NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|445957106|ref|WP_000034961|]
View 

MULTISPECIES: maltodextrin ABC transporter substrate-binding protein [Staphylococcus]

Protein Classification

maltodextrin ABC transporter substrate-binding protein( domain architecture ID 10194644)

maltodextrin ABC transporter substrate-binding protein which is part of the ABC transporter complex involved in maltodextrin import/uptake

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 45-410 0e+00

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: 580.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  45 QLTMWVDGDKQMAFYKKITDQYTKKTGIKVKLVNIGQNDQLENISLDAPAGKGPDIFFLAHDNTGSAYLQGLAAEIKLSK 124
Cdd:cd13658    1 QLTVWVDEDKKMAFIKKIAKQYTKKTGVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 125 DELKGFNKQALKAMNYDNKQLALPAIVETTALFYNKKLVKNAPQTLEEVEANAAKLTDSKKKQYGMLFDAKNFYFNYPFL 204
Cdd:cd13658   81 DKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKDLTKEKGKQYGFLADATNFYYSYGLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 205 FGNDDYIFKKNGSEYDIHQLGLNSKHVVKNAERLQKWYDKGYLPKAATHDVMIGLFKEGKVGQFVTGPWNINEYQEtFGK 284
Cdd:cd13658  161 AGNGGYIFKKNGSDLDINDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAVIDGPWAIQEYQE-AGV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 285 DLGVTTLPT-DGGKPMKPFLGVRGWYLSEYSKHKYWAKDLMLYITSKDTLQKYTDEMSEITGRVDVKS-----SNPNLKV 358
Cdd:cd13658  240 NYGVAPLPTlPNGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTSKENLKKRYDETNEIPPRKDVRSdpeikNNPLTSA 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 445957106 359 FEKQARHAEPMPNIPEMRQVWEPMGNASIFISNG-KNPKQALDEATNDITQNI 410
Cdd:cd13658  320 FAKQASRAVPMPNIPEMGAVWEPANNALFFILSGkKTPKQALNDAVNDIKENI 372
 
Name Accession Description Interval E-value
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 45-410 0e+00

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: 580.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  45 QLTMWVDGDKQMAFYKKITDQYTKKTGIKVKLVNIGQNDQLENISLDAPAGKGPDIFFLAHDNTGSAYLQGLAAEIKLSK 124
Cdd:cd13658    1 QLTVWVDEDKKMAFIKKIAKQYTKKTGVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 125 DELKGFNKQALKAMNYDNKQLALPAIVETTALFYNKKLVKNAPQTLEEVEANAAKLTDSKKKQYGMLFDAKNFYFNYPFL 204
Cdd:cd13658   81 DKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKDLTKEKGKQYGFLADATNFYYSYGLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 205 FGNDDYIFKKNGSEYDIHQLGLNSKHVVKNAERLQKWYDKGYLPKAATHDVMIGLFKEGKVGQFVTGPWNINEYQEtFGK 284
Cdd:cd13658  161 AGNGGYIFKKNGSDLDINDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAVIDGPWAIQEYQE-AGV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 285 DLGVTTLPT-DGGKPMKPFLGVRGWYLSEYSKHKYWAKDLMLYITSKDTLQKYTDEMSEITGRVDVKS-----SNPNLKV 358
Cdd:cd13658  240 NYGVAPLPTlPNGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTSKENLKKRYDETNEIPPRKDVRSdpeikNNPLTSA 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 445957106 359 FEKQARHAEPMPNIPEMRQVWEPMGNASIFISNG-KNPKQALDEATNDITQNI 410
Cdd:cd13658  320 FAKQASRAVPMPNIPEMGAVWEPANNALFFILSGkKTPKQALNDAVNDIKENI 372
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
3-411 1.25e-141

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 410.11  E-value: 1.25e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106   3 KILKCITLAVVMLLIVTACGPNRSKEDidkalnKDNSKDKPNQLTMWVDGDKQmAFYKKITDQYTKKTGIKVKLVNIGQN 82
Cdd:COG2182    4 RLLAALALALALALALAACGSGSSSSG------SSSAAGAGGTLTVWVDDDEA-EALEEAAAAFEEEPGIKVKVVEVPWD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  83 DQLENISLDAPAGKGPDIFFLAHDNTGSAYLQGLAAEIKLSKDELKGFNKQALKAMNYDNKQLALPAIVETTALFYNKKL 162
Cdd:COG2182   77 DLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 163 VK-NAPQTLEEVEANAAKLTDskKKQYGMLFDAKNFYFNYPFLFGNDDYIFKKNGSeyDIHQLGLNSKHVVKNAERLQKW 241
Cdd:COG2182  157 VKaEPPKTWDELIAAAKKLTA--AGKYGLAYDAGDAYYFYPFLAAFGGYLFGKDGD--DPKDVGLNSPGAVAALEYLKDL 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 242 YDKGYLPKAATHDVMIGLFKEGKVGQFVTGPWNINEYQETFGKDLGVTTLPT-DGGKPMKPFLGVRGWYLSEYSKHKYWA 320
Cdd:COG2182  233 IKDGVLPADADYDAADALFAEGKAAMIINGPWAAADLKKALGIDYGVAPLPTlAGGKPAKPFVGVKGFGVSAYSKNKEAA 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 321 KDLMLYITSKDTLQKYTDEMSEITGRVDV-----KSSNPNLKVFEKQARHAEPMPNIPEMRQVWEPMGNASIFISNGK-N 394
Cdd:COG2182  313 QEFAEYLTSPEAQKALFEATGRIPANKAAaedaeVKADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKaD 392

                        410
                 ....*....|....*..
gi 445957106 395 PKQALDEATNDITQNIK 411
Cdd:COG2182  393 PAEALDAAQKQIEAAIA 409
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
45-408 2.43e-65

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 214.11  E-value: 2.43e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  45 QLTMWVDGDKQMAFYKKITDQYTKKTGIKVKLVNigqNDQLEN-ISLDAPAGKGPDIFFLAHDNTGSAYLQGLAAEIKLS 123
Cdd:PRK09474  32 KLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEH---PDKLEEkFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEVTPS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 124 KDELKGFNKQALKAMNYDNKQLALPAIVETTALFYNKKLVKNAPQTLEEVEANAAKLtdSKKKQYGMLFDAKNFYFNYPF 203
Cdd:PRK09474 109 KAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALDKEL--KAKGKSAIMWNLQEPYFTWPL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 204 LFGNDDYIFKKNGSEYDIHQLGLNSKHVVKNAERLQKWYDKGYLPKAATHDVMIGLFKEGKVGQFVTGPW---NIneyqE 280
Cdd:PRK09474 187 IAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWawsNI----D 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 281 TFGKDLGVTTLPTDGGKPMKPFLGVRGWYLSEYSKHKYWAKDLML-YITSKDTLQKYTDEMSeiTGRVDVKS------SN 353
Cdd:PRK09474 263 KSGINYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLETVNKDKP--LGAVALKSfqeelaKD 340

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 445957106 354 PNLKVFEKQARHAEPMPNIPEMRQVWEPMGNASIFISNGKNP-KQALDEATNDITQ 408
Cdd:PRK09474 341 PRIAATMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTvDAALDDAAKRITK 396
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 61-349 6.17e-29

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 114.43  E-value: 6.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106   61 KITDQYTKKTGIKVKLVNIGQNDQLENISLDAPAGKGPDI--FFLAHDNTGSAYLQGLAAEIKLSkDELKGFNkQALKAM 138
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQASNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLADLSDV-DNLDDLP-DALDAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  139 NYDNKQLALP-AIVETTALFYNKKLVKNA---PQTLEEVEANAAKLtdskKKQYGMLFDAKNFYfnYPFLFGNDDYIFKK 214
Cdd:pfam13416  79 GYDGKLYGVPyAASTPTVLYYNKDLLKKAgedPKTWDELLAAAAKL----KGKTGLTDPATGWL--LWALLADGVDLTDD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  215 NGSEYDIHQLglnskhvvknAERLQKWYDKGYLPkaATHDVMIGLFKEGKVGQFVTGPWNINEYQEtFGKDLGVtTLPTD 294
Cdd:pfam13416 153 GKGVEALDEA----------LAYLKKLKDNGKVY--NTGADAVQLFANGEVAMTVNGTWAAAAAKK-AGKKLGA-VVPKD 218

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 445957106  295 GgkpmkPFLGVRGWYLSEYSKHK-YWAKDLMLYITSKDTLQKYTDEMSEITGRVDV 349
Cdd:pfam13416 219 G-----SFLGGKGLVVPAGAKDPrLAALDFIKFLTSPENQAALAEDTGYIPANKSA 269
 
Name Accession Description Interval E-value
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 45-410 0e+00

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: 580.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  45 QLTMWVDGDKQMAFYKKITDQYTKKTGIKVKLVNIGQNDQLENISLDAPAGKGPDIFFLAHDNTGSAYLQGLAAEIKLSK 124
Cdd:cd13658    1 QLTVWVDEDKKMAFIKKIAKQYTKKTGVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 125 DELKGFNKQALKAMNYDNKQLALPAIVETTALFYNKKLVKNAPQTLEEVEANAAKLTDSKKKQYGMLFDAKNFYFNYPFL 204
Cdd:cd13658   81 DKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKDLTKEKGKQYGFLADATNFYYSYGLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 205 FGNDDYIFKKNGSEYDIHQLGLNSKHVVKNAERLQKWYDKGYLPKAATHDVMIGLFKEGKVGQFVTGPWNINEYQEtFGK 284
Cdd:cd13658  161 AGNGGYIFKKNGSDLDINDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAVIDGPWAIQEYQE-AGV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 285 DLGVTTLPT-DGGKPMKPFLGVRGWYLSEYSKHKYWAKDLMLYITSKDTLQKYTDEMSEITGRVDVKS-----SNPNLKV 358
Cdd:cd13658  240 NYGVAPLPTlPNGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTSKENLKKRYDETNEIPPRKDVRSdpeikNNPLTSA 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 445957106 359 FEKQARHAEPMPNIPEMRQVWEPMGNASIFISNG-KNPKQALDEATNDITQNI 410
Cdd:cd13658  320 FAKQASRAVPMPNIPEMGAVWEPANNALFFILSGkKTPKQALNDAVNDIKENI 372
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
3-411 1.25e-141

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 410.11  E-value: 1.25e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106   3 KILKCITLAVVMLLIVTACGPNRSKEDidkalnKDNSKDKPNQLTMWVDGDKQmAFYKKITDQYTKKTGIKVKLVNIGQN 82
Cdd:COG2182    4 RLLAALALALALALALAACGSGSSSSG------SSSAAGAGGTLTVWVDDDEA-EALEEAAAAFEEEPGIKVKVVEVPWD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  83 DQLENISLDAPAGKGPDIFFLAHDNTGSAYLQGLAAEIKLSKDELKGFNKQALKAMNYDNKQLALPAIVETTALFYNKKL 162
Cdd:COG2182   77 DLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 163 VK-NAPQTLEEVEANAAKLTDskKKQYGMLFDAKNFYFNYPFLFGNDDYIFKKNGSeyDIHQLGLNSKHVVKNAERLQKW 241
Cdd:COG2182  157 VKaEPPKTWDELIAAAKKLTA--AGKYGLAYDAGDAYYFYPFLAAFGGYLFGKDGD--DPKDVGLNSPGAVAALEYLKDL 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 242 YDKGYLPKAATHDVMIGLFKEGKVGQFVTGPWNINEYQETFGKDLGVTTLPT-DGGKPMKPFLGVRGWYLSEYSKHKYWA 320
Cdd:COG2182  233 IKDGVLPADADYDAADALFAEGKAAMIINGPWAAADLKKALGIDYGVAPLPTlAGGKPAKPFVGVKGFGVSAYSKNKEAA 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 321 KDLMLYITSKDTLQKYTDEMSEITGRVDV-----KSSNPNLKVFEKQARHAEPMPNIPEMRQVWEPMGNASIFISNGK-N 394
Cdd:COG2182  313 QEFAEYLTSPEAQKALFEATGRIPANKAAaedaeVKADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKaD 392

                        410
                 ....*....|....*..
gi 445957106 395 PKQALDEATNDITQNIK 411
Cdd:COG2182  393 PAEALDAAQKQIEAAIA 409
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 46-406 5.16e-115

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: 340.81  E-value: 5.16e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  46 LTMWVDGDKQMAFYKKITDQYTKKTGIKVKLVNIGQNDQLENISLDAPAGKGPDIFFLAHDNTGSAYLQGLAAEIKLSKD 125
Cdd:cd13586    2 ITVWTDEDGELEYLKELAEEFEKKYGIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 126 ELKGFNKQALKAMNYDNKQLALPAIVETTALFYNKKLVKNAPQTLEEVEANAAKLTDSKKKQYGMLFDAKNFYFNYPFLF 205
Cdd:cd13586   82 VKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPEPPKTWEELIALAKKFNDKAGGKYGFAYDQTNPYFSYPFLA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 206 GNDDYIFKKNGSEYDihQLGLNSKHVVKNAERLQKWYDK-GYLPKAATHDVMIGLFKEGKVGQFVTGPWNINEYQETfGK 284
Cdd:cd13586  162 AFGGYVFGENGGDPT--DIGLNNEGAVKGLKFIKDLKKKyKVLPPDLDYDIADALFKEGKAAMIINGPWDLADYKDA-GI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 285 DLGVTTLPT-DGGKPMKPFLGVRGWYLSEYSKHKYWAKDLMLYITSKDTLQKYTDEMSEITGRVDVKS-----SNPNLKV 358
Cdd:cd13586  239 NFGVAPLPTlPGGKQAAPFVGVQGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALKDALNdaavkNDPLVKA 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 445957106 359 FEKQARHAEPMPNIPEMRQVWEPMGNASIFI-SNGKNPKQALDEATNDI 406
Cdd:cd13586  319 FAEQAQYGVPMPNIPEMAAVWDAMGNALNLVaSGKATPEEAAKDAVAAI 367
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 46-406 1.71e-78

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: 247.29  E-value: 1.71e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  46 LTMW--VDGDKQMAFyKKITDQYTKKTGIKVKLVNIGQNDQLEN-ISLDAPAGKGPDIFFLAHDNTGSAYLQGLAAEI-- 120
Cdd:cd13657    2 ITIWhaLTGAEEDAL-QQIIDEFEAKYPVPNVKVPFEKKPDLQNkLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPIsd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 121 KLSKDELKGFNKQALKAMNYDNKQLALPAIVETTALFYNKKLVKNAPQTLEEVEANAAKLTDSKKKQYGMLFDAKNFYFN 200
Cdd:cd13657   81 YLSEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQPPETTDELLAIMKDHTDPAAGSYGLAYQVSDAYFV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 201 YPFLFGNDDYIFKKNGSeydihQLGLNSKHVVKNAERLQKWYdKGYLPKAATHDVMIGLFKEGKVGQFVTGPWNINEYQE 280
Cdd:cd13657  161 SAWIFGFGGYYFDDETD-----KPGLDTPETIKGIQFLKDFS-WPYMPSDPSYNTQTSLFNEGKAAMIINGPWFIGGIKA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 281 TfGKDLGVTTLPT-DGGKPMKPFLGVRGWYLSEY--SKHKYWAKDLMLYITSKDTLQKYTDEMSEITGRVDV-----KSS 352
Cdd:cd13657  235 A-GIDLGVAPLPTvDGTNPPRPYSGVEGIYVTKYaeRKNKEAALDFAKFFTTAEASKILADENGYVPAATNAyddaeVAA 313

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 445957106 353 NPNLKVFEKQARHAEPMPNIPEMRQVWEPMGNASIFISNGK-NPKQALDEATNDI 406
Cdd:cd13657  314 DPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGqDPQEALAAAQQEI 368
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
45-408 2.43e-65

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 214.11  E-value: 2.43e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  45 QLTMWVDGDKQMAFYKKITDQYTKKTGIKVKLVNigqNDQLEN-ISLDAPAGKGPDIFFLAHDNTGSAYLQGLAAEIKLS 123
Cdd:PRK09474  32 KLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEH---PDKLEEkFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEVTPS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 124 KDELKGFNKQALKAMNYDNKQLALPAIVETTALFYNKKLVKNAPQTLEEVEANAAKLtdSKKKQYGMLFDAKNFYFNYPF 203
Cdd:PRK09474 109 KAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALDKEL--KAKGKSAIMWNLQEPYFTWPL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 204 LFGNDDYIFKKNGSEYDIHQLGLNSKHVVKNAERLQKWYDKGYLPKAATHDVMIGLFKEGKVGQFVTGPW---NIneyqE 280
Cdd:PRK09474 187 IAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWawsNI----D 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 281 TFGKDLGVTTLPTDGGKPMKPFLGVRGWYLSEYSKHKYWAKDLML-YITSKDTLQKYTDEMSeiTGRVDVKS------SN 353
Cdd:PRK09474 263 KSGINYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLETVNKDKP--LGAVALKSfqeelaKD 340

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 445957106 354 PNLKVFEKQARHAEPMPNIPEMRQVWEPMGNASIFISNGKNP-KQALDEATNDITQ 408
Cdd:PRK09474 341 PRIAATMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTvDAALDDAAKRITK 396
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 46-402 6.82e-63

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: 206.88  E-value: 6.82e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  46 LTMWVDGDK-QMAFYKKITDQYTKKT-GIKVKLVNIGQNDQLENISLDAPAGKGPDIFFLAHDNTGSAYLQGLAAEIK-- 121
Cdd:cd13522    2 ITVWHQYDTgENQAVNELIAKFEKAYpGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDey 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 122 LSKDELKGFNkqALKAMNYDNKQLALPAIVETTALFYNKKLV-KNAPQTLEEVEANAakLTDSKKKQYGMLFDAKNFYFN 200
Cdd:cd13522   82 VSKSGKYAPN--TIAAMKLNGKLYGVPVSVGAHLMYYNKKLVpKNPPKTWQELIALA--QGLKAKNVWGLVYNQNEPYFF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 201 YPFLFGNDDYIFKKNGSEYDIhqlGLNSKHVVKNAERLQKWYDK-GYLPKAATHDVMIGLFKEGKVGQFVTGPWNINEYQ 279
Cdd:cd13522  158 AAWIGGFGGQVFKANNGKNNP---TLDTPGAVEALQFLVDLKSKyKIMPPETDYSIADALFKAGKAAMIINGPWDLGDYR 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 280 ETFGKDLGVTTLPT-DGGKPMKPFLGVRGWYLSEYSKHKYWAKDLMLYITSKDTLQKYTDEMSEITGRVDV-----KSSN 353
Cdd:cd13522  235 QALKINLGVAPLPTfSGTKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDIPANLQAyespaVQNK 314

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 445957106 354 PNLKVFEKQARHAEPMPNIPEMRQVWEPMGNA-SIFISNGKNPKQALDEA 402
Cdd:cd13522  315 PAQKASAEQAAYGVPMPNIPEMRAVWDAFRIAvNSVLAGKVTPEAAAKDA 364
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-350 1.45e-61

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 203.35  E-value: 1.45e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106   1 MSKILkcITLAVVMLLIVTACGPNRSKEDidkalnkdnSKDKPNQLTMWVDGDKQMAFYKKITDQYTKKT-GIKVKLVNI 79
Cdd:COG1653    1 MRRLA--LALAAALALALAACGGGGSGAA---------AAAGKVTLTVWHTGGGEAAALEALIKEFEAEHpGIKVEVESV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  80 GQNDQLENISLDAPAGKGPDIFFLAHDNTGSAYLQGLAAE----IKLSKDELKGFNKQALKAMNYDNKQLALPAIVETTA 155
Cdd:COG1653   70 PYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPlddlLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 156 LFYNKKLVKNA----PQTLEEVEANAAKLTDsKKKQYGMLFDAKNFYFNYPFLFGNDDYIFKKNGseydihQLGLNSKHV 231
Cdd:COG1653  150 LYYNKDLFEKAgldpPKTWDELLAAAKKLKA-KDGVYGFALGGKDGAAWLDLLLSAGGDLYDEDG------KPAFDSPEA 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 232 VKNAERLQKWYDKGYLPKAA---THDVMIGLFKEGKVGQFVTGPWNINEYQETFGK-DLGVTTLPT-DGGKPMKPFLGVR 306
Cdd:COG1653  223 VEALEFLKDLVKDGYVPPGAlgtDWDDARAAFASGKAAMMINGSWALGALKDAAPDfDVGVAPLPGgPGGKKPASVLGGS 302

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 445957106 307 GWYLSEYSKHKYWAKDLMLYITSKDTlQKYTDEMSE-ITGRVDVK 350
Cdd:COG1653  303 GLAIPKGSKNPEAAWKFLKFLTSPEA-QAKWDALQAvLLGQKTPE 346
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 45-406 1.48e-57

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


Pssm-ID: 270374 [Multi-domain]  Cd Length: 364  Bit Score: 192.81  E-value: 1.48e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  45 QLTMWVDGDKQMAFYKKITDQYTKKTGIKVKLVNigQNDQLENISLDAPAGKGPDIFFLAHDNTGSAYLQGLAAEIKLSK 124
Cdd:cd13656    2 KLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEH--PDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 125 DELKGFNKQALKAMNYDNKQLALPAIVETTALFYNKKLVKNAPQTLEEVEANAAKLtdSKKKQYGMLFDAKNFYFNYPFL 204
Cdd:cd13656   80 AFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKEL--KAKGKSALMFNLQEPYFTWPLI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 205 FGNDDYIFKKNGSEYDIHQLGLNSKHVVKNAERLQKWYDKGYLPKAATHDVMIGLFKEGKVGQFVTGPW---NIneyqET 281
Cdd:cd13656  158 AADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWawsNI----DT 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 282 FGKDLGVTTLPTDGGKPMKPFLGVRGWYLSEYSKHKYWAKD-LMLYITSKDTLQKYTDEMSeiTGRVDVKS------SNP 354
Cdd:cd13656  234 SKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEfLENYLLTDEGLEAVNKDKP--LGAVALKSyeeelaKDP 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 445957106 355 NLKVFEKQARHAEPMPNIPEMRQVWEPMGNASIFISNGKNP-KQALDEATNDI 406
Cdd:cd13656  312 RIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTvDEALKDAQTRI 364
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 46-406 1.05e-53

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: 183.38  E-value: 1.05e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  46 LTMWV-DGDKQMAFYKKITDQYTKK-TGIKVKLVNIGQNDQLENISLDAPAGKGPDIFFLAHDNTGSAYLQGLAAEI--K 121
Cdd:cd13585    2 LTFWDwGQPAETAALKKLIDAFEKEnPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLddY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 122 LSKDELKG-FNKQALKAMNYDNKQLALPAIVETTALFYNKKLVKNA------PQTLEEVEANAAKLTDSKKKQYGMLFDA 194
Cdd:cd13585   82 IEKDGLDDdFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAgpgpkpPWTWDELLEAAKKLTDKKGGQYGFALRG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 195 K--NFYFNYPFLFGNDDYIFKKNGSEYDIhqlglNSKHVVKNAERLQKWYDKGYLPKAAT--HDVMIGLFKEGKVGQFVT 270
Cdd:cd13585  162 GsgGQTQWYPFLWSNGGDLLDEDDGKATL-----NSPEAVEALQFYVDLYKDGVAPSSATtgGDEAVDLFASGKVAMMID 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 271 GPWNINEY-QETFGKDLGVTTLPTDGGKPMKPFLGVRGWYLSEYSKHKYWAKDLMLYITSKDTLQKYTDEMSEITGRVDV 349
Cdd:cd13585  237 GPWALGTLkDSKVKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAA 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445957106 350 KSSNPN----------LKVFEKQARHAEPMPNIPEMRQVWEPMGNASIFISNGKNPKQALDEATNDI 406
Cdd:cd13585  317 ASAAAPdakpalalaaAADALAAAVPPPVPPPWPEVYPILSEALQEALLGALGKSPEEALKEAAKEI 383
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 46-411 1.33e-46

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: 164.79  E-value: 1.33e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  46 LTMWVDGDKQMA-FYKKITDQYTKKT-GIKVKLVNIGQNDQLENISLDAPAGKGPDIffLAHDNTGSAY---------LQ 114
Cdd:cd14747    2 LTVWAMGNSAEAeLLKELADEFEKENpGIEVKVQVLPWGDAHTKITTAAASGDGPDV--VQLGNTWVAEfaamgaledLT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 115 GLAAEIKLSKDELKGFNKQALkamnYDNKQLALPAIVETTALFYNKKLVK-----NAPQTLEEVEANAAKLTDSKKKQYG 189
Cdd:cd14747   80 PYLEDLGGDKDLFPGLVDTGT----VDGKYYGVPWYADTRALFYRTDLLKkaggdEAPKTWDELEAAAKKIKADGPDVSG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 190 MLFDAKN--FYFNYPFLFGNDDYIFKKNGSEYDIhqlglNSKHVVKNAERLQKWYDKGYLPKAATHDV--MIGLFKEGKV 265
Cdd:cd14747  156 FAIPGKNdvWHNALPFVWGAGGDLATKDKWKATL-----DSPEAVAGLEFYTSLYQKGLSPKSTLENSadVEQAFANGKV 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 266 GQFVTGPWNINEYQETFGKD---LGVTTLPTDGGKPMKPFLGVRGWYLSEYSKHKYWAKDLMLYITSKDTLQKYTDEMSE 342
Cdd:cd14747  231 AMIISGPWEIGAIREAGPDLagkWGVAPLPGGPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGM 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 343 ITGRVDVKSS-----NPNLKVFEKQARHAEPMPNIPEmrqvWEPMGNAS------IFISNGKNPKQALDEATNDITQNIK 411
Cdd:cd14747  311 LPANTSAWDDpslanDPLLAVFAEQLKTGKATPATPE----WGEIEAELvlvleeVWIGVGADVEDALDKAAAEINEILN 386
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 45-406 1.03e-45

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: 162.08  E-value: 1.03e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  45 QLTMWVD-GDKQMAFYKKITDQYTKK-TGIKVKLVNIGQNDQLEN-ISLDAPAGKGPDIFFLAHDNTGSAYLQGLAAE-- 119
Cdd:cd14748    1 EITFWHGmSGPDGKALEELVDEFNKShPDIKVKAVYQGSYDDTLTkLLAALAAGTAPDVAQVDASWVAQLADSGALEPld 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 120 --IKLSKDELKGFNKQALKAMNYDNKQLALPAIVETTALFYNKKLVKNA-------PQTLEEVEANAAKL--TDSKKKQY 188
Cdd:cd14748   81 dyIDKDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAgldpekpPKTWDELEEAAKKLkdKGGKTGRY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 189 GMLFDAKNFYFNY-PFLFGNDDYIFKKNGSEydihqLGLNSKHVVKNAERLQKWYDKGYLPKAATHDVMIGLFKEGKVGQ 267
Cdd:cd14748  161 GFALPPGDGGWTFqALLWQNGGDLLDEDGGK-----VTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFISGKVAM 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 268 FVTGPWNINEYQETFGK-DLGVTTLPTDGGKPMKPFLGVRGWYLSE-YSKHKYWAKDLMLYITSKDTLQKYtdemSEITG 345
Cdd:cd14748  236 TINGTWSLAGIRDKGAGfEYGVAPLPAGKGKKGATPAGGASLVIPKgSSKKKEAAWEFIKFLTSPENQAKW----AKATG 311

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445957106 346 ----RVDVKSS-------NPNLKVFEKQARHAEP-MPNIPEMRQVWEPMGNASIFI-SNGKNPKQALDEATNDI 406
Cdd:cd14748  312 ylpvRKSAAEDpeeflaeNPNYKVAVDQLDYAKPwGPPVPNGAEIRDELNEALEAAlLGKKTPEEALKEAQEKI 385
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 45-403 3.78e-34

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: 130.54  E-value: 3.78e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  45 QLTMWVDGDKQmAFYKKITDQYTKKTG---IKVKLVNIGQNDQLENISLDApaGKGPDIFFLAHDNTGSAYLQGLAAEIK 121
Cdd:cd13655    1 TLTVWGPQEDQ-EWLKEMVDAFKEKHPewkITITIGVVGEADAKDEVLKDP--SAAADVFAFANDQLGELVDAGAIYPLT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 122 LSKDE-LKGFNKQAL-KAMNYDNKQLALPAIVETTALFYNK-KLVKNAPQTLEEVeanAAKLTDSKKKQYgmlFDAKNFY 198
Cdd:cd13655   78 GSAVDkIKNTNSEATvDAVTYNGKLYGYPFTANTWFMYYDKsKLTEDDVKSLDTM---LAKAPDAKGKVS---FDLSNSW 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 199 FNYPFLFGNDDYIFKKNGSeyDIHQLGLNSKHVVKNAERLQKWYDKgylPKAATHD--VMIGLFKEGKVGQFVTGPWNIN 276
Cdd:cd13655  152 YLYAFFFGAGCKLFGNNGG--DTAGCDFNNEKGVAVTNYLVDLVAN---PKFVNDAdgDAISGLKDGTLGAGVSGPWDAA 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 277 EYQETFGKDLGVTTLPT---DGG-KPMKPFLGVRGWYLSEYSKHKYWAKDLMLYITSKDTLQKYTDEMSEITGRVD---- 348
Cdd:cd13655  227 NLKKALGDNYAVAKLPTytlGGKdVQMKSFAGYKAIGVNSNTKNPEAAMALADYLTNEESQLTRFEKRGIGPTNKEaaes 306

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 445957106 349 --VKSSNPNLKVFEKQARHAEPMPNIPEMRQVWEPMGNASIFISNGKNPKQALDEAT 403
Cdd:cd13655  307 daVKADPAAKALIAQSNEASVVQPKLPKMSNFWTPAEAFGKGIVDGTVTAENAQQKL 363
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 57-402 2.93e-31

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: 122.87  E-value: 2.93e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  57 AFYKKITDQYTKKT-GIKVKLVNIGQNDQLENISLDAPAGKGPDIFFLahDNTGSAYLQGLAAEIKLSK----DELKGFN 131
Cdd:cd14751   14 VLYEKLIPAFEKEYpKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRA--DIAWVPEFAKLGYLQPLDGtpafDDIVDYL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 132 KQALKAMNYDNKQLALPAIVETTALFYNKKLVKNA----PQTLEEVEAnAAKLTDSKKKQYGMLFDAKNFYFNYPFLFG- 206
Cdd:cd14751   92 PGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAgtevPKTMDELVA-AAKAIKKKKGRYGLYISGDGPYWLLPFLWSf 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 207 NDDYIFKKNGSEYdihqlgLNSKHVVKNAERLQKWYDKGYLPKAAT--HDVMIGLFKEGKVGQFVTGPWNINEYQETFGK 284
Cdd:cd14751  171 GGDLTDEKKATGY------LNSPESVRALETIVDLYDEGAITPCASggYPNMQDGFKSGRYAMIVNGPWAYADILGGKEF 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 285 D----LGVTTLPTDGGKPMKPflgVRGWYLS--EYSKHKYWAKDLMLYITSKDTLQKYTDEMSEITGRVDVKSS-----N 353
Cdd:cd14751  245 KdpdnLGIAPVPAGPGGSGSP---VGGEDLVifKGSKNKDAAWKFVKFMSSAEAQALTAAKLGLLPTRTSAYESpevanN 321

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 445957106 354 PNLKVFEKQARHAEPMPNIPEMRQVWEPMGNASIFISNGK-NPKQALDEA 402
Cdd:cd14751  322 PMVAAFKPALETAVPRPPIPEWGELFEPLTLAFAKVLRGEkSPREALDEA 371
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 46-407 1.51e-30

The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; possesses type 2 periplasmic binding fold; This group represents the periplasmic component of an ABC transport system XBP1 that shows preference for xylo-oligosaccharides in the order of xylotriose > xylobiose > xylotetraose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270452 [Multi-domain]  Cd Length: 388  Bit Score: 121.33  E-value: 1.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  46 LTMW--VDGDKQMAFYKKITDQYTKKT-GIKVKLVNIGQNDQLENISLDAPAGKGPDIFFLAHdntgSAYLQGLAAEIKL 122
Cdd:cd14749    2 ITYWqyFTGDTKKKYMDELIADFEKENpNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWP----GGWLAEFVKAGLL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 123 --------SKDELKGFNKQALKAMNYDNKQLALPAIVETTALFYNKKLVKNA-----PQTLEEVEANAAKLTDSKKKQYG 189
Cdd:cd14749   78 lpltdyldPNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAggvkpPKTWDELIEAAKKDKFKAKGQTG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 190 M----LFDAKNFYFNYPFLFGNDDYIFKKNGSEYDIhqlglNSKHVVKNAERLQKWYDKGYLPKAATH---DVMIGLFKE 262
Cdd:cd14749  158 FglllGAQGGHWYFQYLVRQAGGGPLSDDGSGKATF-----NDPAFVQALQKLQDLVKAGAFQEGFEGidyDDAGQAFAQ 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 263 GKVGQFVTGPWNINEYQET-FGKDLGVTTLPT--DGGKPMKPFLGVRGWYLSEYSKHKYWAKDLMLYITSKDTLQKYTDE 339
Cdd:cd14749  233 GKAAMNIGGSWDLGAIKAGePGGKIGVFPFPTvgKGAQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQYLED 312

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445957106 340 MSEIT----GRVDVKSSN-----PNLKVFEKQARHAEPMPNIPEMRQVW-EPMGNAsifISNGKNPKQALDEATNDIT 407
Cdd:cd14749  313 VGLLPakevVAKDEDPDPvailgPFADVLNAAGSTPFLDEYWPAAAQVHkDAVQKL---LTGKIDPEQVVKQAQSAAA 387
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 61-349 6.17e-29

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 114.43  E-value: 6.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106   61 KITDQYTKKTGIKVKLVNIGQNDQLENISLDAPAGKGPDI--FFLAHDNTGSAYLQGLAAEIKLSkDELKGFNkQALKAM 138
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQASNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLADLSDV-DNLDDLP-DALDAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  139 NYDNKQLALP-AIVETTALFYNKKLVKNA---PQTLEEVEANAAKLtdskKKQYGMLFDAKNFYfnYPFLFGNDDYIFKK 214
Cdd:pfam13416  79 GYDGKLYGVPyAASTPTVLYYNKDLLKKAgedPKTWDELLAAAAKL----KGKTGLTDPATGWL--LWALLADGVDLTDD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  215 NGSEYDIHQLglnskhvvknAERLQKWYDKGYLPkaATHDVMIGLFKEGKVGQFVTGPWNINEYQEtFGKDLGVtTLPTD 294
Cdd:pfam13416 153 GKGVEALDEA----------LAYLKKLKDNGKVY--NTGADAVQLFANGEVAMTVNGTWAAAAAKK-AGKKLGA-VVPKD 218

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 445957106  295 GgkpmkPFLGVRGWYLSEYSKHK-YWAKDLMLYITSKDTLQKYTDEMSEITGRVDV 349
Cdd:pfam13416 219 G-----SFLGGKGLVVPAGAKDPrLAALDFIKFLTSPENQAALAEDTGYIPANKSA 269
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 54-331 2.14e-21

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: 93.63  E-value: 2.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106   54 KQMAFYKKITDQYTKK-TGIKVKLVNIGQNDQLENISLDAPAGKGP-DIFFLAHDNTGSAYLQGLAAEIKlskdelkgfN 131
Cdd:pfam01547   5 TEAAALQALVKEFEKEhPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLD---------D 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  132 KQALKAMNYDNKQLALPAIVETTALFYNKKLVKNA----PQTLEEVEANAAKLTDSKKK---QYGMLFDAKNFYFNYPFL 204
Cdd:pfam01547  76 YVANYLVLGVPKLYGVPLAAETLGLIYNKDLFKKAgldpPKTWDELLEAAKKLKEKGKSpggAGGGDASGTLGYFTLALL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  205 FGNDDYIFKKNGSEYDiHQLGLNSKHVVKNAERLQKWYDKGYLPKAATHDV--MIGLFKEGKVGQFVTGPWNINEY---- 278
Cdd:pfam01547 156 ASLGGPLFDKDGGGLD-NPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGreALALFEQGKAAMGIVGPWAALAAnkvk 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445957106  279 --------QETFGKDLGVTTLPTDGGKPMkpflGVRGWYLSEYSKHKYWAKDLMLYITSKD 331
Cdd:pfam01547 235 lkvafaapAPDPKGDVGYAPLPAGKGGKG----GGYGLAIPKGSKNKEAAKKFLDFLTSPE 291
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 46-402 4.85e-20

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: 91.20  E-value: 4.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  46 LTMWVDGDKQMA-FYKKITDQYTKKT-GIKVKLVNIGQ--NDQLENISLDAPAG-KGPDIFFLahDN--TGSAYLQGLAA 118
Cdd:cd14750    2 ITFAAGSDGQEGeLLKKAIAAFEKKHpDIKVEIEELPAssDDQRQQLVTALAAGsSAPDVLGL--DViwIPEFAEAGWLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 119 EI--KLSKDELKGFNKQALKAMNYDNKQLALPAIVETTALFYNKKLVK----NAPQTLEEVEANAAKLTDSKKKQYGMLF 192
Cdd:cd14750   80 PLteYLKEEEDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEkygpEPPKTWDELLEAAKKRKAGEPGIWGYVF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 193 DAK-------NFyfnYPFLFGNDDYIFKKNGSEydihqLGLNSKHVVKNAERLQKWYDKGYLPKAAT---HDVMIGLFKE 262
Cdd:cd14750  160 QGKqyeglvcNF---LELLWSNGGDIFDDDSGK-----VTVDSPEALEALQFLRDLIGEGISPKGVLtygEEEARAAFQA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 263 GKVGQFVTGPW---NINEYQETFGKDLGVTTLPTDGGKPMKPFLGvrGWYL--SEYSKHKYWAKDLMLYITSKDTLQKYT 337
Cdd:cd14750  232 GKAAFMRNWPYayaLLQGPESAVAGKVGVAPLPAGPGGGSASTLG--GWNLaiSANSKHKEAAWEFVKFLTSPEVQKRRA 309

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445957106 338 DEMSEITGRVDV------KSSNPNLKVFEKQARHAEPMPNIPEMRQVWEPMGNA-SIFISNGKNPKQALDEA 402
Cdd:cd14750  310 INGGLPPTRRALyddpevLEAYPFLPALLEALENAVPRPVTPKYPEVSTAIQIAlSAALSGQATPEEALKQA 381
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 61-338 1.22e-09

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


Pssm-ID: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 60.03  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  61 KITDQYTKKTGIKVKLVNIGQNDQLENISLDAPAGKGPDIFFLAHDNTGSAYL-QGLAAE----IKLSKDELKGFN-KQA 134
Cdd:cd13580   23 PYTKYLEEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVVNDPQLSITLVkQGALWDltdyLDKYYPNLKKIIeQEG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 135 LKAMNYDNKQLALPAIVE---TTALFYNK----KLVKNAPQTLEEVEANAAKLTDS------KKKQYGMLFDAKNFYFN- 200
Cdd:cd13580  103 WDSASVDGKIYGIPRKRPligRNGLWIRKdwldKLGLEVPKTLDELYEVAKAFTEKdpdgngKKDTYGLTDTKDLIGSGf 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 201 YPFL--FGNDDYIFKKNGS---EYDIHQLGlnskhvVKNA-ERLQKWYDKGYLPKaathDVMIG-------LFKEGKVGQ 267
Cdd:cd13580  183 TGLFgaFGAPPNNWWKDEDgklVPGSIQPE------MKEAlKFLKKLYKEGLIDP----EFAVNdgtkaneKFISGKAGI 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106 268 FVTGPWNINEYQETFGKDLG------VTTLPTDGGK--PMKPFLGVRGWYLSEYSKHkywAKDLMLYI--TSKDTLQKYT 337
Cdd:cd13580  253 FVGNWWDPAWPQASLKKNDPdaewvaVPIPSGPDGKygVWAESGVNGFFVIPKKSKK---PEAILKLLdfLSDPEVQKLL 329


                 .
gi 445957106 338 D 338
Cdd:cd13580  330 D 330
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-181 1.93e-07

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 52.61  E-value: 1.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106   1 MSKILKCITLAVVMLLIVTACGPNRSKEDidkalnkdnskdkpnQLTMWVDGDkqmafY--KKITDQYTKKTGIKVKLVN 78
Cdd:COG0687    1 MSRRSLLGLAAAALAAALAGGAPAAAAEG---------------TLNVYNWGG-----YidPDVLEPFEKETGIKVVYDT 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  79 IGQNDQLENIsLDApAGKGPDIFFLAHDNTGSAYLQGLAAEIKLSKdeLKGFNK--QALKAMNYD-NKQLALPAIVETTA 155
Cdd:COG0687   61 YDSNEEMLAK-LRA-GGSGYDVVVPSDYFVARLIKAGLLQPLDKSK--LPNLANldPRFKDPPFDpGNVYGVPYTWGTTG 136

                        170       180
                 ....*....|....*....|....*...
gi 445957106 156 LFYNKKLVKNAPQTLEEV--EANAAKLT 181
Cdd:COG0687  137 IAYNTDKVKEPPTSWADLwdPEYKGKVA 164
PBP2_polyamine_2 cd13587
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 62-162 1.80e-05

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: 46.27  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  62 ITDQYTKKTGIKVKLVNIGQNDQLENiSLDAPAGKGPDIFFLAHDNTGSAYLQGLAAEIKLSKDELKGFNKQALKAMN-- 139
Cdd:cd13587   15 LLEKFENETGIKVQVTTSNNNEEMIS-KLRATGGGGFDLAQPSQRIAPNYEEFGLYQPIDESKIKVAQFPPSLLESTKlg 93

                         90       100
                 ....*....|....*....|....*
gi 445957106 140 --YDNKQLALPAIVETTALFYNKKL 162
Cdd:cd13587   94 ttINGKRYAVPFDWGTEGLTVNSTK 118
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 62-190 3.47e-04

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 42.23  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  62 ITDQYTKKTGIKVKLVNIGQNDQLENIslDAPAGKGP-DIFFLAH-DNTGSAYLQGLAAEIKLSKDElkgfnkqALKAMN 139
Cdd:COG1840    1 LLEAFEKKTGIKVNVVRGGSGELLARL--KAEGGNPPaDVVWSGDaDALEQLANEGLLQPYKSPELD-------AIPAEF 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 445957106 140 YDNKQLALPAIVETTALFYNKKLVK--NAPQTLEEveanaakLTDSK-KKQYGM 190
Cdd:COG1840   72 RDPDGYWFGFSVRARVIVYNTDLLKelGVPKSWED-------LLDPEyKGKIAM 118
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 64-167 7.67e-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: 41.07  E-value: 7.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  64 DQYTKKTGIKVKLVNIGQNDQLENIsLDAPAGKGPDIFFLAHDNTGSAYLQGLAAEIKLSKDELKGFNKQALKAMNYD-N 142
Cdd:cd13590   17 KAFEKETGVKVNYDTYDSNEEMLAK-LRAGGGSGYDLVVPSDYMVERLIKQGLLEPLDHSKLPNLKNLDPQFLNPPYDpG 95

                         90       100
                 ....*....|....*....|....*
gi 445957106 143 KQLALPAIVETTALFYNKKLVKNAP 167
Cdd:cd13590   96 NRYSVPYQWGTTGIAYNKDKVKEPP 120
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 66-168 2.45e-03

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: 39.59  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  66 YTKKTGIKVKLVNIGQNDqlENISLDAPAGKGPDIFFLAHDNTGSAYLQGLAAEIKLSK-----DELKGFNKqaLKAMNY 140
Cdd:cd13588   19 FEEATGCKVVVKFFGSED--EMVAKLRSGGGDYDVVTPSGDALLRLIAAGLVQPIDTSKipnyaNIDPRLRN--LPWLTV 94

                         90       100
                 ....*....|....*....|....*...
gi 445957106 141 DNKQLALPAIVETTALFYNKKLVKNAPQ 168
Cdd:cd13588   95 DGKVYGVPYDWGANGLAYNTKKVKTPPT 122
PBP2_BitB cd13546
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ...
 58-186 2.52e-03

Substrate binding domain of a putative iron transporter BitB, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270264 [Multi-domain]  Cd Length: 258  Bit Score: 39.55  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445957106  58 FYKKITDQYTKKTGIKVKLVNIGQNDQLENISLDAPAGKGpDIFFlahdntgsaylQGLAAEIKLSKDELKGF---NKQA 134
Cdd:cd13546   12 IIEPIIKEFEEKPGIKVEVVTGGTGELLARIKAEADNPQA-DVMW-----------GGGIETLEAYKDLFEPYespEAAA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 445957106 135 LKAMNYDNKQLALPAIVETTALFYNKKLVKN--APQTLEEveanaakLTDSKKK 186
Cdd:cd13546   80 IPDAYKSPEGLWTGFSVLPVVLMVNTDLVKNigAPKGWKD-------LLDPKWK 126
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH