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Conserved domains on  [gi|2674576668|ref|WP_331741924|]
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MULTISPECIES: extracellular solute-binding protein [unclassified Kitasatospora]

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 ...
 22-343 2.19e-52

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 179.85  E-value: 2.19e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  22 GVAACSSGGDGGSGdggpkAGGTTEVTFWGWAPG----YEEAAAQFNATHQDVRVKFEKIvsGSKGGYAKIFAAVKAGNA 97
Cdd:COG1653    15 ALAACGGGGSGAAA-----AAGKVTLTVWHTGGGeaaaLEALIKEFEAEHPGIKVEVESV--PYDDYRTKLLTALAAGNA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  98 PCLAQVGYESLPSFVVEGAVQDVGKEAAQYQP---QYGEAAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQYGLKPQAT 174
Cdd:COG1653    88 PDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLdkdDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPPKT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 175 WEEFAADADKLRAANpNGYLSVFNPDDPWWFAGMSAQAGGSWFGTDTKgwkvSLGSDPGTAKVANYWQGLVDKGVVKSEQ 254
Cdd:COG1653   168 WDELLAAAKKLKAKD-GVYGFALGGKDGAAWLDLLLSAGGDLYDEDGK----PAFDSPEAVEALEFLKDLVKDGYVPPGA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 255 SGT--PDLYKELQDGTLAAYPGPVWFSSILEQNAaqASGKWAVAPMPQWQDGAKSVGNDGGSSTAVVKGCKNTAAALQFA 332
Cdd:COG1653   243 LGTdwDDARAAFASGKAAMMINGSWALGALKDAA--PDFDVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAAWKFL 320

                         330
                  ....*....|.
gi 2674576668 333 NWMSTDAAAVA 343
Cdd:COG1653   321 KFLTSPEAQAK 331
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 22-343 2.19e-52

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 179.85  E-value: 2.19e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  22 GVAACSSGGDGGSGdggpkAGGTTEVTFWGWAPG----YEEAAAQFNATHQDVRVKFEKIvsGSKGGYAKIFAAVKAGNA 97
Cdd:COG1653    15 ALAACGGGGSGAAA-----AAGKVTLTVWHTGGGeaaaLEALIKEFEAEHPGIKVEVESV--PYDDYRTKLLTALAAGNA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  98 PCLAQVGYESLPSFVVEGAVQDVGKEAAQYQP---QYGEAAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQYGLKPQAT 174
Cdd:COG1653    88 PDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLdkdDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPPKT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 175 WEEFAADADKLRAANpNGYLSVFNPDDPWWFAGMSAQAGGSWFGTDTKgwkvSLGSDPGTAKVANYWQGLVDKGVVKSEQ 254
Cdd:COG1653   168 WDELLAAAKKLKAKD-GVYGFALGGKDGAAWLDLLLSAGGDLYDEDGK----PAFDSPEAVEALEFLKDLVKDGYVPPGA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 255 SGT--PDLYKELQDGTLAAYPGPVWFSSILEQNAaqASGKWAVAPMPQWQDGAKSVGNDGGSSTAVVKGCKNTAAALQFA 332
Cdd:COG1653   243 LGTdwDDARAAFASGKAAMMINGSWALGALKDAA--PDFDVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAAWKFL 320

                         330
                  ....*....|.
gi 2674576668 333 NWMSTDAAAVA 343
Cdd:COG1653   321 KFLTSPEAQAK 331
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 46-414 8.84e-52

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: 178.64  E-value: 8.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  46 EVTFWGWAPG-----YEEAAAQFNATHQDVRVKFEkIVSGSKGGYAKIFAAVKAGNAPCLAQVGYESLPSFVVEGAVQDV 120
Cdd:cd14748     1 EITFWHGMSGpdgkaLEELVDEFNKSHPDIKVKAV-YQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 121 GKEAAQYQP---QYGEAAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQYGL---KPQATWEEFAADADKLRAANPNGY- 193
Cdd:cd14748    80 DDYIDKDGVdddDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLdpeKPPKTWDELEEAAKKLKDKGGKTGr 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 194 --LSVFNPDDPWWFAGMSAQAGGSWFgtDTKGWKVSLgSDPGTAKVANYWQGLV-DKGVVKSEQSGTPDlyKELQDGTLA 270
Cdd:cd14748   160 ygFALPPGDGGWTFQALLWQNGGDLL--DEDGGKVTF-NSPEGVEALEFLVDLVgKDGVSPLNDWGDAQ--DAFISGKVA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 271 AYPGPVWFSSILEQNAaqASGKWAVAPMPQWQDGAKSVGNdGGSSTAVVKGC-KNTAAALQFANWMsTDAAAVATLVEKA 349
Cdd:cd14748   235 MTINGTWSLAGIRDKG--AGFEYGVAPLPAGKGKKGATPA-GGASLVIPKGSsKKKEAAWEFIKFL-TSPENQAKWAKAT 310

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674576668 350 GIYPASTSgtsapALAKPSAYFGNQPVFDVFKQASAQAAPFS-WGPTMTQTSSDLTDAFGAAVASK 414
Cdd:cd14748   311 GYLPVRKS-----AAEDPEEFLAENPNYKVAVDQLDYAKPWGpPVPNGAEIRDELNEALEAALLGK 371
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 53-341 2.61e-24

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: 102.11  E-value: 2.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  53 APGYEEAAAQFNATHQDVRVKFEkiVSGSKGGYAKIFAAVKAGNAPC-LAQVGYESLPSFVVEGAVQDVGKEAAQYqpqy 131
Cdd:pfam01547   7 AAALQALVKEFEKEHPGIKVEVE--SVGSGSLAQKLTTAIAAGDGPAdVFASDNDWIAELAKAGLLLPLDDYVANY---- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 132 geaawnSVKVGGQVYGIPVDMGPMALYYRSDLYAQYGLKPQATWEEFAADADKLRAANPNGYLSVFN---PDDPWWFAGM 208
Cdd:pfam01547  81 ------LVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAGGGdasGTLGYFTLAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 209 SAQAGGSWFGTDTKGWKVSLGSDPGTAKVANYWQGLVDKGVV--KSEQSGTPDLYKELQDGTLAAYPGPVW--------- 277
Cdd:pfam01547 155 LASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKnpGVAGADGREALALFEQGKAAMGIVGPWaalaankvk 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674576668 278 FSSILEQNAAQASGKWAVAPMPQWQDGAksvgnDGGSSTAVVKGCKNTAAALQFANWMSTDAAA 341
Cdd:pfam01547 235 LKVAFAAPAPDPKGDVGYAPLPAGKGGK-----GGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQ 293
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
41-188 3.92e-10

sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 61.35  E-value: 3.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  41 AGGTTEVTFWGWAPG-----YEEAAAQFNATHQDVrvkfeKIVSGSKGGY----AKIFAAVKAGNAPCLAQVGYESLPSF 111
Cdd:PRK10974   22 AQAVTEIPFWHSMEGelgkeVDSLAQRFNASQPDY-----KIVPVYKGNYeqslAAGIAAFRSGNAPAILQVYEVGTATM 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 112 VVEGA---VQDVGKEA------AQYQPQYgeAAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQYGLKPQA---TWEEFA 179
Cdd:PRK10974   97 MASKAikpVYDVFKDAgipfdeSQFVPTV--AGYYSDAKTGHLLSQPFNSSTPVLYYNKDAFKKAGLDPEQppkTWQDLA 174


                  ....*....
gi 2674576668 180 ADADKLRAA 188
Cdd:PRK10974  175 AYAAKLRAA 183
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 22-343 2.19e-52

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 179.85  E-value: 2.19e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  22 GVAACSSGGDGGSGdggpkAGGTTEVTFWGWAPG----YEEAAAQFNATHQDVRVKFEKIvsGSKGGYAKIFAAVKAGNA 97
Cdd:COG1653    15 ALAACGGGGSGAAA-----AAGKVTLTVWHTGGGeaaaLEALIKEFEAEHPGIKVEVESV--PYDDYRTKLLTALAAGNA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  98 PCLAQVGYESLPSFVVEGAVQDVGKEAAQYQP---QYGEAAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQYGLKPQAT 174
Cdd:COG1653    88 PDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLdkdDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPPKT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 175 WEEFAADADKLRAANpNGYLSVFNPDDPWWFAGMSAQAGGSWFGTDTKgwkvSLGSDPGTAKVANYWQGLVDKGVVKSEQ 254
Cdd:COG1653   168 WDELLAAAKKLKAKD-GVYGFALGGKDGAAWLDLLLSAGGDLYDEDGK----PAFDSPEAVEALEFLKDLVKDGYVPPGA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 255 SGT--PDLYKELQDGTLAAYPGPVWFSSILEQNAaqASGKWAVAPMPQWQDGAKSVGNDGGSSTAVVKGCKNTAAALQFA 332
Cdd:COG1653   243 LGTdwDDARAAFASGKAAMMINGSWALGALKDAA--PDFDVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAAWKFL 320

                         330
                  ....*....|.
gi 2674576668 333 NWMSTDAAAVA 343
Cdd:COG1653   321 KFLTSPEAQAK 331
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 46-414 8.84e-52

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: 178.64  E-value: 8.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  46 EVTFWGWAPG-----YEEAAAQFNATHQDVRVKFEkIVSGSKGGYAKIFAAVKAGNAPCLAQVGYESLPSFVVEGAVQDV 120
Cdd:cd14748     1 EITFWHGMSGpdgkaLEELVDEFNKSHPDIKVKAV-YQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 121 GKEAAQYQP---QYGEAAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQYGL---KPQATWEEFAADADKLRAANPNGY- 193
Cdd:cd14748    80 DDYIDKDGVdddDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLdpeKPPKTWDELEEAAKKLKDKGGKTGr 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 194 --LSVFNPDDPWWFAGMSAQAGGSWFgtDTKGWKVSLgSDPGTAKVANYWQGLV-DKGVVKSEQSGTPDlyKELQDGTLA 270
Cdd:cd14748   160 ygFALPPGDGGWTFQALLWQNGGDLL--DEDGGKVTF-NSPEGVEALEFLVDLVgKDGVSPLNDWGDAQ--DAFISGKVA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 271 AYPGPVWFSSILEQNAaqASGKWAVAPMPQWQDGAKSVGNdGGSSTAVVKGC-KNTAAALQFANWMsTDAAAVATLVEKA 349
Cdd:cd14748   235 MTINGTWSLAGIRDKG--AGFEYGVAPLPAGKGKKGATPA-GGASLVIPKGSsKKKEAAWEFIKFL-TSPENQAKWAKAT 310

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674576668 350 GIYPASTSgtsapALAKPSAYFGNQPVFDVFKQASAQAAPFS-WGPTMTQTSSDLTDAFGAAVASK 414
Cdd:cd14748   311 GYLPVRKS-----AAEDPEEFLAENPNYKVAVDQLDYAKPWGpPVPNGAEIRDELNEALEAALLGK 371
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 46-418 1.06e-50

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: 176.06  E-value: 1.06e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  46 EVTFWGWA-----PGYEEAAAQFNATHQDVrvKFEKIVSGSKGGYAKIFAAVKAGNAPCLAQVGYESLPSFVVEGAVQDV 120
Cdd:cd13585     1 TLTFWDWGqpaetAALKKLIDAFEKENPGV--KVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 121 GK--EAAQYQPQYGEAAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQYG--LKPQATWEEFAADADKLRAANPN--GYL 194
Cdd:cd13585    79 DDyiEKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGpgPKPPWTWDELLEAAKKLTDKKGGqyGFA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 195 SVFNPDDPWWFAGMSAQAGGSWFgtDTKGWKVSLGSdPGTAKVANYWQGLVDKGVV-KSEQSGTPDLYKELQDGTLAAYP 273
Cdd:cd13585   159 LRGGSGGQTQWYPFLWSNGGDLL--DEDDGKATLNS-PEAVEALQFYVDLYKDGVApSSATTGGDEAVDLFASGKVAMMI 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 274 GPVWFSSILEQnaAQASGKWAVAPMPQWqDGAKSVGNDGGSSTAVVKGCKNTAAALQFANWMSTDAAAvatlveKAGIYP 353
Cdd:cd13585   236 DGPWALGTLKD--SKVKFKWGVAPLPAG-PGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQ------LKLGGA 306

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674576668 354 ASTSGTSAPALAKPSAYFGNQPVFDVFKQASAQAAPFSWGPTMTQTSSDLTDAFGAAVASKGRLT 418
Cdd:cd13585   307 AGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGALGKS 371
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
22-434 1.31e-45

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 163.20  E-value: 1.31e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  22 GVAACSSGGDGGSGDGGPKAGGTteVTFWGW---APGYEEAAAQFNATHqDVRVKFEKIVSGSkgGYAKIFAAVKAGNAP 98
Cdd:COG2182    18 ALAACGSGSSSSGSSSAAGAGGT--LTVWVDddeAEALEEAAAAFEEEP-GIKVKVVEVPWDD--LREKLTTAAPAGKGP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  99 CLAQVGYESLPSFVVEGAVQDVGKEAAQYQpQYGEAAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQyglKPQATWEEF 178
Cdd:COG2182    93 DVFVGAHDWLGELAEAGLLAPLDDDLADKD-DFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKA---EPPKTWDEL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 179 AADADKLRAANPNGYLsvFNPDDPWWFAGMSAQAGGSWFGTDTK-GWKVSLGSdPGTAKVANYWQGLVDKGVVKSEQSGT 257
Cdd:COG2182   169 IAAAKKLTAAGKYGLA--YDAGDAYYFYPFLAAFGGYLFGKDGDdPKDVGLNS-PGAVAALEYLKDLIKDGVLPADADYD 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 258 pDLYKELQDGTLAAYPGPVWFSsileQNAAQASG-KWAVAPMPQWQDGAKSVGNDGGSSTAVVKGCKNTAAALQFANWMS 336
Cdd:COG2182   246 -AADALFAEGKAAMIINGPWAA----ADLKKALGiDYGVAPLPTLAGGKPAKPFVGVKGFGVSAYSKNKEAAQEFAEYLT 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 337 TDAAAVAtLVEKAGIYPASTSGTSAPALAKpsayfgnQPVFDVFKQASAQAAPFSWGPTMTQTSSDLTDAFGAAVASKGR 416
Cdd:COG2182   321 SPEAQKA-LFEATGRIPANKAAAEDAEVKA-------DPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKAD 392

                         410
                  ....*....|....*...
gi 2674576668 417 LTGALGTVQGKTVDAMKS 434
Cdd:COG2182   393 PAEALDAAQKQIEAAIAQ 410
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 46-415 2.10e-42

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: 154.01  E-value: 2.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  46 EVTFW-----GWAPGYEEAAAQFNATHQDVRVKFEKIVSGSkgGYAKIFAAVKAGNAPCLAQVGYESLPSFVVEGAVQDV 120
Cdd:cd14747     1 TLTVWamgnsAEAELLKELADEFEKENPGIEVKVQVLPWGD--AHTKITTAAASGDGPDVVQLGNTWVAEFAAMGALEDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 121 G---KEAAQYQPQYgEAAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQYG-LKPQATWEEFAADADKLRAANPNGYLSV 196
Cdd:cd14747    79 TpylEDLGGDKDLF-PGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGgDEAPKTWDELEAAAKKIKADGPDVSGFA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 197 FNPDDPWWFAGMS--AQAGGSWFgtdTKGWKVSLGSDPGTAKVANYWQGLVDKGVV-KSEQSGTPDLYKELQDGTLAAYP 273
Cdd:cd14747   158 IPGKNDVWHNALPfvWGAGGDLA---TKDKWKATLDSPEAVAGLEFYTSLYQKGLSpKSTLENSADVEQAFANGKVAMII 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 274 GPVWFSSILEQNAAQASGKWAVAPMPQwQDGAKSVGNDGGSSTAVVKGCKNTAAALQFANWMSTDAAAVAtLVEKAGIYP 353
Cdd:cd14747   235 SGPWEIGAIREAGPDLAGKWGVAPLPG-GPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAA-YAKATGMLP 312

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674576668 354 ASTSGTSAPALAkpsayfgNQPVFDVFKQASAQAAPFSWGPTMTQTSSDLTDAFGAAVASKG 415
Cdd:cd14747   313 ANTSAWDDPSLA-------NDPLLAVFAEQLKTGKATPATPEWGEIEAELVLVLEEVWIGVG 367
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 46-415 1.57e-31

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: 124.41  E-value: 1.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  46 EVTFWGWAPG------YEEAAAQFNATHQDVRVKFEkiVSGSKGGYAKIFAAVKAGNAPCLAQV-GYESLPSFVVEGAVQ 118
Cdd:cd14749     1 TITYWQYFTGdtkkkyMDELIADFEKENPNIKVKVV--VFPYDNYKTKLKTAVAAGEGPDVFNLwPGGWLAEFVKAGLLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 119 DVGKeaaqYQPQYGE------AAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQYG-LKPQATWEEFAADA--DKLRAAN 189
Cdd:cd14749    79 PLTD----YLDPNGVdkrflpGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGgVKPPKTWDELIEAAkkDKFKAKG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 190 PNGY-LSVFNPDDPWWFAGMSAQAGGSWFGTDTKGwKVSLGSDPGTaKVANYWQGLVDKGVVKS--EQSGTPDLYKELQD 266
Cdd:cd14749   155 QTGFgLLLGAQGGHWYFQYLVRQAGGGPLSDDGSG-KATFNDPAFV-QALQKLQDLVKAGAFQEgfEGIDYDDAGQAFAQ 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 267 GTLAAYPGPVWFSSILeqNAAQASGKWAVAPMPQWQDGAKSVGNdGGSSTAVV--KGCKNTAAALQFANWMSTDAAAVAT 344
Cdd:cd14749   233 GKAAMNIGGSWDLGAI--KAGEPGGKIGVFPFPTVGKGAQTSTI-GGSDWAIAisANGKKKEAAVKFLKYLTSPEVMKQY 309

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674576668 345 LvEKAGIYPASTSGTSAPALAKPSAYfgnQPVFDVFKQASAQaapFSWGPTMTQTSSDLTDAFGAAVASKG 415
Cdd:cd14749   310 L-EDVGLLPAKEVVAKDEDPDPVAIL---GPFADVLNAAGST---PFLDEYWPAAAQVHKDAVQKLLTGKI 373
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 56-414 5.74e-27

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: 111.32  E-value: 5.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  56 YEEAAAQFNATHQDVRVKfekIVSGSKGGYA-KIFAAVKAGNAPCLAQVGYESLPSFVVEGAVQDVGKEAAQY-QPQYGE 133
Cdd:cd14751    16 YEKLIPAFEKEYPKIKVK---AVRVPFDGLHnQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDGTPAFDdIVDYLP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 134 AAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQYGLKPQATWEEF-AADADKLRAANPNGYLsvFNPDDPWWFAGMSAQA 212
Cdd:cd14751    93 GPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEVPKTMDELvAAAKAIKKKKGRYGLY--ISGDGPYWLLPFLWSF 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 213 GGSWfgTDTKGWKVSLGSdPGTAKVANYWQGLVDKGVVKSEQSGT-PDLYKELQDGTLA-AYPGPVWFSSILEQNAAQAS 290
Cdd:cd14751   171 GGDL--TDEKKATGYLNS-PESVRALETIVDLYDEGAITPCASGGyPNMQDGFKSGRYAmIVNGPWAYADILGGKEFKDP 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 291 GKWAVAPMPQWQDGAKSVgnDGGSSTAVVKGCKNTAAALQFANWMSTDAAAVATlVEKAGIYPASTSGTSAPALAkpsay 370
Cdd:cd14751   248 DNLGIAPVPAGPGGSGSP--VGGEDLVIFKGSKNKDAAWKFVKFMSSAEAQALT-AAKLGLLPTRTSAYESPEVA----- 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2674576668 371 fgNQPVFDVFKQASAQAAPFSWGPTMTQTSSDLTDAFGAAVASK 414
Cdd:cd14751   320 --NNPMVAAFKPALETAVPRPPIPEWGELFEPLTLAFAKVLRGE 361
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 46-390 1.62e-25

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: 107.00  E-value: 1.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  46 EVTFWGWAPGY----EEAAAQFNATHqDVRVKFEKIVSGSkgGYAKIFAAVKAGNAPCLAQVGYESLPSFVVEGAVQDVG 121
Cdd:cd13586     1 TITVWTDEDGEleylKELAEEFEKKY-GIKVEVVYVDSGD--TREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 122 KEAAQyQPQYGEAAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQyglkPQATWEEFAADADKLRAANPNGYLSVFNPDD 201
Cdd:cd13586    78 EYLAV-KIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPE----PPKTWEELIALAKKFNDKAGGKYGFAYDQTN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 202 PWWFAGMSAQAGGSWFGTDTKGWKVSLGSDPGTAKVANYWQGLVDKGVVKSEQSGTPDLYKELQDGTLAAY-PGPvWfsS 280
Cdd:cd13586   153 PYFSYPFLAAFGGYVFGENGGDPTDIGLNNEGAVKGLKFIKDLKKKYKVLPPDLDYDIADALFKEGKAAMIiNGP-W--D 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 281 IleqNAAQASG-KWAVAPMPQWqDGAKSVGNDGGSSTAVV-KGCKNTAAALQFANWMSTDAAAVAtLVEKAGIYPASTSG 358
Cdd:cd13586   230 L---ADYKDAGiNFGVAPLPTL-PGGKQAAPFVGVQGAFVsAYSKNKEAAVEFAEYLTSDEAQLL-LFEKTGRIPALKDA 304

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2674576668 359 TSAPALAkpsayfgNQPVFDVFKQASAQAAPF 390
Cdd:cd13586   305 LNDAAVK-------NDPLVKAFAEQAQYGVPM 329
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 52-427 5.47e-25

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: 105.84  E-value: 5.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  52 WAPGYEEAAAQFNATHQDVRVKFEKIVSGSKGGYAKIFAAVKAGNAPC-LAQVGYESLPSFVVEGAVQDVGKEAAQ-YQP 129
Cdd:cd14750    12 EGELLKKAIAAFEKKHPDIKVEIEELPASSDDQRQQLVTALAAGSSAPdVLGLDVIWIPEFAEAGWLLPLTEYLKEeEDD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 130 QYGEAAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQYGLKPQATWEEFAADADKLRAANPN--GYLSVFNPDDPW--WF 205
Cdd:cd14750    92 DFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPEPPKTWDELLEAAKKRKAGEPGiwGYVFQGKQYEGLvcNF 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 206 AGMSAQAGGSWFgtDTKGWKVSLGSdPGTAKVANYWQGLVDKGVVKSEQS--GTPDLYKELQDGTlAAYPGpVWFS--SI 281
Cdd:cd14750   172 LELLWSNGGDIF--DDDSGKVTVDS-PEALEALQFLRDLIGEGISPKGVLtyGEEEARAAFQAGK-AAFMR-NWPYayAL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 282 LEQNAAQASGKWAVAPMPQwQDGAKSVGNDGGSSTAVVKGCKNTAAALQFANWMsTDAAAVATLVEKAGIYPAStsgtsa 361
Cdd:cd14750   247 LQGPESAVAGKVGVAPLPA-GPGGGSASTLGGWNLAISANSKHKEAAWEFVKFL-TSPEVQKRRAINGGLPPTR------ 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674576668 362 PALAKPSAYFGNQPVFDVFKQASAQAAPFSWGPTMTQTSSDLTDAFGAAVASKGRLTGALGTVQGK 427
Cdd:cd14750   319 RALYDDPEVLEAYPFLPALLEALENAVPRPVTPKYPEVSTAIQIALSAALSGQATPEEALKQAQEK 384
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 53-341 2.61e-24

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: 102.11  E-value: 2.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  53 APGYEEAAAQFNATHQDVRVKFEkiVSGSKGGYAKIFAAVKAGNAPC-LAQVGYESLPSFVVEGAVQDVGKEAAQYqpqy 131
Cdd:pfam01547   7 AAALQALVKEFEKEHPGIKVEVE--SVGSGSLAQKLTTAIAAGDGPAdVFASDNDWIAELAKAGLLLPLDDYVANY---- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 132 geaawnSVKVGGQVYGIPVDMGPMALYYRSDLYAQYGLKPQATWEEFAADADKLRAANPNGYLSVFN---PDDPWWFAGM 208
Cdd:pfam01547  81 ------LVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAGGGdasGTLGYFTLAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 209 SAQAGGSWFGTDTKGWKVSLGSDPGTAKVANYWQGLVDKGVV--KSEQSGTPDLYKELQDGTLAAYPGPVW--------- 277
Cdd:pfam01547 155 LASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKnpGVAGADGREALALFEQGKAAMGIVGPWaalaankvk 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674576668 278 FSSILEQNAAQASGKWAVAPMPQWQDGAksvgnDGGSSTAVVKGCKNTAAALQFANWMSTDAAA 341
Cdd:pfam01547 235 LKVAFAAPAPDPKGDVGYAPLPAGKGGK-----GGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQ 293
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 47-414 1.65e-19

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: 89.39  E-value: 1.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  47 VTFWGWAPGYE-----EAAAQFNATHQDVRVKFEKIVSgsKGGYAKIFAAVKAGNAPCLAQVGYESLPSFVVEGAVQDVg 121
Cdd:cd13522     2 ITVWHQYDTGEnqavnELIAKFEKAYPGITVEVTYQDT--EARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPL- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 122 keaAQYQPQ---YGEAAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQyglKPQATWEEFAADADKLRAANPNGYlsVFN 198
Cdd:cd13522    79 ---DEYVSKsgkYAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVPK---NPPKTWQELIALAQGLKAKNVWGL--VYN 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 199 PDDPWWFAGMSAQAGGSWFGTDTKGWKVSLGSdPGTAKVANYWQGLVDKGVVKSEQSGTPDLYKELQDGTLAAY-PGPVW 277
Cdd:cd13522   151 QNEPYFFAAWIGGFGGQVFKANNGKNNPTLDT-PGAVEALQFLVDLKSKYKIMPPETDYSIADALFKAGKAAMIiNGPWD 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 278 FSSILEqnaaQASGKWAVAPMPQWQDGAKSVGNDGGSSTAVVKGCKNTAAALQFA-NWMSTDAAAVatLVEKAGIYPAST 356
Cdd:cd13522   230 LGDYRQ----ALKINLGVAPLPTFSGTKHAAPFVGGKGFGINKESQNKAAAVEFVkYLTSYQAQLV--LFDDAGDIPANL 303

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2674576668 357 SGTSAPALAkpsayfgNQPVFDVFKQASAQAAPFSWGPTMTQTSSDLTDAFGAAVASK 414
Cdd:cd13522   304 QAYESPAVQ-------NKPAQKASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGK 354
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 58-366 9.68e-19

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 85.92  E-value: 9.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  58 EAAAQFNATHqDVRVKFEKivSGSKGGYAKIFAAVKAGNAP--CLAQVGYESLPSFVVEGAVQDVGK-EAAQYQPQYGEA 134
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEP--QASNDLQAKLLAAAAAGNAPdlDVVWIAADQLATLAEAGLLADLSDvDNLDDLPDALDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 135 AWnsvkVGGQVYGIPVDMG-PMALYYRSDLYAQYGLKPqATWEEFAADADKLRAAnpNGYlsvfnPDDPWWFAGMSAQAG 213
Cdd:pfam13416  78 AG----YDGKLYGVPYAAStPTVLYYNKDLLKKAGEDP-KTWDELLAAAAKLKGK--TGL-----TDPATGWLLWALLAD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 214 GSWFGTDTKGWkvslgsdPGTAKVANYWQGLVDKGVVKSEQSGTPdlyKELQDGTLAAYPGPVWfsSIleQNAAQASGKW 293
Cdd:pfam13416 146 GVDLTDDGKGV-------EALDEALAYLKKLKDNGKVYNTGADAV---QLFANGEVAMTVNGTW--AA--AAAKKAGKKL 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674576668 294 AVAPMpqwQDGAKSvgndGGSSTAVVKGCKN-TAAALQFANWMsTDAAAVATLVEKAGIYPASTSGTSAPALAK 366
Cdd:pfam13416 212 GAVVP---KDGSFL----GGKGLVVPAGAKDpRLAALDFIKFL-TSPENQAALAEDTGYIPANKSAALSDEVKA 277
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 46-425 2.01e-16

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: 80.50  E-value: 2.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  46 EVTFW-GWAPGYEEA----AAQFNATH--QDVRVKFEKIVSGSkggyAKIFAAVKAGNAPCLAQVGYESLPSFVVEGAVQ 118
Cdd:cd13657     1 TITIWhALTGAEEDAlqqiIDEFEAKYpvPNVKVPFEKKPDLQ----NKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 119 DV-GKEAAQYQPQYGEAAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQyglkPQATWEEFAADADKLRAANPNGYLSVF 197
Cdd:cd13657    77 PIsDYLSEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQ----PPETTDELLAIMKDHTDPAAGSYGLAY 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 198 NPDDPWWFAGMSAQAGGSWFgtDTKGWKVSLGSdPGTAKVANYWQGLVdKGVVKSEQSGtpDLYKEL-QDGTLAAYPGPV 276
Cdd:cd13657   153 QVSDAYFVSAWIFGFGGYYF--DDETDKPGLDT-PETIKGIQFLKDFS-WPYMPSDPSY--NTQTSLfNEGKAAMIINGP 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 277 WFSSILEQNAAqasgKWAVAPMPQWqDGAKSVGNDGGSSTAVV---KGCKNTAAALQFANWMsTDAAAVATLVEKAGIYP 353
Cdd:cd13657   227 WFIGGIKAAGI----DLGVAPLPTV-DGTNPPRPYSGVEGIYVtkyAERKNKEAALDFAKFF-TTAEASKILADENGYVP 300

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674576668 354 ASTSGTSAPALAkpsayfgNQPVFDVFKQASAQAAPFSWGPTMTQTSSDLTDAFGAAVASKGRLTGALGTVQ 425
Cdd:cd13657   301 AATNAYDDAEVA-------ADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQEALAAAQ 365
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 55-398 5.39e-13

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: 69.82  E-value: 5.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  55 GYEEAAAQFnaTHQ-DVRVKFEKIvsGSKGGYAKIFAAVKAGNAPCLAQVGYESLPSFVVEGAVQDVgKEAAQYQPQYGE 133
Cdd:cd13658    14 FIKKIAKQY--TKKtGVKVKLVEV--DQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPI-KLSKDKKKGFTD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 134 AAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQyglkPQATWEEFAADADKLRAANPNGYLSVFNPDDPWWFAGMSAQAG 213
Cdd:cd13658    89 QALKALTYDGKLYGLPAAVETLALYYNKDLVKN----APKTFDELEALAKDLTKEKGKQYGFLADATNFYYSYGLLAGNG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 214 GSWFG-TDTKGWKVSLGSD-PGTAKVANYWQGLVDKGVVKseQSGTPDLYKEL-QDGTLAAYPGPVWfssilEQNAAQAS 290
Cdd:cd13658   165 GYIFKkNGSDLDINDIGLNsPGAVKAVKFLKKWYTEGYLP--KGMTGDVIQGLfKEGKAAAVIDGPW-----AIQEYQEA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 291 GK-WAVAPMPQWQDGAKSVGNDGGSSTAVVKGCKNTAAALQFANWMSTDaAAVATLVEKAGIYPASTSgtsapalAKPSA 369
Cdd:cd13658   238 GVnYGVAPLPTLPNGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTSK-ENLKKRYDETNEIPPRKD-------VRSDP 309

                         330       340
                  ....*....|....*....|....*....
gi 2674576668 370 YFGNQPVFDVFKQASAQAAPFSWGPTMTQ 398
Cdd:cd13658   310 EIKNNPLTSAFAKQASRAVPMPNIPEMGA 338
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 87-338 2.15e-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: 68.51  E-value: 2.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  87 KIFAAVKAGNAPCLAQV-GYESLPSFVVEGAVQDVGKEAAQYQPQY----GEAAWNSVKVGGQVYGIPV---DMGPMALY 158
Cdd:cd13580    49 KLNLALASGDLPDIVVVnDPQLSITLVKQGALWDLTDYLDKYYPNLkkiiEQEGWDSASVDGKIYGIPRkrpLIGRNGLW 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 159 YRSDLYAQYGLKPQATWEEFAADADKLRAANPNGY-------LSVFNPDDPWWFAGMSA--QAGGSWFGTDTKGWKVSLG 229
Cdd:cd13580   129 IRKDWLDKLGLEVPKTLDELYEVAKAFTEKDPDGNgkkdtygLTDTKDLIGSGFTGLFGafGAPPNNWWKDEDGKLVPGS 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 230 SDPGTAKVANYWQGLVDKGV------VKSEQSGTPDLYKelqdGTLAAYPGPVW-FSSILEQNAAQASG-KWAVAPMPQW 301
Cdd:cd13580   209 IQPEMKEALKFLKKLYKEGLidpefaVNDGTKANEKFIS----GKAGIFVGNWWdPAWPQASLKKNDPDaEWVAVPIPSG 284

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2674576668 302 QDGAKSVG-NDGGSSTAVV-KGCKNTAAALQFANWMSTD 338
Cdd:cd13580   285 PDGKYGVWaESGVNGFFVIpKKSKKPEAILKLLDFLSDP 323
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 56-366 3.48e-11

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: 64.29  E-value: 3.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  56 YEEAAAQFNATHQDVRVKFEKIVSGSKGGYAKIFAAVKAgnAPCLAQVGYESLPSFVVEGAVQDVGKEAAQ-YQPQYGEA 134
Cdd:cd13655    14 LKEMVDAFKEKHPEWKITITIGVVGEADAKDEVLKDPSA--AADVFAFANDQLGELVDAGAIYPLTGSAVDkIKNTNSEA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 135 AWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQYGLKpqaTWEEFaadadkLRAANPNGYLSVFNPDDPWWFAGMSAQAGG 214
Cdd:cd13655    92 TVDAVTYNGKLYGYPFTANTWFMYYDKSKLTEDDVK---SLDTM------LAKAPDAKGKVSFDLSNSWYLYAFFFGAGC 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 215 SWFG-TDTKGWKVSLGSDPGTAkVANYWQGLVDKGVVKSEQSGtpDLYKELQDGTLAAYPGPVWfssileqNAAQASGKW 293
Cdd:cd13655   163 KLFGnNGGDTAGCDFNNEKGVA-VTNYLVDLVANPKFVNDADG--DAISGLKDGTLGAGVSGPW-------DAANLKKAL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 294 ----AVAPMPQWQDGAKSV--GNDGGSSTAVVKG-CKNTAAALQFANWMsTDAAAVATLVEKAGIYPASTSGTSAPALAK 366
Cdd:cd13655   233 gdnyAVAKLPTYTLGGKDVqmKSFAGYKAIGVNSnTKNPEAAMALADYL-TNEESQLTRFEKRGIGPTNKEAAESDAVKA 311
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 90-340 3.40e-10

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: 61.70  E-value: 3.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  90 AAVKAGNAP--CLAQVGYESLPSFVVEGAVQDVGKEAAQYqP-------QYGEAAWNSVKVGGQVYGIP---VDMGPMAL 157
Cdd:cd13521    50 LMLASGDLPdiVGADYLKDKFIAYGMEGAFLPLSKYIDQY-PnlkaffkQHPDVLRASTASDGKIYLIPyepPKDVPNQG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 158 YY-RSDLYAQYGLKPQATWEEFAADADKLRAANPNGY-----LSVFNPDDPW-WFAGMSAQAGGSWFGTDTKGWKVSLGS 230
Cdd:cd13521   129 YFiRKDWLDKLNLKTPKTLDELYNVLKAFKEKDPNGNgkadeIPFIDRDPLYgAFRLINSWGARSAGGSTDSDWYEDNGK 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 231 --DPGTAK----VANYWQGLVDKGVVKSEQSGTPDLYKE--LQDGTLAAYPGPvWFSSILEQNAAQAS---GKWAVAPMP 299
Cdd:cd13521   209 fkHPFASEeykdGMKYMNKLYTEGLIDKESFTQKDDQAEqkFSNGKLGGFTHN-WFASDNLFTAQLGKekpMYILLPIAP 287

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2674576668 300 -------QWQDGAKSVGNDGgssTAVVKGCKNTAAALQFANWMSTDAA 340
Cdd:cd13521   288 agnvkgrREEDSPGYTGPDG---VAISKKAKNPVAALKFFDWLASEEG 332
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
41-188 3.92e-10

sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 61.35  E-value: 3.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  41 AGGTTEVTFWGWAPG-----YEEAAAQFNATHQDVrvkfeKIVSGSKGGY----AKIFAAVKAGNAPCLAQVGYESLPSF 111
Cdd:PRK10974   22 AQAVTEIPFWHSMEGelgkeVDSLAQRFNASQPDY-----KIVPVYKGNYeqslAAGIAAFRSGNAPAILQVYEVGTATM 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 112 VVEGA---VQDVGKEA------AQYQPQYgeAAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQYGLKPQA---TWEEFA 179
Cdd:PRK10974   97 MASKAikpVYDVFKDAgipfdeSQFVPTV--AGYYSDAKTGHLLSQPFNSSTPVLYYNKDAFKKAGLDPEQppkTWQDLA 174


                  ....*....
gi 2674576668 180 ADADKLRAA 188
Cdd:PRK10974  175 AYAAKLRAA 183
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 94-338 1.77e-07

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: 53.13  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  94 AGNAPCLAQVGY-ESLPSFVVEGAVQDVGKEAaQYQPQYGEA--AWNSVKV-------GGQVYGIPV---DMGP-MALYY 159
Cdd:cd13583    54 SGDAPDIIPVLYpGEENEFVASGALLPISDYL-DYMPNYKKYveKWGLGKElatgrqsDGKYYSLPGlheDPGVqYSFLY 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 160 RSDLYAQYGLKPQATWEEFAADADKLRAANPNGY----LSVFNPDDPWWFAGMSAQAGGS-------------WFGTDTK 222
Cdd:cd13583   133 RKDIFEKAGIKIPTTWDEFYAALKKLKEKYPDSYpysdRWNSNALLLIAAPAFGTTAGWGfsnytydpdtdkfVYGATTD 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 223 GWK-------------------VSLGSDPGTAK-------VANYWQGLVDKGVVKSEQSGTPDlYKELQDGTLAAYPGPV 276
Cdd:cd13583   213 EYKdmlqyfnklyaeglldpesFTQTDDQAKAKflngksfVITTNPQTVDELQRNLRAADGGN-YEVVSITPPAGPAGKA 291

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674576668 277 WFSSILEqnaaqasgkwavapmpqwqdgaksvgnDGGSSTAVVKGCKNTAAALQFANWMSTD 338
Cdd:cd13583   292 INGSRLE---------------------------NGFMISSKAKDSKNFEALLQFLDWLYSD 326
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 125-299 1.84e-06

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: 49.90  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 125 AQYQPQYGEAAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQyglkPQATWEEFAADADKLRAANPNGYLsvFNPDDPWW 204
Cdd:cd13656    79 KAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPN----PPKTWEEIPALDKELKAKGKSALM--FNLQEPYF 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 205 FAGMSAQAGGSWFGTDTKGWKVS-LGSD-PGTAKVANYWQGLVDKGVVKSEQSGTPDLYKELQDGTLAAYPGPvWFSSIL 282
Cdd:cd13656   153 TWPLIAADGGYAFKYENGKYDIKdVGVDnAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGP-WAWSNI 231

                         170
                  ....*....|....*..
gi 2674576668 283 EQNAAQasgkWAVAPMP 299
Cdd:cd13656   232 DTSKVN----YGVTVLP 244
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
125-250 9.36e-06

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 47.70  E-value: 9.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 125 AQYQPQYGEAAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAQyglkPQATWEEFAADADKLRAANPNGYLsvFNPDDPWW 204
Cdd:PRK09474  109 KAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPT----PPKTWEEIPALDKELKAKGKSAIM--WNLQEPYF 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2674576668 205 FAGMSAQAGGSWFGTDTKGWKVS-LGSD-PGTAKVANYWQGLVDKGVV 250
Cdd:PRK09474  183 TWPLIAADGGYAFKFENGGYDVKdVGVNnAGAKAGLQFLVDLVKNKHM 230
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
39-356 3.86e-05

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 45.67  E-value: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  39 PKAGGTTEVTFWGWaPGY--EEAAAQFNATHqDVRVKFEKIVSGskggyAKIFAAVKAGNAPC-LAQVGYESLPSFVVEG 115
Cdd:COG0687    23 PAAAAEGTLNVYNW-GGYidPDVLEPFEKET-GIKVVYDTYDSN-----EEMLAKLRAGGSGYdVVVPSDYFVARLIKAG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 116 AVQDVGKEAAQYQPQYGEAAWNSVKVGGQVYGIPVDMGPMALYYRSDLYAqyglKPQATWEEFAADADKlraanpnGYLS 195
Cdd:COG0687    96 LLQPLDKSKLPNLANLDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVK----EPPTSWADLWDPEYK-------GKVA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 196 VfnPDDPWWFAGMSAQA-GGSWFGTDTKGWkvslgsDPGTAK-------VANYWqglvdkgvvkseqSGTPDLYKELQDG 267
Cdd:COG0687   165 L--LDDPREVLGAALLYlGYDPNSTDPADL------DAAFELlielkpnVRAFW-------------SDGAEYIQLLASG 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668 268 TLAAypGPVWFSSILeqnAAQASG-KWA-VAP---MPQWQDgaksvgndggsSTAVVKGCKNTAAALQFANWMSTDAAAv 342
Cdd:COG0687   224 EVDL--AVGWSGDAL---ALRAEGpPIAyVIPkegALLWFD-----------NMAIPKGAPNPDLAYAFINFMLSPEVA- 286

                         330
                  ....*....|....
gi 2674576668 343 ATLVEKAGIYPAST 356
Cdd:COG0687   287 AALAEYVGYAPPNK 300
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 46-164 3.97e-03

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


Pssm-ID: 270306 [Multi-domain]  Cd Length: 279  Bit Score: 38.82  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674576668  46 EVTFWGWaPGYEEAaaqfnathqDVRVKFE-----KIVSGSKGGYAKIFAAVKAGNA-PCLAQVGYESLPSFVVEGAVQ- 118
Cdd:cd13588     1 ELNVLTW-PGYADP---------DWVTAFEeatgcKVVVKFFGSEDEMVAKLRSGGGdYDVVTPSGDALLRLIAAGLVQp 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2674576668 119 -DVGK--EAAQYQPQYGEAAWNsvKVGGQVYGIPVDMGPMALYYRSDLY 164
Cdd:cd13588    71 iDTSKipNYANIDPRLRNLPWL--TVDGKVYGVPYDWGANGLAYNTKKV 117
 
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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