NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490296182|ref|WP_004191645|]
View 

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

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; ...
 29-402 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: 570.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  29 QLNVWEDIKKS-AGIKTAVSDFEKQYNVKVNLQEMPYAQQLEKLRLDGPAGIGPDVLVIPNDQLGGAVVQGLLSPLSVDQ 107
Cdd:cd13658    1 QLTVWVDEDKKmAFIKKIAKQYTKKTGVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 108 AKQDAFTPASINAFRMDNALYGIPKAVETLVLIYNKDLVDKPLDSLQAWLDYSK--TQREQNKYGLLAKFDQIYYSWGAI 185
Cdd:cd13658   81 DKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKdlTKEKGKQYGFLADATNFYYSYGLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 186 GPMGGYIFAKNDSGGFnPQQVGLNTPGAVEAVTFLKKFYAEKVFPAGILGDnglnAIDSLFTEKKAAAVINGPWAFQPYE 265
Cdd:cd13658  161 AGNGGYIFKKNGSDLD-INDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGD----VIQGLFKEGKAAAVIDGPWAIQEYQ 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 266 AAGINYGVAPLPTLPDGKPMSSFLGVKGYVVSTWSKDKALAQQFIEFINQPQYVKARYVATGEIPPLKAMIDDPVIKNDQ 345
Cdd:cd13658  236 EAGVNYGVAPLPTLPNGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTSKENLKKRYDETNEIPPRKDVRSDPEIKNNP 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490296182 346 KASAVAIQSARAVAMPGIPEMGEVWGPANAALELSLTGKQAPQAALDNAVKQITMQI 402
Cdd:cd13658  316 LTSAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKTPKQALNDAVNDIKENI 372
 
Name Accession Description Interval E-value
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 29-402 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: 570.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  29 QLNVWEDIKKS-AGIKTAVSDFEKQYNVKVNLQEMPYAQQLEKLRLDGPAGIGPDVLVIPNDQLGGAVVQGLLSPLSVDQ 107
Cdd:cd13658    1 QLTVWVDEDKKmAFIKKIAKQYTKKTGVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 108 AKQDAFTPASINAFRMDNALYGIPKAVETLVLIYNKDLVDKPLDSLQAWLDYSK--TQREQNKYGLLAKFDQIYYSWGAI 185
Cdd:cd13658   81 DKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKdlTKEKGKQYGFLADATNFYYSYGLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 186 GPMGGYIFAKNDSGGFnPQQVGLNTPGAVEAVTFLKKFYAEKVFPAGILGDnglnAIDSLFTEKKAAAVINGPWAFQPYE 265
Cdd:cd13658  161 AGNGGYIFKKNGSDLD-INDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGD----VIQGLFKEGKAAAVIDGPWAIQEYQ 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 266 AAGINYGVAPLPTLPDGKPMSSFLGVKGYVVSTWSKDKALAQQFIEFINQPQYVKARYVATGEIPPLKAMIDDPVIKNDQ 345
Cdd:cd13658  236 EAGVNYGVAPLPTLPNGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTSKENLKKRYDETNEIPPRKDVRSDPEIKNNP 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490296182 346 KASAVAIQSARAVAMPGIPEMGEVWGPANAALELSLTGKQAPQAALDNAVKQITMQI 402
Cdd:cd13658  316 LTSAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKTPKQALNDAVNDIKENI 372
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-404 1.90e-138

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 401.64  E-value: 1.90e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182   1 MKKNTLAALILTTLAAGQLA-----------SLQAHAAGQLNVWEDIKKSAGIKTAVSDFEKQYNVKVNLQEMPYAQQLE 69
Cdd:COG2182    1 MKRRLLAALALALALALALAacgsgssssgsSSAAGAGGTLTVWVDDDEAEALEEAAAAFEEEPGIKVKVVEVPWDDLRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  70 KLRLDGPAGIGPDVLVIPNDQLGGAVVQGLLSPLSVDQAKQDAFTPASINAFRMDNALYGIPKAVETLVLIYNKDLVDK- 148
Cdd:COG2182   81 KLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKAe 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 149 PLDSLQAWLDYSKTQREQNKYGLLAKFDQIYYSWGAIGPMGGYIFAKNDSggfNPQQVGLNTPGAVEAVTFLKKFYAEKV 228
Cdd:COG2182  161 PPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYFYPFLAAFGGYLFGKDGD---DPKDVGLNSPGAVAALEYLKDLIKDGV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 229 FPAgilgDNGLNAIDSLFTEKKAAAVINGPWAFQPY-EAAGINYGVAPLPTLPDGKPMSSFLGVKGYVVSTWSKDKALAQ 307
Cdd:COG2182  238 LPA----DADYDAADALFAEGKAAMIINGPWAAADLkKALGIDYGVAPLPTLAGGKPAKPFVGVKGFGVSAYSKNKEAAQ 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 308 QFIEFINQPQYVKARYVATGEIPPLKAMIDDPVIKNDQKASAVAIQSARAVAMPGIPEMGEVWGPANAALELSLTGKQAP 387
Cdd:COG2182  314 EFAEYLTSPEAQKALFEATGRIPANKAAAEDAEVKADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADP 393

                        410
                 ....*....|....*..
gi 490296182 388 QAALDNAVKQITMQIEA 404
Cdd:COG2182  394 AEALDAAQKQIEAAIAQ 410
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
1-399 1.65e-67

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 219.50  E-value: 1.65e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182   1 MKKNTLAALILTTLAAgQLASLQAHAA---GQLNVWEDIKKS-AGIKTAVSDFEKQYNVKVNLQ-----EMPYAQQlekl 71
Cdd:PRK09474   2 KIKKGLRTLALSALAT-LMFSASALAKieeGKLVIWINGDKGyNGLAEVGKKFEKDTGIKVTVEhpdklEEKFPQV---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  72 rldGPAGIGPDVLVIPNDQLGGAVVQGLLSPLSVDQAKQDAFTPASINAFRMDNALYGIPKAVETLVLIYNKDLVDKPLD 151
Cdd:PRK09474  77 ---AATGDGPDIIFWAHDRFGGYAQSGLLAEVTPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 152 SLQAWLDYSKTQREQNKYGLLAKFDQIYYSWGAIGPMGGYIFAKNDsGGFNPQQVGLNTPGAVEAVTFLKKFYAEKVFPA 231
Cdd:PRK09474 154 TWEEIPALDKELKAKGKSAIMWNLQEPYFTWPLIAADGGYAFKFEN-GGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNA 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 232 GIlgDNGLnaIDSLFTEKKAAAVINGPWAFQPYEAAGINYGVAPLPTLpDGKPMSSFLGVKGYVVSTWSKDKALAQQFIE 311
Cdd:PRK09474 233 DT--DYSI--AEAAFNKGETAMTINGPWAWSNIDKSGINYGVTVLPTF-NGKPSKPFVGVLSAGINAASPNKELAKEFLE 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 312 finqpqyvkaRYVATGE------------IPPLKAMID----DPVIKndqkasAVAIQSARAVAMPGIPEMGEVWGPANA 375
Cdd:PRK09474 308 ----------NYLLTDEgletvnkdkplgAVALKSFQEelakDPRIA------ATMDNAQNGEIMPNIPQMSAFWYAMRT 371

                        410       420
                 ....*....|....*....|....
gi 490296182 376 ALELSLTGKQAPQAALDNAVKQIT 399
Cdd:PRK09474 372 AIINATSGRQTVDAALDDAAKRIT 395
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 45-344 3.19e-41

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 147.17  E-value: 3.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182   45 AVSDFEKQYNVKVNLQEMPYAQQLEKLRLDGPAGIGPDVLVI--PNDQLGGAVVQGLLSPLSVDQAKQDafTPASINAFR 122
Cdd:pfam13416   2 LAKAFEKKTGVTVEVEPQASNDLQAKLLAAAAAGNAPDLDVVwiAADQLATLAEAGLLADLSDVDNLDD--LPDALDAAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  123 MDNALYGIPKAVET-LVLIYNKDLVDKPLDSLQAWLDYSKTQRE-QNKYGLLAKFDQiYYSWGAIgpmggyifakndSGG 200
Cdd:pfam13416  80 YDGKLYGVPYAASTpTVLYYNKDLLKKAGEDPKTWDELLAAAAKlKGKTGLTDPATG-WLLWALL------------ADG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  201 FNPQQVGLNTPGAVEAVTFLKKFYAEKVFPagilgDNGLNAIdSLFTEKKAAAVINGPWAFQPYEAAGINYGVAPLPtlp 280
Cdd:pfam13416 147 VDLTDDGKGVEALDEALAYLKKLKDNGKVY-----NTGADAV-QLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVPK--- 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490296182  281 dgkpMSSFLGVKGYVVSTWSKDKAL-AQQFIEFINQPQYVKARYVATGEIPPLKAMIDDPVIKND 344
Cdd:pfam13416 218 ----DGSFLGGKGLVVPAGAKDPRLaALDFIKFLTSPENQAALAEDTGYIPANKSAALSDEVKAD 278
 
Name Accession Description Interval E-value
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 29-402 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: 570.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  29 QLNVWEDIKKS-AGIKTAVSDFEKQYNVKVNLQEMPYAQQLEKLRLDGPAGIGPDVLVIPNDQLGGAVVQGLLSPLSVDQ 107
Cdd:cd13658    1 QLTVWVDEDKKmAFIKKIAKQYTKKTGVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 108 AKQDAFTPASINAFRMDNALYGIPKAVETLVLIYNKDLVDKPLDSLQAWLDYSK--TQREQNKYGLLAKFDQIYYSWGAI 185
Cdd:cd13658   81 DKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKdlTKEKGKQYGFLADATNFYYSYGLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 186 GPMGGYIFAKNDSGGFnPQQVGLNTPGAVEAVTFLKKFYAEKVFPAGILGDnglnAIDSLFTEKKAAAVINGPWAFQPYE 265
Cdd:cd13658  161 AGNGGYIFKKNGSDLD-INDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGD----VIQGLFKEGKAAAVIDGPWAIQEYQ 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 266 AAGINYGVAPLPTLPDGKPMSSFLGVKGYVVSTWSKDKALAQQFIEFINQPQYVKARYVATGEIPPLKAMIDDPVIKNDQ 345
Cdd:cd13658  236 EAGVNYGVAPLPTLPNGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTSKENLKKRYDETNEIPPRKDVRSDPEIKNNP 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490296182 346 KASAVAIQSARAVAMPGIPEMGEVWGPANAALELSLTGKQAPQAALDNAVKQITMQI 402
Cdd:cd13658  316 LTSAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKTPKQALNDAVNDIKENI 372
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-404 1.90e-138

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 401.64  E-value: 1.90e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182   1 MKKNTLAALILTTLAAGQLA-----------SLQAHAAGQLNVWEDIKKSAGIKTAVSDFEKQYNVKVNLQEMPYAQQLE 69
Cdd:COG2182    1 MKRRLLAALALALALALALAacgsgssssgsSSAAGAGGTLTVWVDDDEAEALEEAAAAFEEEPGIKVKVVEVPWDDLRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  70 KLRLDGPAGIGPDVLVIPNDQLGGAVVQGLLSPLSVDQAKQDAFTPASINAFRMDNALYGIPKAVETLVLIYNKDLVDK- 148
Cdd:COG2182   81 KLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKAe 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 149 PLDSLQAWLDYSKTQREQNKYGLLAKFDQIYYSWGAIGPMGGYIFAKNDSggfNPQQVGLNTPGAVEAVTFLKKFYAEKV 228
Cdd:COG2182  161 PPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYFYPFLAAFGGYLFGKDGD---DPKDVGLNSPGAVAALEYLKDLIKDGV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 229 FPAgilgDNGLNAIDSLFTEKKAAAVINGPWAFQPY-EAAGINYGVAPLPTLPDGKPMSSFLGVKGYVVSTWSKDKALAQ 307
Cdd:COG2182  238 LPA----DADYDAADALFAEGKAAMIINGPWAAADLkKALGIDYGVAPLPTLAGGKPAKPFVGVKGFGVSAYSKNKEAAQ 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 308 QFIEFINQPQYVKARYVATGEIPPLKAMIDDPVIKNDQKASAVAIQSARAVAMPGIPEMGEVWGPANAALELSLTGKQAP 387
Cdd:COG2182  314 EFAEYLTSPEAQKALFEATGRIPANKAAAEDAEVKADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADP 393

                        410
                 ....*....|....*..
gi 490296182 388 QAALDNAVKQITMQIEA 404
Cdd:COG2182  394 AEALDAAQKQIEAAIAQ 410
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 30-398 1.07e-108

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: 324.25  E-value: 1.07e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  30 LNVWEDIKK-SAGIKTAVSDFEKQYNVKVNLQEMPYAQQLEKLRLDGPAGIGPDVLVIPNDQLGGAVVQGLLSPLSVDQA 108
Cdd:cd13586    2 ITVWTDEDGeLEYLKELAEEFEKKYGIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 109 KQDAFTPASINAFRMDNALYGIPKAVETLVLIYNKDLVDKPLDSLQAWLDYSKTQRE--QNKYGLLAKFDQIYYSWGAIG 186
Cdd:cd13586   82 VKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPEPPKTWEELIALAKKFNDkaGGKYGFAYDQTNPYFSYPFLA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 187 PMGGYIFAKNDSGgfnPQQVGLNTPGAVEAVTFLKK-FYAEKVFPAGILGDNglnaIDSLFTEKKAAAVINGPWAFQPYE 265
Cdd:cd13586  162 AFGGYVFGENGGD---PTDIGLNNEGAVKGLKFIKDlKKKYKVLPPDLDYDI----ADALFKEGKAAMIINGPWDLADYK 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 266 AAGINYGVAPLPTLPDGKPMSSFLGVKGYVVSTWSKDKALAQQFIEFINQPQYVKARYVATGEIPPLKAMIDDPVIKNDQ 345
Cdd:cd13586  235 DAGINFGVAPLPTLPGGKQAAPFVGVQGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALKDALNDAAVKNDP 314

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490296182 346 KASAVAIQSARAVAMPGIPEMGEVWGPANAALELSLTGKQAPQAALDNAVKQI 398
Cdd:cd13586  315 LVKAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEEAAKDAVAAI 367
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 42-398 1.81e-69

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: 223.41  E-value: 1.81e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  42 IKTAVSDFEKQY---NVKVNLQEMPyaQQLEKLRLDGPAGIGPDVLVIPNDQLGGAVVQGLLSPLS--VDQAKQDAFTPA 116
Cdd:cd13657   16 LQQIIDEFEAKYpvpNVKVPFEKKP--DLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISdyLSEDDFENYLPT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 117 SINAFRMDNALYGIPKAVETLVLIYNKDLVDKPLDSLQAWLDYSK--TQREQNKYGLLAKFDQIYYSWGAIGPMGGYIFa 194
Cdd:cd13657   94 AVEAVTYKGKVYGLPEAYETVALIYNKALVDQPPETTDELLAIMKdhTDPAAGSYGLAYQVSDAYFVSAWIFGFGGYYF- 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 195 knDSGGFNPqqvGLNTPGAVEAVTFLKKFYAEKVFPagilgDNGLNAIDSLFTEKKAAAVINGPWAFQPYEAAGINYGVA 274
Cdd:cd13657  173 --DDETDKP---GLDTPETIKGIQFLKDFSWPYMPS-----DPSYNTQTSLFNEGKAAMIINGPWFIGGIKAAGIDLGVA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 275 PLPTLPDGKPMSSFLGVKGYVVST--WSKDKALAQQFIEFINQPQYVKARYVATGEIPPLKAMIDDPVIKNDQKASAVAI 352
Cdd:cd13657  243 PLPTVDGTNPPRPYSGVEGIYVTKyaERKNKEAALDFAKFFTTAEASKILADENGYVPAATNAYDDAEVAADPVIAAFKA 322

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 490296182 353 QSARAVAMPGIPEMGEVWGPANAALELSLTGKQAPQAALDNAVKQI 398
Cdd:cd13657  323 QAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQEALAAAQQEI 368
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
1-399 1.65e-67

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 219.50  E-value: 1.65e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182   1 MKKNTLAALILTTLAAgQLASLQAHAA---GQLNVWEDIKKS-AGIKTAVSDFEKQYNVKVNLQ-----EMPYAQQlekl 71
Cdd:PRK09474   2 KIKKGLRTLALSALAT-LMFSASALAKieeGKLVIWINGDKGyNGLAEVGKKFEKDTGIKVTVEhpdklEEKFPQV---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  72 rldGPAGIGPDVLVIPNDQLGGAVVQGLLSPLSVDQAKQDAFTPASINAFRMDNALYGIPKAVETLVLIYNKDLVDKPLD 151
Cdd:PRK09474  77 ---AATGDGPDIIFWAHDRFGGYAQSGLLAEVTPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 152 SLQAWLDYSKTQREQNKYGLLAKFDQIYYSWGAIGPMGGYIFAKNDsGGFNPQQVGLNTPGAVEAVTFLKKFYAEKVFPA 231
Cdd:PRK09474 154 TWEEIPALDKELKAKGKSAIMWNLQEPYFTWPLIAADGGYAFKFEN-GGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNA 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 232 GIlgDNGLnaIDSLFTEKKAAAVINGPWAFQPYEAAGINYGVAPLPTLpDGKPMSSFLGVKGYVVSTWSKDKALAQQFIE 311
Cdd:PRK09474 233 DT--DYSI--AEAAFNKGETAMTINGPWAWSNIDKSGINYGVTVLPTF-NGKPSKPFVGVLSAGINAASPNKELAKEFLE 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 312 finqpqyvkaRYVATGE------------IPPLKAMID----DPVIKndqkasAVAIQSARAVAMPGIPEMGEVWGPANA 375
Cdd:PRK09474 308 ----------NYLLTDEgletvnkdkplgAVALKSFQEelakDPRIA------ATMDNAQNGEIMPNIPQMSAFWYAMRT 371

                        410       420
                 ....*....|....*....|....
gi 490296182 376 ALELSLTGKQAPQAALDNAVKQIT 399
Cdd:PRK09474 372 AIINATSGRQTVDAALDDAAKRIT 395
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 32-398 1.10e-61

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: 203.41  E-value: 1.10e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  32 VWEDIKKSAGIKTAVSDFEKQY-NVKVNLQEMPYAQQLEKLRLDGPAGIGPDVLVIPNDQLGGAVVQGLLSPLSVDQAKQ 110
Cdd:cd13522    6 HQYDTGENQAVNELIAKFEKAYpGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDEYVSKS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 111 DAFTPASINAFRMDNALYGIPKAVETLVLIYNKDLV-DKPLDSLQAWLDYSKTQREQNKYGLLAKFDQIYYSWGAIGPMG 189
Cdd:cd13522   86 GKYAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVpKNPPKTWQELIALAQGLKAKNVWGLVYNQNEPYFFAAWIGGFG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 190 GYIFAKNDsGGFNPqqvGLNTPGAVEAVTFLKKF-YAEKVFPAgilgDNGLNAIDSLFTEKKAAAVINGPWAFQPY-EAA 267
Cdd:cd13522  166 GQVFKANN-GKNNP---TLDTPGAVEALQFLVDLkSKYKIMPP----ETDYSIADALFKAGKAAMIINGPWDLGDYrQAL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 268 GINYGVAPLPTLPDGKPMSSFLGVKGYVVSTWSKDKALAQQFIEFINQPQYVKARYVATGEIPPLKAMIDDPVIKNDQKA 347
Cdd:cd13522  238 KINLGVAPLPTFSGTKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDIPANLQAYESPAVQNKPAQ 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490296182 348 SAVAIQSARAVAMPGIPEMGEVWGPANAALELSLTGKQAPQAALDNAVKQI 398
Cdd:cd13522  318 KASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQQEA 368
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 28-398 2.56e-56

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: 189.34  E-value: 2.56e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  28 GQLNVWEDIKKS-AGIKTAVSDFEKQYNVKVNLQEMPYAQqlEKLRLDGPAGIGPDVLVIPNDQLGGAVVQGLLSPLSVD 106
Cdd:cd13656    1 GKLVIWINGDKGyNGLAEVGKKFEKDTGIKVTVEHPDKLE--EKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 107 QAKQDAFTPASINAFRMDNALYGIPKAVETLVLIYNKDLVDKPLDSLQAWLDYSKTQREQNKYGLLAKFDQIYYSWGAIG 186
Cdd:cd13656   79 KAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 187 PMGGYIFaKNDSGGFNPQQVGLNTPGAVEAVTFLKKFYAEKVFPAGilgdNGLNAIDSLFTEKKAAAVINGPWAFQPYEA 266
Cdd:cd13656  159 ADGGYAF-KYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNAD----TDYSIAEAAFNKGETAMTINGPWAWSNIDT 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 267 AGINYGVAPLPTLpDGKPMSSFLGVKGYVVSTWSKDKALAQQFIEfinqpqyvkaRYVATGE------------IPPLKA 334
Cdd:cd13656  234 SKVNYGVTVLPTF-KGQPSKPFVGVLSAGINAASPNKELAKEFLE----------NYLLTDEgleavnkdkplgAVALKS 302

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490296182 335 MIDDpvIKNDQKASAVAIQSARAVAMPGIPEMGEVWGPANAALELSLTGKQAPQAALDNAVKQI 398
Cdd:cd13656  303 YEEE--LAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTRI 364
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-335 2.49e-50

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 173.69  E-value: 2.49e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182   1 MKKNTLAALILTTLA-----AGQLASLQAHAAGQLNVWEDIKKSAG-IKTAVSDFEKQY-NVKVNLQEMPYAQQLEKLRL 73
Cdd:COG1653    1 MRRLALALAAALALAlaacgGGGSGAAAAAGKVTLTVWHTGGGEAAaLEALIKEFEAEHpGIKVEVESVPYDDYRTKLLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  74 DGPAGIGPDVLVIPNDQLGGAVVQGLLSPLS----VDQAKQDAFTPASINAFRMDNALYGIPKAVETLVLIYNKDLVDK- 148
Cdd:COG1653   81 ALAAGNAPDVVQVDSGWLAEFAAAGALVPLDdlldDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKa 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 149 ---PLDSLQAWLDYSKT-QREQNKYGLLAKFDQIYYSWGAIGPMGGYIFAKNDsggfnpqQVGLNTPGAVEAVTFLKKFY 224
Cdd:COG1653  161 gldPPKTWDELLAAAKKlKAKDGVYGFALGGKDGAAWLDLLLSAGGDLYDEDG-------KPAFDSPEAVEALEFLKDLV 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 225 AEKVFPAGILGDNGLNAIDsLFTEKKAAAVINGPWAFQPYEAA--GINYGVAPLPTLPDGKPMSSFLGVKGYVVSTWSKD 302
Cdd:COG1653  234 KDGYVPPGALGTDWDDARA-AFASGKAAMMINGSWALGALKDAapDFDVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKN 312

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 490296182 303 KALAQQFIEFINQPQYVKAR----YVATGEIPPLKAM 335
Cdd:COG1653  313 PEAAWKFLKFLTSPEAQAKWdalqAVLLGQKTPEEAL 349
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 40-398 1.21e-48

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: 169.51  E-value: 1.21e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  40 AGIKTAVSDFEKQY-NVKVNLQEMPYAQQLEKLRLDGPAGIGPDVLVIPNDQLGGAVVQGLLSPLS---VDQAKQDAFTP 115
Cdd:cd13585   14 AALKKLIDAFEKENpGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDdyiEKDGLDDDFPP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 116 ASINAFRMDNALYGIPKAVETLVLIYNKDLVDK------PLDSLQAWLDYSK--TQREQNKYGLLAKFDQ--IYYSWGAI 185
Cdd:cd13585   94 GLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKagpgpkPPWTWDELLEAAKklTDKKGGQYGFALRGGSggQTQWYPFL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 186 GPMGGYIFAKNDSggfnpqQVGLNTPGAVEAVTFLKKFYAEKVFPAGIlgDNGLNAIDSLFTEKKAAAVINGPWAFQPYE 265
Cdd:cd13585  174 WSNGGDLLDEDDG------KATLNSPEAVEALQFYVDLYKDGVAPSSA--TTGGDEAVDLFASGKVAMMIDGPWALGTLK 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 266 AAGI--NYGVAPLPTLPDGKPmSSFLGVKGYVVSTWSKDKALAQQFIEFI----NQPQYVKARYVATGEIPPLKAMIDDP 339
Cdd:cd13585  246 DSKVkfKWGVAPLPAGPGGKR-ASVLGGWGLAISKNSKHPEAAWKFIKFLtskeNQLKLGGAAGPAALAAAAASAAAPDA 324

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296182 340 VIKNDQKASAVAIQSARAVAMPGIPEmgEVWGPANAALELSLTGKQA--PQAALDNAVKQI 398
Cdd:cd13585  325 KPALALAAAADALAAAVPPPVPPPWP--EVYPILSEALQEALLGALGksPEEALKEAAKEI 383
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 40-398 5.75e-46

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: 162.46  E-value: 5.75e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  40 AGIKTAVSDFEK-QYNVKVNLQEMPYAQQLE-KLRLDGPAGIGPDVLVIPNDQLGGAVVQGLLSPLS--VDQAKQDA--F 113
Cdd:cd14748   14 KALEELVDEFNKsHPDIKVKAVYQGSYDDTLtKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDdyIDKDGVDDddF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 114 TPASINAFRMDNALYGIPKAVETLVLIYNKDL-------VDKPLDSLQAWLDYSK----TQREQNKYGLLAKFDQIYYSW 182
Cdd:cd14748   94 YPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLfeeagldPEKPPKTWDELEEAAKklkdKGGKTGRYGFALPPGDGGWTF 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 183 GA-IGPMGGYIFakNDSGGfnpqQVGLNTPGAVEAVTFLKKFYAEKvfpaGILGDNGLNAIDSLFTEKKAAAVINGPWAF 261
Cdd:cd14748  174 QAlLWQNGGDLL--DEDGG----KVTFNSPEGVEALEFLVDLVGKD----GVSPLNDWGDAQDAFISGKVAMTINGTWSL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 262 QPY--EAAGINYGVAPLPTLPDGKPMSSFLGVKGYVVSTWSKDKALAQQFIEFINQPQYVKARYVATGEIPPLKAMIDDP 339
Cdd:cd14748  244 AGIrdKGAGFEYGVAPLPAGKGKKGATPAGGASLVIPKGSSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRKSAAEDP 323

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296182 340 VI---KNDQKASAVAIQSARAVAMPGIPEMGEVWGPANAALELSLTGKQAPQAALDNAVKQI 398
Cdd:cd14748  324 EEflaENPNYKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 30-399 3.17e-41

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: 149.77  E-value: 3.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  30 LNVW--EDIKKSAGIKTAVSDFEKQY-NVKVNLQEMPYAQQLEKLRLDGPAGIGPDVLVIPNDQLGGAVVQGLLSPLS-- 104
Cdd:cd14747    2 LTVWamGNSAEAELLKELADEFEKENpGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMGALEDLTpy 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 105 VDQAKQD-AFTPASINAFRMDNALYGIPKAVETLVLIYNKDL-----VDKPLDSLQAWLDYSKTQREQ--NKYGLLAKFD 176
Cdd:cd14747   82 LEDLGGDkDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLlkkagGDEAPKTWDELEAAAKKIKADgpDVSGFAIPGK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 177 QIYYS------WGAigpmGGYIFAKNDSGGFnpqqvgLNTPGAVEAVTFLKKFYAEKVFPAGILGDNGlnAIDSLFTEKK 250
Cdd:cd14747  162 NDVWHnalpfvWGA----GGDLATKDKWKAT------LDSPEAVAGLEFYTSLYQKGLSPKSTLENSA--DVEQAFANGK 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 251 AAAVINGPW-----AFQPYEAAGiNYGVAPLPTlPDGKPMSSFLGVKGYVVSTWSKDKALAQQFIEFINQPQYVKARYVA 325
Cdd:cd14747  230 VAMIISGPWeigaiREAGPDLAG-KWGVAPLPG-GPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKA 307

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490296182 326 TGEIPPLKAMIDDPVIKNDQKASAVAIQSARAVAMPGIPEmgevWGPANAALELSLT-----GKQAPQAALDNAVKQIT 399
Cdd:cd14747  308 TGMLPANTSAWDDPSLANDPLLAVFAEQLKTGKATPATPE----WGEIEAELVLVLEevwigVGADVEDALDKAAAEIN 382
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 45-344 3.19e-41

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 147.17  E-value: 3.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182   45 AVSDFEKQYNVKVNLQEMPYAQQLEKLRLDGPAGIGPDVLVI--PNDQLGGAVVQGLLSPLSVDQAKQDafTPASINAFR 122
Cdd:pfam13416   2 LAKAFEKKTGVTVEVEPQASNDLQAKLLAAAAAGNAPDLDVVwiAADQLATLAEAGLLADLSDVDNLDD--LPDALDAAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  123 MDNALYGIPKAVET-LVLIYNKDLVDKPLDSLQAWLDYSKTQRE-QNKYGLLAKFDQiYYSWGAIgpmggyifakndSGG 200
Cdd:pfam13416  80 YDGKLYGVPYAASTpTVLYYNKDLLKKAGEDPKTWDELLAAAAKlKGKTGLTDPATG-WLLWALL------------ADG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  201 FNPQQVGLNTPGAVEAVTFLKKFYAEKVFPagilgDNGLNAIdSLFTEKKAAAVINGPWAFQPYEAAGINYGVAPLPtlp 280
Cdd:pfam13416 147 VDLTDDGKGVEALDEALAYLKKLKDNGKVY-----NTGADAV-QLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVPK--- 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490296182  281 dgkpMSSFLGVKGYVVSTWSKDKAL-AQQFIEFINQPQYVKARYVATGEIPPLKAMIDDPVIKND 344
Cdd:pfam13416 218 ----DGSFLGGKGLVVPAGAKDPRLaALDFIKFLTSPENQAALAEDTGYIPANKSAALSDEVKAD 278
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 29-392 1.06e-38

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: 142.48  E-value: 1.06e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  29 QLNVWEDIKKSAGIKTAVSDFEKQY---NVKVNLQEMPYAQQLEKLRLDGPAGigPDVLVIPNDQLGGAVVQGLLSPL-- 103
Cdd:cd13655    1 TLTVWGPQEDQEWLKEMVDAFKEKHpewKITITIGVVGEADAKDEVLKDPSAA--ADVFAFANDQLGELVDAGAIYPLtg 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 104 SVDQAKQDAFTPASINAFRMDNALYGIPKAVETLVLIYNKDLVD----KPLDSLQAWLDYSKTqreqnKYGLlaKFDQIY 179
Cdd:cd13655   79 SAVDKIKNTNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLTeddvKSLDTMLAKAPDAKG-----KVSF--DLSNSW 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 180 YSWGAIGPMGGYIFAKNDSggfNPQQVGLNTPGAVEAVTFLKKFYAEKVFPAgilgDNGLNAIdSLFTEKKAAAVINGPW 259
Cdd:cd13655  152 YLYAFFFGAGCKLFGNNGG---DTAGCDFNNEKGVAVTNYLVDLVANPKFVN----DADGDAI-SGLKDGTLGAGVSGPW 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 260 AFQPYEAA-GINYGVAPLPTL-PDGK--PMSSFLGVKGYVVSTWSKDKALAQQFIEFINQPQYVKARYVATGEIPPLKAM 335
Cdd:cd13655  224 DAANLKKAlGDNYAVAKLPTYtLGGKdvQMKSFAGYKAIGVNSNTKNPEAAMALADYLTNEESQLTRFEKRGIGPTNKEA 303

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490296182 336 IDDPVIKNDQKASAVAIQSARA-VAMPGIPEMGEVWGPANAALELSLTGKQAPQAALD 392
Cdd:cd13655  304 AESDAVKADPAAKALIAQSNEAsVVQPKLPKMSNFWTPAEAFGKGIVDGTVTAENAQQ 361
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 34-396 2.68e-34

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: 131.35  E-value: 2.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  34 EDIKKSAgIKTAVSDFEKQY-NVKVNLQEMPYAQQLEKLRLDGPAGIGPDVL-VIPNDQLGGAVVQGLLSPLS---VDQA 108
Cdd:cd14749   10 GDTKKKY-MDELIADFEKENpNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPLTdylDPNG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 109 KQDAFTPASINAFRMDNALYGIPKAVETLVLIYNKDLVDK--PLDSLQAW---LDYSKTQREQNK----YGLLAKFD--Q 177
Cdd:cd14749   89 VDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEagGVKPPKTWdelIEAAKKDKFKAKgqtgFGLLLGAQggH 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 178 IYYSWGAIGPMGGYIFAKNDsggfnpQQVGLNTPGAVEAVTFLKKFYAEKVFPAGILGdNGLNAIDSLFTEKKAAAVING 257
Cdd:cd14749  169 WYFQYLVRQAGGGPLSDDGS------GKATFNDPAFVQALQKLQDLVKAGAFQEGFEG-IDYDDAGQAFAQGKAAMNIGG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 258 PWAFQPYEA--AGINYGVAPLPTLPDG-KPMSSFLGVKGYVVSTWSKDKALAQQFIEFINQPQYVKARYVATGEIPPLKA 334
Cdd:cd14749  242 SWDLGAIKAgePGGKIGVFPFPTVGKGaQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQYLEDVGLLPAKEV 321

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296182 335 MIDDPVIKNDQKASAVAIQSARAVAMP----GIPEMGEVW-GPANAALELSLTGKQAPQAALDNAVK 396
Cdd:cd14749  322 VAKDEDPDPVAILGPFADVLNAAGSTPfldeYWPAAAQVHkDAVQKLLTGKIDPEQVVKQAQSAAAK 388
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 46-398 1.92e-32

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: 125.96  E-value: 1.92e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  46 VSDFEKQY-NVKVNLQEMPYAQQLEKLRLDGPAGIGPDVLVIPNDQLGGAVVQGLLSPLSVDQAKQD--AFTPASINAFR 122
Cdd:cd14751   20 IPAFEKEYpKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDGTPAFDDivDYLPGPMETNR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 123 MDNALYGIPKAVETLVLIYNKDLVDK----PLDSLQAWLDYSKTQRE-QNKYGLLAKFDQIYYSWGAIGPMGGYIFAKND 197
Cdd:cd14751  100 YNGHYYGVPQVTNTLALFYNKRLLEEagteVPKTMDELVAAAKAIKKkKGRYGLYISGDGPYWLLPFLWSFGGDLTDEKK 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 198 SGGFnpqqvgLNTPGAVEAVTFLKKFYAEKVFPAGILGDNGlNAIDSlFTEKKAAAVINGPWAF-----QPYEAAGINYG 272
Cdd:cd14751  180 ATGY------LNSPESVRALETIVDLYDEGAITPCASGGYP-NMQDG-FKSGRYAMIVNGPWAYadilgGKEFKDPDNLG 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 273 VAPLPTLPDGKPmsSFLGVKGYVVSTWSKDKALAQQFIEFINQPQYVKARYVATGEIPPLKAMIDDPVIKNDQKASAVAI 352
Cdd:cd14751  252 IAPVPAGPGGSG--SPVGGEDLVIFKGSKNKDAAWKFVKFMSSAEAQALTAAKLGLLPTRTSAYESPEVANNPMVAAFKP 329

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 490296182 353 QSARAVAMPGIPEMGEVWGPANAALELSLTGKQAPQAALDNAVKQI 398
Cdd:cd14751  330 ALETAVPRPPIPEWGELFEPLTLAFAKVLRGEKSPREALDEAAKQW 375
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 35-398 2.26e-31

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: 123.17  E-value: 2.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  35 DIKKSAGIKTAVSDFEKQY-NVKVNLQEMP--YAQQLEKL-RLDGPAGIGPDVLVIpnDQ--LGGAVVQGLLSPLS--VD 106
Cdd:cd14750    9 DGQEGELLKKAIAAFEKKHpDIKVEIEELPasSDDQRQQLvTALAAGSSAPDVLGL--DViwIPEFAEAGWLLPLTeyLK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 107 QAKQDAFTPASINAFRMDNALYGIPKAVETLVLIYNKDLVDKPLDSL-QAWLDYSKT-----QREQNKYGLLAKFDQ--- 177
Cdd:cd14750   87 EEEDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPEPpKTWDELLEAakkrkAGEPGIWGYVFQGKQyeg 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 178 -------IYYSwgaigpMGGYIFakNDSGGfnpqQVGLNTPGAVEAVTFLKKFYAEKVFPAGILGDNGlNAIDSLFTEKK 250
Cdd:cd14750  167 lvcnfleLLWS------NGGDIF--DDDSG----KVTVDSPEALEALQFLRDLIGEGISPKGVLTYGE-EEARAAFQAGK 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 251 AAAVINGPWAFQPYEAAGINY----GVAPLPTLPDGKPmSSFLGVKGYVVSTWSKDKALAQQFIEFINQPQYVKARYVAT 326
Cdd:cd14750  234 AAFMRNWPYAYALLQGPESAVagkvGVAPLPAGPGGGS-ASTLGGWNLAISANSKHKEAAWEFVKFLTSPEVQKRRAING 312

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296182 327 GEIPPLKAMIDDPVIKNDQ---KASAVAIQSarAVAMPGIPEMGEVwgpANA---ALELSLTGKQAPQAALDNAVKQI 398
Cdd:cd14750  313 GLPPTRRALYDDPEVLEAYpflPALLEALEN--AVPRPVTPKYPEV---STAiqiALSAALSGQATPEEALKQAQEKL 385
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 33-320 1.45e-23

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: 99.80  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182   33 WEDIKKSAGIKTAVSDFEKQY-NVKVNLQEMPYAQQLEKLRLDGPAGIGP-DVLVIPNDQLGGAVVQGLLSPLSVDQAKQ 110
Cdd:pfam01547   1 AASLTEAAALQALVKEFEKEHpGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVANY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  111 DAFTpasinafrmDNALYGIPKAVETLVLIYNKDLVDK----PLDSLQAWLDYSKTQREQNKYGLLAKFdqiYYSWGAIG 186
Cdd:pfam01547  81 LVLG---------VPKLYGVPLAAETLGLIYNKDLFKKagldPPKTWDELLEAAKKLKEKGKSPGGAGG---GDASGTLG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  187 PMGGYIFAKNDSGGFNPQQVGLNTPGAVEAVTFLKKFYAEKVFPAGILGDNGLNA----IDSLFTEKKAAAVINGPWAFQ 262
Cdd:pfam01547 149 YFTLALLASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGAdgreALALFEQGKAAMGIVGPWAAL 228

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296182  263 -------------PYEAAGINYGVAPLPTLPDGKPmssflGVKGYVVSTWSKDKALAQQFIEFINQPQYVK 320
Cdd:pfam01547 229 aankvklkvafaaPAPDPKGDVGYAPLPAGKGGKG-----GGYGLAIPKGSKNKEAAKKFLDFLTSPEAQA 294
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-158 1.43e-12

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 68.40  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182   1 MKKNTLAALILTTLAAGQLASLQAHAA-GQLNV--WED-IKKSAgiktaVSDFEKQYNVKVNLQEMPYAQQLE-KLRLDG 75
Cdd:COG0687    1 MSRRSLLGLAAAALAAALAGGAPAAAAeGTLNVynWGGyIDPDV-----LEPFEKETGIKVVYDTYDSNEEMLaKLRAGG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  76 PagiGPDVLVIPNDQLGGAVVQGLLSPLSVDQAKQDAFTPASINAFRMD-NALYGIPKAVETLVLIYNKDLVDKPLDSLQ 154
Cdd:COG0687   76 S---GYDVVVPSDYFVARLIKAGLLQPLDKSKLPNLANLDPRFKDPPFDpGNVYGVPYTWGTTGIAYNTDKVKEPPTSWA 152


                 ....
gi 490296182 155 AWLD 158
Cdd:COG0687  153 DLWD 156
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 46-320 1.41e-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: 59.65  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  46 VSDFEKQYNVKVNLQEMPYAQQLEKLRLDGPAGIGPDVLVIPNDQLG-GAVVQGLLSPLS--VDQAKQDafTPASINAFR 122
Cdd:cd13580   25 TKYLEEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVVNDPQLSiTLVKQGALWDLTdyLDKYYPN--LKKIIEQEG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 123 MDNA-----LYGIPKAVE---TLVLIYNKDLVDK-------PLDSLQAWLDYSKTQR-----EQNKYGLLAKFDQIYYSW 182
Cdd:cd13580  103 WDSAsvdgkIYGIPRKRPligRNGLWIRKDWLDKlglevpkTLDELYEVAKAFTEKDpdgngKKDTYGLTDTKDLIGSGF 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 183 GAIGP---MGGYIFAKNDSGGFNPqqvGLNTPGAVEAVTFLKKFYAEKV----FPAgilgDNGLNAIDSLFTEKKAAAVI 255
Cdd:cd13580  183 TGLFGafgAPPNNWWKDEDGKLVP---GSIQPEMKEALKFLKKLYKEGLidpeFAV----NDGTKANEKFISGKAGIFVG 255

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296182 256 NGPWAFQPYEAA-----GINYGVAPLPTLPDGK--PMSSFLGVKGYVVSTWSKDKALAQQFIEFINQPQYVK 320
Cdd:cd13580  256 NWWDPAWPQASLkkndpDAEWVAVPIPSGPDGKygVWAESGVNGFFVIPKKSKKPEAILKLLDFLSDPEVQK 327
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 46-358 1.79e-09

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


Pssm-ID: 270308 [Multi-domain]  Cd Length: 315  Bit Score: 58.40  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  46 VSDFEKQYNVKVNLQEmpYA---QQLEKLRLDGPAGIgpDVLVIPNDQLGGAVVQGLLSPLsvDQAKQDAFT---PASIN 119
Cdd:cd13590   16 LKAFEKETGVKVNYDT--YDsneEMLAKLRAGGGSGY--DLVVPSDYMVERLIKQGLLEPL--DHSKLPNLKnldPQFLN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 120 AFRMDNALYGIPKAVETLVLIYNKDLVDKPLDSlqaWLDYSKTQREQNKYGLLAKFDqiyyswgaigPMGGYIFAKNdsg 199
Cdd:cd13590   90 PPYDPGNRYSVPYQWGTTGIAYNKDKVKEPPTS---WDLDLWDPALKGRIAMLDDAR----------EVLGAALLAL--- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 200 GFNPqqvglNT--PGAV-EAVTFLKKFyaeKvfpAGILGDNGLNAIDSLFTEKKAAAVI-NGPWAFQPYEAAGINYgVAP 275
Cdd:cd13590  154 GYSP-----NTtdPAELaAAAELLIKQ---K---PNVRAFDSDSYVQDLASGEIWLAQAwSGDALQANRENPNLKF-VIP 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 276 LPTlpdgkpmsSFLGVKGYVVSTWSKDKALAQQFIEFINQPQYVKARYVATGEIPPLKAMID--DPVIKNDQKASAVAIQ 353
Cdd:cd13590  222 KEG--------GLLWVDNMAIPKGAPNPELAHAFINFLLDPEVAAKNAEYIGYATPNKAALEllPPELLDNPALYPPIEP 293


                 ....*
gi 490296182 354 SARAV 358
Cdd:cd13590  294 LAKLL 298
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 46-158 6.41e-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: 47.29  E-value: 6.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  46 VSDFEKQYNVKVNL------QEMpyaqqLEKLRldgpAGIG-PDVLVIPNDQLGGAVVQGLLSPLSVDQAK-QDAFTP-- 115
Cdd:cd13588   16 VTAFEEATGCKVVVkffgseDEM-----VAKLR----SGGGdYDVVTPSGDALLRLIAAGLVQPIDTSKIPnYANIDPrl 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 490296182 116 ASINAFRMDNALYGIPKAVETLVLIYNKDLVDKPLDSLQAWLD 158
Cdd:cd13588   87 RNLPWLTVDGKVYGVPYDWGANGLAYNTKKVKTPPTSWLALLW 129
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 46-158 1.08e-05

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 46.85  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  46 VSDFEKQYNVKVNLQEMPYAQQLEKLRLDGpAGIGPDVLVIPN-DQLGGAVVQGLLSPLSVDQAKQ--DAFTPAsinafr 122
Cdd:COG1840    2 LEAFEKKTGIKVNVVRGGSGELLARLKAEG-GNPPADVVWSGDaDALEQLANEGLLQPYKSPELDAipAEFRDP------ 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490296182 123 mDNALYGIpkAVETLVLIYNKDLVdKPLDSLQAWLD 158
Cdd:COG1840   75 -DGYWFGF--SVRARVIVYNTDLL-KELGVPKSWED 106
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 41-321 4.55e-05

The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270307 [Multi-domain]  Cd Length: 268  Bit Score: 44.91  E-value: 4.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  41 GIKTAVSD-FEKQYNVKVNLQEMPYAQQLEKLRLDGPAgIGPDVLVIPNDQLGGAVVQGLLSPL---SVDQAKQDAFTPA 116
Cdd:cd13589   14 AQRKAVIEpFEKETGIKVVYDTGTSADRLAKLQAQAGN-PQWDVVDLDDGDAARAIAEGLLEPLdysKIPNAAKDKAPAA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 117 SINafrmdnaLYGIPKAVETLVLIYNKDLVDKPLDSlQAWLDYSKTQreqnKYGLLAkfdqIYYSWgaiGPMGGYIFAKN 196
Cdd:cd13589   93 LKT-------GYGVGYTLYSTGIAYNTDKFKEPPTS-WWLADFWDVG----KFPGPR----ILNTS---GLALLEAALLA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 197 DSGGFNPqqvgLNTPGAVEAVTFLKkfyaekvfPAGILGDNGLNAIDSLFTEKKAAAVINGPWAFQPYEAAGINYGVapl 276
Cdd:cd13589  154 DGVDPYP----LDVDRAFAKLKELK--------PNVVTWWTSGAQLAQLLQSGEVDMAPAWNGRAQALIDAGAPVAF--- 218

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 490296182 277 pTLPDGkpmSSFLGVKGYVVSTWSKDKALAQQFIEFINQPQYVKA 321
Cdd:cd13589  219 -VWPKE---GAILGPDTLAIVKGAPNKELAMKFINFALSPEVQAA 259
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 45-318 6.99e-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: 44.75  E-value: 6.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182  45 AVSDFEKQYNVKVNLQEMPYAQQLEKLRLDGPAGIGPDVLVIPN--DQLGGAVVQGLLSPLS--VDQ-----AKQDAFTP 115
Cdd:cd13521   22 VAKEIEKLTNVKLEIVAVTAATSQQKLNLMLASGDLPDIVGADYlkDKFIAYGMEGAFLPLSkyIDQypnlkAFFKQHPD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 116 ASINAFRMDNALYGIP----KAVETLVLIYNKDLVD----KPLDSLQAWLDYSKTQREQ--NKYG-----LLAKFDQIYY 180
Cdd:cd13521  102 VLRASTASDGKIYLIPyeppKDVPNQGYFIRKDWLDklnlKTPKTLDELYNVLKAFKEKdpNGNGkadeiPFIDRDPLYG 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296182 181 SWGAIGPMGGYIFAKNDSGGFNPQQVGLNTPGAVEA----VTFLKKFYAEKVFPAGILgDNGLNAIDSLFTEKKAAAVIN 256
Cdd:cd13521  182 AFRLINSWGARSAGGSTDSDWYEDNGKFKHPFASEEykdgMKYMNKLYTEGLIDKESF-TQKDDQAEQKFSNGKLGGFTH 260

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296182 257 GPWA----FQPYEAAGIN-YGVAPLPTLPDGKP-----MSSFLGVKGYVVSTWSKDKALAQQFIEFINQPQY 318
Cdd:cd13521  261 NWFAsdnlFTAQLGKEKPmYILLPIAPAGNVKGrreedSPGYTGPDGVAISKKAKNPVAALKFFDWLASEEG 332
PRK10005 PRK10005
dihydroxyacetone kinase ADP-binding subunit DhaL;
355-408 1.50e-03

dihydroxyacetone kinase ADP-binding subunit DhaL;


Pssm-ID: 182192 [Multi-domain]  Cd Length: 210  Bit Score: 39.72  E-value: 1.50e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296182 355 ARAVAMPGIPEMGEVWGPANAALELSLTGKQAPQAALDNAVKQ--------ITMQIEAMQAS 408
Cdd:PRK10005 119 SRGKAEPGDKTMCDVWVPVVESLRQSSEQNLSVPAALNAAVSIaesaaqstITMQARKGRAS 180
 
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