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Conserved domains on  [gi|549799198|ref|WP_022562627|]
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MULTISPECIES: ABC transporter substrate-binding protein [Rhizobium/Agrobacterium group]

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 ...
 37-333 5.44e-52

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 178.31  E-value: 5.44e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  37 VWWGSADRSKRTNDVIALYQKANPQTEISGEMIAGSDYWTKLATSMAGRNVADIFQLEPSTIADYSGRGACMELDQFVGK 116
Cdd:COG1653   37 VWHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDD 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 117 S-LDLSTFGKSEIDLCRIDGKLYGVGLGLNSFCMMYDADTLKEAGVSVPQdqiTWKALAELARDFKkngpAKRNYWAVPY 195
Cdd:COG1653  117 DgLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPPK---TWDELLAAAKKLK----AKDGVYGFAL 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 196 GARYHYVFDVWLRQRGKLLF-QDGTIGFNKEDAKEWFAYWEDLRENKLCVSADIQTRDDNTIesNALTLGNSAIGFAYSN 274
Cdd:COG1653  190 GGKDGAAWLDLLLSAGGDLYdEDGKPAFDSPEAVEALEFLKDLVKDGYVPPGALGTDWDDAR--AAFASGKAAMMINGSW 267

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 275 QLVGYQKLNKQT-LSIGMLPGEGPGKPTGHYYRpGLIWSISSTSTNAEAAAKFINFFVND 333
Cdd:COG1653  268 ALGALKDAAPDFdVGVAPLPGGPGGKKPASVLG-GSGLAIPKGSKNPEAAWKFLKFLTSP 326
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 37-333 5.44e-52

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 178.31  E-value: 5.44e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  37 VWWGSADRSKRTNDVIALYQKANPQTEISGEMIAGSDYWTKLATSMAGRNVADIFQLEPSTIADYSGRGACMELDQFVGK 116
Cdd:COG1653   37 VWHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDD 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 117 S-LDLSTFGKSEIDLCRIDGKLYGVGLGLNSFCMMYDADTLKEAGVSVPQdqiTWKALAELARDFKkngpAKRNYWAVPY 195
Cdd:COG1653  117 DgLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPPK---TWDELLAAAKKLK----AKDGVYGFAL 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 196 GARYHYVFDVWLRQRGKLLF-QDGTIGFNKEDAKEWFAYWEDLRENKLCVSADIQTRDDNTIesNALTLGNSAIGFAYSN 274
Cdd:COG1653  190 GGKDGAAWLDLLLSAGGDLYdEDGKPAFDSPEAVEALEFLKDLVKDGYVPPGALGTDWDDAR--AAFASGKAAMMINGSW 267

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 275 QLVGYQKLNKQT-LSIGMLPGEGPGKPTGHYYRpGLIWSISSTSTNAEAAAKFINFFVND 333
Cdd:COG1653  268 ALGALKDAAPDFdVGVAPLPGGPGGKKPASVLG-GSGLAIPKGSKNPEAAWKFLKFLTSP 326
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 37-420 5.84e-44

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: 157.57  E-value: 5.84e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  37 VW-WGSADRSKRTNDVIALYQKANPQTEISGEMIAGSDYWTKLATSMAGRNVADIFQLEPSTIADYSGRGACMELDQFVG 115
Cdd:cd13585    4 FWdWGQPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDDYIE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 116 KSLDLSTFGKSEIDLCRIDGKLYGVGLGLNSFCMMYDADTLKEAGVSVPQDQiTWKALAELARDFKKNGPAKrnY-WAVP 194
Cdd:cd13585   84 KDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPW-TWDELLEAAKKLTDKKGGQ--YgFALR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 195 YGARYHYVFDVWLRQRGKLLF--QDGTIGFNKEDAKEWFAYWEDLRENKLCVSADIQTRDDNTiesNALTLGNSAIGFAY 272
Cdd:cd13585  161 GGSGGQTQWYPFLWSNGGDLLdeDDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAV---DLFASGKVAMMIDG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 273 SNQLVGYQKLN-KQTLSIGMLPGEGPGKPTGHYYrpGLIWSISSTSTNAEAAAKFINFFVNDlEAGKVLGVERGVPPAKV 351
Cdd:cd13585  238 PWALGTLKDSKvKFKWGVAPLPAGPGGKRASVLG--GWGLAISKNSKHPEAAWKFIKFLTSK-ENQLKLGGAAGPAALAA 314

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 352 VREALLPTLNETERKTVDYIESLSgklDPYPEPAPIGANEFDRGVMRPIADSLAF-GRATVDEAAQNLVD 420
Cdd:cd13585  315 AAASAAAPDAKPALALAAAADALA---AAVPPPVPPPWPEVYPILSEALQEALLGaLGKSPEEALKEAAK 381
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 51-333 8.98e-22

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: 94.79  E-value: 8.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198   51 VIALYQKANPQTEISGEMIAGSDYWTKLATSM-AGRNVADIFQLEPSTIADYSGRGACMELDQFVGKSLDLstfgkseid 129
Cdd:pfam01547  13 LVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIaAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYLVL--------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  130 lcrIDGKLYGVGLGLNSFCMMYDADTLKEAGVSVPQdqiTWKALAELARDFKKNGPAKRNYWAVPYGARYHYVFDVWLRQ 209
Cdd:pfam01547  84 ---GVPKLYGVPLAAETLGLIYNKDLFKKAGLDPPK---TWDELLEAAKKLKEKGKSPGGAGGGDASGTLGYFTLALLAS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  210 RGKLLFQDGTIGFNKEDAKEWFAYWEDL----RENKLCVSADIQTRDDNTIEsNALTLGNSAIGFAYSNQ--LVGYQKLN 283
Cdd:pfam01547 158 LGGPLFDKDGGGLDNPEAVDAITYYVDLyakvLLLKKLKNPGVAGADGREAL-ALFEQGKAAMGIVGPWAalAANKVKLK 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 549799198  284 KQTLSIGMLPGEGPGK---PTGHYYRPG-LIWSISSTSTNAEAAAKFINFFVND 333
Cdd:pfam01547 237 VAFAAPAPDPKGDVGYaplPAGKGGKGGgYGLAIPKGSKNKEAAKKFLDFLTSP 290
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
129-333 8.36e-03

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 38.07  E-value: 8.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 129 DLCRIDGKLYGVGLGLNSFCMMYDADTLKEAgvsvPQdqiTWKALAELARDFKKNG------PAKRNYWAVPY-GARYHY 201
Cdd:PRK09474 121 DAVRYNGKLIGYPIAVEALSLIYNKDLVPTP----PK---TWEEIPALDKELKAKGksaimwNLQEPYFTWPLiAADGGY 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 202 VFDvwlRQRGKLLFQDgtIGFNKEDAKEWFAYWEDLRENKLcVSADIqtrdDNTIESNALTLGNSAI----GFAYSNqlv 277
Cdd:PRK09474 194 AFK---FENGGYDVKD--VGVNNAGAKAGLQFLVDLVKNKH-MNADT----DYSIAEAAFNKGETAMtingPWAWSN--- 260

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799198 278 gyqkLNKQTLSIGM--LPG--EGPGKP-TGhyyrpglIWS--ISSTSTNAEAAAKFI-NFFVND 333
Cdd:PRK09474 261 ----IDKSGINYGVtvLPTfnGKPSKPfVG-------VLSagINAASPNKELAKEFLeNYLLTD 313
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 37-333 5.44e-52

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 178.31  E-value: 5.44e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  37 VWWGSADRSKRTNDVIALYQKANPQTEISGEMIAGSDYWTKLATSMAGRNVADIFQLEPSTIADYSGRGACMELDQFVGK 116
Cdd:COG1653   37 VWHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDD 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 117 S-LDLSTFGKSEIDLCRIDGKLYGVGLGLNSFCMMYDADTLKEAGVSVPQdqiTWKALAELARDFKkngpAKRNYWAVPY 195
Cdd:COG1653  117 DgLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPPK---TWDELLAAAKKLK----AKDGVYGFAL 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 196 GARYHYVFDVWLRQRGKLLF-QDGTIGFNKEDAKEWFAYWEDLRENKLCVSADIQTRDDNTIesNALTLGNSAIGFAYSN 274
Cdd:COG1653  190 GGKDGAAWLDLLLSAGGDLYdEDGKPAFDSPEAVEALEFLKDLVKDGYVPPGALGTDWDDAR--AAFASGKAAMMINGSW 267

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 275 QLVGYQKLNKQT-LSIGMLPGEGPGKPTGHYYRpGLIWSISSTSTNAEAAAKFINFFVND 333
Cdd:COG1653  268 ALGALKDAAPDFdVGVAPLPGGPGGKKPASVLG-GSGLAIPKGSKNPEAAWKFLKFLTSP 326
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 37-420 5.84e-44

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: 157.57  E-value: 5.84e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  37 VW-WGSADRSKRTNDVIALYQKANPQTEISGEMIAGSDYWTKLATSMAGRNVADIFQLEPSTIADYSGRGACMELDQFVG 115
Cdd:cd13585    4 FWdWGQPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDDYIE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 116 KSLDLSTFGKSEIDLCRIDGKLYGVGLGLNSFCMMYDADTLKEAGVSVPQDQiTWKALAELARDFKKNGPAKrnY-WAVP 194
Cdd:cd13585   84 KDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPW-TWDELLEAAKKLTDKKGGQ--YgFALR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 195 YGARYHYVFDVWLRQRGKLLF--QDGTIGFNKEDAKEWFAYWEDLRENKLCVSADIQTRDDNTiesNALTLGNSAIGFAY 272
Cdd:cd13585  161 GGSGGQTQWYPFLWSNGGDLLdeDDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAV---DLFASGKVAMMIDG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 273 SNQLVGYQKLN-KQTLSIGMLPGEGPGKPTGHYYrpGLIWSISSTSTNAEAAAKFINFFVNDlEAGKVLGVERGVPPAKV 351
Cdd:cd13585  238 PWALGTLKDSKvKFKWGVAPLPAGPGGKRASVLG--GWGLAISKNSKHPEAAWKFIKFLTSK-ENQLKLGGAAGPAALAA 314

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 352 VREALLPTLNETERKTVDYIESLSgklDPYPEPAPIGANEFDRGVMRPIADSLAF-GRATVDEAAQNLVD 420
Cdd:cd13585  315 AAASAAAPDAKPALALAAAADALA---AAVPPPVPPPWPEVYPILSEALQEALLGaLGKSPEEALKEAAK 381
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 38-421 3.30e-32

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: 125.87  E-value: 3.30e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  38 WWGSADRsKRTNDVIALYQKANPQTEISGEMIAGSDYW-TKLATSMAGRNVADIFQLEPSTIADYSGRGACMELDQFVGK 116
Cdd:cd14748    7 GMSGPDG-KALEELVDEFNKSHPDIKVKAVYQGSYDDTlTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDDYIDK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 117 S-LDLSTFGKSEIDLCRIDGKLYGVGLGLNSFCMMYDADTLKEAGVSVPQDQITWKALAELARDFKKNGPAKRNY-WAVP 194
Cdd:cd14748   86 DgVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKDKGGKTGRYgFALP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 195 YGARYHYvFDVWLRQRGKLLFQD--GTIGFNKEDAKEWFAYWEDLRENKlcvSADIQTRDDNTieSNALTLGNSAIGFAY 272
Cdd:cd14748  166 PGDGGWT-FQALLWQNGGDLLDEdgGKVTFNSPEGVEALEFLVDLVGKD---GVSPLNDWGDA--QDAFISGKVAMTING 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 273 SNQLVGYQKLNKQ-TLSIGMLP---GEGPGKPTGhyyrpGLIWSISSTST-NAEAAAKFINFFVNDlEAGKVLGVERGVP 347
Cdd:cd14748  240 TWSLAGIRDKGAGfEYGVAPLPagkGKKGATPAG-----GASLVIPKGSSkKKEAAWEFIKFLTSP-ENQAKWAKATGYL 313

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799198 348 PakvVREALLPTLNETERKTVDYIESLSGKLDPYPEPAPIGANEFDRGVMRPIADSLAFGRATVDEAAQNLVDT 421
Cdd:cd14748  314 P---VRKSAAEDPEEFLAENPNYKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEK 384
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 49-385 3.15e-28

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: 114.78  E-value: 3.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  49 NDVIALYQKANPQTEISGEMIAGSDYWTKLATSMAGRNVADIFQLEPST-IADYSGRGACMELDQFVGKSLDLSTFGKSE 127
Cdd:cd14749   18 DELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPGGwLAEFVKAGLLLPLTDYLDPNGVDKRFLPGL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 128 IDLCRIDGKLYGVGLGLNSFCMMYDADTLKEAG-VSVPQdqiTWKALAELARDFKKNGPAKRNYWAVPYGARYHYVFDVW 206
Cdd:cd14749   98 ADAVTFNGKVYGIPFAARALALFYNKDLFEEAGgVKPPK---TWDELIEAAKKDKFKAKGQTGFGLLLGAQGGHWYFQYL 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 207 LRQRGKLLFQD---GTIGFNKEDAKEWFAYWEDLRENKLCVSADIQ-TRDDNTIESN----ALTLGNSAIGFAYSNQLVG 278
Cdd:cd14749  175 VRQAGGGPLSDdgsGKATFNDPAFVQALQKLQDLVKAGAFQEGFEGiDYDDAGQAFAqgkaAMNIGGSWDLGAIKAGEPG 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 279 yqklnkqtLSIG--MLPGEGPGKPTGHYYRPGLIWSISSTSTNAEAAAKFINFFVNDlEAGKVLGVERGVPPAK-VVREA 355
Cdd:cd14749  255 --------GKIGvfPFPTVGKGAQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSP-EVMKQYLEDVGLLPAKeVVAKD 325

                        330       340       350
                 ....*....|....*....|....*....|..
gi 549799198 356 LLPTLNETERKTVDYIESLSG--KLDPYPEPA 385
Cdd:cd14749  326 EDPDPVAILGPFADVLNAAGStpFLDEYWPAA 357
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
37-349 6.25e-25

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 105.80  E-value: 6.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  37 VWWGSADRSKRTNDVIALYQKAnPQTEISGEMIAGSDYWTKLATSMAGRNVADIFQLEPSTIADYSGRGACMELDQFVGk 116
Cdd:COG2182   42 TVWVDDDEAEALEEAAAAFEEE-PGIKVKVVEVPWDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLA- 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 117 slDLSTFGKSEIDLCRIDGKLYGVGLGLNSFCMMYDADTLKEagvSVPQdqiTWKALAELARDFKKNG------PAKRNY 190
Cdd:COG2182  120 --DKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKA---EPPK---TWDELIAAAKKLTAAGkyglayDAGDAY 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 191 WAVP----YGAryhYVFdvwlrqrGKLLFQDGTIGFNKEDAKEWFAYWEDLRENKLcVSADIqtrdDNTIESNALTLGNS 266
Cdd:COG2182  192 YFYPflaaFGG---YLF-------GKDGDDPKDVGLNSPGAVAALEYLKDLIKDGV-LPADA----DYDAADALFAEGKA 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 267 AI----GFAYSNqlvgYQKLNKQTLSIGMLPGEGPGKPTGHYYRpGLIWSISSTSTNAEAAAKFINFFVNDlEAGKVLGV 342
Cdd:COG2182  257 AMiingPWAAAD----LKKALGIDYGVAPLPTLAGGKPAKPFVG-VKGFGVSAYSKNKEAAQEFAEYLTSP-EAQKALFE 330


                 ....*..
gi 549799198 343 ERGVPPA 349
Cdd:COG2182  331 ATGRIPA 337
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 51-333 8.98e-22

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: 94.79  E-value: 8.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198   51 VIALYQKANPQTEISGEMIAGSDYWTKLATSM-AGRNVADIFQLEPSTIADYSGRGACMELDQFVGKSLDLstfgkseid 129
Cdd:pfam01547  13 LVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIaAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYLVL--------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  130 lcrIDGKLYGVGLGLNSFCMMYDADTLKEAGVSVPQdqiTWKALAELARDFKKNGPAKRNYWAVPYGARYHYVFDVWLRQ 209
Cdd:pfam01547  84 ---GVPKLYGVPLAAETLGLIYNKDLFKKAGLDPPK---TWDELLEAAKKLKEKGKSPGGAGGGDASGTLGYFTLALLAS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  210 RGKLLFQDGTIGFNKEDAKEWFAYWEDL----RENKLCVSADIQTRDDNTIEsNALTLGNSAIGFAYSNQ--LVGYQKLN 283
Cdd:pfam01547 158 LGGPLFDKDGGGLDNPEAVDAITYYVDLyakvLLLKKLKNPGVAGADGREAL-ALFEQGKAAMGIVGPWAalAANKVKLK 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 549799198  284 KQTLSIGMLPGEGPGK---PTGHYYRPG-LIWSISSTSTNAEAAAKFINFFVND 333
Cdd:pfam01547 237 VAFAAPAPDPKGDVGYaplPAGKGGKGGgYGLAIPKGSKNKEAAKKFLDFLTSP 290
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 37-333 4.60e-20

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: 91.22  E-value: 4.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  37 VW-WGSADRSKRTNDVIALYQKANPQTEISGEMIAGSDYWTKLATSMAGRNVADIFQLEPSTIADYSGRGACMELDQFVG 115
Cdd:cd14747    4 VWaMGNSAEAELLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMGALEDLTPYLE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 116 KSLDLSTFGKSEIDLCRIDGKLYGVGLGLNSFCMMYDADTLKEAG-VSVPQdqiTWKALAELARDFKKNGPAKRNYwAVP 194
Cdd:cd14747   84 DLGGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGgDEAPK---TWDELEAAAKKIKADGPDVSGF-AIP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 195 YGARYHYVFDVWLRQRG-KLLFQD-GTIGFNKEDAKEWFAYWEDLRENKLCVSADIQTRDDntIESNaltLGNSAIGFAY 272
Cdd:cd14747  160 GKNDVWHNALPFVWGAGgDLATKDkWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSAD--VEQA---FANGKVAMII 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 273 SN-----QLVGYQKLNKQTLSIGMLPGeGPGKPtghyyRP----GLIWSISSTSTNAEAAAKFINFFVND 333
Cdd:cd14747  235 SGpweigAIREAGPDLAGKWGVAPLPG-GPGGG-----SPsfagGSNLAVFKGSKNKDLAWKFIEFLSSP 298
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 37-421 1.26e-18

The periplasmic-binding component of ABC transport systems specific for maltose and related polysaccharides; possess type 2 periplasmic binding fold; This subfamily represents the periplasmic binding component of ABC transport systems involved in uptake of polysaccharides including maltose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270304 [Multi-domain]  Cd Length: 367  Bit Score: 86.97  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  37 VWWGSADRSKRTNDVIALYQKANPQTEI--SGEMIAGSDywtKLATSMAGRNVADIFQLEPSTIADYSGRGACMELDQFV 114
Cdd:cd13586    4 VWTDEDGELEYLKELAEEFEKKYGIKVEvvYVDSGDTRE---KFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 115 GKSLDLStfgKSEIDLCRIDGKLYGVGLGLNSFCMMYDADTLKEagvsVPQdqiTWKALAELARDFKKNGPAKrnyWAVP 194
Cdd:cd13586   81 AVKIKNL---PVALAAVTYNGKLYGVPVSVETIALFYNKDLVPE----PPK---TWEELIALAKKFNDKAGGK---YGFA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 195 YGARYHYVFDVWLRQRGKLLF-QDG----TIGFNKEDAKEWFAYWEDLRENKLCVSADIqtrdDNTIESNALTLGNSAIG 269
Cdd:cd13586  148 YDQTNPYFSYPFLAAFGGYVFgENGgdptDIGLNNEGAVKGLKFIKDLKKKYKVLPPDL----DYDIADALFKEGKAAMI 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 270 FAYSNQLVGYQKLnKQTLSIGMLPGEGPGKPtghyYRP---GLIWSISSTSTNAEAAAKFINFFVNDlEAGKVLGVERGV 346
Cdd:cd13586  224 INGPWDLADYKDA-GINFGVAPLPTLPGGKQ----AAPfvgVQGAFVSAYSKNKEAAVEFAEYLTSD-EAQLLLFEKTGR 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 347 PPakvvreALLPTLNETERKTVDYIeSLSGKLDPYPEPAPI--------GAnefdrgvMRPIADSLAFGRATVDEAAQNL 418
Cdd:cd13586  298 IP------ALKDALNDAAVKNDPLV-KAFAEQAQYGVPMPNipemaavwDA-------MGNALNLVASGKATPEEAAKDA 363


                 ...
gi 549799198 419 VDT 421
Cdd:cd13586  364 VAA 366
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 50-349 5.41e-18

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 83.61  E-value: 5.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198   50 DVIALYQKANpQTEISGEMIAGSDYWTKLATSMAGRNV--ADIFQLEPSTIADYSGRGACMELDQFVGKSlDLSTFgkse 127
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNApdLDVVWIAADQLATLAEAGLLADLSDVDNLD-DLPDA---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  128 IDLCRIDGKLYGVGLGLNS-FCMMYDADTLKEAGVSVPqdqiTWKALAELARDFKKN----GPAKRNYWAVPYGAryhyv 202
Cdd:pfam13416  75 LDAAGYDGKLYGVPYAASTpTVLYYNKDLLKKAGEDPK----TWDELLAAAAKLKGKtgltDPATGWLLWALLAD----- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  203 fdvwlrqrGKLLFQDGTigfNKEDAKEWFAYWEDLRENKLCVSADIQTRDdntiesnALTLGNSAIGFAYSNQLVGYQKL 282
Cdd:pfam13416 146 --------GVDLTDDGK---GVEALDEALAYLKKLKDNGKVYNTGADAVQ-------LFANGEVAMTVNGTWAAAAAKKA 207

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799198  283 NKQtlsIGML-PGEGPgkPTGhyyrpGLIWSISSTSTNAEAAA-KFINFFVNDlEAGKVLGVERGVPPA 349
Cdd:pfam13416 208 GKK---LGAVvPKDGS--FLG-----GKGLVVPAGAKDPRLAAlDFIKFLTSP-ENQAALAEDTGYIPA 265
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 37-416 5.97e-18

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: 84.77  E-value: 5.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  37 VW-WGSADRSKRTNDVIALYQKANPQTEISGEMIAGSDYWTKLATSMAGRNVADIFQLEPSTIADYSGRGACMELDQFVG 115
Cdd:cd13522    4 VWhQYDTGENQAVNELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDEYVS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 116 KSLDLSTFGkseIDLCRIDGKLYGVGLGLNSFCMMYDADTLkeagvsVPQDQITWKALAELARDFKKngpakRNYWAVPY 195
Cdd:cd13522   84 KSGKYAPNT---IAAMKLNGKLYGVPVSVGAHLMYYNKKLV------PKNPPKTWQELIALAQGLKA-----KNVWGLVY 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 196 GARYHYVFDVWLRQRGKLLFQDG----TIGFNKEDAKEWFAYWEDLRENKLCVSADiqtrDDNTIESNALTLGNSAIGFA 271
Cdd:cd13522  150 NQNEPYFFAAWIGGFGGQVFKANngknNPTLDTPGAVEALQFLVDLKSKYKIMPPE----TDYSIADALFKAGKAAMIIN 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 272 YSNQLVGYQKLNKQTLSIGMLPGegpgKPTGHYYRP---GLIWSISSTSTNAEAAAKFINFFVNDlEAGKVLGVERGVPP 348
Cdd:cd13522  226 GPWDLGDYRQALKINLGVAPLPT----FSGTKHAAPfvgGKGFGINKESQNKAAAVEFVKYLTSY-QAQLVLFDDAGDIP 300

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 349 AKV-VREALLPTLNETERKTVDYIEslsgkldpYPEPAP-IGANEFDRGVMRPIADSLAFGRATVDEAAQ 416
Cdd:cd13522  301 ANLqAYESPAVQNKPAQKASAEQAA--------YGVPMPnIPEMRAVWDAFRIAVNSVLAGKVTPEAAAK 362
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 37-418 1.33e-13

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: 71.64  E-value: 1.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  37 VWW--GSADRSKRTNDVIALYQKANPQTEISGEMIAGSDYWTKLATSMAGRNVADIFQLEPSTIADYSGRGACMELDQFV 114
Cdd:cd14751    3 TFWhtSSDEEKVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDGTP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 115 GKSlDLSTFGKSEIDLCRIDGKLYGVGLGLNSFCMMYDADTLKEAGVSVPQDQITWKALAELARDFK-KNGPAKRN---Y 190
Cdd:cd14751   83 AFD-DIVDYLPGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEVPKTMDELVAAAKAIKKKKgRYGLYISGdgpY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 191 WAVPygarYHYVFDvwlrqrGKLLFQDG-TIGFNKEDAKEWFAYWEDLRENKLcVSADIQTRDDNTieSNALTLGNSAI- 268
Cdd:cd14751  162 WLLP----FLWSFG------GDLTDEKKaTGYLNSPESVRALETIVDLYDEGA-ITPCASGGYPNM--QDGFKSGRYAMi 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 269 --G-FAYSNQLVGYQKLNKQTLSIGMLPGEGPGKPT---GHYYrpgliwSISSTSTNAEAAAKFINFFVNDlEAGKVLGV 342
Cdd:cd14751  229 vnGpWAYADILGGKEFKDPDNLGIAPVPAGPGGSGSpvgGEDL------VIFKGSKNKDAAWKFVKFMSSA-EAQALTAA 301

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799198 343 ERGVPPakvVREALLPTLNETERKTVD-YIESLSGKLdPYPePAPIGANEFDrgVMRPIADSLAFGRATVDEAAQNL 418
Cdd:cd14751  302 KLGLLP---TRTSAYESPEVANNPMVAaFKPALETAV-PRP-PIPEWGELFE--PLTLAFAKVLRGEKSPREALDEA 371
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 48-343 2.90e-12

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: 68.12  E-value: 2.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  48 TNDVIALYQKANPQTEISGEMIAGSDYWTKLATSMAGRNVADIFQL-EPSTIADYSGRGACMELDQFVGK-SLDLSTFGK 125
Cdd:cd13580   20 DDNPYTKYLEEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVVnDPQLSITLVKQGALWDLTDYLDKyYPNLKKIIE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 126 SEIDLC-RIDGKLYGVGLGLNS---FCMMYDADTLKEAGVSVPQdqiTWKALAELARDFKKNGPAKrNYWAVPYGARYH- 200
Cdd:cd13580  100 QEGWDSaSVDGKIYGIPRKRPLigrNGLWIRKDWLDKLGLEVPK---TLDELYEVAKAFTEKDPDG-NGKKDTYGLTDTk 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 201 -------YVFDVWL--RQRGKLLFQDGTI--GFNKEDAKEWFAYWEDLRENKLcVSADIQTRDDNTIEsNALTLGNSAIG 269
Cdd:cd13580  176 dligsgfTGLFGAFgaPPNNWWKDEDGKLvpGSIQPEMKEALKFLKKLYKEGL-IDPEFAVNDGTKAN-EKFISGKAGIF 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 270 FAYSNQLVGYQKLNKQtlsigMLPGE------GPGKPTGHYYRP-----GLIWSISSTSTNAEAAAKFINFFVNDlEAGK 338
Cdd:cd13580  254 VGNWWDPAWPQASLKK-----NDPDAewvavpIPSGPDGKYGVWaesgvNGFFVIPKKSKKPEAILKLLDFLSDP-EVQK 327


                 ....*..
gi 549799198 339 VL--GVE 343
Cdd:cd13580  328 LLdyGIE 334
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 119-354 1.38e-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: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 119 DLSTFGKSEIDLCRIDGKLYGVGLGLNSFCMMYDADTLKEAgvsvPQdqiTWKALAELARDFkkNGPAKRNY-----WA- 192
Cdd:cd13658   82 KKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNA----PK---TFDELEALAKDL--TKEKGKQYgfladATn 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 193 --------VPYGAryhYVFdvwlRQRGKLLFQdGTIGFNKEDAKEWFAYWEDLRENKLcVSADIQtrdDNTIESnALTLG 264
Cdd:cd13658  153 fyysygllAGNGG---YIF----KKNGSDLDI-NDIGLNSPGAVKAVKFLKKWYTEGY-LPKGMT---GDVIQG-LFKEG 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 265 NSA--IGFAYSNQlvGYQ--KLNkqtLSIGMLPGEGPGKPTgHYYRPGLIWSISSTSTNAEAAAKFINFFVNDlEAGKVL 340
Cdd:cd13658  220 KAAavIDGPWAIQ--EYQeaGVN---YGVAPLPTLPNGKPM-APFLGVKGWYLSAYSKHKEWAQKFMEFLTSK-ENLKKR 292

                        250
                 ....*....|....*
gi 549799198 341 GVERG-VPPAKVVRE 354
Cdd:cd13658  293 YDETNeIPPRKDVRS 307
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 62-343 1.83e-07

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: 53.23  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  62 TEISGEMIAGSDYWTKLATSMAGRNVADIF--QLEPSTIADYSGRGACMELDQFVGKSLDLSTFGKSEIDLCR----IDG 135
Cdd:cd13521   32 VKLEIVAVTAATSQQKLNLMLASGDLPDIVgaDYLKDKFIAYGMEGAFLPLSKYIDQYPNLKAFFKQHPDVLRastaSDG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 136 KLYGVG----LGLNSFCMMYDADTLKEAGVSVPQdqiTWKALAEL-----ARDFKKNGPAKR----------------NY 190
Cdd:cd13521  112 KIYLIPyeppKDVPNQGYFIRKDWLDKLNLKTPK---TLDELYNVlkafkEKDPNGNGKADEipfidrdplygafrliNS 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 191 W-AVPYGARYHYVFDVwlrQRGKLlfqdgTIGFNKEDAKEWFAYWEDLRENKLcVSADIQTRDDNTIESNaLTLGNSAI- 268
Cdd:cd13521  189 WgARSAGGSTDSDWYE---DNGKF-----KHPFASEEYKDGMKYMNKLYTEGL-IDKESFTQKDDQAEQK-FSNGKLGGf 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 269 ---GFAYSNQLVGYQKLNK-QTLSIGMLPGEGPGKPTGHYYRPGL---IWSISSTSTNAEAAAKFINFFVNdlEAGKVL- 340
Cdd:cd13521  259 thnWFASDNLFTAQLGKEKpMYILLPIAPAGNVKGRREEDSPGYTgpdGVAISKKAKNPVAALKFFDWLAS--EEGRELa 336


                 ....*
gi 549799198 341 --GVE 343
Cdd:cd13521  337 nfGIE 341
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 67-330 5.85e-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: 270299 [Multi-domain]  Cd Length: 490  Bit Score: 41.92  E-value: 5.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  67 EMIAGSDYWTKLATSMAGRNVADIF---QLEPSTIADYSGRGACMELDQF-------VGKSLDLSTFGKSEIDlcRIDGK 136
Cdd:cd13581   37 ETVPEDAWAEKKNLMLASGDLPDAFlgaGASDADLMTYGKQGLFLPLEDLidkyapnLKALFDENPDIKAAIT--APDGH 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 137 LYGV------GLGLNSFCMMYDADTLKEAGVSVPQdqiTWKALAELARDFK-----KNGPAKRNYWAVPyGARYHYVFDV 205
Cdd:cd13581  115 IYALpsvnecYHCSYGQRMWINKKWLDKLGLEMPT---TTDELYEVLKAFKeqdpnGNGKADEIPLSFS-GLNGGTDDPA 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 206 WL---------RQRGKLLF-QDGTI--GFNKEDAKEWFAYWEDLRENKLcVSADIQTRDDNTIesnaLTLGNSA-----I 268
Cdd:cd13581  191 FLlnsfgindgGYGGYGFVvKDGKViyTATDPEYKEALAYLNKLYKEGL-IDPEAFTQDYDQL----AAKGKAStakvgV 265

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549799198 269 GFAYSNQLVGYQKLNKQTLSigMLPGEGPG--KPTGHYYRPGL-IWS--ISSTSTNAEAAAKFINFF 330
Cdd:cd13581  266 FFGWDPGLFFGEERYEQYVP--LPPLKGPNgdQLAWVGNSSGYgRGGfvITSKNKNPEAAIRWADFL 330
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
135-329 6.96e-04

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 41.43  E-value: 6.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 135 GKLYGVGLGLNSFCMMYDADTLKEAgvsvPQdqiTWKALaelardFKKNGPAKRNYWAVPYgaryhYVFDVWLRQRGKll 214
Cdd:COG0687  123 GNVYGVPYTWGTTGIAYNTDKVKEP----PT---SWADL------WDPEYKGKVALLDDPR-----EVLGAALLYLGY-- 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 215 fqdgtiGFNKEDAKEWFAYWEDLRENKlcvsADIQTRDDNTIES-NALTLGNSAIGFAYSNQlvgYQKLNKQTLSIGM-L 292
Cdd:COG0687  183 ------DPNSTDPADLDAAFELLIELK----PNVRAFWSDGAEYiQLLASGEVDLAVGWSGD---ALALRAEGPPIAYvI 249

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 549799198 293 PGEGpgkptghyyrpGLIW----SISSTSTNAEAAAKFINF 329
Cdd:COG0687  250 PKEG-----------ALLWfdnmAIPKGAPNPDLAYAFINF 279
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 39-183 3.46e-03

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


Pssm-ID: 270373 [Multi-domain]  Cd Length: 363  Bit Score: 39.25  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198  39 WGSADRSKRTNDVIALYQKANPQ------TEISGEMIAGSDYwtkLATSMAGrnvADIFQLEPSTIADYSGRGACMELDQ 112
Cdd:cd13655    5 WGPQEDQEWLKEMVDAFKEKHPEwkititIGVVGEADAKDEV---LKDPSAA---ADVFAFANDQLGELVDAGAIYPLTG 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549799198 113 FVGKSLDlSTFGKSEIDLCRIDGKLYGVGLGLNSFCMMYDADTLKEAGVSvpqdqiTWKALAELARDFKKN 183
Cdd:cd13655   79 SAVDKIK-NTNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLTEDDVK------SLDTMLAKAPDAKGK 142
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
129-333 8.36e-03

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 38.07  E-value: 8.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 129 DLCRIDGKLYGVGLGLNSFCMMYDADTLKEAgvsvPQdqiTWKALAELARDFKKNG------PAKRNYWAVPY-GARYHY 201
Cdd:PRK09474 121 DAVRYNGKLIGYPIAVEALSLIYNKDLVPTP----PK---TWEEIPALDKELKAKGksaimwNLQEPYFTWPLiAADGGY 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 202 VFDvwlRQRGKLLFQDgtIGFNKEDAKEWFAYWEDLRENKLcVSADIqtrdDNTIESNALTLGNSAI----GFAYSNqlv 277
Cdd:PRK09474 194 AFK---FENGGYDVKD--VGVNNAGAKAGLQFLVDLVKNKH-MNADT----DYSIAEAAFNKGETAMtingPWAWSN--- 260

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 549799198 278 gyqkLNKQTLSIGM--LPG--EGPGKP-TGhyyrpglIWS--ISSTSTNAEAAAKFI-NFFVND 333
Cdd:PRK09474 261 ----IDKSGINYGVtvLPTfnGKPSKPfVG-------VLSagINAASPNKELAKEFLeNYLLTD 313
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 222-329 8.43e-03

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


Pssm-ID: 270308 [Multi-domain]  Cd Length: 315  Bit Score: 37.98  E-value: 8.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799198 222 FNKEDAKEWFAYWEDLRENKlcvsADIQTRDDNTIEsNALTLGNSAIGFAYSNQLVgyqKLNKQTLSIG-MLPGEGpgkp 300
Cdd:cd13590  157 PNTTDPAELAAAAELLIKQK----PNVRAFDSDSYV-QDLASGEIWLAQAWSGDAL---QANRENPNLKfVIPKEG---- 224

                         90       100       110
                 ....*....|....*....|....*....|...
gi 549799198 301 tghyyrpGLIW----SISSTSTNAEAAAKFINF 329
Cdd:cd13590  225 -------GLLWvdnmAIPKGAPNPELAHAFINF 250
 
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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