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Conserved domains on  [gi|739208333|ref|WP_037071721|]
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sugar ABC transporter substrate-binding protein [Rhizobium sp. CF142]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 10194401)

ABC transporter substrate-binding protein functions as the initial receptor in the active transport of one or more from a variety of substrates including sugars and contains type 2 periplasmic binding fold

CATH:  3.40.190.10
Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
PubMed:  26517916|24638992|25750732
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 24-423 9.01e-89

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: 274.67  E-value: 9.01e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  24 TLTIATVNNGDMI-RMQKLTDDFKAKNPGIDLEWVTLEENVLRQKVTTDIATkGGQYDVLTIGTYEVPIWAKKGWLLPLD 102
Cdd:cd13585    1 TLTFWDWGQPAETaALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAA-GTAPDVFYVDGPWVPEFASNGALLDLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 103 NLGANYDVDD-LLPAIRSGISQDGKLYAAPFYGESSMVMYRKDLFDAAGLKMPDAPTWDFIADAAKKITNKDKEVYGICL 181
Cdd:cd13585   80 DYIEKDGLDDdFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTDKKGGQYGFAL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 182 RgkaGWGENMAFLTAMSNSFGARWFDEQ-WKPQFDQPEWKDTLTFYVNLMKEAGPPGASSNGFNENLALFQTGKCGMWID 260
Cdd:cd13585  160 R---GGSGGQTQWYPFLWSNGGDLLDEDdGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFASGKVAMMID 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 261 ATVAASFVADPKqsqVADKVGFALAPDKGLGKRGNWLWAWNLAIPAGSQKSEAAEKFIAWATSkdytnlvaeKEGWLNAP 340
Cdd:cd13585  237 GPWALGTLKDSK---VKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTS---------KENQLKLG 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 341 PGTRSSLYANADYQKAASFAKMTLDSINSADPTKPTVKPVPYVGVQFVAIPEFQGIGTAVGQQFsaalagQISVDQALQS 420
Cdd:cd13585  305 GAAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGAL------GKSPEEALKE 378


                 ...
gi 739208333 421 AQQ 423
Cdd:cd13585  379 AAK 381
 
Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 24-423 9.01e-89

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: 274.67  E-value: 9.01e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  24 TLTIATVNNGDMI-RMQKLTDDFKAKNPGIDLEWVTLEENVLRQKVTTDIATkGGQYDVLTIGTYEVPIWAKKGWLLPLD 102
Cdd:cd13585    1 TLTFWDWGQPAETaALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAA-GTAPDVFYVDGPWVPEFASNGALLDLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 103 NLGANYDVDD-LLPAIRSGISQDGKLYAAPFYGESSMVMYRKDLFDAAGLKMPDAPTWDFIADAAKKITNKDKEVYGICL 181
Cdd:cd13585   80 DYIEKDGLDDdFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTDKKGGQYGFAL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 182 RgkaGWGENMAFLTAMSNSFGARWFDEQ-WKPQFDQPEWKDTLTFYVNLMKEAGPPGASSNGFNENLALFQTGKCGMWID 260
Cdd:cd13585  160 R---GGSGGQTQWYPFLWSNGGDLLDEDdGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFASGKVAMMID 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 261 ATVAASFVADPKqsqVADKVGFALAPDKGLGKRGNWLWAWNLAIPAGSQKSEAAEKFIAWATSkdytnlvaeKEGWLNAP 340
Cdd:cd13585  237 GPWALGTLKDSK---VKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTS---------KENQLKLG 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 341 PGTRSSLYANADYQKAASFAKMTLDSINSADPTKPTVKPVPYVGVQFVAIPEFQGIGTAVGQQFsaalagQISVDQALQS 420
Cdd:cd13585  305 GAAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGAL------GKSPEEALKE 378


                 ...
gi 739208333 421 AQQ 423
Cdd:cd13585  379 AAK 381
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 5-326 4.04e-76

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 241.49  E-value: 4.04e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333   5 TLLLGACSAMAFAGMASAE--TLTIATVNNGDMIRMQKLTDDFKAKNPGIDLEWVTLEENVLRQKVTTDIATkGGQYDVL 82
Cdd:COG1653   13 ALALAACGGGGSGAAAAAGkvTLTVWHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAA-GNAPDVV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  83 TIGTYEVPIWAKKGWLLPLDNL--GANYDVDDLLPAIRSGISQDGKLYAAPFYGESSMVMYRKDLFDAAGLKMPDapTWD 160
Cdd:COG1653   92 QVDSGWLAEFAAAGALVPLDDLldDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPPK--TWD 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 161 FIADAAKKITnKDKEVYGICLRGKAGWgenmaFLTAMSNSFGARWFDEQWKPQFDQPEWKDTLTFYVNLMKE-AGPPGAS 239
Cdd:COG1653  170 ELLAAAKKLK-AKDGVYGFALGGKDGA-----AWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKDgYVPPGAL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 240 SNGFNENLALFQTGKCGMWIDATVAASFVADPKQSqvaDKVGFALAPDKGLGKRGN-WLWAWNLAIPAGSQKSEAAEKFI 318
Cdd:COG1653  244 GTDWDDARAAFASGKAAMMINGSWALGALKDAAPD---FDVGVAPLPGGPGGKKPAsVLGGSGLAIPKGSKNPEAAWKFL 320


                 ....*...
gi 739208333 319 AWATSKDY 326
Cdd:COG1653  321 KFLTSPEA 328
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 34-326 5.74e-49

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: 168.75  E-value: 5.74e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333   34 DMIRMQKLTDDFKAKNPGIDLEWVTLEENVLRQKVTTDIATKGGQYDVLTIGTYEVPIWAKKGWLLPLDNLGANYDVDDl 113
Cdd:pfam01547   6 EAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYLVLG- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  114 lpairsgisqDGKLYAAPFYGESSMVMYRKDLFDAAGLKMPdaPTWDFIADAAKKITNKDKEVYGicLRGKAGWGENMAF 193
Cdd:pfam01547  85 ----------VPKLYGVPLAAETLGLIYNKDLFKKAGLDPP--KTWDELLEAAKKLKEKGKSPGG--AGGGDASGTLGYF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  194 LTAMSNSFGARWFDEQWKpQFDQPEWKDTLTFYVNLM------KEAGPPGASSNGFNENLALFQTGKCGMWIDATVAA-- 265
Cdd:pfam01547 151 TLALLASLGGPLFDKDGG-GLDNPEAVDAITYYVDLYakvlllKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAAla 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739208333  266 ------SFVADPKQSQVADKVGFALAPDKGLGKRGnwlwAWNLAIPAGSQKSEAAEKFIAWATSKDY 326
Cdd:pfam01547 230 ankvklKVAFAAPAPDPKGDVGYAPLPAGKGGKGG----GYGLAIPKGSKNKEAAKKFLDFLTSPEA 292
 
Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 24-423 9.01e-89

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: 274.67  E-value: 9.01e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  24 TLTIATVNNGDMI-RMQKLTDDFKAKNPGIDLEWVTLEENVLRQKVTTDIATkGGQYDVLTIGTYEVPIWAKKGWLLPLD 102
Cdd:cd13585    1 TLTFWDWGQPAETaALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAA-GTAPDVFYVDGPWVPEFASNGALLDLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 103 NLGANYDVDD-LLPAIRSGISQDGKLYAAPFYGESSMVMYRKDLFDAAGLKMPDAPTWDFIADAAKKITNKDKEVYGICL 181
Cdd:cd13585   80 DYIEKDGLDDdFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTDKKGGQYGFAL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 182 RgkaGWGENMAFLTAMSNSFGARWFDEQ-WKPQFDQPEWKDTLTFYVNLMKEAGPPGASSNGFNENLALFQTGKCGMWID 260
Cdd:cd13585  160 R---GGSGGQTQWYPFLWSNGGDLLDEDdGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFASGKVAMMID 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 261 ATVAASFVADPKqsqVADKVGFALAPDKGLGKRGNWLWAWNLAIPAGSQKSEAAEKFIAWATSkdytnlvaeKEGWLNAP 340
Cdd:cd13585  237 GPWALGTLKDSK---VKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTS---------KENQLKLG 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 341 PGTRSSLYANADYQKAASFAKMTLDSINSADPTKPTVKPVPYVGVQFVAIPEFQGIGTAVGQQFsaalagQISVDQALQS 420
Cdd:cd13585  305 GAAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGAL------GKSPEEALKE 378


                 ...
gi 739208333 421 AQQ 423
Cdd:cd13585  379 AAK 381
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 5-326 4.04e-76

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 241.49  E-value: 4.04e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333   5 TLLLGACSAMAFAGMASAE--TLTIATVNNGDMIRMQKLTDDFKAKNPGIDLEWVTLEENVLRQKVTTDIATkGGQYDVL 82
Cdd:COG1653   13 ALALAACGGGGSGAAAAAGkvTLTVWHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAA-GNAPDVV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  83 TIGTYEVPIWAKKGWLLPLDNL--GANYDVDDLLPAIRSGISQDGKLYAAPFYGESSMVMYRKDLFDAAGLKMPDapTWD 160
Cdd:COG1653   92 QVDSGWLAEFAAAGALVPLDDLldDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPPK--TWD 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 161 FIADAAKKITnKDKEVYGICLRGKAGWgenmaFLTAMSNSFGARWFDEQWKPQFDQPEWKDTLTFYVNLMKE-AGPPGAS 239
Cdd:COG1653  170 ELLAAAKKLK-AKDGVYGFALGGKDGA-----AWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKDgYVPPGAL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 240 SNGFNENLALFQTGKCGMWIDATVAASFVADPKQSqvaDKVGFALAPDKGLGKRGN-WLWAWNLAIPAGSQKSEAAEKFI 318
Cdd:COG1653  244 GTDWDDARAAFASGKAAMMINGSWALGALKDAAPD---FDVGVAPLPGGPGGKKPAsVLGGSGLAIPKGSKNPEAAWKFL 320


                 ....*...
gi 739208333 319 AWATSKDY 326
Cdd:COG1653  321 KFLTSPEA 328
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 24-423 9.06e-65

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: 212.54  E-value: 9.06e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  24 TLTIATVNNGDMIR-MQKLTDDFKAKNPGIDLEWVTL--EENVLRQKVTTDIATKGGQYDVLTIGTYEVPIWAKKGWLLP 100
Cdd:cd14750    1 TITFAAGSDGQEGElLKKAIAAFEKKHPDIKVEIEELpaSSDDQRQQLVTALAAGSSAPDVLGLDVIWIPEFAEAGWLLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 101 LDNLGANYDVDDLLPAIRSGISQDGKLYAAPFYGESSMVMYRKDLFDAAGLKMPDapTWDFIADAAKKITNKDKEVYGIC 180
Cdd:cd14750   81 LTEYLKEEEDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPEPPK--TWDELLEAAKKRKAGEPGIWGYV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 181 LRGKAGWGENMAFLTAMsNSFGARWFDEQ-WKPQFDQPEWKDTLTFYVNLMKE-AGPPGASSNGFNENLALFQTGKCGM- 257
Cdd:cd14750  159 FQGKQYEGLVCNFLELL-WSNGGDIFDDDsGKVTVDSPEALEALQFLRDLIGEgISPKGVLTYGEEEARAAFQAGKAAFm 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 258 --WIdatvAASFVADPKQSQVADKVGFALAPDKGLGKRGNWLWAWNLAIPAGSQKSEAAEKFIAWATSKDYTNLVAEKEG 335
Cdd:cd14750  238 rnWP----YAYALLQGPESAVAGKVGVAPLPAGPGGGSASTLGGWNLAISANSKHKEAAWEFVKFLTSPEVQKRRAINGG 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 336 WlnaPPgTRSSLYANADYQKAASFAKMTLDSINSAdptkpTVKPVpyvgvqfvaIPEFQGIGTAVGQQFSAALAGQISVD 415
Cdd:cd14750  314 L---PP-TRRALYDDPEVLEAYPFLPALLEALENA-----VPRPV---------TPKYPEVSTAIQIALSAALSGQATPE 375


                 ....*...
gi 739208333 416 QALQSAQQ 423
Cdd:cd14750  376 EALKQAQE 383
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 38-423 4.23e-54

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: 184.80  E-value: 4.23e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  38 MQKLTDDFKAKNPGIDLEWVTLEE-NVLRQKVTTDIATkGGQYDVLTIGTYEVPIWAKKGWLLPLDNL--GANYDVDDLL 114
Cdd:cd14748   16 LEELVDEFNKSHPDIKVKAVYQGSyDDTLTKLLAALAA-GTAPDVAQVDASWVAQLADSGALEPLDDYidKDGVDDDDFY 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 115 PAIRSGISQDGKLYAAPFYGESSMVMYRKDLFDAAGLKMPDAP-TWDFIADAAKKITNKDK--EVYGICLRGKAGWGenm 191
Cdd:cd14748   95 PAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPkTWDELEEAAKKLKDKGGktGRYGFALPPGDGGW--- 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 192 aFLTAMSNSFGARWFDEQ-WKPQFDQPEWKDTLTFYVNLMKEAGPpgASSNGFNENLALFQTGKCGMWIDATVAASFVad 270
Cdd:cd14748  172 -TFQALLWQNGGDLLDEDgGKVTFNSPEGVEALEFLVDLVGKDGV--SPLNDWGDAQDAFISGKVAMTINGTWSLAGI-- 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 271 pKQSQVADKVGFALAPDKGLGKRGNWLWAWNLAIPAG-SQKSEAAEKFIAWATSKDYTNLVAEKEGWLnapPGTRSSLYA 349
Cdd:cd14748  247 -RDKGAGFEYGVAPLPAGKGKKGATPAGGASLVIPKGsSKKKEAAWEFIKFLTSPENQAKWAKATGYL---PVRKSAAED 322

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739208333 350 NADYQKAASFAKMTLDSINSADPTKPTVkpvpyvgvqfvaiPEFQGIGTAVGQQFSAALAGQISVDQALQSAQQ 423
Cdd:cd14748  323 PEEFLAENPNYKVAVDQLDYAKPWGPPV-------------PNGAEIRDELNEALEAALLGKKTPEEALKEAQE 383
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 34-326 5.74e-49

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: 168.75  E-value: 5.74e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333   34 DMIRMQKLTDDFKAKNPGIDLEWVTLEENVLRQKVTTDIATKGGQYDVLTIGTYEVPIWAKKGWLLPLDNLGANYDVDDl 113
Cdd:pfam01547   6 EAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYLVLG- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  114 lpairsgisqDGKLYAAPFYGESSMVMYRKDLFDAAGLKMPdaPTWDFIADAAKKITNKDKEVYGicLRGKAGWGENMAF 193
Cdd:pfam01547  85 ----------VPKLYGVPLAAETLGLIYNKDLFKKAGLDPP--KTWDELLEAAKKLKEKGKSPGG--AGGGDASGTLGYF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  194 LTAMSNSFGARWFDEQWKpQFDQPEWKDTLTFYVNLM------KEAGPPGASSNGFNENLALFQTGKCGMWIDATVAA-- 265
Cdd:pfam01547 151 TLALLASLGGPLFDKDGG-GLDNPEAVDAITYYVDLYakvlllKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAAla 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739208333  266 ------SFVADPKQSQVADKVGFALAPDKGLGKRGnwlwAWNLAIPAGSQKSEAAEKFIAWATSKDY 326
Cdd:pfam01547 230 ankvklKVAFAAPAPDPKGDVGYAPLPAGKGGKGG----GYGLAIPKGSKNKEAAKKFLDFLTSPEA 292
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 38-423 1.50e-42

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: 154.01  E-value: 1.50e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  38 MQKLTDDFKAKNPGIDLEWVTLEENVLRQKVTTDIATKGGQyDVLTIGTYEVPIWAKKGWLLPLDN-LGANYDVDDLLPA 116
Cdd:cd14747   16 LKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGP-DVVQLGNTWVAEFAAMGALEDLTPyLEDLGGDKDLFPG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 117 IRSGISQDGKLYAAPFYGESSMVMYRKDLFDAAG-LKMPDapTWDFIADAAKKITNKDKEVYGICLRGKAGWGENmaFLT 195
Cdd:cd14747   95 LVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGgDEAPK--TWDELEAAAKKIKADGPDVSGFAIPGKNDVWHN--ALP 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 196 AMSNSFGARWFDEQWKPQFDQPEWKDTLTFYVNLMKEAGPPGASSNGFNENLALFQTGKCGMWIDATVAASFVADPkQSQ 275
Cdd:cd14747  171 FVWGAGGDLATKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSADVEQAFANGKVAMIISGPWEIGAIREA-GPD 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 276 VADKVGFALAPDKGLGKRGNWLWAWNLAIPAGSQKSEAAEKFIAWATSKDYTNLVAEKEGWLNAPPGTRSSLYANADyQK 355
Cdd:cd14747  250 LAGKWGVAPLPGGPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGMLPANTSAWDDPSLAND-PL 328

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739208333 356 AASFAKMtldsinsadptKPTVKPVPyvgvqfvAIPEFQGIGTAVGQQFSAALAG-QISVDQALQSAQQ 423
Cdd:cd14747  329 LAVFAEQ-----------LKTGKATP-------ATPEWGEIEAELVLVLEEVWIGvGADVEDALDKAAA 379
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 24-424 5.41e-39

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: 144.44  E-value: 5.41e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  24 TLTIATVNNGDMIR--MQKLTDDFKAKNPGIDLEWVTLEENVLRQKVTTDIATKGGQyDVLTIGTY-EVPIWAKKGWLLP 100
Cdd:cd14749    1 TITYWQYFTGDTKKkyMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGP-DVFNLWPGgWLAEFVKAGLLLP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 101 LDNLGANYDVDDL-LPAIRSGISQDGKLYAAPFYGESSMVMYRKDLFDAAGLKMPDApTWDFIADAAKKITNKDKEVYGI 179
Cdd:cd14749   80 LTDYLDPNGVDKRfLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGVKPPK-TWDELIEAAKKDKFKAKGQTGF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 180 CLRGKAGWGenMAFLTAMSNSFGARWFDEQW--KPQFDQPEWKDTLTFYVNLMKE-AGPPGASSNGFNENLALFQTGKCG 256
Cdd:cd14749  159 GLLLGAQGG--HWYFQYLVRQAGGGPLSDDGsgKATFNDPAFVQALQKLQDLVKAgAFQEGFEGIDYDDAGQAFAQGKAA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 257 MWIDATVAasfVADPKQSQVADKVGFALAPDKGLGKRGNWLWA--WNLAIPAGSQKSEAAEKFIAWATSKDYTNLVAEKE 334
Cdd:cd14749  237 MNIGGSWD---LGAIKAGEPGGKIGVFPFPTVGKGAQTSTIGGsdWAIAISANGKKKEAAVKFLKYLTSPEVMKQYLEDV 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 335 GWLNA-PPGTRSSLYANADYQKAASFAKMTLDSINSADPTKPTVKPVPYVGVQfvaipefqgigtavgqqfsAALAGQIS 413
Cdd:cd14749  314 GLLPAkEVVAKDEDPDPVAILGPFADVLNAAGSTPFLDEYWPAAAQVHKDAVQ-------------------KLLTGKID 374

                        410
                 ....*....|.
gi 739208333 414 VDQALQSAQQL 424
Cdd:cd14749  375 PEQVVKQAQSA 385
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
5-423 3.96e-37

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 140.08  E-value: 3.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333   5 TLLLGACS-----AMAFAGMASAETLTIAtVNNGDMIRMQKLTDDFKAKnPGIDLEWVTLEENVLRQKVTTDIATKGGqY 79
Cdd:COG2182   16 ALALAACGsgsssSGSSSAAGAGGTLTVW-VDDDEAEALEEAAAAFEEE-PGIKVKVVEVPWDDLREKLTTAAPAGKG-P 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  80 DVLTIGTYEVPIWAKKGWLLPLDNLGAnyDVDDLLPAIRSGISQDGKLYAAPFYGESSMVMYRKDLFDAaglkmpDAP-T 158
Cdd:COG2182   93 DVFVGAHDWLGELAEAGLLAPLDDDLA--DKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKA------EPPkT 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 159 WDFIADAAKKITnkDKEVYGICLRGKAGWgENMAFLTAmsnsFGARWFDEQ----WKPQFDQPEWKDTLTFYVNLMKEAG 234
Cdd:COG2182  165 WDELIAAAKKLT--AAGKYGLAYDAGDAY-YFYPFLAA----FGGYLFGKDgddpKDVGLNSPGAVAALEYLKDLIKDGV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 235 PPgaSSNGFNENLALFQTGKCGMWIDAT-VAASFVADPKqsqvaDKVGFALAPDKGLGKRGN-WLWAWNLAIPAGSQKSE 312
Cdd:COG2182  238 LP--ADADYDAADALFAEGKAAMIINGPwAAADLKKALG-----IDYGVAPLPTLAGGKPAKpFVGVKGFGVSAYSKNKE 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 313 AAEKFIAWATSKDYTNLVAEKEGwlNAPpgTRSSLYANADyQKAASFAKMTLDSINSAdptkptvKPVPyvgvqfvAIPE 392
Cdd:COG2182  311 AAQEFAEYLTSPEAQKALFEATG--RIP--ANKAAAEDAE-VKADPLIAAFAEQAEYA-------VPMP-------NIPE 371

                        410       420       430
                 ....*....|....*....|....*....|.
gi 739208333 393 FQGIGTAVGQQFSAALAGQISVDQALQSAQQ 423
Cdd:COG2182  372 MGAVWTPLGTALQAIASGKADPAEALDAAQK 402
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 29-421 7.86e-34

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: 130.19  E-value: 7.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  29 TVNNGDMIRMQKLTDDFKAKNPGIDLEWVTLEENVLRQKVTTdiATKGGQY-DVLTIGTYEVPIWAKKGWLLPLDNLGAN 107
Cdd:cd14751    7 TSSDEEKVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKT--AAAGGQApDVMRADIAWVPEFAKLGYLQPLDGTPAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 108 YDVDDLLPAIRSGISQDGKLYAAPFYGESSMVMYRKDLFDAAGLKMPdaPTWDFIADAAKKITNKdKEVYGICLRGKAGW 187
Cdd:cd14751   85 DDIVDYLPGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEVP--KTMDELVAAAKAIKKK-KGRYGLYISGDGPY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 188 genmaFLTAMSNSFGARWFDEQWKP-QFDQPEWKDTLTFYVNLMKEAGPPGASSNGFNENLALFQTGKCGMWIDATVAAS 266
Cdd:cd14751  162 -----WLLPFLWSFGGDLTDEKKATgYLNSPESVRALETIVDLYDEGAITPCASGGYPNMQDGFKSGRYAMIVNGPWAYA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 267 FVADPKQSQVADKVGFALAPdKGLGKRGNWLWAWNLAIPAGSQKSEAAEKFIAWATSKDYTNLVAEKEGWLnaPpgTRSS 346
Cdd:cd14751  237 DILGGKEFKDPDNLGIAPVP-AGPGGSGSPVGGEDLVIFKGSKNKDAAWKFVKFMSSAEAQALTAAKLGLL--P--TRTS 311

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739208333 347 LYaNADYQKAASFAKMTLDSINSADPTKPtvkpvpyvgvqfvaIPEFQGIGTAVGQQFSAALAGQISVDQALQSA 421
Cdd:cd14751  312 AY-ESPEVANNPMVAAFKPALETAVPRPP--------------IPEWGELFEPLTLAFAKVLRGEKSPREALDEA 371
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 39-424 4.19e-23

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: 99.79  E-value: 4.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  39 QKLTDDFKAKNPGIDLEWVTLEENVLRQKVTTDIATKGGQyDVLTIGTYEVPIWAKKGWLLPLDNLGANydVDDLLPAIR 118
Cdd:cd13522   17 NELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGP-DVVFGPSDSLGPFAAAGLLAPLDEYVSK--SGKYAPNTI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 119 SGISQDGKLYAAPFYGESSMVMYRKDLFdaaglkmPDAP--TWDFIADAAKKitNKDKEVYGICLRGKAGWgenmaFLTA 196
Cdd:cd13522   94 AAMKLNGKLYGVPVSVGAHLMYYNKKLV-------PKNPpkTWQELIALAQG--LKAKNVWGLVYNQNEPY-----FFAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 197 MSNSFGARWFDEQ---WKPQFDQPEWKDTLTFYVNLMKEAGPPGASSNGFNENlALFQTGKCGMWIDAtvaaSFVADPKQ 273
Cdd:cd13522  160 WIGGFGGQVFKANngkNNPTLDTPGAVEALQFLVDLKSKYKIMPPETDYSIAD-ALFKAGKAAMIING----PWDLGDYR 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 274 SQVADKVGFALAPDKGLGKRGN-WLWAWNLAIPAGSQKSEAAEKFIAWATSKDYTNLVAEKEGWLnapPgtrsslyANAD 352
Cdd:cd13522  235 QALKINLGVAPLPTFSGTKHAApFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDI---P-------ANLQ 304

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739208333 353 YQKaasfakmtlDSINSADPTKPTVKPVPYVGVQFVAIPEFQGIGTAVGQQFSAALAGQISVDQALQSAQQL 424
Cdd:cd13522  305 AYE---------SPAVQNKPAQKASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQQE 367
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 38-423 4.68e-22

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: 97.06  E-value: 4.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  38 MQKLTDDFKAKNPGIDLEwVTLEENV-LRQKVTTDIATKGGQyDVLT-----IGTyevpiWAKKGWLLPLDNLGANYDVD 111
Cdd:cd13657   16 LQQIIDEFEAKYPVPNVK-VPFEKKPdLQNKLLTAIPAGEGP-DLFIwahdwIGQ-----FAEAGLLVPISDYLSEDDFE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 112 DLLPAIRSGISQDGKLYAAPFYGESSMVMYRKDLfdaaglkMPDAP-TWDFIADAAKKITNKDKEVYGIclrgkaGWGEN 190
Cdd:cd13657   89 NYLPTAVEAVTYKGKVYGLPEAYETVALIYNKAL-------VDQPPeTTDELLAIMKDHTDPAAGSYGL------AYQVS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 191 MA-FLTAMSNSFGARWFD-EQWKPQFDQPEWKDTLTFYVNLMKEAGPPGASsngFNENLALFQTGKCGMWIdatVAASFV 268
Cdd:cd13657  156 DAyFVSAWIFGFGGYYFDdETDKPGLDTPETIKGIQFLKDFSWPYMPSDPS---YNTQTSLFNEGKAAMII---NGPWFI 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 269 ADPKQSQVadKVGFALAPDkglGKRGNWLW------AWNLAIPAGSQKSEAAEKFIAWATSKDYTNLVAEKEGWlnAPpg 342
Cdd:cd13657  230 GGIKAAGI--DLGVAPLPT---VDGTNPPRpysgveGIYVTKYAERKNKEAALDFAKFFTTAEASKILADENGY--VP-- 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 343 TRSSLYANADYQkaasfakmtldsinsADPTKPTVKPVPYVGVQFVAIPEFQGIGTAVGQQFSAALAGQISVDQALQSAQ 422
Cdd:cd13657  301 AATNAYDDAEVA---------------ADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQEALAAAQ 365


                 .
gi 739208333 423 Q 423
Cdd:cd13657  366 Q 366
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 40-359 1.88e-21

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 93.62  E-value: 1.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333   40 KLTDDFKAKNpGIDLEWVTLEENVLRQKVTTDIAT-KGGQYDVLTIGTYEVPIWAKKGWLLPLDNLGANYDVDDLLPAIR 118
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAgNAPDLDVVWIAADQLATLAEAGLLADLSDVDNLDDLPDALDAAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  119 SgisqDGKLYAAPFYGESSMVM-YRKDLFDAAGlkmPDAPTWDFIADAAKKITNKdkevygiclRGKAGWGENMAFLTAM 197
Cdd:pfam13416  80 Y----DGKLYGVPYAASTPTVLyYNKDLLKKAG---EDPKTWDELLAAAAKLKGK---------TGLTDPATGWLLWALL 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  198 SNsfGARWFDEQWKPqfdqPEWKDTLTFYVNLmkeaGPPGASSNGFNENLALFQTGKCGMWIDATVAASFVADPKQsqva 277
Cdd:pfam13416 144 AD--GVDLTDDGKGV----EALDEALAYLKKL----KDNGKVYNTGADAVQLFANGEVAMTVNGTWAAAAAKKAGK---- 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  278 dKVGFALAPDkglgkrGNWLWAWNLAIPAGSQKSE-AAEKFIAWATSKDYTNLVAEKEGWLNAppgtRSSLYANADYQKA 356
Cdd:pfam13416 210 -KLGAVVPKD------GSFLGGKGLVVPAGAKDPRlAALDFIKFLTSPENQAALAEDTGYIPA----NKSAALSDEVKAD 278


                  ...
gi 739208333  357 ASF 359
Cdd:pfam13416 279 PAL 281
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 24-423 7.80e-20

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: 90.43  E-value: 7.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  24 TLTIATVNNGDMIRMQKLTDDFKAKNpGIDLEWVTLEENVLRQKVTTdiATKGGQYDVLTIGTYE-VPIWAKKGWLLPLD 102
Cdd:cd13586    1 TITVWTDEDGELEYLKELAEEFEKKY-GIKVEVVYVDSGDTREKFIT--AGPAGKGPDVFFGPHDwLGELAAAGLLAPIP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 103 NLGAnyDVDDLLPAIRSGISQDGKLYAAPFYGESSMVMYRKDLfdaaglkMPDAP-TWDFIADAAKKITNKDKEVYGICL 181
Cdd:cd13586   78 EYLA--VKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDL-------VPEPPkTWEELIALAKKFNDKAGGKYGFAY 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 182 rgKAGWGENMAFLTAmsnSFGARWFDEQ----WKPQFDQPEWKDTLTFYVNLMKEAGPPGASSNGFNENlALFQTGKCGM 257
Cdd:cd13586  149 --DQTNPYFSYPFLA---AFGGYVFGENggdpTDIGLNNEGAVKGLKFIKDLKKKYKVLPPDLDYDIAD-ALFKEGKAAM 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 258 WIDATVAasfVADPKQSqvadKVGFALAPDKGLGKR-------GNWLWAwnlaIPAGSQKSEAAEKFIAWATSKDYTNLV 330
Cdd:cd13586  223 IINGPWD---LADYKDA----GINFGVAPLPTLPGGkqaapfvGVQGAF----VSAYSKNKEAAVEFAEYLTSDEAQLLL 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 331 AEKegwLNAPPgtrsslyANADYQKAASFAKmtldsinsaDP-TKPTVKPVPYvGVQFVAIPEFQGIGTAVGQQFSAALA 409
Cdd:cd13586  292 FEK---TGRIP-------ALKDALNDAAVKN---------DPlVKAFAEQAQY-GVPMPNIPEMAAVWDAMGNALNLVAS 351

                        410
                 ....*....|....
gi 739208333 410 GQISVDQALQSAQQ 423
Cdd:cd13586  352 GKATPEEAAKDAVA 365
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 51-329 1.17e-16

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: 81.60  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  51 GIDLEWVTLEENVLRQKVTTDIATkGGQYDVLTI-GTYEVPIWAKKGWLLPLD--------NLGANYDVDDLLPAirsgi 121
Cdd:cd13580   33 NIDVKVKWVPDSSYDEKLNLALAS-GDLPDIVVVnDPQLSITLVKQGALWDLTdyldkyypNLKKIIEQEGWDSA----- 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 122 SQDGKLYAAPFYGESSM---VMYRKDLFDAAGLKMPDapTWDFIADAAKKITNKD------KEVYGICLRgkaGWGENMA 192
Cdd:cd13580  107 SVDGKIYGIPRKRPLIGrngLWIRKDWLDKLGLEVPK--TLDELYEVAKAFTEKDpdgngkKDTYGLTDT---KDLIGSG 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 193 FLTAMsNSFGA----RWFDEQWK--PQFDQPEWKDTLTFYVNLMKEagppGA--------SSNGFNEnlaLFQTGKCGMW 258
Cdd:cd13580  182 FTGLF-GAFGAppnnWWKDEDGKlvPGSIQPEMKEALKFLKKLYKE----GLidpefavnDGTKANE---KFISGKAGIF 253

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739208333 259 IDATVAASFVADPKQSQVAD----KVGFALAPDkglGKRGNWLWAWN---LAIPAGSQKSEAAEKFIAWATSKDYTNL 329
Cdd:cd13580  254 VGNWWDPAWPQASLKKNDPDaewvAVPIPSGPD---GKYGVWAESGVngfFVIPKKSKKPEAILKLLDFLSDPEVQKL 328
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-347 5.13e-14

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 73.02  E-value: 5.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333   1 MTLRTLLLGACSAMAFAGMASAETLTIAtvNNGDMIRmQKLTDDFKAKNpGIDLEWVTLEEN-VLRQKvttdIATKGGQY 79
Cdd:COG0687    7 LGLAAAALAAALAGGAPAAAAEGTLNVY--NWGGYID-PDVLEPFEKET-GIKVVYDTYDSNeEMLAK----LRAGGSGY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  80 DVLTIGTYEVPIWAKKGWLLPLD--NLgANYdvDDLLPAIRSGISQDGKLYAAPFYGESSMVMYRKDLFDAAglkmPDap 157
Cdd:COG0687   79 DVVVPSDYFVARLIKAGLLQPLDksKL-PNL--ANLDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEP----PT-- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 158 TWDFIADA--AKKIT--NKDKEVYGICLRGKagwGENMAFLTamsnsfgarwfDEQWKPQFDQ-PEWKDTLTFYvnlmke 232
Cdd:COG0687  150 SWADLWDPeyKGKVAllDDPREVLGAALLYL---GYDPNSTD-----------PADLDAAFELlIELKPNVRAF------ 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 233 agppgasSNGFNENLALFQTGKcgmwIDATVAASFVADPKQSQvADKVGFAlAPdkglgKRGNWLWAWNLAIPAGSQKSE 312
Cdd:COG0687  210 -------WSDGAEYIQLLASGE----VDLAVGWSGDALALRAE-GPPIAYV-IP-----KEGALLWFDNMAIPKGAPNPD 271

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 739208333 313 AAEKFIAWATSKDYTNLVAEKEGWLNAPPGTRSSL 347
Cdd:COG0687  272 LAYAFINFMLSPEVAAALAEYVGYAPPNKAARELL 306
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 108-330 7.42e-10

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: 60.83  E-value: 7.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 108 YDVDDLLPAIRSgisQDGKLYAAPFYGESSMV----MYRKDLFDAAGLKMPDapTWDFIADAAKKITNKDKEVYGICLRG 183
Cdd:cd13583   98 WGLGKELATGRQ---SDGKYYSLPGLHEDPGVqysfLYRKDIFEKAGIKIPT--TWDEFYAALKKLKEKYPDSYPYSDRW 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 184 KAGWGENMAFLTAMSNSFGAR------WFDEQWKPQFDQPEWKDTLTFYVNLMKEaG--PPGASSNGFNENLALFQTGKC 255
Cdd:cd13583  173 NSNALLLIAAPAFGTTAGWGFsnytydPDTDKFVYGATTDEYKDMLQYFNKLYAE-GllDPESFTQTDDQAKAKFLNGKS 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 256 gMWIDATvAASFVADPKQSQVADKVGFAL------APDKGLGKRGNWLWAWNL--AIPAGSQKSEAAEKFIAWATSKDYT 327
Cdd:cd13583  252 -FVITTN-PQTVDELQRNLRAADGGNYEVvsitppAGPAGKAINGSRLENGFMisSKAKDSKNFEALLQFLDWLYSDEGQ 329


                 ...
gi 739208333 328 NLV 330
Cdd:cd13583  330 ELA 332
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 39-318 2.09e-09

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


Pssm-ID: 270308 [Multi-domain]  Cd Length: 315  Bit Score: 58.40  E-value: 2.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  39 QKLTDDFKAKNpGIDLEWVTLEEN-VLRQKVTtdiATKGGQYDVLTIGTYEVPIWAKKGWLLPLD-NLGANYdvDDLLPA 116
Cdd:cd13590   13 PEVLKAFEKET-GVKVNYDTYDSNeEMLAKLR---AGGGSGYDLVVPSDYMVERLIKQGLLEPLDhSKLPNL--KNLDPQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 117 IRSGISQDGKLYAAPFYGESSMVMYRKDlfdaaglKMPDAPTW---DFIADAAK-KIT--NKDKEVYGICLRgkagwgen 190
Cdd:cd13590   87 FLNPPYDPGNRYSVPYQWGTTGIAYNKD-------KVKEPPTSwdlDLWDPALKgRIAmlDDAREVLGAALL-------- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 191 mafltAMSNSFgARWFDEQWKPQFDqpewkdtltfyvnLMKEAGP--PGASSNGFNENLAlfqTGkcgmwiDATVAASFV 268
Cdd:cd13590  152 -----ALGYSP-NTTDPAELAAAAE-------------LLIKQKPnvRAFDSDSYVQDLA---SG------EIWLAQAWS 203

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 739208333 269 ADPKQSQVAD-KVGFALaPDKGLGkrgnwLWAWNLAIPAGSQKSEAAEKFI 318
Cdd:cd13590  204 GDALQANRENpNLKFVI-PKEGGL-----LWVDNMAIPKGAPNPELAHAFI 248
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 45-329 1.09e-08

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This family represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria and related proteins. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. In Sphingomonas sp. A1, the transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins AlgQ1 and AlgQ2. Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270239 [Multi-domain]  Cd Length: 483  Bit Score: 57.08  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  45 FKAKNPGIDLEWVTLEENVlrQKVTTDIATkgGQYDVLTIGTY---EVPIWAKKGWLLPLDNL-----------GANYDV 110
Cdd:cd13521   27 EKLTNVKLEIVAVTAATSQ--QKLNLMLAS--GDLPDIVGADYlkdKFIAYGMEGAFLPLSKYidqypnlkaffKQHPDV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 111 DDLLPAIrsgisqDGKLYAAPFYGESSMVMY----RKDLFDAAGLKMPDapTWDFIADAAKKITNKDKEVYG-------I 179
Cdd:cd13521  103 LRASTAS------DGKIYLIPYEPPKDVPNQgyfiRKDWLDKLNLKTPK--TLDELYNVLKAFKEKDPNGNGkadeipfI 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 180 CLRGKAGWGENMAFLTAMSnSFGARWFDeqW-------KPQFDQPEWKDTLTFYVNLMKEA-GPPGASSNGFNENLALFQ 251
Cdd:cd13521  175 DRDPLYGAFRLINSWGARS-AGGSTDSD--WyedngkfKHPFASEEYKDGMKYMNKLYTEGlIDKESFTQKDDQAEQKFS 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 252 TGKCGMWIDATVAASFVADPKQSQvaDKVGFAL---APDKGLGKRGNWLWA-----WNLAIPAGSQKSEAAEKFIAWATS 323
Cdd:cd13521  252 NGKLGGFTHNWFASDNLFTAQLGK--EKPMYILlpiAPAGNVKGRREEDSPgytgpDGVAISKKAKNPVAALKFFDWLAS 329


                 ....*.
gi 739208333 324 KDYTNL 329
Cdd:cd13521  330 EEGREL 335
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 51-318 1.07e-06

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: 270299 [Multi-domain]  Cd Length: 490  Bit Score: 50.78  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  51 GIDLEWVTLEENVLRQKVTTDIAtkGGQYDVLTIGTYEVPI----WAKKGWLLPLDNLGANY-----DVDDLLPAIRSGI 121
Cdd:cd13581   31 GIKIEWETVPEDAWAEKKNLMLA--SGDLPDAFLGAGASDAdlmtYGKQGLFLPLEDLIDKYapnlkALFDENPDIKAAI 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 122 SQ-DGKLYAAP-----FYGESSMVMY-RKDLFDAAGLKMPDapTWDFIADAAKKITNKD-------KEVYGICLRGKAGW 187
Cdd:cd13581  109 TApDGHIYALPsvnecYHCSYGQRMWiNKKWLDKLGLEMPT--TTDELYEVLKAFKEQDpngngkaDEIPLSFSGLNGGT 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 188 GeNMAFLTamsNSFG----------ARWFDEQWKPQFDQPEWKDTLTFYVNLMKEaG--PPGASSNGFNENLALF--QTG 253
Cdd:cd13581  187 D-DPAFLL---NSFGindggyggygFVVKDGKVIYTATDPEYKEALAYLNKLYKE-GliDPEAFTQDYDQLAAKGkaSTA 261

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739208333 254 KCGMWIDATVAASFVADPKQSQVadkvgfALAPDKGLGKRGNWLWA-------WNLAIPAGSQKSEAAEKFI 318
Cdd:cd13581  262 KVGVFFGWDPGLFFGEERYEQYV------PLPPLKGPNGDQLAWVGnssgygrGGFVITSKNKNPEAAIRWA 327
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 39-426 2.25e-06

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: 49.40  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  39 QKLTDDFKAKNpGIDLEWVTLEENVLRQKVTTDiATKGGQYDVLTIGTYEVPIWAKKGWLLPLDNlgANYDVDDLLPAIR 118
Cdd:cd13658   16 KKIAKQYTKKT-GVKVKLVEVDQLDQLEKLSLD-GPAGKGPDVMVAPHDRIGSAVLQGLLSPIKL--SKDKKKGFTDQAL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 119 SGISQDGKLYAAPFYGESSMVMYRKDLfdaaglkMPDAP-TWDFIADAAKKITNKDKEVYGIClrgkAGWGE---NMAFL 194
Cdd:cd13658   92 KALTYDGKLYGLPAAVETLALYYNKDL-------VKNAPkTFDELEALAKDLTKEKGKQYGFL----ADATNfyySYGLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 195 TAMsnsfGARWFDEQWKPQF------DQPEWKDTLTFYVNLMKEAG-PPGASSNGFNenlALFQTGKCGMWIDATVAAsf 267
Cdd:cd13658  161 AGN----GGYIFKKNGSDLDindiglNSPGAVKAVKFLKKWYTEGYlPKGMTGDVIQ---GLFKEGKAAAVIDGPWAI-- 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 268 vadpkQSQVADKVGFALAP----DKG------LGKRGnWLwawnlaIPAGSQKSEAAEKFIAWATSKDYTNLVAEKEGWL 337
Cdd:cd13658  232 -----QEYQEAGVNYGVAPlptlPNGkpmapfLGVKG-WY------LSAYSKHKEWAQKFMEFLTSKENLKKRYDETNEI 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 338 naPPGTRSSLYAN-ADYQKAASFAKMTldsinsadptkPTVKPVPyvgvqfvAIPEFQGIGTAVGQQFSAALAGQISVDQ 416
Cdd:cd13658  300 --PPRKDVRSDPEiKNNPLTSAFAKQA-----------SRAVPMP-------NIPEMGAVWEPANNALFFILSGKKTPKQ 359

                        410
                 ....*....|
gi 739208333 417 ALQSAQQLTT 426
Cdd:cd13658  360 ALNDAVNDIK 369
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 78-325 1.80e-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: 46.07  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  78 QYDVLTIGTYEVPIWAKKGWLLPLD-NLGANYDVDDLLPAIRSGisqdgklYAAPFYGESSMVMYRKDLFDAAGlkmPDA 156
Cdd:cd13589   53 QWDVVDLDDGDAARAIAEGLLEPLDySKIPNAAKDKAPAALKTG-------YGVGYTLYSTGIAYNTDKFKEPP---TSW 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 157 PTWDFiaDAAKKITNKDkevygiclrgkAGWGENMAFLTAMSNSFGARWFDEQWKPQFDQ-PEWKDTLTFYvnlmkeagp 235
Cdd:cd13589  123 WLADF--WDVGKFPGPR-----------ILNTSGLALLEAALLADGVDPYPLDVDRAFAKlKELKPNVVTW--------- 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 236 pgasSNGFNENLALFQTGKcgmwIDATVAASFVADPKQSQVADkvgFALAPDKGlgkrGNWLWAWNLAIPAGSQKSEAAE 315
Cdd:cd13589  181 ----WTSGAQLAQLLQSGE----VDMAPAWNGRAQALIDAGAP---VAFVWPKE----GAILGPDTLAIVKGAPNKELAM 245

                        250
                 ....*....|
gi 739208333 316 KFIAWATSKD 325
Cdd:cd13589  246 KFINFALSPE 255
PBP2_Thiaminase_I cd13524
Thiaminase-I has high structural homology to the type 2 periplasmic binding proteins of active ...
 42-149 2.10e-05

Thiaminase-I has high structural homology to the type 2 periplasmic binding proteins of active transport systems; Thiaminase-I, a thiamin-(vitamin B1) degrading enzyme, is a monomer in its biologically active form, with two distinct globular domains (N- and C-domains) separated by a deep groove. It has a structural topology similar to the periplasmic substrate-domains of ABC-type transport systems, such as thiamin-binding protein (TbpA), that possess the type 2 periplasmic binding protein fold. The PBP2 proteins 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 majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea.


Pssm-ID: 270242  Cd Length: 363  Bit Score: 46.38  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  42 TDDFKAKNPGIDLEWVTLEENVL--RQKVTTDIATKGGQYDVLTIGTYEVPIWAKKGWLLPLDNLGANydvdDLLPAIRS 119
Cdd:cd13524   22 TDQWQRQEPGVDLDFVDWAKLDDsySADPPDLNQLGAGALDVVEIDTIFLGHLVDAGYLLPFGIDQAR----DYLPFALQ 97

                         90       100       110
                 ....*....|....*....|....*....|
gi 739208333 120 GISQDGKLYAAPFYGESSMVMYRKDLFDAA 149
Cdd:cd13524   98 AVSRNGEVYGVPQLLCTNLLFYRSPDLGQA 127
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 70-168 6.52e-05

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


Pssm-ID: 270306 [Multi-domain]  Cd Length: 279  Bit Score: 44.59  E-value: 6.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  70 TDIATKGGQYDVLTIGTYEVPIWAKKGWLLPLD-NLGANYdvDDLLPAIR--SGISQDGKLYAAPFYGESSMVMYRKDLF 146
Cdd:cd13588   40 AKLRSGGGDYDVVTPSGDALLRLIAAGLVQPIDtSKIPNY--ANIDPRLRnlPWLTVDGKVYGVPYDWGANGLAYNTKKV 117

                         90       100
                 ....*....|....*....|..
gi 739208333 147 daaglkmPDAPTWDFIADAAKK 168
Cdd:cd13588  118 -------KTPPTSWLALLWDPK 132
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 38-167 2.36e-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: 40.02  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  38 MQKLTDDFKAKNPGIDLEW--VTLEENVLRQKVTTDIATKGgqyDVLTIGTYEVPIWAKKGWLLPLDNLGANYDVDDLLP 115
Cdd:cd13655   14 LKEMVDAFKEKHPEWKITItiGVVGEADAKDEVLKDPSAAA---DVFAFANDQLGELVDAGAIYPLTGSAVDKIKNTNSE 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 739208333 116 AIRSGISQDGKLYAAPFYGESSMVMYRKDLFDAAGLKmpdapTWDFIADAAK 167
Cdd:cd13655   91 ATVDAVTYNGKLYGYPFTANTWFMYYDKSKLTEDDVK-----SLDTMLAKAP 137
PBP2_polyamine_2 cd13587
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 73-342 7.12e-03

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


Pssm-ID: 270305 [Multi-domain]  Cd Length: 292  Bit Score: 38.18  E-value: 7.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  73 ATKGGQYDVLTIGTYEVPIWAKKGWLLPLD--NLGANYDVDDLLPAIRSGISQDGKLYAAPF-YGESSMVMYRKDLFDAA 149
Cdd:cd13587   44 ATGGGGFDLAQPSQRIAPNYEEFGLYQPIDesKIKVAQFPPSLLESTKLGTTINGKRYAVPFdWGTEGLTVNSTKAPDVS 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 150 GLKMPDapTWDfiADAAKKITNKDKEVygicLRGKAGWGENMAFLTamSNSFGARWFDEQWKPQFDQPEWKdtltfyvnL 229
Cdd:cd13587  124 GFSYGD--LWA--PEYAGKVAYRLKSP----LTGLGLYADATGEDP--FNRYLDYKDEAKYQKILDQVLQF--------L 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 230 MKEAGPPGASSNGFNENLALFQTGKCgmWIdatvaasfvadpkqSQVADKVGFALAPDK-----GLGKRGNWLWAWNLAI 304
Cdd:cd13587  186 IERKANVKAYWNNADEALAAFRSGGC--VI--------------GQTWDSTGLKLNRENppidyGAPKEGALGWIDTFAI 249

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 739208333 305 PAGSQKSEAAEKFIAWATSKDYTNLVAEKEGWLNAPPG 342
Cdd:cd13587  250 PAKAENVDQAYAFINFMLRPEIAAMFTNATGYNTAAVG 287
PBP2_PotD_PotF_like_2 cd13663
The periplasmic substrate-binding component of an uncharacterized active transport system ...
 24-190 7.17e-03

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


Pssm-ID: 270381 [Multi-domain]  Cd Length: 323  Bit Score: 38.43  E-value: 7.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333  24 TLTIAtvNNGDMIRMqKLTDDFKAKNpGIDLEWVTLEENvlrQKVTTDIATKGGQYDVLTIGTYEVPIWAKKGWLLPLDN 103
Cdd:cd13663    1 TLKVY--NWGEYIDP-DLIDDFEKET-GIKVNYETFDSN---EEMYTKIKTGGTSYDVIVPSDYMIEKLIKEDLLQPLDY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739208333 104 -LGANYD-VDDLLPAIRSGISQDGKLYAAP-FYGESSMVmYRKDLFDaaglkMPDAPTWDFI--ADAAKKITNKD--KEV 176
Cdd:cd13663   74 sKLPNVDkNINIQPDLLNLAFDPINEYSVPyFWGTLGIV-YNKTKVS-----LEELSWWNILwnKKYKGKILMYDspRDA 147

                        170
                 ....*....|....
gi 739208333 177 YGICLrGKAGWGEN 190
Cdd:cd13663  148 FMVAL-KALGYSLN 160
 
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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