402 1.22e-13

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 72.14  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 136 PVAFSTKALYWNKDLFKQAGLDPEVPPKTWAEEIAFAKQIKEKTGVAGY-----------------GLPAKTfdntmhqf 198
Cdd:PRK10974 141 PFNSSTPVLYYNKDAFKKAGLDPEQPPKTWQDLAAYAAKLRAAGMKCGYasgwqgwiqlenfsawhGLPFAS-------- 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 199 mhwvyTNNGkvIDGD--KITVDSPQVLAALKAYKDITPysvEGPTAY--EQNEIRAIFLDGKVGMIQAGSGA-ATRLQET 273
Cdd:PRK10974 213 -----KNNG--FDGTdaVLEFNKPEQVKHIALLEEMNK---KGDFTYvgRKDESTEKFYNGDCAITTASSGSlANIRKYA 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 274 KINWGIATLPLGPEAKG-PGTLLITD-SLAIFKGtgvEEKAT-----EFAKFITSPGPQGE--------------YELQG 332
Cdd:PRK10974 283 KFNYGVGMMPYDADVKGaPQNAIIGGaSLWVMQG---KDKETykgvaKFLDFLAKPENAAEwhqktgylpittaaYDLTR 359

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489612332 333 GAGLTPLRPSPKV--DEFIAKDPfwKPLIDGIAYGGPEPLFTdykgfqdTMIEMVQSVVTGKATPEDAAKKA 402
Cdd:PRK10974 360 EQGFYEKNPGADTatRQMLNKPP--LPFTKGLRLGNMPQIRT-------IVDEELESVWTGKKTPQQALDSA 422
 
Name Accession Description Interval E-value
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 35-406 2.64e-72

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: 231.41  E-value: 2.64e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  35 WIYCGDKMDPIHEKYIKEWEGKNAGWKVVPEVVGWAQ-CQDKATTLAAAGTPVAMAYVGSRTLKQFAQNDLIVPVP---- 109
Cdd:cd14748    5 WHGMSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDdTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDdyid 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 110 MTEDEKKTYYPNIVDTVTFEDTQWGVPVAFSTKALYWNKDLFKQAGLDPEVPPKTWAEEIAFAKQIK---EKTGVAGYGL 186
Cdd:cd14748   85 KDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKdkgGKTGRYGFAL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 187 PAktfDNTMHQFMHWVYTNNGKVIDGD--KITVDSPQVLAALKAYKDItpYSVEGPTAYE-QNEIRAIFLDGKVGMIQAG 263
Cdd:cd14748  165 PP---GDGGWTFQALLWQNGGDLLDEDggKVTFNSPEGVEALEFLVDL--VGKDGVSPLNdWGDAQDAFISGKVAMTING 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 264 SGAATRLQET--KINWGIATLPlGPEAKGPGTLLITDSLAIFKGTGVEEKAT-EFAKFITSPGPQGEYELQGgaGLTPLR 340
Cdd:cd14748  240 TWSLAGIRDKgaGFEYGVAPLP-AGKGKKGATPAGGASLVIPKGSSKKKEAAwEFIKFLTSPENQAKWAKAT--GYLPVR 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489612332 341 PSPKVDE--FIAKDPFWKPLIDGIAYGGPE-PLFTDYKGFQDTMIEMVQSVVTGKATPEDAAKKASAAL 406
Cdd:cd14748  317 KSAAEDPeeFLAENPNYKVAVDQLDYAKPWgPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 8-409 5.73e-70

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 224.54  E-value: 5.73e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332   8 LALCAFAFAG-STALGTVAAHAADKEISWIYCGDKMDPIHEKYIKEWEGKNAGWKVVPEVVGWAQCQDKATTLAAAGTPV 86
Cdd:COG1653    9 AAALALALAAcGGGGSGAAAAAGKVTLTVWHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  87 AMAYVGSRTLKQFAQNDLIVP----VPMTEDEKKTYYPNIVDTVTFEDTQWGVPVAFSTKALYWNKDLFKQAGLDpevPP 162
Cdd:COG1653   89 DVVQVDSGWLAEFAAAGALVPlddlLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLD---PP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 163 KTWAEEIAFAKQIKEKTGVAGYGLPAKTFDntmhQFMHWVYTNNGKVIDGD-KITVDSPQVLAALKAYKDI--TPYSVEG 239
Cdd:COG1653  166 KTWDELLAAAKKLKAKDGVYGFALGGKDGA----AWLDLLLSAGGDLYDEDgKPAFDSPEAVEALEFLKDLvkDGYVPPG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 240 PTAYEQNEIRAIFLDGKVGMIQAGSGAATRLQET--KINWGIATLPLGPEAKGPGTLLITDSLAIFKGTGVEEKATEFAK 317
Cdd:COG1653  242 ALGTDWDDARAAFASGKAAMMINGSWALGALKDAapDFDVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAAWKFLK 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 318 FITSPGPQGEYelqggagltplrpspkvdefiakdpfwkplidgiayggpeplftdykgfqdtmiEMVQSVVTGKATPED 397
Cdd:COG1653  322 FLTSPEAQAKW------------------------------------------------------DALQAVLLGQKTPEE 347

                        410
                 ....*....|..
gi 489612332 398 AAKKASAALEQY 409
Cdd:COG1653  348 ALDAAQAAANAA 359
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 47-406 1.59e-66

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: 216.50  E-value: 1.59e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  47 EKYIKEWEGKNAGWKVVPEVVGWAQCQDKATTLAAAGTPVAMAYVGSRTLKQFAQNDLIVPV--PMTEDEKKT-YYPNIV 123
Cdd:cd13585   17 KKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLddYIEKDGLDDdFPPGLL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 124 DTVTFEDTQWGVPVAFSTKALYWNKDLFKQAGLDPEvPPKTWAEEIAFAKQIKE-KTGVAGYGLPAKtfDNTMHQFMHWV 202
Cdd:cd13585   97 DAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPK-PPWTWDELLEAAKKLTDkKGGQYGFALRGG--SGGQTQWYPFL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 203 YTNNGKVIDGD--KITVDSPQVLAALKAYKD-ITPYSVEGPTAYEQNEIRAIFLDGKVGMIQAGSGAATRLQETKI--NW 277
Cdd:cd13585  174 WSNGGDLLDEDdgKATLNSPEAVEALQFYVDlYKDGVAPSSATTGGDEAVDLFASGKVAMMIDGPWALGTLKDSKVkfKW 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 278 GIATLPLGPeAKGPGTLLITDSLAIFKGTGVEEKATEFAKFITSPGPQGEYELQGGAGLTPLRPSPKVDEFIAKDPFWKP 357
Cdd:cd13585  254 GVAPLPAGP-GGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAASAAAPDAKPALALAA 332

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489612332 358 LIDGIAYGGPEPLFTDYKGFQDTMIEMVQSVVTGK--ATPEDAAKKASAAL 406
Cdd:cd13585  333 AADALAAAVPPPVPPPWPEVYPILSEALQEALLGAlgKSPEEALKEAAKEI 383
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 36-407 1.91e-56

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: 190.28  E-value: 1.91e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  36 IYCGDKMDPIHEKYIKEWEGKNAGWKVVPEVVGWAQCQDKATTLAAAGT-PVAMAYVGSRTLKQFAQNDLIVPVPMTEDE 114
Cdd:cd14749    7 YFTGDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEgPDVFNLWPGGWLAEFVKAGLLLPLTDYLDP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 115 ---KKTYYPNIVDTVTFEDTQWGVPVAFSTKALYWNKDLFKQAGldPEVPPKTWAEEIAFAKQIKEK-TGVAGYGLPAKt 190
Cdd:cd14749   87 ngvDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAG--GVKPPKTWDELIEAAKKDKFKaKGQTGFGLLLG- 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 191 FDNTMHQFMHWVYTNNGKVID---GDKITVDSPQVLAALKAYKDI--TPYSVEGPTAYEQNEIRAIFLDGKVGMIQAGSG 265
Cdd:cd14749  164 AQGGHWYFQYLVRQAGGGPLSddgSGKATFNDPAFVQALQKLQDLvkAGAFQEGFEGIDYDDAGQAFAQGKAAMNIGGSW 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 266 AATRL--QETKINWGIATLPLGPEAKGPGTLLITD-SLAIFKGTGVEEKATEFAKFITSPGPQGEYELQGgaGLTPLRPS 342
Cdd:cd14749  244 DLGAIkaGEPGGKIGVFPFPTVGKGAQTSTIGGSDwAIAISANGKKKEAAVKFLKYLTSPEVMKQYLEDV--GLLPAKEV 321

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489612332 343 PKVDEFIAKDPFWKPLIDGIAYGGPEPLFTDYKG-FQDTMIEMVQSVVTGKATPEDAAKKASAALE 407
Cdd:cd14749  322 VAKDEDPDPVAILGPFADVLNAAGSTPFLDEYWPaAAQVHKDAVQKLLTGKIDPEQVVKQAQSAAA 387
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
7-408 4.77e-55

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 187.08  E-value: 4.77e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332   7 GLALCAfafAGSTALGTVAAHAADKEISWIYCGDKMDPIhEKYIKEWEGKNaGWKVVPEVVGWAQCQDKATTLAAAGTPV 86
Cdd:COG2182   18 ALAACG---SGSSSSGSSSAAGAGGTLTVWVDDDEAEAL-EEAAAAFEEEP-GIKVKVVEVPWDDLREKLTTAAPAGKGP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  87 AMAYVGSRTLKQFAQNDLIVPVPMTEDEKKTYYPNIVDTVTFEDTQWGVPVAFSTKALYWNKDLFkqagldPEVPPKTWA 166
Cdd:COG2182   93 DVFVGAHDWLGELAEAGLLAPLDDDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLV------KAEPPKTWD 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 167 EEIAFAKQIKeKTGVAGYGLPAKTFdntmHQFMHWVYTNNGKVI-----DGDKITVDSPQVLAALKAYKDITPYSVeGPT 241
Cdd:COG2182  167 ELIAAAKKLT-AAGKYGLAYDAGDA----YYFYPFLAAFGGYLFgkdgdDPKDVGLNSPGAVAALEYLKDLIKDGV-LPA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 242 AYEQNEIRAIFLDGKVGMIQAGSGAATRLQE-TKINWGIATLPLGPEAKGPGTLLITDSLAIFKGTGVEEKATEFAKFIT 320
Cdd:COG2182  241 DADYDAADALFAEGKAAMIINGPWAAADLKKaLGIDYGVAPLPTLAGGKPAKPFVGVKGFGVSAYSKNKEAAQEFAEYLT 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 321 SpgPQGEYELQGGAGLTPLRPSPKVDEFIAKDPFWKPLIDGIAYGGPEPLFTDYKGFQDTMIEMVQSVVTGKATPEDAAK 400
Cdd:COG2182  321 S--PEAQKALFEATGRIPANKAAAEDAEVKADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPAEALD 398


                 ....*...
gi 489612332 401 KASAALEQ 408
Cdd:COG2182  399 AAQKQIEA 406
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 39-408 6.76e-51

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: 175.58  E-value: 6.76e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  39 GDKMDPIHEKYIKEwegkNAGWKVVPEVVGWAQCQDKATTLAAAGTPVAMAYVGSRTLKQFAQNDLIVPV-PMTEDEK-- 115
Cdd:cd14747   13 AELLKELADEFEKE----NPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMGALEDLtPYLEDLGgd 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 116 KTYYPNIVDTVTFEDTQWGVPVAFSTKALYWNKDLFKQAGldPEVPPKTWAEEIAFAKQIKEKTG-VAGYGLPAKtfDNT 194
Cdd:cd14747   89 KDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAG--GDEAPKTWDELEAAAKKIKADGPdVSGFAIPGK--NDV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 195 MHQFMHWVYTNNGKVIDGDK--ITVDSPQVLAALKAYKDI-TPYSVEGPTAYEQNEIRAIFLDGKVGMIQAGSGAATRLQ 271
Cdd:cd14747  165 WHNALPFVWGAGGDLATKDKwkATLDSPEAVAGLEFYTSLyQKGLSPKSTLENSADVEQAFANGKVAMIISGPWEIGAIR 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 272 E----TKINWGIATLPlGPEAKGPGTLLITDSLAIFKGTGVEEKATEFAKFITSPGPQGEYelQGGAGLTPLRPSPKVDE 347
Cdd:cd14747  245 EagpdLAGKWGVAPLP-GGPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAY--AKATGMLPANTSAWDDP 321

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489612332 348 FIAKDPFWKPLIDGIAYGGPEPLFTDYKGFQDTMIEMVQSVVTG-KATPEDAAKKASAALEQ 408
Cdd:cd14747  322 SLANDPLLAVFAEQLKTGKATPATPEWGEIEAELVLVLEEVWIGvGADVEDALDKAAAEINE 383
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 47-407 2.87e-41

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: 149.84  E-value: 2.87e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  47 EKYIKEWEGKNAGWKVVPEVVGWAQCQDKATTLAAAGTPVAMAYVGSRTLKQFAQNDLIVPVPMTE--DEKKTYYPNIVD 124
Cdd:cd14751   17 EKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDGTPafDDIVDYLPGPME 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 125 TVTFEDTQWGVPVAFSTKALYWNKDLFKQAGLDpevPPKTWAEEIAFAKQIKEKTGVAGYGLPAktfDNTmHQFMHWVYT 204
Cdd:cd14751   97 TNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTE---VPKTMDELVAAAKAIKKKKGRYGLYISG---DGP-YWLLPFLWS 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 205 NNGKVIDGDK--ITVDSPQVLAALKAYKDITPYSVEGPTA-YEQNEIRAIFLDGKVGMIQAGSGAATRLQETKI-----N 276
Cdd:cd14751  170 FGGDLTDEKKatGYLNSPESVRALETIVDLYDEGAITPCAsGGYPNMQDGFKSGRYAMIVNGPWAYADILGGKEfkdpdN 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 277 WGIATLPLGPeaKGPGTLLITDSLAIFKGTGVEEKATEFAKFITSPGPQGeyELQGGAGLTPLRPSPKVDEFIAKDPFWK 356
Cdd:cd14751  250 LGIAPVPAGP--GGSGSPVGGEDLVIFKGSKNKDAAWKFVKFMSSAEAQA--LTAAKLGLLPTRTSAYESPEVANNPMVA 325

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489612332 357 PLIDGIAYGGPEPLFTDYKGFQDTMIEMVQSVVTGKATPEDAAKKASAALE 407
Cdd:cd14751  326 AFKPALETAVPRPPIPEWGELFEPLTLAFAKVLRGEKSPREALDEAAKQWD 376
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 32-406 3.41e-41

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: 149.75  E-value: 3.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  32 EISWIYCGDKMDP-IHEKYIKEWEGKNAGWKVVPEVVGW---AQCQDKATTLAAAGTPVAMAYVGSRTLKQFAQNDLIVP 107
Cdd:cd14750    1 TITFAAGSDGQEGeLLKKAIAAFEKKHPDIKVEIEELPAssdDQRQQLVTALAAGSSAPDVLGLDVIWIPEFAEAGWLLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 108 VP--MTEDEKKTYYPNIVDTVTFEDTQWGVPVAFSTKALYWNKDLFKQAGLDpevPPKTWAEEIAFAKQIK-EKTGVAGY 184
Cdd:cd14750   81 LTeyLKEEEDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPE---PPKTWDELLEAAKKRKaGEPGIWGY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 185 GLPAKTFDNTMHQFMHWVYTNNGKVIDGD--KITVDSPQVLAALKAYKDI--TPYSVEGPTAYEQNEIRAIFLDGKVGMI 260
Cdd:cd14750  158 VFQGKQYEGLVCNFLELLWSNGGDIFDDDsgKVTVDSPEALEALQFLRDLigEGISPKGVLTYGEEEARAAFQAGKAAFM 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 261 QAGSGAATRLQETKIN----WGIATLPLGPEAKGPGTLLITdSLAIFKGTGVEEKATEFAKFITSPgPQGEYELQGGAGL 336
Cdd:cd14750  238 RNWPYAYALLQGPESAvagkVGVAPLPAGPGGGSASTLGGW-NLAISANSKHKEAAWEFVKFLTSP-EVQKRRAINGGLP 315

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 337 TPLRPSPKVDEFIAKDPFWKPLIDGIAYGGPEPLFTDYKGFQDTMIEMVQSVVTGKATPEDAAKKASAAL 406
Cdd:cd14750  316 PTRRALYDDPEVLEAYPFLPALLEALENAVPRPVTPKYPEVSTAIQIALSAALSGQATPEEALKQAQEKL 385
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 47-405 5.02e-34

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: 130.11  E-value: 5.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  47 EKYIKEWEGKNaGWKVVPEVVGWAQCQDKATTLAAAGTPVAMAYVGSRTLKQFAQNDLIVPVPMTEDEKKTYYPNIVDTV 126
Cdd:cd13586   16 KELAEEFEKKY-GIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLAVKIKNLPVALAAV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 127 TFEDTQWGVPVAFSTKALYWNKDLFKQagldpevPPKTWAEEIAFAKQIKEKTGvAGYGLPAKtFDNTMHQFM------H 200
Cdd:cd13586   95 TYNGKLYGVPVSVETIALFYNKDLVPE-------PPKTWEELIALAKKFNDKAG-GKYGFAYD-QTNPYFSYPflaafgG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 201 WVYTNNGKviDGDKITVDSPQVLAALKAYKD------ITPYSVEGPTAyeqneiRAIFLDGKVGMIQAGSGAATRLQETK 274
Cdd:cd13586  166 YVFGENGG--DPTDIGLNNEGAVKGLKFIKDlkkkykVLPPDLDYDIA------DALFKEGKAAMIINGPWDLADYKDAG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 275 INWGIATLPLGPEAKGPGTLLITDSLAIFKGTGVEEKATEFAKFITSpgPQGEYELQGGAGLTPLRPSPKVDEFIAKDPF 354
Cdd:cd13586  238 INFGVAPLPTLPGGKQAAPFVGVQGAFVSAYSKNKEAAVEFAEYLTS--DEAQLLLFEKTGRIPALKDALNDAAVKNDPL 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489612332 355 WKPLIDGIAYGGPEPLFTDYKGFQDTMIEMVQSVVTGKATPEDAAKKASAA 405
Cdd:cd13586  316 VKAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEEAAKDAVAA 366
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 42-405 1.29e-28

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: 115.20  E-value: 1.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  42 MDPIHEKY----IKEWEGKNAGWKVVPEVVGWAQCQDKATTLAAAGTPVAMAYVGSRTLKQFAQNDLIVPVPMTEDEKKT 117
Cdd:cd13522    8 YDTGENQAvnelIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDEYVSKSGK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 118 YYPNIVDTVTFEDTQWGVPVAFSTKALYWNKDLFkqagldPEVPPKTWAEEIAFAKQIKEKTG---VAGYGLPaktfdnt 194
Cdd:cd13522   88 YAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLV------PKNPPKTWQELIALAQGLKAKNVwglVYNQNEP------- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 195 mHQFMHWVYTNNGKVIDGD----KITVDSPQVLAALKAYKD-ITPYSVEGPTAYEQNEiRAIFLDGKVGMIQAGSGA-AT 268
Cdd:cd13522  155 -YFFAAWIGGFGGQVFKANngknNPTLDTPGAVEALQFLVDlKSKYKIMPPETDYSIA-DALFKAGKAAMIINGPWDlGD 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 269 RLQETKINWGIATLPLGPEAKGPGTLLITDSLAIFKGTGVEEKATEFAKFITSPGPQGEY--ELQGGAGLTPLRPSPKVD 346
Cdd:cd13522  233 YRQALKINLGVAPLPTFSGTKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLfdDAGDIPANLQAYESPAVQ 312

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489612332 347 EfiakDPFWKPLIDGIAYGGPEPLFTDYKGFQDTMIEMVQSVVTGKATPEDAAKKASAA 405
Cdd:cd13522  313 N----KPAQKASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQQE 367
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 48-353 1.27e-27

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 110.57  E-value: 1.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332   48 KYIKEWEGKNaGWKVVPEVVGWAQCQDKATTLAAAGTP--VAMAYVGSRTLKQFAQNDLIVPvpMTEDEKKTYYPNIVDT 125
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNApdLDVVWIAADQLATLAEAGLLAD--LSDVDNLDDLPDALDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  126 VTFEDTQWGVPVAFSTK-ALYWNKDLFKQAGLDPevppKTWAEEIAFAKQIKEKTGVAGYGlpaktfdNTMHQFMHWVyt 204
Cdd:pfam13416  78 AGYDGKLYGVPYAASTPtVLYYNKDLLKKAGEDP----KTWDELLAAAAKLKGKTGLTDPA-------TGWLLWALLA-- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  205 nNGKVIDGD-KITVDSPQVLAALKAYKDitpysvEGPTAYEQNEIRAIFLDGKVGMIQAGSGAATRLQETKINWGIAtlp 283
Cdd:pfam13416 145 -DGVDLTDDgKGVEALDEALAYLKKLKD------NGKVYNTGADAVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAV--- 214

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489612332  284 lgpeAKGPGTLLITDSLAIFKGTGVEEKAT-EFAKFITSpgPQGEYELQGGAGLTPLRPSPKVDEFIAKDP 353
Cdd:pfam13416 215 ----VPKDGSFLGGKGLVVPAGAKDPRLAAlDFIKFLTS--PENQAALAEDTGYIPANKSAALSDEVKADP 279
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 47-325 5.67e-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: 103.65  E-value: 5.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332   47 EKYIKEWEGKNAGWKVVPEVVGWAQCQDKATTLAAAGTPVA-MAYVGSRTLKQFAQNDLIVPV-PMTEDEKKTYYPnivd 124
Cdd:pfam01547  11 QALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPAdVFASDNDWIAELAKAGLLLPLdDYVANYLVLGVP---- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  125 tvtfedTQWGVPVAFSTKALYWNKDLFKQAGLDPevpPKTWAEEIAFAKQIKEKTGVAGYGLPAKTFDNTMHQFMHWVYT 204
Cdd:pfam01547  87 ------KLYGVPLAAETLGLIYNKDLFKKAGLDP---PKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGYFTLALLAS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  205 NNGKVIDGDKITVDSPQVLAALKAYKDITPYSVE-------GPTAYEQNEIRAIFLDGKVGMIQAGSGAATRLQ------ 271
Cdd:pfam01547 158 LGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLlkklknpGVAGADGREALALFEQGKAAMGIVGPWAALAANkvklkv 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489612332  272 -------ETKINWGIATLPLGPEAKGpgtllITDSLAIFKGTGVEEKATEFAKFITSPGPQ 325
Cdd:pfam01547 238 afaapapDPKGDVGYAPLPAGKGGKG-----GGYGLAIPKGSKNKEAAKKFLDFLTSPEAQ 293
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 47-402 4.82e-22

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: 96.78  E-value: 4.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  47 EKYIKEWEG---KNAGWKVVPEVVGWAQCQDKATTLAAAGT-PVAMAYVGSRTLKQFAQNdLIVPVPMTEDEKKTYYPNI 122
Cdd:cd13658   12 MAFIKKIAKqytKKTGVKVKLVEVDQLDQLEKLSLDGPAGKgPDVMVAPHDRIGSAVLQG-LLSPIKLSKDKKKGFTDQA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 123 VDTVTFEDTQWGVPVAFSTKALYWNKDLFKQAgldpevpPKTWAEEIAFAKQI---KEKTgvagYGLPAKtFDNTMHQFM 199
Cdd:cd13658   91 LKALTYDGKLYGLPAAVETLALYYNKDLVKNA-------PKTFDELEALAKDLtkeKGKQ----YGFLAD-ATNFYYSYG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 200 ------HWVYTNNGKVIDGDKITVDSPqvlAALKAYKDITPYSVEG--PTAYEQNEIRAIFLDGKVGMIQAGSGAATRLQ 271
Cdd:cd13658  159 llagngGYIFKKNGSDLDINDIGLNSP---GAVKAVKFLKKWYTEGylPKGMTGDVIQGLFKEGKAAAVIDGPWAIQEYQ 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 272 ETKINWGIATLPLGPEAKGPGTLLITDSLAIFKGTGVEEKATEFAKFITSpgPQGEYELQGGAGLTPLRPSPKVDEFIAK 351
Cdd:cd13658  236 EAGVNYGVAPLPTLPNGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTS--KENLKKRYDETNEIPPRKDVRSDPEIKN 313

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489612332 352 DPFWKPLIDGIAYGGPEPLFTDYKGFQDTMIEMVQSVVTGKATPEDAAKKA 402
Cdd:cd13658  314 NPLTSAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKTPKQALNDA 364
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 98-406 3.10e-21

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: 94.37  E-value: 3.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  98 QFAQNDLIVPVP--MTEDEKKTYYPNIVDTVTFEDTQWGVPVAFSTKALYWNKDLFKQagldpevPPKTWAEEIAFAKQI 175
Cdd:cd13657   68 QFAEAGLLVPISdyLSEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQ-------PPETTDELLAIMKDH 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 176 KeKTGVAGYGLPAKtfDNTMHQFMHWVYTNNGKVID--GDKITVDSPQVLAALKAYKD-ITPYSvegPTAYEQNEIRAIF 252
Cdd:cd13657  141 T-DPAAGSYGLAYQ--VSDAYFVSAWIFGFGGYYFDdeTDKPGLDTPETIKGIQFLKDfSWPYM---PSDPSYNTQTSLF 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 253 LDGKVGMIQAGSGAATRLQETKINWGIATLPLGPEAKGPGTLLITDSLAIFKGTGVEEK--ATEFAKFITSPGPQGEYEL 330
Cdd:cd13657  215 NEGKAAMIINGPWFIGGIKAAGIDLGVAPLPTVDGTNPPRPYSGVEGIYVTKYAERKNKeaALDFAKFFTTAEASKILAD 294

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489612332 331 QGGAglTPLRPSPKVDEFIAKDPFWKPLIDGIAYGGPEPLFTDYKGFQDTMIEMVQSVVTGKATPEDAAKKASAAL 406
Cdd:cd13657  295 ENGY--VPAATNAYDDAEVAADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQEALAAAQQEI 368
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
136-402 1.22e-13

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 72.14  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 136 PVAFSTKALYWNKDLFKQAGLDPEVPPKTWAEEIAFAKQIKEKTGVAGY-----------------GLPAKTfdntmhqf 198
Cdd:PRK10974 141 PFNSSTPVLYYNKDAFKKAGLDPEQPPKTWQDLAAYAAKLRAAGMKCGYasgwqgwiqlenfsawhGLPFAS-------- 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 199 mhwvyTNNGkvIDGD--KITVDSPQVLAALKAYKDITPysvEGPTAY--EQNEIRAIFLDGKVGMIQAGSGA-ATRLQET 273
Cdd:PRK10974 213 -----KNNG--FDGTdaVLEFNKPEQVKHIALLEEMNK---KGDFTYvgRKDESTEKFYNGDCAITTASSGSlANIRKYA 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 274 KINWGIATLPLGPEAKG-PGTLLITD-SLAIFKGtgvEEKAT-----EFAKFITSPGPQGE--------------YELQG 332
Cdd:PRK10974 283 KFNYGVGMMPYDADVKGaPQNAIIGGaSLWVMQG---KDKETykgvaKFLDFLAKPENAAEwhqktgylpittaaYDLTR 359

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489612332 333 GAGLTPLRPSPKV--DEFIAKDPfwKPLIDGIAYGGPEPLFTdykgfqdTMIEMVQSVVTGKATPEDAAKKA 402
Cdd:PRK10974 360 EQGFYEKNPGADTatRQMLNKPP--LPFTKGLRLGNMPQIRT-------IVDEELESVWTGKKTPQQALDSA 422
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 48-291 9.43e-13

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: 69.66  E-value: 9.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  48 KYIKEWEGKNAGWKVVPevvgWAQCQDKATTLAAAGT-PVAMAYVGSRTLKQFAQNDLIVPV-PMTEDE----KKTYYPN 121
Cdd:cd13580   26 KYLEEKTNIDVKVKWVP----DSSYDEKLNLALASGDlPDIVVVNDPQLSITLVKQGALWDLtDYLDKYypnlKKIIEQE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 122 IVDTVTFEDTQWGVPV---AFSTKALYWNKDLFKQAGLDPevpPKTWAE--EI--AFAKQIKEKTGVA-GYGL------- 186
Cdd:cd13580  102 GWDSASVDGKIYGIPRkrpLIGRNGLWIRKDWLDKLGLEV---PKTLDElyEVakAFTEKDPDGNGKKdTYGLtdtkdli 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 187 --PAKTFDNTMHQFMH-WVYTNNGKVIDGdkitVDSPQVLAALKAYKD------ITPysvEGPTaYEQNEIRAIFLDGKV 257
Cdd:cd13580  179 gsGFTGLFGAFGAPPNnWWKDEDGKLVPG----SIQPEMKEALKFLKKlykeglIDP---EFAV-NDGTKANEKFISGKA 250

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 489612332 258 GMIQAGSGAATRLQETKIN------WGIATLPLGPEAKGP 291
Cdd:cd13580  251 GIFVGNWWDPAWPQASLKKndpdaeWVAVPIPSGPDGKYG 290
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
8-353 4.19e-12

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 66.86  E-value: 4.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332   8 LALCAFAFAGSTALGTvAAHAADKEISwIYC-GDKMDPiheKYIKEWEgKNAGWKVVPEVVG-WAQCQDKattLAAAGTP 85
Cdd:COG0687    7 LGLAAAALAAALAGGA-PAAAAEGTLN-VYNwGGYIDP---DVLEPFE-KETGIKVVYDTYDsNEEMLAK---LRAGGSG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  86 VAMAYVGSRTLKQFAQNDLIVPVPMTEDE-KKTYYPNIVDTVTFEDTQWGVPVAFSTKALYWNKDLFKQagldpevPPKT 164
Cdd:COG0687   78 YDVVVPSDYFVARLIKAGLLQPLDKSKLPnLANLDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKE-------PPTS 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 165 WAeeIAFAKQIKEKtgVAGYGLPAKTFDNTMHQFMHWVYTNNGKVIDgdkitvdspQVLAALKAYKD-ITPYSVEGPTAY 243
Cdd:COG0687  151 WA--DLWDPEYKGK--VALLDDPREVLGAALLYLGYDPNSTDPADLD---------AAFELLIELKPnVRAFWSDGAEYI 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 244 EQneiraiFLDGKVGMIQAGSGAATRLQETKINWGIATlplgPEakgPGTLLITDSLAIFKGTGVEEKATEFAKFITSPG 323
Cdd:COG0687  218 QL------LASGEVDLAVGWSGDALALRAEGPPIAYVI----PK---EGALLWFDNMAIPKGAPNPDLAYAFINFMLSPE 284

                        330       340       350
                 ....*....|....*....|....*....|
gi 489612332 324 PQGEYELQGGAGLTPLRPSPKVDEFIAKDP 353
Cdd:COG0687  285 VAAALAEYVGYAPPNKAARELLPPELAANP 314
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 56-403 1.23e-11

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: 65.70  E-value: 1.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  56 KNAGWKVVPEVVGWAQcqDKATTLAAAGTPVAMAYVGSRTLKQFAQNDLIVPVPMTEDEKKTYYPNIVDTVTFEDTQWGV 135
Cdd:cd13656   25 KDTGIKVTVEHPDKLE--EKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAY 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 136 PVAFSTKALYWNKDLFKQagldpevPPKTWAEEIAFAKQIKEKtgvagyGLPAKTFDNTMHQFMHWVYTNNGKVI----- 210
Cdd:cd13656  103 PIAVEALSLIYNKDLLPN-------PPKTWEEIPALDKELKAK------GKSALMFNLQEPYFTWPLIAADGGYAfkyen 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 211 ---DGDKITVDSPQVLAALKAYKD-ITPYSVEGPTAYEQNEirAIFLDGKVGMIQAGSGAATRLQETKINWGIATLPlGP 286
Cdd:cd13656  170 gkyDIKDVGVDNAGAKAGLTFLVDlIKNKHMNADTDYSIAE--AAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLP-TF 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 287 EAKGPGTLLITDSLAIFKGTGVEEKATEFAK--FITSPGpqgeyeLQGGAGLTPL-RPSPK-VDEFIAKDPFWKPLIDGI 362
Cdd:cd13656  247 KGQPSKPFVGVLSAGINAASPNKELAKEFLEnyLLTDEG------LEAVNKDKPLgAVALKsYEEELAKDPRIAATMENA 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 489612332 363 AYGGPEPLFTDYKGFQDTMIEMVQSVVTGKATPEDAAKKAS 403
Cdd:cd13656  321 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQ 361
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
8-283 1.23e-11

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 65.80  E-value: 1.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332   8 LALCAFAFAGsTALGTVAAHAADKEISWIYcGDKMDPIHEKYIKEWEgKNAGWKVVPEVVGwaQCQDKATTLAAAGT-PV 86
Cdd:PRK09474  10 LALSALATLM-FSASALAKIEEGKLVIWIN-GDKGYNGLAEVGKKFE-KDTGIKVTVEHPD--KLEEKFPQVAATGDgPD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  87 AMAYVGSRtLKQFAQNDLIVPVPMTEDEKKTYYPNIVDTVTFEDTQWGVPVAFSTKALYWNKDLFKQagldpevPPKTWA 166
Cdd:PRK09474  85 IIFWAHDR-FGGYAQSGLLAEVTPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPT-------PPKTWE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 167 EEIAFAKQIKEKtgvagyGLPAKTFDNTMHQFMHWVYTNNG----KVIDGD----KITVDSPQVLAALKAYKDITPYSVE 238
Cdd:PRK09474 157 EIPALDKELKAK------GKSAIMWNLQEPYFTWPLIAADGgyafKFENGGydvkDVGVNNAGAKAGLQFLVDLVKNKHM 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 489612332 239 GPTA-YEQNEirAIFLDGKVGMIQAGSGAATRLQETKINWGIATLP 283
Cdd:PRK09474 231 NADTdYSIAE--AAFNKGETAMTINGPWAWSNIDKSGINYGVTVLP 274
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 50-401 1.36e-06

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: 50.04  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332  50 IKEWEGKNAGWKV--VPEVVGWAQCQDKATTLAAAGTPVAMayVGSRTLKQFAQNDLIVPVP--MTEDEKKTYYPNIVDT 125
Cdd:cd13655   18 VDAFKEKHPEWKItiTIGVVGEADAKDEVLKDPSAAADVFA--FANDQLGELVDAGAIYPLTgsAVDKIKNTNSEATVDA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 126 VTFEDTQWGVPVAFSTKALYWNKDLFKqagldpevppktwAEEIAFAKQIKEKTGVAGYGLpakTFDNTMHQFMHWVYTN 205
Cdd:cd13655   96 VTYNGKLYGYPFTANTWFMYYDKSKLT-------------EDDVKSLDTMLAKAPDAKGKV---SFDLSNSWYLYAFFFG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 206 NGKVIDGD------KITVDSPQVLAALKAYKDItpysVEGPTAYEQNEIRAI--FLDGKVGMIQAGSGAATRLQET-KIN 276
Cdd:cd13655  160 AGCKLFGNnggdtaGCDFNNEKGVAVTNYLVDL----VANPKFVNDADGDAIsgLKDGTLGAGVSGPWDAANLKKAlGDN 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 277 WGIATLplgPEAKGPGTLLITDSLAIFKGTGVE------EKATEFAKFITSPGPQGE-YELQggaGLTPLRPSPKVDEFI 349
Cdd:cd13655  236 YAVAKL---PTYTLGGKDVQMKSFAGYKAIGVNsntknpEAAMALADYLTNEESQLTrFEKR---GIGPTNKEAAESDAV 309

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489612332 350 AKDPFWKPLIDGIAYGG-PEPLFTDYKGFQDTMIEMVQSVVTGKATPEDAAKK 401
Cdd:cd13655  310 KADPAAKALIAQSNEASvVQPKLPKMSNFWTPAEAFGKGIVDGTVTAENAQQK 362
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 134-328 4.05e-05

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: 44.91  E-value: 4.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 134 GVPVAFSTKALYWNKDLFKQAgldpevPPKTWAEEIAFAKQIkektgvAGYGLPAKTFDNTMHQFMHwvytnngkvIDGD 213
Cdd:cd13589   98 GVGYTLYSTGIAYNTDKFKEP------PTSWWLADFWDVGKF------PGPRILNTSGLALLEAALL---------ADGV 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612332 214 KITVDSPQvlAALKAYKDITPYSVEGPTAYEQneIRAIFLDGKVGMIQAGSGAATRLQEtkinwgiATLPLGPEAKGPGT 293
Cdd:cd13589  157 DPYPLDVD--RAFAKLKELKPNVVTWWTSGAQ--LAQLLQSGEVDMAPAWNGRAQALID-------AGAPVAFVWPKEGA 225

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489612332 294 LLITDSLAIFKGTGVEEKATEFAKFITSPGPQGEY 328
Cdd:cd13589  226 ILGPDTLAIVKGAPNKELAMKFINFALSPEVQAAL 260
 
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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