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Conserved domains on  [gi|2087804054|ref|WP_222288470|]
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ABC transporter substrate-binding protein, partial [Rhizobium leguminosarum]

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
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 ...
1-336 9.56e-43

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 152.12  E-value: 9.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054   1 MNKFLSSAAVAVVMMA----GLSAAHAADVKEVQMLHWWTSGGEAAALNVLKQDLSKE--GFAWKDVPVaggGGDAAMTA 74
Cdd:COG1653     1 MRRLALALAAALALALaacgGGGSGAAAAAGKVTLTVWHTGGGEAAALEALIKEFEAEhpGIKVEVESV---PYDDYRTK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  75 LKAMVAAGTYPTASQMLGYTVLDYAQAGVMGDLTETAKKEGWDKS-VPAALQKFSVYDGKWVAAPVNVHSVNwLWINKAV 153
Cdd:COG1653    78 LLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDdFLPGALDAGTYDGKLYGVPFNTDTLG-LYYNKDL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 154 MDKIGGTEPKTFDELIALLDKAKA-AGVIPLALGGQNWQEATMFdsivLSTGGPEFYkkafNDLDDESLKSDTMKKSFDN 232
Cdd:COG1653   157 FEKAGLDPPKTWDELLAAAKKLKAkDGVYGFALGGKDGAAWLDL----LLSAGGDLY----DEDGKPAFDSPEAVEALEF 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 233 LATIIK--YVDPNFSGRDWNLATAMVIKGDALVQVMGDWAKGEFVAAKktPDTDFLCYRFPGTDG----SVVYNSDMFGM 306
Cdd:COG1653   229 LKDLVKdgYVPPGALGTDWDDARAAFASGKAAMMINGSWALGALKDAA--PDFDVGVAPLPGGPGgkkpASVLGGSGLAI 306
                         330       340       350
                  ....*....|....*....|....*....|
gi 2087804054 307 FNVPDDRKAAqVALATATLSKSFQSAFNVV 336
Cdd:COG1653   307 PKGSKNPEAA-WKFLKFLTSPEAQAKWDAL 335
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
1-336 9.56e-43

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 152.12  E-value: 9.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054   1 MNKFLSSAAVAVVMMA----GLSAAHAADVKEVQMLHWWTSGGEAAALNVLKQDLSKE--GFAWKDVPVaggGGDAAMTA 74
Cdd:COG1653     1 MRRLALALAAALALALaacgGGGSGAAAAAGKVTLTVWHTGGGEAAALEALIKEFEAEhpGIKVEVESV---PYDDYRTK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  75 LKAMVAAGTYPTASQMLGYTVLDYAQAGVMGDLTETAKKEGWDKS-VPAALQKFSVYDGKWVAAPVNVHSVNwLWINKAV 153
Cdd:COG1653    78 LLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDdFLPGALDAGTYDGKLYGVPFNTDTLG-LYYNKDL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 154 MDKIGGTEPKTFDELIALLDKAKA-AGVIPLALGGQNWQEATMFdsivLSTGGPEFYkkafNDLDDESLKSDTMKKSFDN 232
Cdd:COG1653   157 FEKAGLDPPKTWDELLAAAKKLKAkDGVYGFALGGKDGAAWLDL----LLSAGGDLY----DEDGKPAFDSPEAVEALEF 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 233 LATIIK--YVDPNFSGRDWNLATAMVIKGDALVQVMGDWAKGEFVAAKktPDTDFLCYRFPGTDG----SVVYNSDMFGM 306
Cdd:COG1653   229 LKDLVKdgYVPPGALGTDWDDARAAFASGKAAMMINGSWALGALKDAA--PDFDVGVAPLPGGPGgkkpASVLGGSGLAI 306
                         330       340       350
                  ....*....|....*....|....*....|
gi 2087804054 307 FNVPDDRKAAqVALATATLSKSFQSAFNVV 336
Cdd:COG1653   307 PKGSKNPEAA-WKFLKFLTSPEAQAKWDAL 335
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
67-349 2.46e-22

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: 97.07  E-value: 2.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  67 GGDAAMTALKAMVAAGTYPTASQMLGYTVL-DYAQAGVMGDLTETAKKEGWDKSVPAALQKFSVYDGKWVAAPVNVhSVN 145
Cdd:cd14749    39 PYDNYKTKLKTAVAAGEGPDVFNLWPGGWLaEFVKAGLLLPLTDYLDPNGVDKRFLPGLADAVTFNGKVYGIPFAA-RAL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 146 WLWINKAVMDKIGGTE-PKTFDELI--ALLDKAKAAGVIPLALGGqNWQEATM-FDSIVLSTGGPEFykkaFNDLDDesl 221
Cdd:cd14749   118 ALFYNKDLFEEAGGVKpPKTWDELIeaAKKDKFKAKGQTGFGLLL-GAQGGHWyFQYLVRQAGGGPL----SDDGSG--- 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 222 ksdtmKKSFDNLATI-----------IKYVDPNFSGRDWNLATAMVIKGDALVQVMGDWAKGEFVAAKKTPDTDFlcYRF 290
Cdd:cd14749   190 -----KATFNDPAFVqalqklqdlvkAGAFQEGFEGIDYDDAGQAFAQGKAAMNIGGSWDLGAIKAGEPGGKIGV--FPF 262
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087804054 291 PGTDG----SVVYNSDMFGMFNVPDDRKAAQVALATATLSKSFQSAFNVVKGSVPARTDVPDT 349
Cdd:cd14749   263 PTVGKgaqtSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQYLEDVGLLPAKEVVAKD 325
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
60-295 3.86e-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: 75.15  E-value: 3.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  60 DVPVAGGGGDAAMTALKAMVAAGTYPTA-SQMLGYTVLDYAQAGVMGDLTETAKKEGWDKsvpaalqkfsvyDGKWVAAP 138
Cdd:pfam01547  25 KVEVESVGSGSLAQKLTTAIAAGDGPADvFASDNDWIAELAKAGLLLPLDDYVANYLVLG------------VPKLYGVP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 139 VNVHSvNWLWINKAVMDKIGGTEPKTFDELIALLDKAKAAG-VIPLALGGQNWQEATMFDSIVLSTGGPEFYKKAFNDLD 217
Cdd:pfam01547  93 LAAET-LGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGkSPGGAGGGDASGTLGYFTLALLASLGGPLFDKDGGGLD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 218 DESLK--SDTMKKSFDNLATIIKYVDPNFSGRDWNLATAMVIKGDALVQVMGDWAKGEFVAAKKTPDTDFLCYRFPGTDG 295
Cdd:pfam01547 172 NPEAVdaITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAANKVKLKVAFAAPAPDPKGDVG 251
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
98-179 9.13e-04

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 40.77  E-value: 9.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  98 YAQAGVMGDLTETAKKEgwDKSVPAALQKFSvYDGKWVAAPVNVHSVNwLWINKAVMDkiggTEPKTFDELIALLDKAKA 177
Cdd:PRK09474   96 YAQSGLLAEVTPSKAFK--DKLVPFTWDAVR-YNGKLIGYPIAVEALS-LIYNKDLVP----TPPKTWEEIPALDKELKA 167

                  ..
gi 2087804054 178 AG 179
Cdd:PRK09474  168 KG 169
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
1-336 9.56e-43

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 152.12  E-value: 9.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054   1 MNKFLSSAAVAVVMMA----GLSAAHAADVKEVQMLHWWTSGGEAAALNVLKQDLSKE--GFAWKDVPVaggGGDAAMTA 74
Cdd:COG1653     1 MRRLALALAAALALALaacgGGGSGAAAAAGKVTLTVWHTGGGEAAALEALIKEFEAEhpGIKVEVESV---PYDDYRTK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  75 LKAMVAAGTYPTASQMLGYTVLDYAQAGVMGDLTETAKKEGWDKS-VPAALQKFSVYDGKWVAAPVNVHSVNwLWINKAV 153
Cdd:COG1653    78 LLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDdFLPGALDAGTYDGKLYGVPFNTDTLG-LYYNKDL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 154 MDKIGGTEPKTFDELIALLDKAKA-AGVIPLALGGQNWQEATMFdsivLSTGGPEFYkkafNDLDDESLKSDTMKKSFDN 232
Cdd:COG1653   157 FEKAGLDPPKTWDELLAAAKKLKAkDGVYGFALGGKDGAAWLDL----LLSAGGDLY----DEDGKPAFDSPEAVEALEF 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 233 LATIIK--YVDPNFSGRDWNLATAMVIKGDALVQVMGDWAKGEFVAAKktPDTDFLCYRFPGTDG----SVVYNSDMFGM 306
Cdd:COG1653   229 LKDLVKdgYVPPGALGTDWDDARAAFASGKAAMMINGSWALGALKDAA--PDFDVGVAPLPGGPGgkkpASVLGGSGLAI 306
                         330       340       350
                  ....*....|....*....|....*....|
gi 2087804054 307 FNVPDDRKAAqVALATATLSKSFQSAFNVV 336
Cdd:COG1653   307 PKGSKNPEAA-WKFLKFLTSPEAQAKWDAL 335
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
67-349 2.46e-22

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: 97.07  E-value: 2.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  67 GGDAAMTALKAMVAAGTYPTASQMLGYTVL-DYAQAGVMGDLTETAKKEGWDKSVPAALQKFSVYDGKWVAAPVNVhSVN 145
Cdd:cd14749    39 PYDNYKTKLKTAVAAGEGPDVFNLWPGGWLaEFVKAGLLLPLTDYLDPNGVDKRFLPGLADAVTFNGKVYGIPFAA-RAL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 146 WLWINKAVMDKIGGTE-PKTFDELI--ALLDKAKAAGVIPLALGGqNWQEATM-FDSIVLSTGGPEFykkaFNDLDDesl 221
Cdd:cd14749   118 ALFYNKDLFEEAGGVKpPKTWDELIeaAKKDKFKAKGQTGFGLLL-GAQGGHWyFQYLVRQAGGGPL----SDDGSG--- 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 222 ksdtmKKSFDNLATI-----------IKYVDPNFSGRDWNLATAMVIKGDALVQVMGDWAKGEFVAAKKTPDTDFlcYRF 290
Cdd:cd14749   190 -----KATFNDPAFVqalqklqdlvkAGAFQEGFEGIDYDDAGQAFAQGKAAMNIGGSWDLGAIKAGEPGGKIGV--FPF 262
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087804054 291 PGTDG----SVVYNSDMFGMFNVPDDRKAAQVALATATLSKSFQSAFNVVKGSVPARTDVPDT 349
Cdd:cd14749   263 PTVGKgaqtSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQYLEDVGLLPAKEVVAKD 325
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
3-346 4.73e-18

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 84.62  E-value: 4.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054   3 KFLSSAAVAVVMMAGLSA---------AHAADVKEVQmLHWWTSGGEAAALNVLKQDLSKEgfAWKDVPVAGGGGDAAMT 73
Cdd:COG2182     4 RLLAALALALALALALAAcgsgssssgSSSAAGAGGT-LTVWVDDDEAEALEEAAAAFEEE--PGIKVKVVEVPWDDLRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  74 ALKAMVAAGTYP----TASQMLGytvlDYAQAGVMGDLTETAKKegWDKSVPAALQKFSvYDGKWVAAPVNVHSVNwLWI 149
Cdd:COG2182    81 KLTTAAPAGKGPdvfvGAHDWLG----ELAEAGLLAPLDDDLAD--KDDFLPAALDAVT-YDGKLYGVPYAVETLA-LYY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 150 NKAVMDKiggTEPKTFDELIALLDKAKAAGVIPLALGGQNWQEATMFdsiVLSTGGPEFYKKAfNDLDDESLKSDTMKKS 229
Cdd:COG2182   153 NKDLVKA---EPPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYFYPF---LAAFGGYLFGKDG-DDPKDVGLNSPGAVAA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 230 FDNLATIIK--YVDPNFsgrDWNLATAMVIKGDALVQVMGDWAKGEFVAAKKtpdTDFLCYRFPGTDGSVVYNSdMFG-- 305
Cdd:COG2182   226 LEYLKDLIKdgVLPADA---DYDAADALFAEGKAAMIINGPWAAADLKKALG---IDYGVAPLPTLAGGKPAKP-FVGvk 298
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2087804054 306 --MFNVPDDRKAAQVALATATLSKSFQSAFNVVKGSVPARTDV 346
Cdd:COG2182   299 gfGVSAYSKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAA 341
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
63-342 1.39e-15

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: 77.06  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  63 VAGGGGDAAMTALKAMVAAGTYPTASQMLGYTVLDYAQAGVMGDLTETAKKEGWDKSVPAALQKFSVYDGKWVAAPVNVh 142
Cdd:cd13585    34 VVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDDYIEKDGLDDDFPPGLLDAGTYDGKLYGLPFDA- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 143 SVNWLWINKAVMDKIGG--TEPKTFDELIAL--LDKAKAAGVIPLALGGQNWQeATMFDSIVLSTGGpefykKAFNDLDD 218
Cdd:cd13585   113 DTLVLFYNKDLFDKAGPgpKPPWTWDELLEAakKLTDKKGGQYGFALRGGSGG-QTQWYPFLWSNGG-----DLLDEDDG 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 219 ES-LKSDTMKKSFDNLATIIKY-VDPNFSGRDWNLATAMVIKGDALVQVMGDWAKGEFVAAKKTPDTDFLCY-RFPGTDG 295
Cdd:cd13585   187 KAtLNSPEAVEALQFYVDLYKDgVAPSSATTGGDEAVDLFASGKVAMMIDGPWALGTLKDSKVKFKWGVAPLpAGPGGKR 266
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2087804054 296 SVVYNSDMFGMFNVPDDRKAAQVALATATlSKSFQSAFNVVKGSVPA 342
Cdd:cd13585   267 ASVLGGWGLAISKNSKHPEAAWKFIKFLT-SKENQLKLGGAAGPAAL 312
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
28-352 3.02e-15

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: 76.18  E-value: 3.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  28 EVQMLHWWTsGGEAAALNVLKQDLSKEGFAWKDVPVAGGGGDAAMTALKAMVAAGTYPTASQMLGYTVLDYAQAGVMGDL 107
Cdd:cd14748     1 EITFWHGMS-GPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 108 TETAKKEGWDKS--VPAALQKFSvYDGKWVAAPVNVHSVNwLWINKAVMDKIGG---TEPKTFDELIA----LLDKAKAA 178
Cdd:cd14748    80 DDYIDKDGVDDDdfYPAALDAGT-YDGKLYGLPFDTSTPV-LYYNKDLFEEAGLdpeKPPKTWDELEEaakkLKDKGGKT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 179 GVIPLALggQNWQEATMFDSIVLSTGG----PEFYKKAFNdlddeslkSDTMKKSFDNLATIIkYVDPNFSGRDWNLATA 254
Cdd:cd14748   158 GRYGFAL--PPGDGGWTFQALLWQNGGdlldEDGGKVTFN--------SPEGVEALEFLVDLV-GKDGVSPLNDWGDAQD 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 255 MVIKGDALVQVMGDWAKGEFvaAKKTPDTDF-LCY--RFPGTDGSVVYNSDMFGMFNVPDDRKAAQVALATATLSKSFQS 331
Cdd:cd14748   227 AFISGKVAMTINGTWSLAGI--RDKGAGFEYgVAPlpAGKGKKGATPAGGASLVIPKGSSKKKEAAWEFIKFLTSPENQA 304
                         330       340
                  ....*....|....*....|.
gi 2087804054 332 AFNVVKGSVPARTDVPDTDFD 352
Cdd:cd14748   305 KWAKATGYLPVRKSAAEDPEE 325
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
60-295 3.86e-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: 75.15  E-value: 3.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  60 DVPVAGGGGDAAMTALKAMVAAGTYPTA-SQMLGYTVLDYAQAGVMGDLTETAKKEGWDKsvpaalqkfsvyDGKWVAAP 138
Cdd:pfam01547  25 KVEVESVGSGSLAQKLTTAIAAGDGPADvFASDNDWIAELAKAGLLLPLDDYVANYLVLG------------VPKLYGVP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 139 VNVHSvNWLWINKAVMDKIGGTEPKTFDELIALLDKAKAAG-VIPLALGGQNWQEATMFDSIVLSTGGPEFYKKAFNDLD 217
Cdd:pfam01547  93 LAAET-LGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGkSPGGAGGGDASGTLGYFTLALLASLGGPLFDKDGGGLD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 218 DESLK--SDTMKKSFDNLATIIKYVDPNFSGRDWNLATAMVIKGDALVQVMGDWAKGEFVAAKKTPDTDFLCYRFPGTDG 295
Cdd:pfam01547 172 NPEAVdaITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAANKVKLKVAFAAPAPDPKGDVG 251
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
61-351 5.68e-11

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 62.42  E-value: 5.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  61 VPVAGGGGDAAMTALKAMVAAGTYPTASQMLGYT--VLDYAQAGVMGDLTETAKKEGWDKSVPAALqkfsvYDGKWVAAP 138
Cdd:pfam13416  14 VEVEPQASNDLQAKLLAAAAAGNAPDLDVVWIAAdqLATLAEAGLLADLSDVDNLDDLPDALDAAG-----YDGKLYGVP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 139 VNVHSVNWLWINKAVMDKiGGTEPKTFDELIALLDKAKAAGVIPLAlgGQNWQEATMFDSIVlstggpefykkAFNDLDD 218
Cdd:pfam13416  89 YAASTPTVLYYNKDLLKK-AGEDPKTWDELLAAAAKLKGKTGLTDP--ATGWLLWALLADGV-----------DLTDDGK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 219 ESLKSDTMKKSFDNLATIIKYVDpnfsgrDWNLATAMVIKGDALVQVMGDWAkgeFVAAKKTPDTdfLCYRFPGtDGSVV 298
Cdd:pfam13416 155 GVEALDEALAYLKKLKDNGKVYN------TGADAVQLFANGEVAMTVNGTWA---AAAAKKAGKK--LGAVVPK-DGSFL 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2087804054 299 yNSDMFGMFNVPDDRKAAQVALATATLSKSFQSAFNVVKGSVPARTDVPDTDF 351
Cdd:pfam13416 223 -GGKGLVVPAGAKDPRLAALDFIKFLTSPENQAALAEDTGYIPANKSAALSDE 274
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
35-346 1.70e-10

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: 61.54  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  35 WTS-GGEAAALNVLKQDLSKEgfAWKDVPVAGGGGDAAMTALKAMVAAGTYP----TASQMLGytvlDYAQAGVMGDLTE 109
Cdd:cd13586     5 WTDeDGELEYLKELAEEFEKK--YGIKVEVVYVDSGDTREKFITAGPAGKGPdvffGPHDWLG----ELAAAGLLAPIPE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 110 TAKKEgwDKSVPAALQKFSvYDGKWVAAPVNVHSVNwLWINKavmDKIGgTEPKTFDELIAL--LDKAKAAGVIPLALgg 187
Cdd:cd13586    79 YLAVK--IKNLPVALAAVT-YNGKLYGVPVSVETIA-LFYNK---DLVP-EPPKTWEELIALakKFNDKAGGKYGFAY-- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 188 qNWQEATMFDSIVLSTGGPEFyKKAFNDLDDESLKSDTMKKSFDNLATIIKYVDPNFSGRDWNLATAMVIKGDALVQVMG 267
Cdd:cd13586   149 -DQTNPYFSYPFLAAFGGYVF-GENGGDPTDIGLNNEGAVKGLKFIKDLKKKYKVLPPDLDYDIADALFKEGKAAMIING 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 268 DWAKGEFVAAKktpdTDFLCYRFPGTDGSVVYN--SDMFGMF-NVPDDRKAAQVALATATLSKSFQSAFNVVKGSVPART 344
Cdd:cd13586   227 PWDLADYKDAG----INFGVAPLPTLPGGKQAApfVGVQGAFvSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALK 302

                  ..
gi 2087804054 345 DV 346
Cdd:cd13586   303 DA 304
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
98-350 1.28e-09

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: 58.96  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  98 YAQAGVMGDLTETAKKEGWDKSVPAALQKfsvYDGKWVAAPVNVHSVNWLWINKavmdKIGGTEPKTFDELIALLDKAKA 177
Cdd:cd13522    69 FAAAGLLAPLDEYVSKSGKYAPNTIAAMK---LNGKLYGVPVSVGAHLMYYNKK----LVPKNPPKTWQELIALAQGLKA 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 178 AGVIPLALGGqnwQEATMFDSIVLSTGGPEFykKAFNDLDDESLKSDTMKKSFDNLATIIKYVDPNFSGRDWNLATAMVI 257
Cdd:cd13522   142 KNVWGLVYNQ---NEPYFFAAWIGGFGGQVF--KANNGKNNPTLDTPGAVEALQFLVDLKSKYKIMPPETDYSIADALFK 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 258 KGDALVQVMGDWAKGEFVAAKKtpdTDFLCYR---FPGTDGSVVYNSDMFGMFNVPDDRKAAQVALATATLSKSFQSAFN 334
Cdd:cd13522   217 AGKAAMIINGPWDLGDYRQALK---INLGVAPlptFSGTKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLF 293
                         250
                  ....*....|....*.
gi 2087804054 335 VVKGSVPARTDVPDTD 350
Cdd:cd13522   294 DDAGDIPANLQAYESP 309
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
99-269 3.12e-09

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: 58.07  E-value: 3.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  99 AQAGVMGDLTETAKKEGWDKSVPAALQKfSVYDGKWVAAPVNVhSVNWLWINKAVMDKIGGTEPKTFDELI--ALLDKAK 176
Cdd:cd14750    73 AEAGWLLPLTEYLKEEEDDDFLPATVEA-NTYDGKLYALPWFT-DAGLLYYRKDLLEKYGPEPPKTWDELLeaAKKRKAG 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 177 AAGVIPLALGGQNWQEAT-MFDSIVLSTGGpefykKAFNDLDDES-LKSDTMKKSFDNLATII--KYVDPNFSGRDWNLA 252
Cdd:cd14750   151 EPGIWGYVFQGKQYEGLVcNFLELLWSNGG-----DIFDDDSGKVtVDSPEALEALQFLRDLIgeGISPKGVLTYGEEEA 225
                         170
                  ....*....|....*..
gi 2087804054 253 TAMVIKGDALvqVMGDW 269
Cdd:cd14750   226 RAAFQAGKAA--FMRNW 240
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
28-277 5.69e-06

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: 47.76  E-value: 5.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  28 EVQMLHWWTsGGEAAALNVLKQDLSKEgFAWKDVPVAGGGGDAAMTALKAMVAAGTYPtasQMLGYT---VLDYAQAGVM 104
Cdd:cd13657     1 TITIWHALT-GAEEDALQQIIDEFEAK-YPVPNVKVPFEKKPDLQNKLLTAIPAGEGP---DLFIWAhdwIGQFAEAGLL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 105 GDLTETAKKEGWDKSVPAALQKFSvYDGKWVAAPVNVHSVNwLWINKAVMDkiggTEPKTFDELIALLDK--AKAAGVIP 182
Cdd:cd13657    76 VPISDYLSEDDFENYLPTAVEAVT-YKGKVYGLPEAYETVA-LIYNKALVD----QPPETTDELLAIMKDhtDPAAGSYG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 183 LAlggQNWQEATMFDSIVLSTGGPEFYKKAFNdlddESLKSDTMKKSFDNLAT-IIKYVDPNFSgrdWNLATAMVIKGDA 261
Cdd:cd13657   150 LA---YQVSDAYFVSAWIFGFGGYYFDDETDK----PGLDTPETIKGIQFLKDfSWPYMPSDPS---YNTQTSLFNEGKA 219
                         250
                  ....*....|....*.
gi 2087804054 262 LVQVMGDWAKGEFVAA 277
Cdd:cd13657   220 AMIINGPWFIGGIKAA 235
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
69-205 1.44e-05

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: 46.54  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  69 DAAMTALKAMVAAGTYPTASQmLGYT-VLDYAQAGVMGDLTETAKKEGWDKSVPAALQKFSVYDGKWVAAPVNVhSVNWL 147
Cdd:cd14747    40 GDAHTKITTAAASGDGPDVVQ-LGNTwVAEFAAMGALEDLTPYLEDLGGDKDLFPGLVDTGTVDGKYYGVPWYA-DTRAL 117
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2087804054 148 WINKAVMDKIGGTE-PKTFDELIALLDKAKAAG--VIPLALGGQN--WQEATMFdsiVLSTGG 205
Cdd:cd14747   118 FYRTDLLKKAGGDEaPKTWDELEAAAKKIKADGpdVSGFAIPGKNdvWHNALPF---VWGAGG 177
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
69-176 3.97e-05

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: 45.06  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  69 DAAMTALKAMVAAGTYPTASQMLGYTVLDYAQAGVMGDLTETAKKEGWDKSVPAALqKFSVYDGKWVAAPVNVHSVNWLW 148
Cdd:cd14751    40 DGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDGTPAFDDIVDYLPGPM-ETNRYNGHYYGVPQVTNTLALFY 118
                          90       100
                  ....*....|....*....|....*...
gi 2087804054 149 iNKAVMDKIGGTEPKTFDELIALLDKAK 176
Cdd:cd14751   119 -NKRLLEEAGTEVPKTMDELVAAAKAIK 145
PBP2_AlgQ_like_3 cd13582
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
73-224 8.90e-05

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: 270300 [Multi-domain]  Cd Length: 504  Bit Score: 44.23  E-value: 8.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  73 TALKAMVAAGTYPTASQMLGYTVLdYAQAGVMGDLTETAKKEG-WDKSV--PAALQKFSVYDGK-WVAAPVNVHSVNW-- 146
Cdd:cd13582    45 QKIGLMIASGDLPDLIYAKGDTDK-LIEAGALVPLDDLIEKYGpNIKKWygDYLLKKLRSEDGHiYYLPNYRVEDAPWyp 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 147 ---LWINKAVMDKIGGTEPKTFDELIALLDKAKAA-------GVIPLALGGQNWQeatmfdsIVLSTGGPEFYKKAFND- 215
Cdd:cd13582   124 nggFWLQHDVLKELGYPKIKTLDDYENLIKDYKKKyptingqPTIGFTALTDDWR-------FLISVTNPAFLAGYPNDg 196
                         170
                  ....*....|..
gi 2087804054 216 ---LDDESLKSD 224
Cdd:cd13582   197 evyVDPKTLKAK 208
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
75-309 5.44e-04

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: 41.93  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  75 LKAMVAAGTYPTASQ-MLGYTVLDYAQAGVMGDLTETAKKEGWD--KSVPAALQKFSVYDGKWVAAPV--NVHSVNWLWI 149
Cdd:cd13580    50 LNLALASGDLPDIVVvNDPQLSITLVKQGALWDLTDYLDKYYPNlkKIIEQEGWDSASVDGKIYGIPRkrPLIGRNGLWI 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 150 NKAVMDKIGGTEPKTFDELIALL--------DKAKAAGVIPLALGGQNWqeATMFDSIVLSTGGPEFYKKAFNDLDDE-S 220
Cdd:cd13580   130 RKDWLDKLGLEVPKTLDELYEVAkaftekdpDGNGKKDTYGLTDTKDLI--GSGFTGLFGAFGAPPNNWWKDEDGKLVpG 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 221 LKSDTMKKSFDNLATIIK--YVDPNFSGRDWNLATAMVIKGDALVQVMGDWAKGEFVAAKKT--PDTDFLCY-RFPGTDG 295
Cdd:cd13580   208 SIQPEMKEALKFLKKLYKegLIDPEFAVNDGTKANEKFISGKAGIFVGNWWDPAWPQASLKKndPDAEWVAVpIPSGPDG 287
                         250
                  ....*....|....*
gi 2087804054 296 -SVVYNSDMFGMFNV 309
Cdd:cd13580   288 kYGVWAESGVNGFFV 302
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
97-270 7.70e-04

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: 41.04  E-value: 7.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  97 DYAQAGVMGDLTETAKKEgwDKSVPAALQKFSvYDGKWVAAPVNVHSVNWLWiNKAVMDkiggTEPKTFDELIALLDKAK 176
Cdd:cd13656    65 GYAQSGLLAEITPDKAFQ--DKLYPFTWDAVR-YNGKLIAYPIAVEALSLIY-NKDLLP----NPPKTWEEIPALDKELK 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 177 AAGVIPLALggqNWQEATMFDSIVLSTGGPEF-YKKAFNDLDDESLKSDTMKKSFDNLATIIKYVDPNfSGRDWNLATAM 255
Cdd:cd13656   137 AKGKSALMF---NLQEPYFTWPLIAADGGYAFkYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMN-ADTDYSIAEAA 212
                         170
                  ....*....|....*
gi 2087804054 256 VIKGDALVQVMGDWA 270
Cdd:cd13656   213 FNKGETAMTINGPWA 227
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
98-179 9.13e-04

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 40.77  E-value: 9.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  98 YAQAGVMGDLTETAKKEgwDKSVPAALQKFSvYDGKWVAAPVNVHSVNwLWINKAVMDkiggTEPKTFDELIALLDKAKA 177
Cdd:PRK09474   96 YAQSGLLAEVTPSKAFK--DKLVPFTWDAVR-YNGKLIGYPIAVEALS-LIYNKDLVP----TPPKTWEEIPALDKELKA 167

                  ..
gi 2087804054 178 AG 179
Cdd:PRK09474  168 KG 169
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
112-220 1.50e-03

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: 40.42  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054 112 KKEGWDKSVPAALQkfsvYDGKWVAAPV--NVHSVNWLW-INKAVMDKIGGTEPKTFDELIALLDKAKAAG--VIPLAlg 186
Cdd:cd13583    96 EKWGLGKELATGRQ----SDGKYYSLPGlhEDPGVQYSFlYRKDIFEKAGIKIPTTWDEFYAALKKLKEKYpdSYPYS-- 169
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2087804054 187 gQNWQEATMFDSIVLSTGGPEFYKKAFNDLDDES 220
Cdd:cd13583   170 -DRWNSNALLLIAAPAFGTTAGWGFSNYTYDPDT 202
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
75-177 2.35e-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: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087804054  75 LKAMVAAGTYP--TASQMLGYTVLDYAQAGVMGDLTETAKK----EGWDKSVPAALQKFSVYDGKWVAAP-VNVHSVN-- 145
Cdd:cd13521    48 LNLMLASGDLPdiVGADYLKDKFIAYGMEGAFLPLSKYIDQypnlKAFFKQHPDVLRASTASDGKIYLIPyEPPKDVPnq 127
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2087804054 146 WLWINKAVMDKIGGTEPKTFDELIALLDKAKA 177
Cdd:cd13521   128 GYFIRKDWLDKLNLKTPKTLDELYNVLKAFKE 159
 
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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