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Conserved domains on  [gi|1550319097|gb|RVP86180|]
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sugar ABC transporter substrate-binding protein [Sinorhizobium meliloti]

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 2.82e-88

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: 273.51  E-value: 2.82e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  24 TLTIATVNNGDMI-RMQKLTDDFTSKNPDIQLEWVTLEENVLRQRVTTDIATkGGQYDIMTIGTYEVPIWAKQGWLLPLD 102
Cdd:cd13585     1 TLTFWDWGQPAETaALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAA-GTAPDVFYVDGPWVPEFASNGALLDLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 103 DLGPEYDVDD-LLPAIRSGLTIDGKLYAAPFYGESSMVMYRKDLFEKAGLTMPDAPTWDFIADAARKITDKGNEIYGICL 181
Cdd:cd13585    80 DYIEKDGLDDdFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTDKKGGQYGFAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 182 RgkaGWGENMAFLTATANAFGARWFDE-NWKPQFDQPEWKNALDFYVKLMNDAGPPGASSNGFNENLSLFQTGKCGMWID 260
Cdd:cd13585   160 R---GGSGGQTQWYPFLWSNGGDLLDEdDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFASGKVAMMID 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 261 ATVAASFVTNPKestVADKVGFALAPDTGLGKRGNWLWAWNLAIPAGSQKAESAQKFIAWATGkdylklvaeKEGWANVP 340
Cdd:cd13585   237 GPWALGTLKDSK---VKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTS---------KENQLKLG 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 341 PGTRTSLYENPEYQKAAPFAKMTLDSINAADPKNPAVKPVPYVGVQFVAIPEFQGLGTAVGQvfsaalAGQMSVDQALAS 420
Cdd:cd13585   305 GAAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLG------ALGKSPEEALKE 378


                  ...
gi 1550319097 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 2.82e-88

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: 273.51  E-value: 2.82e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  24 TLTIATVNNGDMI-RMQKLTDDFTSKNPDIQLEWVTLEENVLRQRVTTDIATkGGQYDIMTIGTYEVPIWAKQGWLLPLD 102
Cdd:cd13585     1 TLTFWDWGQPAETaALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAA-GTAPDVFYVDGPWVPEFASNGALLDLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 103 DLGPEYDVDD-LLPAIRSGLTIDGKLYAAPFYGESSMVMYRKDLFEKAGLTMPDAPTWDFIADAARKITDKGNEIYGICL 181
Cdd:cd13585    80 DYIEKDGLDDdFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTDKKGGQYGFAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 182 RgkaGWGENMAFLTATANAFGARWFDE-NWKPQFDQPEWKNALDFYVKLMNDAGPPGASSNGFNENLSLFQTGKCGMWID 260
Cdd:cd13585   160 R---GGSGGQTQWYPFLWSNGGDLLDEdDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFASGKVAMMID 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 261 ATVAASFVTNPKestVADKVGFALAPDTGLGKRGNWLWAWNLAIPAGSQKAESAQKFIAWATGkdylklvaeKEGWANVP 340
Cdd:cd13585   237 GPWALGTLKDSK---VKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTS---------KENQLKLG 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 341 PGTRTSLYENPEYQKAAPFAKMTLDSINAADPKNPAVKPVPYVGVQFVAIPEFQGLGTAVGQvfsaalAGQMSVDQALAS 420
Cdd:cd13585   305 GAAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLG------ALGKSPEEALKE 378


                  ...
gi 1550319097 421 AQQ 423
Cdd:cd13585   379 AAK 381
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 5-332 1.13e-76

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 243.03  E-value: 1.13e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097   5 TFLLGTCSAVALAGLAQAE--TLTIATVNNGDMIRMQKLTDDFTSKNPDIQLEWVTLEENVLRQRVTTDIATkGGQYDIM 82
Cdd:COG1653    13 ALALAACGGGGSGAAAAAGkvTLTVWHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAA-GNAPDVV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  83 TIGTYEVPIWAKQGWLLPLDDL--GPEYDVDDLLPAIRSGLTIDGKLYAAPFYGESSMVMYRKDLFEKAGLTMPDapTWD 160
Cdd:COG1653    92 QVDSGWLAEFAAAGALVPLDDLldDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPPK--TWD 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 161 FIADAARKITDKgNEIYGICLRGKAGWgenmaFLTATANAFGARWFDENWKPQFDQPEWKNALDFYVKLMND-AGPPGAS 239
Cdd:COG1653   170 ELLAAAKKLKAK-DGVYGFALGGKDGA-----AWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKDgYVPPGAL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 240 SNGFNENLSLFQTGKCGMWIDATVAASFVTNPKEStvaDKVGFALAPDTGLGKRGN-WLWAWNLAIPAGSQKAESAQKFI 318
Cdd:COG1653   244 GTDWDDARAAFASGKAAMMINGSWALGALKDAAPD---FDVGVAPLPGGPGGKKPAsVLGGSGLAIPKGSKNPEAAWKFL 320

                         330
                  ....*....|....
gi 1550319097 319 AWATGKDYLKLVAE 332
Cdd:COG1653   321 KFLTSPEAQAKWDA 334
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 34-326 1.53e-47

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: 164.90  E-value: 1.53e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  34 DMIRMQKLTDDFTSKNPDIQLEWVTLEENVLRQRVTTDIATKGGQYDIMTIGTYEVPIWAKQGWLLPLDDLGPEYDVDDl 113
Cdd:pfam01547   6 EAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYLVLG- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 114 lpairsgltiDGKLYAAPFYGESSMVMYRKDLFEKAGLTMPdaPTWDFIADAARKITDKGNEIYGicLRGKAGWGENMAF 193
Cdd:pfam01547  85 ----------VPKLYGVPLAAETLGLIYNKDLFKKAGLDPP--KTWDELLEAAKKLKEKGKSPGG--AGGGDASGTLGYF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 194 LTATANAFGARWFDENWKpQFDQPEWKNALDFYVKLMNDA------GPPGASSNGFNENLSLFQTGKCGMWIDATVAASF 267
Cdd:pfam01547 151 TLALLASLGGPLFDKDGG-GLDNPEAVDAITYYVDLYAKVlllkklKNPGVAGADGREALALFEQGKAAMGIVGPWAALA 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550319097 268 VTNPKESTVADKVGFALAPDTGL----GKRGNWLWAWNLAIPAGSQKAESAQKFIAWATGKDY 326
Cdd:pfam01547 230 ANKVKLKVAFAAPAPDPKGDVGYaplpAGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEA 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 2.82e-88

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: 273.51  E-value: 2.82e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  24 TLTIATVNNGDMI-RMQKLTDDFTSKNPDIQLEWVTLEENVLRQRVTTDIATkGGQYDIMTIGTYEVPIWAKQGWLLPLD 102
Cdd:cd13585     1 TLTFWDWGQPAETaALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAA-GTAPDVFYVDGPWVPEFASNGALLDLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 103 DLGPEYDVDD-LLPAIRSGLTIDGKLYAAPFYGESSMVMYRKDLFEKAGLTMPDAPTWDFIADAARKITDKGNEIYGICL 181
Cdd:cd13585    80 DYIEKDGLDDdFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTDKKGGQYGFAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 182 RgkaGWGENMAFLTATANAFGARWFDE-NWKPQFDQPEWKNALDFYVKLMNDAGPPGASSNGFNENLSLFQTGKCGMWID 260
Cdd:cd13585   160 R---GGSGGQTQWYPFLWSNGGDLLDEdDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFASGKVAMMID 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 261 ATVAASFVTNPKestVADKVGFALAPDTGLGKRGNWLWAWNLAIPAGSQKAESAQKFIAWATGkdylklvaeKEGWANVP 340
Cdd:cd13585   237 GPWALGTLKDSK---VKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTS---------KENQLKLG 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 341 PGTRTSLYENPEYQKAAPFAKMTLDSINAADPKNPAVKPVPYVGVQFVAIPEFQGLGTAVGQvfsaalAGQMSVDQALAS 420
Cdd:cd13585   305 GAAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLG------ALGKSPEEALKE 378


                  ...
gi 1550319097 421 AQQ 423
Cdd:cd13585   379 AAK 381
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 5-332 1.13e-76

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 243.03  E-value: 1.13e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097   5 TFLLGTCSAVALAGLAQAE--TLTIATVNNGDMIRMQKLTDDFTSKNPDIQLEWVTLEENVLRQRVTTDIATkGGQYDIM 82
Cdd:COG1653    13 ALALAACGGGGSGAAAAAGkvTLTVWHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAA-GNAPDVV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  83 TIGTYEVPIWAKQGWLLPLDDL--GPEYDVDDLLPAIRSGLTIDGKLYAAPFYGESSMVMYRKDLFEKAGLTMPDapTWD 160
Cdd:COG1653    92 QVDSGWLAEFAAAGALVPLDDLldDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPPK--TWD 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 161 FIADAARKITDKgNEIYGICLRGKAGWgenmaFLTATANAFGARWFDENWKPQFDQPEWKNALDFYVKLMND-AGPPGAS 239
Cdd:COG1653   170 ELLAAAKKLKAK-DGVYGFALGGKDGA-----AWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKDgYVPPGAL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 240 SNGFNENLSLFQTGKCGMWIDATVAASFVTNPKEStvaDKVGFALAPDTGLGKRGN-WLWAWNLAIPAGSQKAESAQKFI 318
Cdd:COG1653   244 GTDWDDARAAFASGKAAMMINGSWALGALKDAAPD---FDVGVAPLPGGPGGKKPAsVLGGSGLAIPKGSKNPEAAWKFL 320

                         330
                  ....*....|....
gi 1550319097 319 AWATGKDYLKLVAE 332
Cdd:COG1653   321 KFLTSPEAQAKWDA 334
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 24-423 2.31e-68

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: 222.17  E-value: 2.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  24 TLTIATVNNGDMIR-MQKLTDDFTSKNPDIQLEWVTL--EENVLRQRVTTDIATKGGQYDIMTIGTYEVPIWAKQGWLLP 100
Cdd:cd14750     1 TITFAAGSDGQEGElLKKAIAAFEKKHPDIKVEIEELpaSSDDQRQQLVTALAAGSSAPDVLGLDVIWIPEFAEAGWLLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 101 LDDLGPEYDVDDLLPAIRSGLTIDGKLYAAPFYGESSMVMYRKDLFEKAGLTMPDapTWDFIADAARKITDKGNEIYGIC 180
Cdd:cd14750    81 LTEYLKEEEDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPEPPK--TWDELLEAAKKRKAGEPGIWGYV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 181 LRGKAGWGenmafLTATA----NAFGARWFDE-NWKPQFDQPEWKNALDFYVKLMND-AGPPGASSNGFNENLSLFQTGK 254
Cdd:cd14750   159 FQGKQYEG-----LVCNFlellWSNGGDIFDDdSGKVTVDSPEALEALQFLRDLIGEgISPKGVLTYGEEEARAAFQAGK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 255 CGM---WIdatvAASFVTNPKESTVADKVGFALAPDTGLGKRGNWLWAWNLAIPAGSQKAESAQKFIAWATGKDYLKLVA 331
Cdd:cd14750   234 AAFmrnWP----YAYALLQGPESAVAGKVGVAPLPAGPGGGSASTLGGWNLAISANSKHKEAAWEFVKFLTSPEVQKRRA 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 332 EKEGWanvPPgTRTSLYENPEYQKAAPFAKMTLDSINAADPknpavKPVpyvgvqfvaIPEFQGLGTAVGQVFSAALAGQ 411
Cdd:cd14750   310 INGGL---PP-TRRALYDDPEVLEAYPFLPALLEALENAVP-----RPV---------TPKYPEVSTAIQIALSAALSGQ 371

                         410
                  ....*....|..
gi 1550319097 412 MSVDQALASAQQ 423
Cdd:cd14750   372 ATPEEALKQAQE 383
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 38-423 2.44e-59

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: 198.67  E-value: 2.44e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  38 MQKLTDDFTSKNPDIQLEWVTLEE-NVLRQRVTTDIATkGGQYDIMTIGTYEVPIWAKQGWLLPLDDL--GPEYDVDDLL 114
Cdd:cd14748    16 LEELVDEFNKSHPDIKVKAVYQGSyDDTLTKLLAALAA-GTAPDVAQVDASWVAQLADSGALEPLDDYidKDGVDDDDFY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 115 PAIRSGLTIDGKLYAAPFYGESSMVMYRKDLFEKAGLTMPDAP-TWDFIADAARK--ITDKGNEIYGICLRGKAGWGENM 191
Cdd:cd14748    95 PAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPkTWDELEEAAKKlkDKGGKTGRYGFALPPGDGGWTFQ 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 192 AFLtataNAFGARWFDE-NWKPQFDQPEWKNALDFYVKLMNDAGPPGASSNGFNENlsLFQTGKCGMWIDATVAASFVTN 270
Cdd:cd14748   175 ALL----WQNGGDLLDEdGGKVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQD--AFISGKVAMTINGTWSLAGIRD 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 271 PKEStvaDKVGFALAPDTGLGKRGNWLWAWNLAIPAG-SQKAESAQKFIAWATGKDYLKLVAEKEGWanvpPGTRTSLYE 349
Cdd:cd14748   249 KGAG---FEYGVAPLPAGKGKKGATPAGGASLVIPKGsSKKKEAAWEFIKFLTSPENQAKWAKATGY----LPVRKSAAE 321

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550319097 350 NPE-YQKAAPFAKMTLDSINAADPKNPAVkpvpyvgvqfvaiPEFQGLGTAVGQVFSAALAGQMSVDQALASAQQ 423
Cdd:cd14748   322 DPEeFLAENPNYKVAVDQLDYAKPWGPPV-------------PNGAEIRDELNEALEAALLGKKTPEEALKEAQE 383
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 34-326 1.53e-47

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: 164.90  E-value: 1.53e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  34 DMIRMQKLTDDFTSKNPDIQLEWVTLEENVLRQRVTTDIATKGGQYDIMTIGTYEVPIWAKQGWLLPLDDLGPEYDVDDl 113
Cdd:pfam01547   6 EAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYLVLG- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 114 lpairsgltiDGKLYAAPFYGESSMVMYRKDLFEKAGLTMPdaPTWDFIADAARKITDKGNEIYGicLRGKAGWGENMAF 193
Cdd:pfam01547  85 ----------VPKLYGVPLAAETLGLIYNKDLFKKAGLDPP--KTWDELLEAAKKLKEKGKSPGG--AGGGDASGTLGYF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 194 LTATANAFGARWFDENWKpQFDQPEWKNALDFYVKLMNDA------GPPGASSNGFNENLSLFQTGKCGMWIDATVAASF 267
Cdd:pfam01547 151 TLALLASLGGPLFDKDGG-GLDNPEAVDAITYYVDLYAKVlllkklKNPGVAGADGREALALFEQGKAAMGIVGPWAALA 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550319097 268 VTNPKESTVADKVGFALAPDTGL----GKRGNWLWAWNLAIPAGSQKAESAQKFIAWATGKDY 326
Cdd:pfam01547 230 ANKVKLKVAFAAPAPDPKGDVGYaplpAGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEA 292
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-423 2.34e-42

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 154.34  E-value: 2.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097   1 MNLRTFLLGTCSAVALAGLA----------------QAETLTIAtVNNGDMIRMQKLTDDFTSKnPDIQLEWVTLEENVL 64
Cdd:COG2182     1 MKRRLLAALALALALALALAacgsgssssgsssaagAGGTLTVW-VDDDEAEALEEAAAAFEEE-PGIKVKVVEVPWDDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  65 RQRVTTDIATKGGqYDIMTIGTYEVPIWAKQGWLLPLDDLGPeyDVDDLLPAIRSGLTIDGKLYAAPFYGESSMVMYRKD 144
Cdd:COG2182    79 REKLTTAAPAGKG-PDVFVGAHDWLGELAEAGLLAPLDDDLA--DKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 145 LFEKagltmpDAP-TWDFIADAARKITDKGNeiYGICLRGKAGWgENMAFLTatanAFGARWFDEN----WKPQFDQPEW 219
Cdd:COG2182   156 LVKA------EPPkTWDELIAAAKKLTAAGK--YGLAYDAGDAY-YFYPFLA----AFGGYLFGKDgddpKDVGLNSPGA 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 220 KNALDFYVKLMNDAGPPgaSSNGFNENLSLFQTGKCGMWIDAT-VAASFVTNPKestvaDKVGFALAPDTGLGKRGN-WL 297
Cdd:COG2182   223 VAALEYLKDLIKDGVLP--ADADYDAADALFAEGKAAMIINGPwAAADLKKALG-----IDYGVAPLPTLAGGKPAKpFV 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 298 WAWNLAIPAGSQKAESAQKFIAWATGKDYLKLVAEKegwANVPPgTRTSLYENPEyQKAAPFAKMTLDSINAAdpknpav 377
Cdd:COG2182   296 GVKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALFEA---TGRIP-ANKAAAEDAE-VKADPLIAAFAEQAEYA------- 363

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1550319097 378 KPVPyvgvqfvAIPEFQGLGTAVGQVFSAALAGQMSVDQALASAQQ 423
Cdd:COG2182   364 VPMP-------NIPEMGAVWTPLGTALQAIASGKADPAEALDAAQK 402
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 24-424 5.98e-40

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: 147.14  E-value: 5.98e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  24 TLTIATVNNGDMIR--MQKLTDDFTSKNPDIQLEWVTLEENVLRQRVTTDIATKGGQYDIMTIGTYEVPIWAKQGWLLPL 101
Cdd:cd14749     1 TITYWQYFTGDTKKkyMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPGGWLAEFVKAGLLLPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 102 DDLGPEYDVDDL-LPAIRSGLTIDGKLYAAPFYGESSMVMYRKDLFEKAGLTMPDApTWDFIADAARKITDKGNEIYGIC 180
Cdd:cd14749    81 TDYLDPNGVDKRfLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGVKPPK-TWDELIEAAKKDKFKAKGQTGFG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 181 LRGKAGWGenMAFLTATANAFGARWFDENW--KPQFDQPEWKNALDFYVKLMND-AGPPGASSNGFNENLSLFQTGKCGM 257
Cdd:cd14749   160 LLLGAQGG--HWYFQYLVRQAGGGPLSDDGsgKATFNDPAFVQALQKLQDLVKAgAFQEGFEGIDYDDAGQAFAQGKAAM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 258 WIDATVAASFVTNPKestVADKVGFALAPDTGLGKRGNWLWA--WNLAIPAGSQKAESAQKFIAWATGKDYLKLVAEKEG 335
Cdd:cd14749   238 NIGGSWDLGAIKAGE---PGGKIGVFPFPTVGKGAQTSTIGGsdWAIAISANGKKKEAAVKFLKYLTSPEVMKQYLEDVG 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 336 wanVPPgtrtslyENPEYQKAAPFAKMTLDSINAADPKNPAVKPVpyvgVQFVAIPEFQGLGTAVGQVfsaaLAGQMSVD 415
Cdd:cd14749   315 ---LLP-------AKEVVAKDEDPDPVAILGPFADVLNAAGSTPF----LDEYWPAAAQVHKDAVQKL----LTGKIDPE 376


                  ....*....
gi 1550319097 416 QALASAQQL 424
Cdd:cd14749   377 QVVKQAQSA 385
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 38-423 8.62e-40

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: 146.69  E-value: 8.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  38 MQKLTDDFTSKNPDIQLEWVTLEENVLRQRVTTDIATKGGQyDIMTIGTYEVPIWAKQGWLLPLDDLGPE-YDVDDLLPA 116
Cdd:cd14747    16 LKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGP-DVVQLGNTWVAEFAAMGALEDLTPYLEDlGGDKDLFPG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 117 IRSGLTIDGKLYAAPFYGESSMVMYRKDLFEKAG-LTMPDapTWDFIADAARKITDKGNEIYGICLRGKAGWGENmaFLT 195
Cdd:cd14747    95 LVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGgDEAPK--TWDELEAAAKKIKADGPDVSGFAIPGKNDVWHN--ALP 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 196 ATANAFGARWFDENWKPQFDQPEWKNALDFYVKLMNDAGPPGASSNGFNENLSLFQTGKCGMWIDAT-VAASFVTNPKEs 274
Cdd:cd14747   171 FVWGAGGDLATKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSADVEQAFANGKVAMIISGPwEIGAIREAGPD- 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 275 tVADKVGFALAPDTGLGKRGNWLWAWNLAIPAGSQKAESAQKFIAWATGKDYLKLVAEKEGWanVPPgtRTSLYENPEYQ 354
Cdd:cd14747   250 -LAGKWGVAPLPGGPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGM--LPA--NTSAWDDPSLA 324

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550319097 355 K---AAPFAKMTLDSinaadpknpavKPVPyvgvqfvAIPEFQGLGTAVGQVFSAALAG-QMSVDQALASAQQ 423
Cdd:cd14747   325 NdplLAVFAEQLKTG-----------KATP-------ATPEWGEIEAELVLVLEEVWIGvGADVEDALDKAAA 379
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 29-421 2.60e-35

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: 134.43  E-value: 2.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  29 TVNNGDMIRMQKLTDDFTSKNPDIQLEWVTLEENVLRQRVTTdiATKGGQY-DIMTIGTYEVPIWAKQGWLLPLDDLGPE 107
Cdd:cd14751     7 TSSDEEKVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKT--AAAGGQApDVMRADIAWVPEFAKLGYLQPLDGTPAF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 108 YDVDDLLPAIRSGLTIDGKLYAAPFYGESSMVMYRKDLFEKAGLTMPdaPTWDFIADAARKITDKGNEiYGICLRGKAGW 187
Cdd:cd14751    85 DDIVDYLPGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEVP--KTMDELVAAAKAIKKKKGR-YGLYISGDGPY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 188 genmaFLTATANAFGARWFDE-NWKPQFDQPEWKNALDFYVKLMNDAGPPGASSNGFNENLSLFQTGKCGMWIDATVAAS 266
Cdd:cd14751   162 -----WLLPFLWSFGGDLTDEkKATGYLNSPESVRALETIVDLYDEGAITPCASGGYPNMQDGFKSGRYAMIVNGPWAYA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 267 FVTNPKESTVADKVGFALAPdTGLGKRGNWLWAWNLAIPAGSQKAESAQKFIAWATGKDYLKLVAEKEGwaNVPpgTRTS 346
Cdd:cd14751   237 DILGGKEFKDPDNLGIAPVP-AGPGGSGSPVGGEDLVIFKGSKNKDAAWKFVKFMSSAEAQALTAAKLG--LLP--TRTS 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550319097 347 LYENPEyQKAAPFAKMTLDSINAADPKNPavkpvpyvgvqfvaIPEFQGLGTAVGQVFSAALAGQMSVDQALASA 421
Cdd:cd14751   312 AYESPE-VANNPMVAAFKPALETAVPRPP--------------IPEWGELFEPLTLAFAKVLRGEKSPREALDEA 371
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 38-423 6.43e-27

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: 110.93  E-value: 6.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  38 MQKLTDDFTSKNPDIQLEwVTLEENV-LRQRVTTDIATKGGQyDIMT-----IGTyevpiWAKQGWLLPLDDLGPEYDVD 111
Cdd:cd13657    16 LQQIIDEFEAKYPVPNVK-VPFEKKPdLQNKLLTAIPAGEGP-DLFIwahdwIGQ-----FAEAGLLVPISDYLSEDDFE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 112 DLLPAIRSGLTIDGKLYAAPFYGESSMVMYRKDLfekagltMPDAP-TWDFIADAARKITDKGNEIYGIclrgkaGWGEN 190
Cdd:cd13657    89 NYLPTAVEAVTYKGKVYGLPEAYETVALIYNKAL-------VDQPPeTTDELLAIMKDHTDPAAGSYGL------AYQVS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 191 MA-FLTATANAFGARWFD-ENWKPQFDQPEWKNALDFYVKLMNDAGPPGASsngFNENLSLFQTGKCGMWIdatVAASFV 268
Cdd:cd13657   156 DAyFVSAWIFGFGGYYFDdETDKPGLDTPETIKGIQFLKDFSWPYMPSDPS---YNTQTSLFNEGKAAMII---NGPWFI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 269 TNPKEStvADKVGFALAPDtglGKRGNWLW------AWNLAIPAGSQKAESAQKFIAWATGKDYLKLVAEKEGWanVPpg 342
Cdd:cd13657   230 GGIKAA--GIDLGVAPLPT---VDGTNPPRpysgveGIYVTKYAERKNKEAALDFAKFFTTAEASKILADENGY--VP-- 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 343 TRTSLYENPEYqkaapfakmtldsinAADPKNPAVKPVPYVGVQFVAIPEFQGLGTAVGQVFSAALAGQMSVDQALASAQ 422
Cdd:cd13657   301 AATNAYDDAEV---------------AADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQEALAAAQ 365


                  .
gi 1550319097 423 Q 423
Cdd:cd13657   366 Q 366
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 40-357 2.25e-22

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 96.32  E-value: 2.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  40 KLTDDFTSKNpDIQLEWVTLEENVLRQRVTTDIAT-KGGQYDIMTIGTYEVPIWAKQGWLLPLDDLGPEYDVDDLLPAir 118
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAgNAPDLDVVWIAADQLATLAEAGLLADLSDVDNLDDLPDALDA-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 119 sgLTIDGKLYAAPFYGESSMVM-YRKDLFEKAGltmPDAPTWDFIADAARKITdkgneiygiclrGKAGWGENMA-FLTA 196
Cdd:pfam13416  78 --AGYDGKLYGVPYAASTPTVLyYNKDLLKKAG---EDPKTWDELLAAAAKLK------------GKTGLTDPATgWLLW 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 197 TANAFGARWFDENWKPqfdqPEWKNALDFYVKLmndaGPPGASSNGFNENLSLFQTGKcgmwidatvAASFVTNPKESTV 276
Cdd:pfam13416 141 ALLADGVDLTDDGKGV----EALDEALAYLKKL----KDNGKVYNTGADAVQLFANGE---------VAMTVNGTWAAAA 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 277 ADKVGFALApdTGLGKRGNWLWAWNLAIPAGS-QKAESAQKFIAWATGKDYLKLVAEKEGwaNVPPgtRTSLYENPEYQK 355
Cdd:pfam13416 204 AKKAGKKLG--AVVPKDGSFLGGKGLVVPAGAkDPRLAALDFIKFLTSPENQAALAEDTG--YIPA--NKSAALSDEVKA 277


                  ..
gi 1550319097 356 AA 357
Cdd:pfam13416 278 DP 279
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 39-424 8.60e-20

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: 90.16  E-value: 8.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  39 QKLTDDFTSKNPDIQLEWVTLEENVLRQRVTTdiATKGGQYDIMTIGTYE-VPIWAKQGWLLPLDDLGPeyDVDDLLPAI 117
Cdd:cd13522    17 NELIAKFEKAYPGITVEVTYQDTEARRQFFST--AAAGGKGPDVVFGPSDsLGPFAAAGLLAPLDEYVS--KSGKYAPNT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 118 RSGLTIDGKLYAAPFYGESSMVMYRKDLFekagltmPDAP--TWDFIADAARKITDKGneIYGICLRGKAGWgenmaFLT 195
Cdd:cd13522    93 IAAMKLNGKLYGVPVSVGAHLMYYNKKLV-------PKNPpkTWQELIALAQGLKAKN--VWGLVYNQNEPY-----FFA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 196 ATANAFGARWFDEN---WKPQFDQPEWKNALDFYVKLMNDAGPPGASSNGFNENlSLFQTGKCGMWIDAtvaaSFVTNPK 272
Cdd:cd13522   159 AWIGGFGGQVFKANngkNNPTLDTPGAVEALQFLVDLKSKYKIMPPETDYSIAD-ALFKAGKAAMIING----PWDLGDY 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 273 ESTVADKVGFALAPDTGLGKRGN-WLWAWNLAIPAGSQKAESAQKFIAWATGKDYLKLVAEKEGWAnvpPGtRTSLYENP 351
Cdd:cd13522   234 RQALKINLGVAPLPTFSGTKHAApFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDI---PA-NLQAYESP 309

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550319097 352 EYQKAAPfakMTLDSINAAdpknpavkpvpyVGVQFVAIPEFQGLGTAVGQVFSAALAGQMSVDQALASAQQL 424
Cdd:cd13522   310 AVQNKPA---QKASAEQAA------------YGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQQE 367
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 24-423 5.77e-18

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: 85.04  E-value: 5.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  24 TLTIATVNNGDMIRMQKLTDDFTSKNpDIQLEWVTLEENVLRQRVTTdiATKGGQYDIMTIGTYE-VPIWAKQGWLLPLD 102
Cdd:cd13586     1 TITVWTDEDGELEYLKELAEEFEKKY-GIKVEVVYVDSGDTREKFIT--AGPAGKGPDVFFGPHDwLGELAAAGLLAPIP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 103 -DLGPEYDVddlLPAIRSGLTIDGKLYAAPFYGESSMVMYRKDLfekagltMPDAP-TWDFIADAARKITDKGNEIYGIC 180
Cdd:cd13586    78 eYLAVKIKN---LPVALAAVTYNGKLYGVPVSVETIALFYNKDL-------VPEPPkTWEELIALAKKFNDKAGGKYGFA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 181 LrgKAGWGENMAFLTAtanAFGARWFDEN----WKPQFDQPEWKNALDFYVKLMNDAGPPGASSNGFNENlSLFQTGKCG 256
Cdd:cd13586   148 Y--DQTNPYFSYPFLA---AFGGYVFGENggdpTDIGLNNEGAVKGLKFIKDLKKKYKVLPPDLDYDIAD-ALFKEGKAA 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 257 MWIDAT-VAASFVTNpkestvadKVGFALAPDTGLGKR-------GNWLWAwnlaIPAGSQKAESAQKFIAWATGKDYLK 328
Cdd:cd13586   222 MIINGPwDLADYKDA--------GINFGVAPLPTLPGGkqaapfvGVQGAF----VSAYSKNKEAAVEFAEYLTSDEAQL 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 329 LVAEKegwANVPPgTRTSLYENPEYQKaapfakmtldsinaadpkNPAVKPV----PYvGVQFVAIPEFQGLGTAVGQVF 404
Cdd:cd13586   290 LLFEK---TGRIP-ALKDALNDAAVKN------------------DPLVKAFaeqaQY-GVPMPNIPEMAAVWDAMGNAL 346

                         410
                  ....*....|....*....
gi 1550319097 405 SAALAGQMSVDQALASAQQ 423
Cdd:cd13586   347 NLVASGKATPEEAAKDAVA 365
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 79-320 4.39e-17

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: 83.15  E-value: 4.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  79 YDIMTI-GTYEVPIWAKQGWLLPLDDL----GPEY----DVDDLLPAirsglTIDGKLYAAPFYGESS--MVMY-RKDLF 146
Cdd:cd13580    60 PDIVVVnDPQLSITLVKQGALWDLTDYldkyYPNLkkiiEQEGWDSA-----SVDGKIYGIPRKRPLIgrNGLWiRKDWL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 147 EKAGLTMPDapTWDFIADAARKITDKG------NEIYGICLRGkagWGENMAFlTATANAFGA----RWFDENWK--PQF 214
Cdd:cd13580   135 DKLGLEVPK--TLDELYEVAKAFTEKDpdgngkKDTYGLTDTK---DLIGSGF-TGLFGAFGAppnnWWKDEDGKlvPGS 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 215 DQPEWKNALDFYVKLMNDagppGA--------SSNGFNEnlsLFQTGKCGMWIDATVAASFVTNPKESTVAD----KVGF 282
Cdd:cd13580   209 IQPEMKEALKFLKKLYKE----GLidpefavnDGTKANE---KFISGKAGIFVGNWWDPAWPQASLKKNDPDaewvAVPI 281

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1550319097 283 ALAPDtglGKRGNWLWAWN---LAIPAGSQKAESAQKFIAW 320
Cdd:cd13580   282 PSGPD---GKYGVWAESGVngfFVIPKKSKKPEAILKLLDF 319
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-359 1.54e-15

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 77.26  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097   1 MNLRTFLLGTCSAVALAGL------AQAETLTIAtvNNGDMIRmQKLTDDFTSKNpDIQLEWVTLEENVLRQrvtTDIAT 74
Cdd:COG0687     1 MSRRSLLGLAAAALAAALAggapaaAAEGTLNVY--NWGGYID-PDVLEPFEKET-GIKVVYDTYDSNEEML---AKLRA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  75 KGGQYDIMTIGTYEVPIWAKQGWLLPLD-DLGPEYDvdDLLPAIRSGLTIDGKLYAAPFYGESSMVMYRKDLFEKAgltm 153
Cdd:COG0687    74 GGSGYDVVVPSDYFVARLIKAGLLQPLDkSKLPNLA--NLDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEP---- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 154 PDapTWDFIADAArkitdkgneiygicLRGKAGWGENMA-FLTATANAFGARWFDEnwkpqfDQPEWKNALDFYVKLMND 232
Cdd:COG0687   148 PT--SWADLWDPE--------------YKGKVALLDDPReVLGAALLYLGYDPNST------DPADLDAAFELLIELKPN 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 233 AGppgASSNGFNENLSLFQTGKC--GMWIDATVAASFVTNPKestvadkVGFAlAPdtglgKRGNWLWAWNLAIPAGSQK 310
Cdd:COG0687   206 VR---AFWSDGAEYIQLLASGEVdlAVGWSGDALALRAEGPP-------IAYV-IP-----KEGALLWFDNMAIPKGAPN 269

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1550319097 311 AESAQKFIAWATGKDYLKLVAEKEGWANVPPGTRTSLyeNPEYQKAAPF 359
Cdd:COG0687   270 PDLAYAFINFMLSPEVAAALAEYVGYAPPNKAARELL--PPELAANPAI 316
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 92-232 1.23e-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: 63.14  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  92 WAKQGWLLPLD---DLGP-------EYDVDDLLPAIRSGltiDGKLYAAPFYGESSMV----MYRKDLFEKAGLTMPDap 157
Cdd:cd13583    72 FVASGALLPISdylDYMPnykkyveKWGLGKELATGRQS---DGKYYSLPGLHEDPGVqysfLYRKDIFEKAGIKIPT-- 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 158 TWDFIADAARKITDKGNEIYGICLRGKAGWGENMAFLTATANAFGAR------WFDENWKPQFDQPEWKNALDFYVKLMN 231
Cdd:cd13583   147 TWDEFYAALKKLKEKYPDSYPYSDRWNSNALLLIAAPAFGTTAGWGFsnytydPDTDKFVYGATTDEYKDMLQYFNKLYA 226


                  .
gi 1550319097 232 D 232
Cdd:cd13583   227 E 227
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 39-426 5.09e-10

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: 60.96  E-value: 5.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  39 QKLTDDFTSKNpDIQLEWVTLEENVLRQRVTTDiATKGGQYDIMTIGTYEVPIWAKQGWLLP--LDDLgpeyDVDDLLPA 116
Cdd:cd13658    16 KKIAKQYTKKT-GVKVKLVEVDQLDQLEKLSLD-GPAGKGPDVMVAPHDRIGSAVLQGLLSPikLSKD----KKKGFTDQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 117 IRSGLTIDGKLYAAPFYGESSMVMYRKDLfekagltMPDAP-TWDFIADAARKITDKGNEIYGIClrgkAGWGeNMAFLT 195
Cdd:cd13658    90 ALKALTYDGKLYGLPAAVETLALYYNKDL-------VKNAPkTFDELEALAKDLTKEKGKQYGFL----ADAT-NFYYSY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 196 ATANAFGARWFDENWKPQF------DQPEWKNALDFYVKLMNDAG-PPGASSNGFNenlSLFQTGKCGMWIDATVAAsfv 268
Cdd:cd13658   158 GLLAGNGGYIFKKNGSDLDindiglNSPGAVKAVKFLKKWYTEGYlPKGMTGDVIQ---GLFKEGKAAAVIDGPWAI--- 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 269 tnpkESTVADKVGFALAP----------DTGLGKRGnWLwawnlaIPAGSQKAESAQKFIAWATGKDYLKLVAEKEGwaN 338
Cdd:cd13658   232 ----QEYQEAGVNYGVAPlptlpngkpmAPFLGVKG-WY------LSAYSKHKEWAQKFMEFLTSKENLKKRYDETN--E 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 339 VPPgtRTSLYENPEYQKaapfakmtldsinaaDPKNPAVKPVPYVGVQFVAIPEFQGLGTAVGQVFSAALAGQMSVDQAL 418
Cdd:cd13658   299 IPP--RKDVRSDPEIKN---------------NPLTSAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKTPKQAL 361


                  ....*...
gi 1550319097 419 ASAQQLST 426
Cdd:cd13658   362 NDAVNDIK 369
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 51-229 5.26e-07

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: 51.55  E-value: 5.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  51 DIQLEWVTLEENVLRQRVTTDIAtkGGQY-DIM---TIGTYEVPIWAKQGWLLPLDDL----GPEY-DVDDLLPAIRSGL 121
Cdd:cd13581    31 GIKIEWETVPEDAWAEKKNLMLA--SGDLpDAFlgaGASDADLMTYGKQGLFLPLEDLidkyAPNLkALFDENPDIKAAI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 122 T-IDGKLYAAP-----FYGESSMVMY-RKDLFEKAGLTMPDapTWDFIADAARKI-------TDKGNEIYGICLRGKAGW 187
Cdd:cd13581   109 TaPDGHIYALPsvnecYHCSYGQRMWiNKKWLDKLGLEMPT--TTDELYEVLKAFkeqdpngNGKADEIPLSFSGLNGGT 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1550319097 188 GeNMAFLtatANAFGARWFDENW----------KPQFDQPEWKNALDFYVKL 229
Cdd:cd13581   187 D-DPAFL---LNSFGINDGGYGGygfvvkdgkvIYTATDPEYKEALAYLNKL 234
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 70-345 1.29e-06

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


Pssm-ID: 270306 [Multi-domain]  Cd Length: 279  Bit Score: 49.60  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  70 TDIATKGGQYDIMTIGTYEVPIWAKQGWLLPLD-DLGPEYDvdDLLPAIR--SGLTIDGKLYAAPFYGESSMVMYRKDLF 146
Cdd:cd13588    40 AKLRSGGGDYDVVTPSGDALLRLIAAGLVQPIDtSKIPNYA--NIDPRLRnlPWLTVDGKVYGVPYDWGANGLAYNTKKV 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 147 ekagltmPDAPTWDFIADAARKitdkgneiygicLRGK-AGW-GENMAFLTAtANAFGARWFDENWKPQFDQpewknALD 224
Cdd:cd13588   118 -------KTPPTSWLALLWDPK------------YKGRvAARdDPIDAIADA-ALYLGQDPPFNLTDEQLDA-----VKA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 225 FYVKLMndaGPPGASSNGFNENLSLFQTGKcgmwIDATVAASFVTNPKEStvADKVGFALAPdtglgKRGNWLWAWNLAI 304
Cdd:cd13588   173 KLREQR---PLVRKYWSDGAELVQLFANGE----VVAATAWSGQVNALQK--AGKPVAYVIP-----KEGATGWVDTWMI 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1550319097 305 PAGSQKAESAQKFIAWATGKDYLKLVAEKEGWANVPPGTRT 345
Cdd:cd13588   239 LKDAKNPDCAYKWLNYMLSPKVQAAVAEWTGYAPSNPEACA 279
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 78-333 2.45e-06

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: 48.76  E-value: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  78 QYDIMTIGTYEVPIWAKQGWLLPLD-DLGPEYDVDDLLPAIRSGltidgklYAAPFYGESSMVMYRKDLFekagltmPDA 156
Cdd:cd13589    53 QWDVVDLDDGDAARAIAEGLLEPLDySKIPNAAKDKAPAALKTG-------YGVGYTLYSTGIAYNTDKF-------KEP 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 157 PTWDFIADAArkitDKGNeIYGIclrgKAGWGENMAFLTATANAFGARWFDENWKPQFDQ-PEWKNALDFYVKLMNDAgp 235
Cdd:cd13589   119 PTSWWLADFW----DVGK-FPGP----RILNTSGLALLEAALLADGVDPYPLDVDRAFAKlKELKPNVVTWWTSGAQL-- 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 236 pgassngfnenLSLFQTGKCGM----------WIDATVAASFVTnPKESTVADkvgfalaPDTglgkrgnwlwawnLAIP 305
Cdd:cd13589   188 -----------AQLLQSGEVDMapawngraqaLIDAGAPVAFVW-PKEGAILG-------PDT-------------LAIV 235

                         250       260
                  ....*....|....*....|....*...
gi 1550319097 306 AGSQKAESAQKFIAWATGKDYLKLVAEK 333
Cdd:cd13589   236 KGAPNKELAMKFINFALSPEVQAALAEA 263
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 49-326 3.55e-05

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: 45.91  E-value: 3.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  49 NPDIQLEWVTLEENVlrQRVTTDIATkgGQY-DIMTIGTYEVPIWAKQ--GWLLPLD---DLGPE--------YDVDDLL 114
Cdd:cd13521    31 NVKLEIVAVTAATSQ--QKLNLMLAS--GDLpDIVGADYLKDKFIAYGmeGAFLPLSkyiDQYPNlkaffkqhPDVLRAS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 115 PairsglTIDGKLYAAPFYGESSMVMY----RKDLFEKAGLtmPDAPTWDFIADAARKITDKGNEIYG-------ICLRG 183
Cdd:cd13521   107 T------ASDGKIYLIPYEPPKDVPNQgyfiRKDWLDKLNL--KTPKTLDELYNVLKAFKEKDPNGNGkadeipfIDRDP 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097 184 KAGWGENMAFlTATANAFGARWFDenW-------KPQFDQPEWKNALDFYVKLMNDA-GPPGASSNGFNENLSLFQTGKC 255
Cdd:cd13521   179 LYGAFRLINS-WGARSAGGSTDSD--WyedngkfKHPFASEEYKDGMKYMNKLYTEGlIDKESFTQKDDQAEQKFSNGKL 255

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1550319097 256 GMWIDATVAAS-FVTNPKESTVADKVGFALAPDTGLGKRGNWLWA-----WNLAIPAGSQKAESAQKFIAWATGKDY 326
Cdd:cd13521   256 GGFTHNWFASDnLFTAQLGKEKPMYILLPIAPAGNVKGRREEDSPgytgpDGVAISKKAKNPVAALKFFDWLASEEG 332
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 39-182 3.67e-04

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: 42.22  E-value: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  39 QKLTDDFTSKNpDIQLEWVTLEEN-VLRQRVTtdiATKGGQYDIMTIGTYEVPIWAKQGWLLPLD-DLGPEYdvDDLLPA 116
Cdd:cd13590    13 PEVLKAFEKET-GVKVNYDTYDSNeEMLAKLR---AGGGSGYDLVVPSDYMVERLIKQGLLEPLDhSKLPNL--KNLDPQ 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550319097 117 IRSGLTIDGKLYAAPFYGESSMVMYRKDLFekagltmPDAPT-WDFIADAAR---KIT--DKGNEIYGICLR 182
Cdd:cd13590    87 FLNPPYDPGNRYSVPYQWGTTGIAYNKDKV-------KEPPTsWDLDLWDPAlkgRIAmlDDAREVLGAALL 151
PBP2_Thiaminase_I cd13524
Thiaminase-I has high structural homology to the type 2 periplasmic binding proteins of active ...
 42-156 7.15e-03

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: 38.29  E-value: 7.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550319097  42 TDDFTSKNPDIQLEWVTLEENVL--RQRVTTDIATKGGQYDIMTIGTYEVPIWAKQGWLLPLDDLGPEydvdDLLPAIRS 119
Cdd:cd13524    22 TDQWQRQEPGVDLDFVDWAKLDDsySADPPDLNQLGAGALDVVEIDTIFLGHLVDAGYLLPFGIDQAR----DYLPFALQ 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1550319097 120 GLTIDGKLYAAPFYGESSMVMYRKD----------LFEKAGLTMPDA 156
Cdd:cd13524    98 AVSRNGEVYGVPQLLCTNLLFYRSPdlgqatdiasLYKKIGTSHPSG 144
 
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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