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Conserved domains on  [gi|517053626|ref|WP_018242444|]
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MULTISPECIES: ABC transporter substrate-binding protein [Rhizobium]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 11447308)

ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of one or more from a variety of substrates including carbohydrates

Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
PubMed:  26517916|24638992|25750732|26517916
SCOP:  3000083
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 7-354 7.62e-50

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 172.92  E-value: 7.62e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626   7 ALLGLATAFVMSSALPNLAKADELTLCWAAWDPAN--ALVELSKDFTAKT-GTQMKFEFVPWTSYADRFLNELNShGKLC 83
Cdd:COG1653   10 AALALALAACGGGGSGAAAAAGKVTLTVWHTGGGEaaALEALIKEFEAEHpGIKVEVESVPYDDYRTKLLTALAA-GNAP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  84 DLIIGDSQWIGGSAENGHYVKLNDFFDKEGIKMDDFVPATVVGYsewpknTPN--YWALPAMGDVVGWTYRKDWFEKpel 161
Cdd:COG1653   89 DVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDAG------TYDgkLYGVPFNTDTLGLYYNKDLFEK--- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 162 qkefkakYGrdLAAPKTYDELKQIAEFFQKReidgKTVYGASIYTERGsegitMGVTNVLYDWGFQYENPkkpyDMEGFV 241
Cdd:COG1653  160 -------AG--LDPPKTWDELLAAAKKLKAK----DGVYGFALGGKDG-----AAWLDLLLSAGGDLYDE----DGKPAF 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 242 NSADAVKGLEFYKSLYD-CCTPPGSSNVYMVESADAFKSGQVAMQMNFAFTWPGLYKDEkvGGDRIGFFPNPAEKA---H 317
Cdd:COG1653  218 DSPEAVEALEFLKDLVKdGYVPPGALGTDWDDARAAFASGKAAMMINGSWALGALKDAA--PDFDVGVAPLPGGPGgkkP 295

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 517053626 318 FAQLGGQGISVVSYSDKRDAALQYIKWFAQPDVQAKW 354
Cdd:COG1653  296 ASVLGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQAKW 332
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 7-354 7.62e-50

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 172.92  E-value: 7.62e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626   7 ALLGLATAFVMSSALPNLAKADELTLCWAAWDPAN--ALVELSKDFTAKT-GTQMKFEFVPWTSYADRFLNELNShGKLC 83
Cdd:COG1653   10 AALALALAACGGGGSGAAAAAGKVTLTVWHTGGGEaaALEALIKEFEAEHpGIKVEVESVPYDDYRTKLLTALAA-GNAP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  84 DLIIGDSQWIGGSAENGHYVKLNDFFDKEGIKMDDFVPATVVGYsewpknTPN--YWALPAMGDVVGWTYRKDWFEKpel 161
Cdd:COG1653   89 DVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDAG------TYDgkLYGVPFNTDTLGLYYNKDLFEK--- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 162 qkefkakYGrdLAAPKTYDELKQIAEFFQKReidgKTVYGASIYTERGsegitMGVTNVLYDWGFQYENPkkpyDMEGFV 241
Cdd:COG1653  160 -------AG--LDPPKTWDELLAAAKKLKAK----DGVYGFALGGKDG-----AAWLDLLLSAGGDLYDE----DGKPAF 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 242 NSADAVKGLEFYKSLYD-CCTPPGSSNVYMVESADAFKSGQVAMQMNFAFTWPGLYKDEkvGGDRIGFFPNPAEKA---H 317
Cdd:COG1653  218 DSPEAVEALEFLKDLVKdGYVPPGALGTDWDDARAAFASGKAAMMINGSWALGALKDAA--PDFDVGVAPLPGGPGgkkP 295

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 517053626 318 FAQLGGQGISVVSYSDKRDAALQYIKWFAQPDVQAKW 354
Cdd:COG1653  296 ASVLGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQAKW 332
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 34-431 2.27e-39

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: 145.63  E-value: 2.27e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  34 WAAWDPANALVELSKDFTAK-TGTQMKFEFVPWTSYADRFLNELNShGKLCDLIIGDSQWIGGSAENGHYVKLNDFFDKE 112
Cdd:cd13585    7 WGQPAETAALKKLIDAFEKEnPGVKVEVVPVPYDDYWTKLTTAAAA-GTAPDVFYVDGPWVPEFASNGALLDLDDYIEKD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 113 GIkmDDFVPATVVGYSEWPKNtpnYWALPAMGDVVGWTYRKDWFEKpelqkefkakYGRDLAAPKTYDELKQIAEFFQKR 192
Cdd:cd13585   86 GL--DDDFPPGLLDAGTYDGK---LYGLPFDADTLVLFYNKDLFDK----------AGPGPKPPWTWDELLEAAKKLTDK 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 193 EIDgktVYGASIyteRGSEGITMGVTNVLYDWGFQY--ENPKKPYdmegfVNSADAVKGLEFYKSLYDCCTPPGSSNVYM 270
Cdd:cd13585  151 KGG---QYGFAL---RGGSGGQTQWYPFLWSNGGDLldEDDGKAT-----LNSPEAVEALQFYVDLYKDGVAPSSATTGG 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 271 VESADAFKSGQVAMQMNFAFTWPGlYKDEKVGGDrIGFFPNPAEKAH--FAQLGGQGISVVSYSDKRDAALQYIKWFAQP 348
Cdd:cd13585  220 DEAVDLFASGKVAMMIDGPWALGT-LKDSKVKFK-WGVAPLPAGPGGkrASVLGGWGLAISKNSKHPEAAWKFIKFLTSK 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 349 DVQAKWWELGGFSCLNSV--VNAPGFAKSQPYAQAFLDSMAIVKDFWAEPSYASLLQAMQKRVHNYVVAGNG-TAKEALD 425
Cdd:cd13585  298 ENQLKLGGAAGPAALAAAaaSAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGALGkSPEEALK 377


                 ....*.
gi 517053626 426 GLVKDW 431
Cdd:cd13585  378 EAAKEI 383
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 45-377 2.06e-15

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 76.29  E-value: 2.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626   45 ELSKDFTAKTGTQMKFEFVPWTSYADRFLNELNShGKLCDLII--GDSQWIGGSAENGHYVKLNDffDKEGIKMDDFVPA 122
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQASNDLQAKLLAAAAA-GNAPDLDVvwIAADQLATLAEAGLLADLSD--VDNLDDLPDALDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  123 tvvgyseWPKNTPNYWALPAMGDVVGWTYRKDWFEKpelqkefkakygrDLAAPKTYDELKQIAEffqkrEIDGKTVYGA 202
Cdd:pfam13416  78 -------AGYDGKLYGVPYAASTPTVLYYNKDLLKK-------------AGEDPKTWDELLAAAA-----KLKGKTGLTD 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  203 SiytergsegitmgvTNVLYDWGFQYENPKKPYDMEGFVNSADAvkgLEFYKSLYDcctppgssNVYMVES----ADAFK 278
Cdd:pfam13416 133 P--------------ATGWLLWALLADGVDLTDDGKGVEALDEA---LAYLKKLKD--------NGKVYNTgadaVQLFA 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  279 SGQVAMqmnfAFTWPGLYKDEKVGGDRIGF-FPNPAekahfAQLGGQGISVVSYSDKRD-AALQYIKWFAQPDVQAKWWE 356
Cdd:pfam13416 188 NGEVAM----TVNGTWAAAAAKKAGKKLGAvVPKDG-----SFLGGKGLVVPAGAKDPRlAALDFIKFLTSPENQAALAE 258

                         330       340
                  ....*....|....*....|.
gi 517053626  357 LGGFSCLNSVVNAPGFAKSQP 377
Cdd:pfam13416 259 DTGYIPANKSAALSDEVKADP 279
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 7-354 7.62e-50

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 172.92  E-value: 7.62e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626   7 ALLGLATAFVMSSALPNLAKADELTLCWAAWDPAN--ALVELSKDFTAKT-GTQMKFEFVPWTSYADRFLNELNShGKLC 83
Cdd:COG1653   10 AALALALAACGGGGSGAAAAAGKVTLTVWHTGGGEaaALEALIKEFEAEHpGIKVEVESVPYDDYRTKLLTALAA-GNAP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  84 DLIIGDSQWIGGSAENGHYVKLNDFFDKEGIKMDDFVPATVVGYsewpknTPN--YWALPAMGDVVGWTYRKDWFEKpel 161
Cdd:COG1653   89 DVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDAG------TYDgkLYGVPFNTDTLGLYYNKDLFEK--- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 162 qkefkakYGrdLAAPKTYDELKQIAEFFQKReidgKTVYGASIYTERGsegitMGVTNVLYDWGFQYENPkkpyDMEGFV 241
Cdd:COG1653  160 -------AG--LDPPKTWDELLAAAKKLKAK----DGVYGFALGGKDG-----AAWLDLLLSAGGDLYDE----DGKPAF 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 242 NSADAVKGLEFYKSLYD-CCTPPGSSNVYMVESADAFKSGQVAMQMNFAFTWPGLYKDEkvGGDRIGFFPNPAEKA---H 317
Cdd:COG1653  218 DSPEAVEALEFLKDLVKdGYVPPGALGTDWDDARAAFASGKAAMMINGSWALGALKDAA--PDFDVGVAPLPGGPGgkkP 295

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 517053626 318 FAQLGGQGISVVSYSDKRDAALQYIKWFAQPDVQAKW 354
Cdd:COG1653  296 ASVLGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQAKW 332
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 34-431 2.27e-39

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: 145.63  E-value: 2.27e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  34 WAAWDPANALVELSKDFTAK-TGTQMKFEFVPWTSYADRFLNELNShGKLCDLIIGDSQWIGGSAENGHYVKLNDFFDKE 112
Cdd:cd13585    7 WGQPAETAALKKLIDAFEKEnPGVKVEVVPVPYDDYWTKLTTAAAA-GTAPDVFYVDGPWVPEFASNGALLDLDDYIEKD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 113 GIkmDDFVPATVVGYSEWPKNtpnYWALPAMGDVVGWTYRKDWFEKpelqkefkakYGRDLAAPKTYDELKQIAEFFQKR 192
Cdd:cd13585   86 GL--DDDFPPGLLDAGTYDGK---LYGLPFDADTLVLFYNKDLFDK----------AGPGPKPPWTWDELLEAAKKLTDK 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 193 EIDgktVYGASIyteRGSEGITMGVTNVLYDWGFQY--ENPKKPYdmegfVNSADAVKGLEFYKSLYDCCTPPGSSNVYM 270
Cdd:cd13585  151 KGG---QYGFAL---RGGSGGQTQWYPFLWSNGGDLldEDDGKAT-----LNSPEAVEALQFYVDLYKDGVAPSSATTGG 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 271 VESADAFKSGQVAMQMNFAFTWPGlYKDEKVGGDrIGFFPNPAEKAH--FAQLGGQGISVVSYSDKRDAALQYIKWFAQP 348
Cdd:cd13585  220 DEAVDLFASGKVAMMIDGPWALGT-LKDSKVKFK-WGVAPLPAGPGGkrASVLGGWGLAISKNSKHPEAAWKFIKFLTSK 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 349 DVQAKWWELGGFSCLNSV--VNAPGFAKSQPYAQAFLDSMAIVKDFWAEPSYASLLQAMQKRVHNYVVAGNG-TAKEALD 425
Cdd:cd13585  298 ENQLKLGGAAGPAALAAAaaSAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGALGkSPEEALK 377


                 ....*.
gi 517053626 426 GLVKDW 431
Cdd:cd13585  378 EAAKEI 383
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-437 1.65e-34

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 132.77  E-value: 1.65e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626   1 MQKTSKALLGLATAFVM-----------SSALPNLAKADELTLcWAAWDPANALVELSKDFTAKTGTQMKFEFVPWTSYA 69
Cdd:COG2182    1 MKRRLLAALALALALALalaacgsgsssSGSSSAAGAGGTLTV-WVDDDEAEALEEAAAAFEEEPGIKVKVVEVPWDDLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  70 DRFLNELNShGKLCDLIIGDSQWIGGSAENGHYVKLNDFFDKEgikmDDFVPATV--VGYSEwpkntpNYWALPAMGDVV 147
Cdd:COG2182   80 EKLTTAAPA-GKGPDVFVGAHDWLGELAEAGLLAPLDDDLADK----DDFLPAALdaVTYDG------KLYGVPYAVETL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 148 GWTYRKDWFEKpelqkefkakygrdlAAPKTYDELKQIAEFFqkreidgktvygasiyTERGSEGITMGVTNVLYDWGFQ 227
Cdd:COG2182  149 ALYYNKDLVKA---------------EPPKTWDELIAAAKKL----------------TAAGKYGLAYDAGDAYYFYPFL 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 228 Y--------ENPKKPYDMEgfVNSADAVKGLEFYKSLYDcctppgssNVYMVESAD------AFKSGQVAMqmnfAFTWP 293
Cdd:COG2182  198 AafggylfgKDGDDPKDVG--LNSPGAVAALEYLKDLIK--------DGVLPADADydaadaLFAEGKAAM----IINGP 263

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 294 GLYKD-EKVGGDRIGFFPNPAEK-----AHFaqLGGQGISVVSYSDKRDAALQYIKWFAQPDVQAKWWELGGF-SCLNSV 366
Cdd:COG2182  264 WAAADlKKALGIDYGVAPLPTLAggkpaKPF--VGVKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALFEATGRiPANKAA 341

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517053626 367 VNAPGFaKSQPYAQAFLDSMAIVKDFWAEPSYASLLQAMQKRVHNyVVAGNGTAKEALDGLVKDWSDVFKD 437
Cdd:COG2182  342 AEDAEV-KADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQA-IASGKADPAEALDAAQKQIEAAIAQ 410
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 45-425 2.05e-32

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: 126.64  E-value: 2.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  45 ELSKDFTAKTGtQMKFEFVPWTSYADRFLNELNSH----GKLCDLIIGDSQWIGGSAENGHYVKLNDFFDKEGIkmDDFV 120
Cdd:cd14750   18 KAIAAFEKKHP-DIKVEIEELPASSDDQRQQLVTAlaagSSAPDVLGLDVIWIPEFAEAGWLLPLTEYLKEEED--DDFL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 121 PATVvgysEWPKNTPNYWALPAMGDVVGWTYRKDWFEKPELQkefkakygrdlaAPKTYDELKQIAEFFQKRE--IDGKT 198
Cdd:cd14750   95 PATV----EANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPE------------PPKTWDELLEAAKKRKAGEpgIWGYV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 199 VYGASIytergsEGItmgVTNVL-YDWGF---QYENPKKpydmEGFVNSADAVKGLEFYKSLYDCCTPPGSSNVYMVESA 274
Cdd:cd14750  159 FQGKQY------EGL---VCNFLeLLWSNggdIFDDDSG----KVTVDSPEALEALQFLRDLIGEGISPKGVLTYGEEEA 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 275 -DAFKSGQVAMQMNFAFTWPGLYKDEKVGGDRIGFFPNPA--EKAHFAQLGGQGISVVSYSDKRDAALQYIKWFAQPDVQ 351
Cdd:cd14750  226 rAAFQAGKAAFMRNWPYAYALLQGPESAVAGKVGVAPLPAgpGGGSASTLGGWNLAISANSKHKEAAWEFVKFLTSPEVQ 305

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517053626 352 AKWWELGGFSCLN-SVVNAPGFAKSQPYAQAFLDSMAIVKDFWAEPSYASLLQAMQKRVHNyVVAGNGTAKEALD 425
Cdd:cd14750  306 KRRAINGGLPPTRrALYDDPEVLEAYPFLPALLEALENAVPRPVTPKYPEVSTAIQIALSA-ALSGQATPEEALK 379
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 29-429 1.44e-31

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: 124.33  E-value: 1.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  29 ELTLcWAAW--DPANALVELSKDFTAK-TGTQMKFEFVPW-TSYADRFLNELNShGKLCDLIIGDSQWIGGSAENGHYVK 104
Cdd:cd14748    1 EITF-WHGMsgPDGKALEELVDEFNKShPDIKVKAVYQGSyDDTLTKLLAALAA-GTAPDVAQVDASWVAQLADSGALEP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 105 LNDFFDKEGIKMDDFVPATVVGYSEWPKntpnYWALPAMGDVVGWTYRKDWFEKpelqkefkakYGRD-LAAPKTYDELK 183
Cdd:cd14748   79 LDDYIDKDGVDDDDFYPAALDAGTYDGK----LYGLPFDTSTPVLYYNKDLFEE----------AGLDpEKPPKTWDELE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 184 QIAEFFqKREIDGKTVYGASIYTERGSegitmgvtNVLYDWGFQY------ENPKKPYdmegfVNSADAVKGLEFYKSLY 257
Cdd:cd14748  145 EAAKKL-KDKGGKTGRYGFALPPGDGG--------WTFQALLWQNggdlldEDGGKVT-----FNSPEGVEALEFLVDLV 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 258 dccTPPGSSNVYMVESA-DAFKSGQVAMQMNFAFTWPGL---YKDEKVGgdrIGFFPNPAEKAHFAQLGGQGISVVSYSD 333
Cdd:cd14748  211 ---GKDGVSPLNDWGDAqDAFISGKVAMTINGTWSLAGIrdkGAGFEYG---VAPLPAGKGKKGATPAGGASLVIPKGSS 284

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 334 KR-DAALQYIKWFAQPDVQAKWWELGG-FSCLNSVVNAPG-FAKSQPYAQAFLDSMAIVK-DFWAEPSYASLLQAMQKRV 409
Cdd:cd14748  285 KKkEAAWEFIKFLTSPENQAKWAKATGyLPVRKSAAEDPEeFLAENPNYKVAVDQLDYAKpWGPPVPNGAEIRDELNEAL 364

                        410       420
                 ....*....|....*....|
gi 517053626 410 hNYVVAGNGTAKEALDGLVK 429
Cdd:cd14748  365 -EAALLGKKTPEEALKEAQE 383
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 34-425 3.69e-24

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: 103.16  E-value: 3.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  34 WAAWDPANALV--ELSKDFTAKT-GTQMKFEFVPWTSYADRFLNELNShGKLCDLIIGDSQWIGGSAENGHYVKLNDFFD 110
Cdd:cd14747    5 WAMGNSAEAELlkELADEFEKENpGIEVKVQVLPWGDAHTKITTAAAS-GDGPDVVQLGNTWVAEFAAMGALEDLTPYLE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 111 KEGIkMDDFVPATV--VGYSEwpkntpNYWALPAMGDVVGWTYRKDWFEKpelqkefkakyGRDLAAPKTYDELKQIAEf 188
Cdd:cd14747   84 DLGG-DKDLFPGLVdtGTVDG------KYYGVPWYADTRALFYRTDLLKK-----------AGGDEAPKTWDELEAAAK- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 189 fqKREIDGKTVYGASIYterGSEGITMGVTNVLYDWGFQYENPKKpydMEGFVNSADAVKGLEFYKSLYDCCTPPGSSNV 268
Cdd:cd14747  145 --KIKADGPDVSGFAIP---GKNDVWHNALPFVWGAGGDLATKDK---WKATLDSPEAVAGLEFYTSLYQKGLSPKSTLE 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 269 YMVESADAFKSGQVAMQMNFAFTWPGLYKDEKVGGDRIGFFPNPA--EKAHFAQLGGQGISVVSYSDKRDAALQYIKWFA 346
Cdd:cd14747  217 NSADVEQAFANGKVAMIISGPWEIGAIREAGPDLAGKWGVAPLPGgpGGGSPSFAGGSNLAVFKGSKNKDLAWKFIEFLS 296

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517053626 347 QPDVQAKWWELGGFSCLNSVVNAPGFAKSQPYAQAFLDSMAIVKDFWAEPSYASLLQAMQKRVHNYVVAGNGTAKEALD 425
Cdd:cd14747  297 SPENQAAYAKATGMLPANTSAWDDPSLANDPLLAVFAEQLKTGKATPATPEWGEIEAELVLVLEEVWIGVGADVEDALD 375
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 38-431 1.61e-21

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: 95.44  E-value: 1.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  38 DPANALVELSKDFTAKTGTQMKFEFVPwTSYADRFLNELNSHGKLCDLIIGDSQWIGGSAENGHYVKLNDFFDKEGIKMD 117
Cdd:cd13586   10 GELEYLKELAEEFEKKYGIKVEVVYVD-SGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLAVKIKNLP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 118 DFVPATVVGysewpkntPNYWALPAMGDVVGWTYRKDWFEKPelqkefkakygrdlaaPKTYDELKQIAEFFQKREIDGK 197
Cdd:cd13586   89 VALAAVTYN--------GKLYGVPVSVETIALFYNKDLVPEP----------------PKTWEELIALAKKFNDKAGGKY 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 198 tvygasiytergseGITMGVTNVLYDWGFQYENPKKPYDMEGF------VNSADAVKGLEFYKSLYDCCTPPGSSNVYMV 271
Cdd:cd13586  145 --------------GFAYDQTNPYFSYPFLAAFGGYVFGENGGdptdigLNNEGAVKGLKFIKDLKKKYKVLPPDLDYDI 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 272 ESAdAFKSGQVAMQMNFAFTWPGlYKDEKV--GGDRIGFFPNPAEKAHFaqLGGQGISVVSYSDKRDAALQYIKWFAQPD 349
Cdd:cd13586  211 ADA-LFKEGKAAMIINGPWDLAD-YKDAGInfGVAPLPTLPGGKQAAPF--VGVQGAFVSAYSKNKEAAVEFAEYLTSDE 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 350 VQAKWWELGGF-SCLNSVVNAPGFAKSqPYAQAFLDSMAIVKDFWAEPSYASLLQAMqKRVHNYVVAGNGTAKEALDGLV 428
Cdd:cd13586  287 AQLLLFEKTGRiPALKDALNDAAVKND-PLVKAFAEQAQYGVPMPNIPEMAAVWDAM-GNALNLVASGKATPEEAAKDAV 364


                 ...
gi 517053626 429 KDW 431
Cdd:cd13586  365 AAI 367
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 55-431 7.27e-18

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: 84.74  E-value: 7.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  55 GTQMKFEFVPWTSYADRFLNELNShGKLCDLIIGDSQWIGGSAENGHYVKLNDFFDKEGIKmdDFVPatvvGYSEWPKNT 134
Cdd:cd14751   29 KIKVKAVRVPFDGLHNQIKTAAAG-GQAPDVMRADIAWVPEFAKLGYLQPLDGTPAFDDIV--DYLP----GPMETNRYN 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 135 PNYWALPAMGDVVGWTYRKDWFEKpelqkefkAKygrdLAAPKTYDELKQIAeffqKREIDGKTVYGasiYTERGSEGit 214
Cdd:cd14751  102 GHYYGVPQVTNTLALFYNKRLLEE--------AG----TEVPKTMDELVAAA----KAIKKKKGRYG---LYISGDGP-- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 215 MGVTNVLYDWGFQYENPKKpydMEGFVNSADAVKGLEFYKSLYDCCTPPGSSNVYMVESADAFKSGQVAMQMNfaftWPG 294
Cdd:cd14751  161 YWLLPFLWSFGGDLTDEKK---ATGYLNSPESVRALETIVDLYDEGAITPCASGGYPNMQDGFKSGRYAMIVN----GPW 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 295 LYKDEKVG-----GDRIGFFPNPAEKA-HFAQLGGQGISVVSYSDKRDAALQYIKWFAQPDVQAKwwELGGFSCL---NS 365
Cdd:cd14751  234 AYADILGGkefkdPDNLGIAPVPAGPGgSGSPVGGEDLVIFKGSKNKDAAWKFVKFMSSAEAQAL--TAAKLGLLptrTS 311

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517053626 366 VVNAPGFAKSqPYAQAFLDSmaiVKDFWAEPS-------YASLLQAMQKrvhnyVVAGNGTAKEALDGLVKDW 431
Cdd:cd14751  312 AYESPEVANN-PMVAAFKPA---LETAVPRPPipewgelFEPLTLAFAK-----VLRGEKSPREALDEAAKQW 375
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 45-427 1.43e-17

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: 83.97  E-value: 1.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  45 ELSKDFTAKT-GTQMKFEFVPWTSYADRFlNELNSHGKLCDLI-IGDSQWIGGSAENGHYVKLNDFFDKEGIKmDDFVPA 122
Cdd:cd14749   19 ELIADFEKENpNIKVKVVVFPYDNYKTKL-KTAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPLTDYLDPNGVD-KRFLPG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 123 TVVGYSewpKNTpNYWALPAMGDVVGWTYRKDWFEKpelqkefkakYGRDlAAPKTYDELKQIAEffqKREIDGKTVYGa 202
Cdd:cd14749   97 LADAVT---FNG-KVYGIPFAARALALFYNKDLFEE----------AGGV-KPPKTWDELIEAAK---KDKFKAKGQTG- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 203 siYTERGSEGITMGVTNVL-----YDWGFQYENPKKPYDMEGFVnsadavKGLEFYKSL-YDCCTPPGSSNVYMVESADA 276
Cdd:cd14749  158 --FGLLLGAQGGHWYFQYLvrqagGGPLSDDGSGKATFNDPAFV------QALQKLQDLvKAGAFQEGFEGIDYDDAGQA 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 277 FKSGQVAMqmNFAFTWP-GLYKDEKVGGDrIGFFPNP--AEKAHFAQLGGQ--GISVVSYSDKRDAALQYIKWFAQPDVQ 351
Cdd:cd14749  230 FAQGKAAM--NIGGSWDlGAIKAGEPGGK-IGVFPFPtvGKGAQTSTIGGSdwAIAISANGKKKEAAVKFLKYLTSPEVM 306

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517053626 352 AKWWELGG-FSCLNSVVNAPGFAKSQPYAqAFLDSMAIVK-DFWAEPSYASLLQAMQKRVhNYVVAGNGTAKEALDGL 427
Cdd:cd14749  307 KQYLEDVGlLPAKEVVAKDEDPDPVAILG-PFADVLNAAGsTPFLDEYWPAAAQVHKDAV-QKLLTGKIDPEQVVKQA 382
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 45-377 2.06e-15

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 76.29  E-value: 2.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626   45 ELSKDFTAKTGTQMKFEFVPWTSYADRFLNELNShGKLCDLII--GDSQWIGGSAENGHYVKLNDffDKEGIKMDDFVPA 122
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQASNDLQAKLLAAAAA-GNAPDLDVvwIAADQLATLAEAGLLADLSD--VDNLDDLPDALDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  123 tvvgyseWPKNTPNYWALPAMGDVVGWTYRKDWFEKpelqkefkakygrDLAAPKTYDELKQIAEffqkrEIDGKTVYGA 202
Cdd:pfam13416  78 -------AGYDGKLYGVPYAASTPTVLYYNKDLLKK-------------AGEDPKTWDELLAAAA-----KLKGKTGLTD 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  203 SiytergsegitmgvTNVLYDWGFQYENPKKPYDMEGFVNSADAvkgLEFYKSLYDcctppgssNVYMVES----ADAFK 278
Cdd:pfam13416 133 P--------------ATGWLLWALLADGVDLTDDGKGVEALDEA---LAYLKKLKD--------NGKVYNTgadaVQLFA 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  279 SGQVAMqmnfAFTWPGLYKDEKVGGDRIGF-FPNPAekahfAQLGGQGISVVSYSDKRD-AALQYIKWFAQPDVQAKWWE 356
Cdd:pfam13416 188 NGEVAM----TVNGTWAAAAAKKAGKKLGAvVPKDG-----SFLGGKGLVVPAGAKDPRlAALDFIKFLTSPENQAALAE 258

                         330       340
                  ....*....|....*....|.
gi 517053626  357 LGGFSCLNSVVNAPGFAKSQP 377
Cdd:pfam13416 259 DTGYIPANKSAALSDEVKADP 279
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 39-352 2.33e-15

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: 76.30  E-value: 2.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626   39 PANALVELSKDFTAK-TGTQMKFEFVPWTSYADRFLNELNSHGKLCDLIIGDSQWIGGSAENGHYVKLNDFFDKEGIKMD 117
Cdd:pfam01547   6 EAAALQALVKEFEKEhPGIKVEVESVGSGSLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYLVLGV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  118 dfvpatvvgysewpkntPNYWALPAMGDVVGWTYRKDWFEKPELQkefkakygrdlaAPKTYDELKQIAeffqkREIDGK 197
Cdd:pfam01547  86 -----------------PKLYGVPLAAETLGLIYNKDLFKKAGLD------------PPKTWDELLEAA-----KKLKEK 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  198 TVYGASIYteRGSEGITMGVTNVLYDWGF---QYENPKKPYDMEGFVNSADAVKGLEFYKSLYDCCTPPGSSNVYMVESA 274
Cdd:pfam01547 132 GKSPGGAG--GGDASGTLGYFTLALLASLggpLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREAL 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  275 DAFKSGQVAMQMNFAFTWPGLYKDEKVGGDR---------IGFFPNPAEKAhfAQLGGQGISVVSYSDKRDAALQYIKWF 345
Cdd:pfam01547 210 ALFEQGKAAMGIVGPWAALAANKVKLKVAFAapapdpkgdVGYAPLPAGKG--GKGGGYGLAIPKGSKNKEAAKKFLDFL 287


                  ....*..
gi 517053626  346 AQPDVQA 352
Cdd:pfam01547 288 TSPEAQA 294
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 29-353 5.32e-15

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: 75.88  E-value: 5.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  29 ELTLcWAAWDPA--NALVELSKDFTAKTG-TQMKFEFVPWTSYADRFLNELnSHGKLCDLIIGDSQWIGGSAENGHYVKL 105
Cdd:cd13657    1 TITI-WHALTGAeeDALQQIIDEFEAKYPvPNVKVPFEKKPDLQNKLLTAI-PAGEGPDLFIWAHDWIGQFAEAGLLVPI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 106 NDFFDKEgiKMDDFVPATVvgysewpkNTPNY----WALPAMGDVVGWTYRKDWFEKPelqkefkakygrdlaaPKTYDE 181
Cdd:cd13657   79 SDYLSED--DFENYLPTAV--------EAVTYkgkvYGLPEAYETVALIYNKALVDQP----------------PETTDE 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 182 LKQIAEFFQKReidgktvygasiytERGSEGITMGVTNVLYDWGFQY--------ENPKKPYdmegfVNSADAVKGLEFY 253
Cdd:cd13657  133 LLAIMKDHTDP--------------AAGSYGLAYQVSDAYFVSAWIFgfggyyfdDETDKPG-----LDTPETIKGIQFL 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 254 KSLYDCCTPPGSSNVYMVesaDAFKSGQVAMqmnfAFTWPGLYKDEKVGGDRIGFFPNPAEKAHFAQ---LGGQGISVVS 330
Cdd:cd13657  194 KDFSWPYMPSDPSYNTQT---SLFNEGKAAM----IINGPWFIGGIKAAGIDLGVAPLPTVDGTNPPrpySGVEGIYVTK 266

                        330       340
                 ....*....|....*....|....*
gi 517053626 331 YSD--KRDAALQYIKWFAQPDVQAK 353
Cdd:cd13657  267 YAErkNKEAALDFAKFFTTAEASKI 291
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 72-429 4.59e-13

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: 70.13  E-value: 4.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  72 FLNELNSHGKLCDLIIGDSQWIGGSAENGHYVKLNDFFDKEGIKMDDFVPATVVGYSewpkntpnYWALPAMGDVVGWTY 151
Cdd:cd13522   45 FFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDEYVSKSGKYAPNTIAAMKLNGK--------LYGVPVSVGAHLMYY 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 152 RKDWFEKPelqkefkakygrdlaAPKTYDELKQIAEffqkreidGKTVYGASiytergseGITMGVTNVLYDWGFQYENP 231
Cdd:cd13522  117 NKKLVPKN---------------PPKTWQELIALAQ--------GLKAKNVW--------GLVYNQNEPYFFAAWIGGFG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 232 KKPYDMEGF-----VNSADAVKGLEFYKSLYDC--CTPPgSSNVYMVESAdaFKSGQVAMQMNFAFTWpGLYkDEKVGGD 304
Cdd:cd13522  166 GQVFKANNGknnptLDTPGAVEALQFLVDLKSKykIMPP-ETDYSIADAL--FKAGKAAMIINGPWDL-GDY-RQALKIN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 305 ----RIGFFPNPAEKAHFaqLGGQGISVVSYSDKRDAALQYIKWFAQPDVQAKWWE-LGGFSCLNSVVNAPgFAKSQPYA 379
Cdd:cd13522  241 lgvaPLPTFSGTKHAAPF--VGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDdAGDIPANLQAYESP-AVQNKPAQ 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 517053626 380 QAFLDSMAIVKDFWAEPSYASLLQAMQKRVhNYVVAGNGTAKEALDGLVK 429
Cdd:cd13522  318 KASAEQAAYGVPMPNIPEMRAVWDAFRIAV-NSVLAGKVTPEAAAKDAQQ 366
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 53-351 2.01e-11

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: 65.43  E-value: 2.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  53 KTGTQMKFEFVPWTSYADRFLNELNShGKLCDLI-IGDSQWIGGSAENGHYVKLNDFFDKegiKMDDFvpATVVGYSEWP 131
Cdd:cd13580   31 KTNIDVKVKWVPDSSYDEKLNLALAS-GDLPDIVvVNDPQLSITLVKQGALWDLTDYLDK---YYPNL--KKIIEQEGWD 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 132 KNTPN--YWALP---AMGDVVGWTYRKDWFEKPELQkefkakygrdlaAPKTYDELKQIAEFFQKREIDG---------- 196
Cdd:cd13580  105 SASVDgkIYGIPrkrPLIGRNGLWIRKDWLDKLGLE------------VPKTLDELYEVAKAFTEKDPDGngkkdtyglt 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 197 --KTVYGASIYTERGSEGITMGVTNVLYDWGFQYenpkkpydmeGFVNsaDAVK-GLEFYKSLYDcctppgssNVYM--- 270
Cdd:cd13580  173 dtKDLIGSGFTGLFGAFGAPPNNWWKDEDGKLVP----------GSIQ--PEMKeALKFLKKLYK--------EGLIdpe 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 271 ------VESADAFKSGQVAM---QMNFAFTWPGLYKDEKVGGD--RIGFFPNPAEKAHF-AQLGGQGISVVSY-SDKRDA 337
Cdd:cd13580  233 favndgTKANEKFISGKAGIfvgNWWDPAWPQASLKKNDPDAEwvAVPIPSGPDGKYGVwAESGVNGFFVIPKkSKKPEA 312

                        330
                 ....*....|....
gi 517053626 338 ALQYIKWFAQPDVQ 351
Cdd:cd13580  313 ILKLLDFLSDPEVQ 326
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 45-430 1.22e-07

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: 53.26  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  45 ELSKDFTAKTGTQMKFEFVPWTSYADRfLNELNSHGKLCDLIIGDSQWIGGSAENGHY--VKLNDffdkegIKMDDFVPA 122
Cdd:cd13658   17 KIAKQYTKKTGVKVKLVEVDQLDQLEK-LSLDGPAGKGPDVMVAPHDRIGSAVLQGLLspIKLSK------DKKKGFTDQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 123 TVvgysewpkNTPNY----WALPAMGDVVGWTYRKDwfekpeLQKEfkakygrdlaAPKTYDELKQIAEFFQKReidgkt 198
Cdd:cd13658   90 AL--------KALTYdgklYGLPAAVETLALYYNKD------LVKN----------APKTFDELEALAKDLTKE------ 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 199 vygasiytERGSEGITMGVTNVLYDWGF----------QYENPKKPYDMEgfVNSADAVKGLEFYKSLYDCCTPPGSSNV 268
Cdd:cd13658  140 --------KGKQYGFLADATNFYYSYGLlagnggyifkKNGSDLDINDIG--LNSPGAVKAVKFLKKWYTEGYLPKGMTG 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 269 YMVESadAFKSGQVAMQMNFAFTWPGlYKDEKV--GGDRIGFFPNPAEKAHFaqLGGQGISVVSYSDKRDAALQYIKWFA 346
Cdd:cd13658  210 DVIQG--LFKEGKAAAVIDGPWAIQE-YQEAGVnyGVAPLPTLPNGKPMAPF--LGVKGWYLSAYSKHKEWAQKFMEFLT 284

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 347 QPDVQAKWW-ELGGFSCLNSVVNAPGFaKSQPYAQAF------------LDSMAIVkdfWaEPSyasllqamqKRVHNYV 413
Cdd:cd13658  285 SKENLKKRYdETNEIPPRKDVRSDPEI-KNNPLTSAFakqasravpmpnIPEMGAV---W-EPA---------NNALFFI 350

                        410
                 ....*....|....*..
gi 517053626 414 VAGNGTAKEALDGLVKD 430
Cdd:cd13658  351 LSGKKTPKQALNDAVND 367
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
3-364 5.58e-07

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 51.45  E-value: 5.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626   3 KTSKALLGLATAFVMSSALPNLAKADELT-LCWA-AWDPanalvELSKDFTAKTGtqMKFEFVPWTSYADRFlNELNSHG 80
Cdd:COG0687    4 RSLLGLAAAALAAALAGGAPAAAAEGTLNvYNWGgYIDP-----DVLEPFEKETG--IKVVYDTYDSNEEML-AKLRAGG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  81 KLCDLIIGDSQWIGGSAENGHYVKLndffDKEGIKMDDFVPATVVGYSEWPKNTpnyWALPAMGDVVGWTYRKDWFEKPe 160
Cdd:COG0687   76 SGYDVVVPSDYFVARLIKAGLLQPL----DKSKLPNLANLDPRFKDPPFDPGNV---YGVPYTWGTTGIAYNTDKVKEP- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 161 lqkefkakygrdlaaPKTYDELkqiaefFQKrEIDGKTVYgasiyteRGSEGITMGVTnvLYDWGFQYeNPKKPYDMEGF 240
Cdd:COG0687  148 ---------------PTSWADL------WDP-EYKGKVAL-------LDDPREVLGAA--LLYLGYDP-NSTDPADLDAA 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 241 VNSADAVKG--LEFYKSlydcctppgssnvyMVESADAFKSGQVAMQMnfafTWPGLYKDEKVGGDRIGFFPnPAEKahf 318
Cdd:COG0687  196 FELLIELKPnvRAFWSD--------------GAEYIQLLASGEVDLAV----GWSGDALALRAEGPPIAYVI-PKEG--- 253

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 517053626 319 AQLGGQGISVVSYSDKRDAALQYIKWFAQPDVQAKWWELGGFSCLN 364
Cdd:COG0687  254 ALLWFDNMAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPN 299
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 29-354 1.82e-06

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


Pssm-ID: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 50.05  E-value: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  29 ELTLCWAAWDPANALVE----LSKDFTAKTGTQMKFEFVPWTSYADRfLNELNSHGKLCDLIIG-----DSQWIGGsaen 99
Cdd:cd13583    1 PLTLSMMYRDHPNYPVKddwlIWKEIEEKTNVKFKRTPIPSSDYETK-RSLLIASGDAPDIIPVlypgeENEFVAS---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 100 GHYVKLNDFFD----------KEGIKMDDfvpATVVGYSEWPKNTPNYWALPAMGdvVGWTYRKDWFEKpelqkefkakY 169
Cdd:cd13583   76 GALLPISDYLDympnykkyveKWGLGKEL---ATGRQSDGKYYSLPGLHEDPGVQ--YSFLYRKDIFEK----------A 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 170 GrdLAAPKTYDELKQIAEFFQkrEIDGKTVYgasiYTERGSEGITMGVTNVLYD----WGFQYENpkkpYDMEG-----F 240
Cdd:cd13583  141 G--IKIPTTWDEFYAALKKLK--EKYPDSYP----YSDRWNSNALLLIAAPAFGttagWGFSNYT----YDPDTdkfvyG 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 241 VNSADAVKGLEFYKSLY-DCCTPPGssnvYMVESADAFKSGQVAMQMNFAFTWPG-----LYKDEKVGGD-----RIGFF 309
Cdd:cd13583  209 ATTDEYKDMLQYFNKLYaEGLLDPE----SFTQTDDQAKAKFLNGKSFVITTNPQtvdelQRNLRAADGGnyevvSITPP 284

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 517053626 310 PNPAEKAHFAQLGGQGI---SVVSYSDKRDAALQYIKWFAQPDVQ--AKW 354
Cdd:cd13583  285 AGPAGKAINGSRLENGFmisSKAKDSKNFEALLQFLDWLYSDEGQelATW 334
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 272-361 2.60e-03

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: 39.52  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 272 ESADAFKSGQVAMqmnfAFTWPGLYKDEKVGGDRIGFFPNpaekAHFAQLGGQGISVVSYSDKRDAALQYIKWFAQPDVQ 351
Cdd:cd13589  186 QLAQLLQSGEVDM----APAWNGRAQALIDAGAPVAFVWP----KEGAILGPDTLAIVKGAPNKELAMKFINFALSPEVQ 257

                         90
                 ....*....|
gi 517053626 352 AKWWELGGFS 361
Cdd:cd13589  258 AALAEALGYG 267
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 37-196 3.16e-03

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: 39.75  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  37 WDPANALVelSKDFTAKTGTQMKFEFVPWTSYADRFlNELNSHGKLCDLIIGD--SQWIGGSAENGHYVKLNDFFDKeGI 114
Cdd:cd13521   15 VDDENWPV--AKEIEKLTNVKLEIVAVTAATSQQKL-NLMLASGDLPDIVGADylKDKFIAYGMEGAFLPLSKYIDQ-YP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 115 KMDDFVPATVVGYSEWPKNTPNYWALPAMGDVVGWTY----RKDWFEKPELQKefkakygrdlaaPKTYDELKQIAEFFQ 190
Cdd:cd13521   91 NLKAFFKQHPDVLRASTASDGKIYLIPYEPPKDVPNQgyfiRKDWLDKLNLKT------------PKTLDELYNVLKAFK 158


                 ....*.
gi 517053626 191 KREIDG 196
Cdd:cd13521  159 EKDPNG 164
PBP2_AlgQ1_2 cd13584
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 ...
 38-196 3.98e-03

Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 periplasmic binding fold; This group represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria such as Sphingomonas sp. A1. 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 includes 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: 270302 [Multi-domain]  Cd Length: 481  Bit Score: 39.34  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626  38 DPANALVELSKDFTAKTGTQMKFEFVPWTSYADRFLNELNSHGKLCDLIIGDsqWIGGS------AENGHYVKLNDFFDK 111
Cdd:cd13584   14 WPNDNDLPVYKEMERKTNVKLNFVANPVAQNSQEQFNLMMASGQLPDIIGGD--WLKDKggfekyGEDGAFLPLNDLIDQ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053626 112 EGIKMDDFVPAtvvgYSEWPK--NTP--NYWALPAM--GDVV----GWTYRKDWFEKPELQkefkakygrdlaAPKTYDE 181
Cdd:cd13584   92 YAPNLKKFLDE----HPDVKKaiTTDdgNIYGFPYLpdGDVAkearGYFIRKDWLDKLGLK------------TPSTIDE 155

                        170
                 ....*....|....*
gi 517053626 182 LKQIAEFFQKREIDG 196
Cdd:cd13584  156 WYTVLKAFKERDPNG 170
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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