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Conserved domains on  [gi|686540696|gb|AIQ51393|]
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hypothetical protein R70331_07610 [Paenibacillus sp. FSL R7-0331]

Protein Classification

type 2 periplasmic-binding domain-containing protein( domain architecture ID 229383)

type 2 periplasmic-binding protein (PBP2) is typically comprised of two globular subdomains connected by a flexible hinge; it binds its ligand in the cleft between these domains in a manner resembling a Venus flytrap; similar to the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Periplasmic_Binding_Protein_Type_2 super family cl21456
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 63-586 1.02e-89

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically 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 origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. 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. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


The actual alignment was detected with superfamily member cd13580:

Pssm-ID: 473866 [Multi-domain]  Cd Length: 471  Bit Score: 284.99  E-value: 1.02e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  63 TPVKLNVgfaFASDFkMQGQETESQNTWMDLYKEN-GYNITPMYSVDASQgETKLSTAIASGSYPDVFTVSASELVK-YA 140
Cdd:cd13580    1 EPVTITI---VANLG-GNPKPDPDDNPYTKYLEEKtNIDVKVKWVPDSSY-DEKLNLALASGDLPDIVVVNDPQLSItLV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 141 QTNVIADISEVYEKYAtPELNEYLnvdEGASLASAKVDGKLYAIPKMSSGFdGVMMMFVRQDWLDNLGLKMPATMDELVE 220
Cdd:cd13580   76 KQGALWDLTDYLDKYY-PNLKKII---EQEGWDSASVDGKIYGIPRKRPLI-GRNGLWIRKDWLDKLGLEVPKTLDELYE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 221 VASAFTKNDPDGNGKADTYGLALnGKEGFamLSGLQAFFEGYGAAPGHWngkfsLIEKDGKVVWGGALPdEMKKGLTALQ 300
Cdd:cd13580  151 VAKAFTEKDPDGNGKKDTYGLTD-TKDLI--GSGFTGLFGAFGAPPNNW-----WKDEDGKLVPGSIQP-EMKEALKFLK 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 301 AMYNEGSLAKNFGTMDLTAINKDLGSGKAGIFFAPMWGAMTSIMDAIKSDPNAHFTSARIPDGNgEGSSKAYMPTLPESY 380
Cdd:cd13580  222 KLYKEGLIDPEFAVNDGTKANEKFISGKAGIFVGNWWDPAWPQASLKKNDPDAEWVAVPIPSGP-DGKYGVWAESGVNGF 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 381 FVISSKAKNPEALIKLINlsvqKLIHPSNEDEFNkYYGQTDVYSGWKFSLTQTLNPLKNLENyykesQALQTGDTSELNV 460
Cdd:cd13580  301 FVIPKKSKKPEAILKLLD----FLSDPEVQKLLD-YGIEGVHYTVKDGGPVNIIPPDKQEVG-----DATLDYFQGSLAL 370

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 461 EQKGDYDKMKYYLDAVEAGTAKDMIAANDstflsgaslytvfgdpqggeatvdliktsgAYNLSAYNYIPTETMS----A 536
Cdd:cd13580  371 EKYKLTNNGERKSDAKKEALDERVVNAND------------------------------EENENIAVGPPTETLVspteK 420

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 686540696 537 KYSTLDKMALETIVKIIYGD-SVDSYDKFLQSWKALGGETVTKEAQEWYDS 586
Cdd:cd13580  421 YGATLDKLEDDAFTKIIMGQiPLDEFDKFVEEWKKSGGDEITKEVNEWYKE 471
 
Name Accession Description Interval E-value
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 63-586 1.02e-89

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: 284.99  E-value: 1.02e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  63 TPVKLNVgfaFASDFkMQGQETESQNTWMDLYKEN-GYNITPMYSVDASQgETKLSTAIASGSYPDVFTVSASELVK-YA 140
Cdd:cd13580    1 EPVTITI---VANLG-GNPKPDPDDNPYTKYLEEKtNIDVKVKWVPDSSY-DEKLNLALASGDLPDIVVVNDPQLSItLV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 141 QTNVIADISEVYEKYAtPELNEYLnvdEGASLASAKVDGKLYAIPKMSSGFdGVMMMFVRQDWLDNLGLKMPATMDELVE 220
Cdd:cd13580   76 KQGALWDLTDYLDKYY-PNLKKII---EQEGWDSASVDGKIYGIPRKRPLI-GRNGLWIRKDWLDKLGLEVPKTLDELYE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 221 VASAFTKNDPDGNGKADTYGLALnGKEGFamLSGLQAFFEGYGAAPGHWngkfsLIEKDGKVVWGGALPdEMKKGLTALQ 300
Cdd:cd13580  151 VAKAFTEKDPDGNGKKDTYGLTD-TKDLI--GSGFTGLFGAFGAPPNNW-----WKDEDGKLVPGSIQP-EMKEALKFLK 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 301 AMYNEGSLAKNFGTMDLTAINKDLGSGKAGIFFAPMWGAMTSIMDAIKSDPNAHFTSARIPDGNgEGSSKAYMPTLPESY 380
Cdd:cd13580  222 KLYKEGLIDPEFAVNDGTKANEKFISGKAGIFVGNWWDPAWPQASLKKNDPDAEWVAVPIPSGP-DGKYGVWAESGVNGF 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 381 FVISSKAKNPEALIKLINlsvqKLIHPSNEDEFNkYYGQTDVYSGWKFSLTQTLNPLKNLENyykesQALQTGDTSELNV 460
Cdd:cd13580  301 FVIPKKSKKPEAILKLLD----FLSDPEVQKLLD-YGIEGVHYTVKDGGPVNIIPPDKQEVG-----DATLDYFQGSLAL 370

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 461 EQKGDYDKMKYYLDAVEAGTAKDMIAANDstflsgaslytvfgdpqggeatvdliktsgAYNLSAYNYIPTETMS----A 536
Cdd:cd13580  371 EKYKLTNNGERKSDAKKEALDERVVNAND------------------------------EENENIAVGPPTETLVspteK 420

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 686540696 537 KYSTLDKMALETIVKIIYGD-SVDSYDKFLQSWKALGGETVTKEAQEWYDS 586
Cdd:cd13580  421 YGATLDKLEDDAFTKIIMGQiPLDEFDKFVEEWKKSGGDEITKEVNEWYKE 471
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 79-398 1.36e-37

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 142.88  E-value: 1.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  79 MQGQETESQNTWMDLY-KEN-GYNITPMYsVDASQGETKLSTAIASGSYPDVFTVSASELVKYAQTNVIADISEVYEKYA 156
Cdd:COG1653   40 TGGGEAAALEALIKEFeAEHpGIKVEVES-VPYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDG 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 157 TpELNEYLnvdeGASLASAKVDGKLYAIPKMSSgfdgVMMMFVRQDWLDNLGLKMPATMDELVEVASAFTKndpdgngKA 236
Cdd:COG1653  119 L-DKDDFL----PGALDAGTYDGKLYGVPFNTD----TLGLYYNKDLFEKAGLDPPKTWDELLAAAKKLKA-------KD 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 237 DTYGLALNGKEGFAMLsglqAFFEGYGAapghwngkfSLIEKDGKVVWGGalpDEMKKGLTALQAMYNEGSLAKNFGTMD 316
Cdd:COG1653  183 GVYGFALGGKDGAAWL----DLLLSAGG---------DLYDEDGKPAFDS---PEAVEALEFLKDLVKDGYVPPGALGTD 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 317 LTAINKDLGSGKAGIFFAPMWgAMTSIMDAiksDPNAHFTSARIPDGNGEGSSKAYMPTlpeSYFVISSKAKNPEALIKL 396
Cdd:COG1653  247 WDDARAAFASGKAAMMINGSW-ALGALKDA---APDFDVGVAPLPGGPGGKKPASVLGG---SGLAIPKGSKNPEAAWKF 319


                 ..
gi 686540696 397 IN 398
Cdd:COG1653  320 LK 321
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 95-398 5.20e-11

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: 63.97  E-value: 5.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696   95 KENGYNITPMYsVDASQGETKLSTAIASGSYP-DVFTVSASELVKYAQTNVIADISEVYEKYAtpelneylnvdegasla 173
Cdd:pfam01547  20 EHPGIKVEVES-VGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVANYL----------------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  174 sAKVDGKLYAIPKMSSgfdgVMMMFVRQDWLDNLGLKMPATMDELVEVASAFTKNDPDGNGKADTYGLALNGkegfamlS 253
Cdd:pfam01547  82 -VLGVPKLYGVPLAAE----TLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLG-------Y 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  254 GLQAFFEGYGAAPGHWNGkfsliekdGKVVWGGALPDEMKKGLTALQAMYNEGSLAKNFGTMDLTAINKDLGSGKAGIFF 333
Cdd:pfam01547 150 FTLALLASLGGPLFDKDG--------GGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGI 221

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686540696  334 APMWGAMTSI-------MDAIKSDPNAHFTSARIPDGNGEGSSkaymptlpESYFVISSKAKNPEALIKLIN 398
Cdd:pfam01547 222 VGPWAALAANkvklkvaFAAPAPDPKGDVGYAPLPAGKGGKGG--------GYGLAIPKGSKNKEAAKKFLD 285
 
Name Accession Description Interval E-value
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 63-586 1.02e-89

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: 284.99  E-value: 1.02e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  63 TPVKLNVgfaFASDFkMQGQETESQNTWMDLYKEN-GYNITPMYSVDASQgETKLSTAIASGSYPDVFTVSASELVK-YA 140
Cdd:cd13580    1 EPVTITI---VANLG-GNPKPDPDDNPYTKYLEEKtNIDVKVKWVPDSSY-DEKLNLALASGDLPDIVVVNDPQLSItLV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 141 QTNVIADISEVYEKYAtPELNEYLnvdEGASLASAKVDGKLYAIPKMSSGFdGVMMMFVRQDWLDNLGLKMPATMDELVE 220
Cdd:cd13580   76 KQGALWDLTDYLDKYY-PNLKKII---EQEGWDSASVDGKIYGIPRKRPLI-GRNGLWIRKDWLDKLGLEVPKTLDELYE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 221 VASAFTKNDPDGNGKADTYGLALnGKEGFamLSGLQAFFEGYGAAPGHWngkfsLIEKDGKVVWGGALPdEMKKGLTALQ 300
Cdd:cd13580  151 VAKAFTEKDPDGNGKKDTYGLTD-TKDLI--GSGFTGLFGAFGAPPNNW-----WKDEDGKLVPGSIQP-EMKEALKFLK 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 301 AMYNEGSLAKNFGTMDLTAINKDLGSGKAGIFFAPMWGAMTSIMDAIKSDPNAHFTSARIPDGNgEGSSKAYMPTLPESY 380
Cdd:cd13580  222 KLYKEGLIDPEFAVNDGTKANEKFISGKAGIFVGNWWDPAWPQASLKKNDPDAEWVAVPIPSGP-DGKYGVWAESGVNGF 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 381 FVISSKAKNPEALIKLINlsvqKLIHPSNEDEFNkYYGQTDVYSGWKFSLTQTLNPLKNLENyykesQALQTGDTSELNV 460
Cdd:cd13580  301 FVIPKKSKKPEAILKLLD----FLSDPEVQKLLD-YGIEGVHYTVKDGGPVNIIPPDKQEVG-----DATLDYFQGSLAL 370

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 461 EQKGDYDKMKYYLDAVEAGTAKDMIAANDstflsgaslytvfgdpqggeatvdliktsgAYNLSAYNYIPTETMS----A 536
Cdd:cd13580  371 EKYKLTNNGERKSDAKKEALDERVVNAND------------------------------EENENIAVGPPTETLVspteK 420

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 686540696 537 KYSTLDKMALETIVKIIYGD-SVDSYDKFLQSWKALGGETVTKEAQEWYDS 586
Cdd:cd13580  421 YGATLDKLEDDAFTKIIMGQiPLDEFDKFVEEWKKSGGDEITKEVNEWYKE 471
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 107-399 3.83e-39

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: 149.78  E-value: 3.83e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 107 VDASQGETKLSTAIASGSYPDVF---TVSASELVKYAQTNVIADISEVYEKYAtPELNEYLNVDEGASLASAKVDGKLYA 183
Cdd:cd13581   39 VPEDAWAEKKNLMLASGDLPDAFlgaGASDADLMTYGKQGLFLPLEDLIDKYA-PNLKALFDENPDIKAAITAPDGHIYA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 184 IPKMSSGFDGVMM--MFVRQDWLDNLGLKMPATMDELVEVASAFTKNDPDGNGKADTYGLALNGKEGFAML-SGLQAFFe 260
Cdd:cd13581  118 LPSVNECYHCSYGqrMWINKKWLDKLGLEMPTTTDELYEVLKAFKEQDPNGNGKADEIPLSFSGLNGGTDDpAFLLNSF- 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 261 GYGAAPGHWNGkfsLIEKDGKVVWGGALPdEMKKGLTALQAMYNEGSLAKNFGTMDLTAiNKDLGSGKAGIFFAPMWGam 340
Cdd:cd13581  197 GINDGGYGGYG---FVVKDGKVIYTATDP-EYKEALAYLNKLYKEGLIDPEAFTQDYDQ-LAAKGKASTAKVGVFFGW-- 269

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 686540696 341 tsimdaiksDPNAHFTSARIPD----------GNGEGSSKAYMPTLPESYFVISSKAKNPEALIKLINL 399
Cdd:cd13581  270 ---------DPGLFFGEERYEQyvplpplkgpNGDQLAWVGNSSGYGRGGFVITSKNKNPEAAIRWADF 329
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 79-398 1.36e-37

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 142.88  E-value: 1.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  79 MQGQETESQNTWMDLY-KEN-GYNITPMYsVDASQGETKLSTAIASGSYPDVFTVSASELVKYAQTNVIADISEVYEKYA 156
Cdd:COG1653   40 TGGGEAAALEALIKEFeAEHpGIKVEVES-VPYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDG 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 157 TpELNEYLnvdeGASLASAKVDGKLYAIPKMSSgfdgVMMMFVRQDWLDNLGLKMPATMDELVEVASAFTKndpdgngKA 236
Cdd:COG1653  119 L-DKDDFL----PGALDAGTYDGKLYGVPFNTD----TLGLYYNKDLFEKAGLDPPKTWDELLAAAKKLKA-------KD 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 237 DTYGLALNGKEGFAMLsglqAFFEGYGAapghwngkfSLIEKDGKVVWGGalpDEMKKGLTALQAMYNEGSLAKNFGTMD 316
Cdd:COG1653  183 GVYGFALGGKDGAAWL----DLLLSAGG---------DLYDEDGKPAFDS---PEAVEALEFLKDLVKDGYVPPGALGTD 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 317 LTAINKDLGSGKAGIFFAPMWgAMTSIMDAiksDPNAHFTSARIPDGNGEGSSKAYMPTlpeSYFVISSKAKNPEALIKL 396
Cdd:COG1653  247 WDDARAAFASGKAAMMINGSW-ALGALKDA---APDFDVGVAPLPGGPGGKKPASVLGG---SGLAIPKGSKNPEAAWKF 319


                 ..
gi 686540696 397 IN 398
Cdd:COG1653  320 LK 321
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 69-585 1.21e-34

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: 136.82  E-value: 1.21e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  69 VGFAFASDFKMQGQETESQNTWMDLYKENGYNITPMYSVDASQGEtKLSTAIASGSYPDVFTVS--ASELVKYAQTNVIA 146
Cdd:cd13521    2 LTLSVLMAFNDNWVDDENWPVAKEIEKLTNVKLEIVAVTAATSQQ-KLNLMLASGDLPDIVGADylKDKFIAYGMEGAFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 147 DISEVYEKYatPELNEYLNVDEGASLASAKVDGKLYAIPKMSSGFDGVMMMFVRQDWLDNLGLKMPATMDELVEVASAFT 226
Cdd:cd13521   81 PLSKYIDQY--PNLKAFFKQHPDVLRASTASDGKIYLIPYEPPKDVPNQGYFIRKDWLDKLNLKTPKTLDELYNVLKAFK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 227 KNDPDGNGKADTYGLALNGKEGFAMlsGLQAFFEGYGAAPGHWNGKFsliEKDGKVVWGGAlPDEMKKGLTALQAMYNEG 306
Cdd:cd13521  159 EKDPNGNGKADEIPFIDRDPLYGAF--RLINSWGARSAGGSTDSDWY---EDNGKFKHPFA-SEEYKDGMKYMNKLYTEG 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 307 SLAKNFGTMDLTAINKDLGSGKAGIFFAPMWGAMTSIMDAIKSDPNAHFTSARIPDGNGEGSSKAYMPTLP-ESYFVISS 385
Cdd:cd13521  233 LIDKESFTQKDDQAEQKFSNGKLGGFTHNWFASDNLFTAQLGKEKPMYILLPIAPAGNVKGRREEDSPGYTgPDGVAISK 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 386 KAKNPEALIKLINlsvqklihpsnedefnkYYGQTDVYSGWKFSLTQTlnplknleNYYKESQALQTGDTSelnVEQKGD 465
Cdd:cd13521  313 KAKNPVAALKFFD-----------------WLASEEGRELANFGIEGV--------HYNKDNGKKRTKDPV---KKSDQP 364

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 466 YDKMKYYLDAVEAGTAKdmiaaNDSTFLSGASLYtVFGDPQggEATVDLIKTSGAYNLSAYNYIPTETMSAKYST----L 541
Cdd:cd13521  365 GDNQLYDLPAFIKGGFW-----NEYTYPRPQWGV-LTGDSA--RLPIDMYIKPKYSPPKPEGANLTIEEREQVSIdnteL 436

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 686540696 542 DKMALETIVKIIYG--DSVDSYDKFLQSWKALGGETVTKEAQEWYD 585
Cdd:cd13521  437 KDIMMEMTQKWIMGtkEKDEEWDAYQEQLKSAGLYQVTEEVQKAYD 482
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 80-397 3.19e-28

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: 116.74  E-value: 3.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  80 QGQETESQNTWMDLYKENGYNITPMY-SVDASQGETKLSTAIASGSYPDVFTVSASELVKYAQTNVIADISEVYEKyatp 158
Cdd:cd13585    9 QPAETAALKKLIDAFEKENPGVKVEVvPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDDYIEK---- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 159 elNEYLNVDEGASLASAKVDGKLYAIPKMSSgfdgVMMMFVRQDWLDNLG--LKMPATMDELVEVASAFTKndpdgnGKA 236
Cdd:cd13585   85 --DGLDDDFPPGLLDAGTYDGKLYGLPFDAD----TLVLFYNKDLFDKAGpgPKPPWTWDELLEAAKKLTD------KKG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 237 DTYGLALNGKegfamlSGLQAFFEGYGAApghWNGKFsLIEKDGKVVWGGalpDEMKKGLTALQAMYNEGsLAKNFGTMD 316
Cdd:cd13585  153 GQYGFALRGG------SGGQTQWYPFLWS---NGGDL-LDEDDGKATLNS---PEAVEALQFYVDLYKDG-VAPSSATTG 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 317 LTAINKDLGSGKAGIFFAPMWgamtSIMDAIKSDPNAHFTSARIPDGNGEGSSkaymPTLPESYFVISSKAKNPEALIKL 396
Cdd:cd13585  219 GDEAVDLFASGKVAMMIDGPW----ALGTLKDSKVKFKWGVAPLPAGPGGKRA----SVLGGWGLAISKNSKHPEAAWKF 290


                 .
gi 686540696 397 I 397
Cdd:cd13585  291 I 291
PBP2_AlgQ1_2 cd13584
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 ...
 109-585 1.17e-23

Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 periplasmic binding fold; This group represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria such as Sphingomonas sp. A1. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that includes alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270302 [Multi-domain]  Cd Length: 481  Bit Score: 104.44  E-value: 1.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 109 ASQGETKLSTAIASGSYPDVFTVS----ASELVKYAQTNVIADISEVYEKYAtPELNEYLNVDEGASLASAKVDGKLYAI 184
Cdd:cd13584   42 AQNSQEQFNLMMASGQLPDIIGGDwlkdKGGFEKYGEDGAFLPLNDLIDQYA-PNLKKFLDEHPDVKKAITTDDGNIYGF 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 185 PKMSSG-----FDGvmmMFVRQDWLDNLGLKMPATMDELVEVASAFTKNDPDGNGKADTYGLALNgkegfamlsgLQAFF 259
Cdd:cd13584  121 PYLPDGdvakeARG---YFIRKDWLDKLGLKTPSTIDEWYTVLKAFKERDPNGNGKADEVPLILT----------KPGYD 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 260 EgYGAAPGHWNGKFSLIEKDGKVVWGGALPdEMKKGLTALQAMYNEGSLAKNFGTMDLTAINKDLGSGKAG----IFFAP 335
Cdd:cd13584  188 E-TGRLINAWGAYMDFYQENGKVKYGPLEP-GFKDFLKTMNQWYKEGLIDPDFFTRKAKAREQNIMNGNIGgfthDWFAS 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 336 MWGAMTSIMDAiksDPNAHFTSARIPDGN-GEGSSKAYMPTLPESY-FVISSKAKNPEALIKLinlsvqklihpsnedeF 413
Cdd:cd13584  266 TGTFNLALLKN---VPDFKLVAVPPPVLNkGQTPYEEDSRQIAKGDgAAITASNKNPVLAIKW----------------L 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 414 NKYYGQ--TDVYSGWKFSLTQTlnpLKNLENYYKEsqalqtgdtselnveqkgdyDKMKYYLDAVEAgTAKDMIAANDST 491
Cdd:cd13584  327 DYAYSEegRLLSNFGVEGESYT---IKNGKPVFTD--------------------DVLKDPQPLVNA-LSLYYGAQIPGG 382

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 492 FLSGASLYTVFGDPQGGEATVDLIKtsGAYNLSAYNYIPTETMSAKY----STLDKMALETIVKIIYG--DSVDSYDKFL 565
Cdd:cd13584  383 FWQDYEYEEQWTTPEALESKDIYAK--NKYVMPLPPVTLTEEERSIYdsimTDIDTYVNEMGQKWIMGkeDADDNWDEYQ 460

                        490       500
                 ....*....|....*....|
gi 686540696 566 QSWKALGGETVTKEAQEWYD 585
Cdd:cd13584  461 KKLKSLGLYEALEIQQAAYD 480
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 95-398 7.27e-23

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: 100.83  E-value: 7.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  95 KENGYNITPMYSVDASQGETKLSTAIASGSYPDVFTVSASELVKYAQTNVIADISEVYEKyatpeLNEYLNVDEGASLAS 174
Cdd:cd14748   26 SHPDIKVKAVYQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDDYIDK-----DGVDDDDFYPAALDA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 175 AKVDGKLYAIPKMSSgfdgVMMMFVRQDWLDNLGL---KMPATMDELVEVASAFTKNDpdgnGKADTYGLALNGkegfam 251
Cdd:cd14748  101 GTYDGKLYGLPFDTS----TPVLYYNKDLFEEAGLdpeKPPKTWDELEEAAKKLKDKG----GKTGRYGFALPP------ 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 252 lSGLQAFFEGYGAApghWNGKFsLIEKDGKVVWGGalpDEMKKGLTALQAMYNEGSLAKNFgtmDLTAINKDLGSGKAGI 331
Cdd:cd14748  167 -GDGGWTFQALLWQ---NGGDL-LDEDGGKVTFNS---PEGVEALEFLVDLVGKDGVSPLN---DWGDAQDAFISGKVAM 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 686540696 332 FFAPMWgAMTSIMDAiksDPNAHFTSARIPDGNGEgssKAYMPTLPESYFVISSKAKNPEALIKLIN 398
Cdd:cd14748  236 TINGTW-SLAGIRDK---GAGFEYGVAPLPAGKGK---KGATPAGGASLVIPKGSSKKKEAAWEFIK 295
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
95-398 1.09e-20

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 94.63  E-value: 1.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  95 KENGYNITPMYsVDASQGETKLSTAIASGSYPDVFTVSASELVKYAQTNVIADISEVYEKYAtpelneylNVDEGAsLAS 174
Cdd:COG2182   62 EEPGIKVKVVE-VPWDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLADKD--------DFLPAA-LDA 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 175 AKVDGKLYAIPKmssgFDGVMMMFVRQDWLDNlglKMPATMDELVEVASAFTkndpdgngKADTYGLALNGKEGFAMLsg 254
Cdd:COG2182  132 VTYDGKLYGVPY----AVETLALYYNKDLVKA---EPPKTWDELIAAAKKLT--------AAGKYGLAYDAGDAYYFY-- 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 255 lqAFFEGYGAapghwngkfSLIEKDGKVVWGGAL-PDEMKKGLTALQAMYNEGSLAKNfgtMDLTAINKDLGSGKAGIFF 333
Cdd:COG2182  195 --PFLAAFGG---------YLFGKDGDDPKDVGLnSPGAVAALEYLKDLIKDGVLPAD---ADYDAADALFAEGKAAMII 260

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686540696 334 APMWGAmtsimDAIKSDPNAHFTSARIPDGNGEGSSKAYMPTlpeSYFVISSKAKNPEALIKLIN 398
Cdd:COG2182  261 NGPWAA-----ADLKKALGIDYGVAPLPTLAGGKPAKPFVGV---KGFGVSAYSKNKEAAQEFAE 317
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 95-403 1.20e-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: 94.30  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  95 KEN-GYNITPMYsVDASQGETKLSTAIASGSYPDVFTVSASELVKYAQTNVIADISEVYEkyatpELNEYLNVDEGAsLA 173
Cdd:cd14747   25 KENpGIEVKVQV-LPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMGALEDLTPYLE-----DLGGDKDLFPGL-VD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 174 SAKVDGKLYAIPkmssGFDGVMMMFVRQDWLDNLG-LKMPATMDELVEVASAFTKNDPDGngkadtYGLALNGKEGfaml 252
Cdd:cd14747   98 TGTVDGKYYGVP----WYADTRALFYRTDLLKKAGgDEAPKTWDELEAAAKKIKADGPDV------SGFAIPGKND---- 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 253 sglqaffEGYGAAPGHWNGKFSLIEKDGkvvWGGALPD-EMKKGLTALQAMYNEGSLAKNfGTMDLTAINKDLGSGKAGI 331
Cdd:cd14747  164 -------VWHNALPFVWGAGGDLATKDK---WKATLDSpEAVAGLEFYTSLYQKGLSPKS-TLENSADVEQAFANGKVAM 232

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 686540696 332 FFAPMWgaMTSIMDAIKSDPNAHFTSARIPDGNGEGSSkaymptlpeSYF-----VISSKAKNPEALIKLINLSVQK 403
Cdd:cd14747  233 IISGPW--EIGAIREAGPDLAGKWGVAPLPGGPGGGSP---------SFAggsnlAVFKGSKNKDLAWKFIEFLSSP 298
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 90-398 1.05e-17

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: 86.26  E-value: 1.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  90 WMDLYKENGYNITPMYsVDASQGETKLSTAIASGSYPDVFTV-SASELVKYAQTNVIADISEvYEKYATPELNEYLNVDE 168
Cdd:cd13583   23 WKEIEEKTNVKFKRTP-IPSSDYETKRSLLIASGDAPDIIPVlYPGEENEFVASGALLPISD-YLDYMPNYKKYVEKWGL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 169 GASLASAK-VDGKLYAIPKMSSGFDGVMMMFVRQDWLDNLGLKMPATMDELVEVASAFTKNDPDgngkadTYGLALNGKE 247
Cdd:cd13583  101 GKELATGRqSDGKYYSLPGLHEDPGVQYSFLYRKDIFEKAGIKIPTTWDEFYAALKKLKEKYPD------SYPYSDRWNS 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 248 GfAMLSGLQAFFegygAAPGHWNGKFSLIEKDGKVVWGGALPDEMKKGLTALQAMYNEGSLAKNFGTMDLTAINKDLGSG 327
Cdd:cd13583  175 N-ALLLIAAPAF----GTTAGWGFSNYTYDPDTDKFVYGATTDEYKDMLQYFNKLYAEGLLDPESFTQTDDQAKAKFLNG 249

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 686540696 328 KAGIFFApMWGAMTSIMDAIKSDPNAHFTSARIPDGNGEgSSKAYMPTLPESYFVISSKA---KNPEALIKLIN 398
Cdd:cd13583  250 KSFVITT-NPQTVDELQRNLRAADGGNYEVVSITPPAGP-AGKAINGSRLENGFMISSKAkdsKNFEALLQFLD 321
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 71-397 7.42e-16

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: 79.65  E-value: 7.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  71 FAFASDFKMQGQETESQNTWMDLYKENGYNITPMYSvDASQGETKLSTAIASGS-YPDVFTVSASELVKYAQTNVIADIs 149
Cdd:cd14750    4 FAAGSDGQEGELLKKAIAAFEKKHPDIKVEIEELPA-SSDDQRQQLVTALAAGSsAPDVLGLDVIWIPEFAEAGWLLPL- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 150 evYEKYATPELNEYLnvdeGASLASAKVDGKLYAIPkmssGFDGVMMMFVRQDWLDNLGLKMPATMDELVEVASAFTKnd 229
Cdd:cd14750   82 --TEYLKEEEDDDFL----PATVEANTYDGKLYALP----WFTDAGLLYYRKDLLEKYGPEPPKTWDELLEAAKKRKA-- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 230 pdgnGKADTYGLALNGKEGfamlSGL-QAFFEGYGAAPGHWngkfsLIEKDGKVVWGGalpDEMKKGLTALQAMYNEGSL 308
Cdd:cd14750  150 ----GEPGIWGYVFQGKQY----EGLvCNFLELLWSNGGDI-----FDDDSGKVTVDS---PEALEALQFLRDLIGEGIS 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 309 AKNFGTMDLTAINKDLGSGKAGifFAPMWGAMTSIMDAIKSDPNAHFTSARIPDGNGEGSSkaymPTLPESYFVISSKAK 388
Cdd:cd14750  214 PKGVLTYGEEEARAAFQAGKAA--FMRNWPYAYALLQGPESAVAGKVGVAPLPAGPGGGSA----STLGGWNLAISANSK 287


                 ....*....
gi 686540696 389 NPEALIKLI 397
Cdd:cd14750  288 HKEAAWEFV 296
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 114-398 2.45e-15

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: 78.19  E-value: 2.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 114 TKLSTAIASGSYPDVF-TVSASELVKYAQTNVIADISEVYEKYAtpELNEYLNVdegaSLASAKVDGKLYAIPKMSSgfd 192
Cdd:cd14749   45 TKLKTAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPLTDYLDPNG--VDKRFLPG----LADAVTFNGKVYGIPFAAR--- 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 193 gVMMMFVRQDWLDNLG-LKMPATMDELVEVAsaftKNDPDGNGKADTYGLALNGKEGFAMLSGLQAFFegygaapghwNG 271
Cdd:cd14749  116 -ALALFYNKDLFEEAGgVKPPKTWDELIEAA----KKDKFKAKGQTGFGLLLGAQGGHWYFQYLVRQA----------GG 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 272 KFSLIEKDGKVVWggALPDEMkKGLTALQAMYNEGSLAKNFGTMDLTAINKDLGSGKAGIFFAPMWGamtsIMDAIKSDP 351
Cdd:cd14749  181 GPLSDDGSGKATF--NDPAFV-QALQKLQDLVKAGAFQEGFEGIDYDDAGQAFAQGKAAMNIGGSWD----LGAIKAGEP 253

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 686540696 352 NAHFTSARIP---DGNGEGSSKAymptlpeSYFV--ISSKAKNPEALIKLIN 398
Cdd:cd14749  254 GGKIGVFPFPtvgKGAQTSTIGG-------SDWAiaISANGKKKEAAVKFLK 298
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 94-397 1.17e-12

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: 69.63  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  94 YKENGYNITPMYsVDASQGETKLSTAIASGSYPDVFTVSASELVKYAQTNVIADISEvyekyatPELNEYLNVDegASLA 173
Cdd:cd13586   23 EKKYGIKVEVVY-VDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPE-------YLAVKIKNLP--VALA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 174 SAKVDGKLYAIPKMSsgfdGVMMMFVRQDWLDNlglkMPATMDELVEVASAFtkndpdGNGKADTYGLALNGKEGFAMls 253
Cdd:cd13586   93 AVTYNGKLYGVPVSV----ETIALFYNKDLVPE----PPKTWEELIALAKKF------NDKAGGKYGFAYDQTNPYFS-- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 254 glQAFFEGYGAAPGHWNGKFSliekdGKVVWGGAlpdEMKKGLTALQAM-YNEGSLAKNfgtMDLTAINKDLGSGKAGIF 332
Cdd:cd13586  157 --YPFLAAFGGYVFGENGGDP-----TDIGLNNE---GAVKGLKFIKDLkKKYKVLPPD---LDYDIADALFKEGKAAMI 223

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686540696 333 FAPMWgamtSIMDAIKSDPNahFTSARIPDGNGegsSKAYMPTLPESYFVISSKAKNPEALIKLI 397
Cdd:cd13586  224 INGPW----DLADYKDAGIN--FGVAPLPTLPG---GKQAAPFVGVQGAFVSAYSKNKEAAVEFA 279
PBP2_AlgQ_like_3 cd13582
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 95-406 8.29e-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: 270300 [Multi-domain]  Cd Length: 504  Bit Score: 67.73  E-value: 8.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  95 KENGYNITPMYSVdaSQGETKLSTAIASGSYPDVFTVSaSELVKYAQTNVIADISEVYEKYATpelneylNVDEGASLAS 174
Cdd:cd13582   28 ELTGVTLEIEYLV--GGEKQKIGLMIASGDLPDLIYAK-GDTDKLIEAGALVPLDDLIEKYGP-------NIKKWYGDYL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 175 AKV----DGKLYAIP---KMSSGFDGVMMMFVRQDWLDNLGLKMPATMDELVEVASAFTKNDPDGNGKaDTYGLALNGkE 247
Cdd:cd13582   98 LKKlrseDGHIYYLPnyrVEDAPWYPNGGFWLQHDVLKELGYPKIKTLDDYENLIKDYKKKYPTINGQ-PTIGFTALT-D 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 248 GFAMLSglqAFFEGYGAAPGHWNGKFSLIEKDGKVVWGGALPdEMKKGLTALQAMYNEGSLAKNFGTMDLTAINKDLGSG 327
Cdd:cd13582  176 DWRFLI---SVTNPAFLAGYPNDGEVYVDPKTLKAKFHYTRP-YYKEYYKWLNELWNEGLLDKESFTQKYDQYLAKIASG 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 328 KAGIFFAPMWGamtsIMDAIKSDPNAHFTSARI---PDGNGEGSSKAYM---PTLPESYFVISSKAKNPEALIKLIN--- 398
Cdd:cd13582  252 RVLGFYDAGWD----IGNAITALKAKGKDERLYayyPVAVGVDDKDYNYgdpGYLGGDGIAITKSCKDPERAFKFLDwla 327


                 ....*....
gi 686540696 399 -LSVQKLIH 406
Cdd:cd13582  328 sEEAQKLIN 336
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 95-398 5.20e-11

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: 63.97  E-value: 5.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696   95 KENGYNITPMYsVDASQGETKLSTAIASGSYP-DVFTVSASELVKYAQTNVIADISEVYEKYAtpelneylnvdegasla 173
Cdd:pfam01547  20 EHPGIKVEVES-VGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVANYL----------------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  174 sAKVDGKLYAIPKMSSgfdgVMMMFVRQDWLDNLGLKMPATMDELVEVASAFTKNDPDGNGKADTYGLALNGkegfamlS 253
Cdd:pfam01547  82 -VLGVPKLYGVPLAAE----TLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLG-------Y 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  254 GLQAFFEGYGAAPGHWNGkfsliekdGKVVWGGALPDEMKKGLTALQAMYNEGSLAKNFGTMDLTAINKDLGSGKAGIFF 333
Cdd:pfam01547 150 FTLALLASLGGPLFDKDG--------GGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGI 221

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686540696  334 APMWGAMTSI-------MDAIKSDPNAHFTSARIPDGNGEGSSkaymptlpESYFVISSKAKNPEALIKLIN 398
Cdd:pfam01547 222 VGPWAALAANkvklkvaFAAPAPDPKGDVGYAPLPAGKGGKGG--------GYGLAIPKGSKNKEAAKKFLD 285
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 103-397 3.41e-10

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: 62.01  E-value: 3.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 103 PMYSVDA-----SQGETKLSTAIASGSYPDVFTVSASELVKYAQTNVIADISEvyekyaTPELNEYLNVDEGAsLASAKV 177
Cdd:cd14751   28 PKIKVKAvrvpfDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDG------TPAFDDIVDYLPGP-METNRY 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 178 DGKLYAIPKMSSgfdgVMMMFVRQDWLDNLGLKMPATMDELVEVASAFTKndpdgngKADTYGLALNGKEGFAMLSGLQA 257
Cdd:cd14751  101 NGHYYGVPQVTN----TLALFYNKRLLEEAGTEVPKTMDELVAAAKAIKK-------KKGRYGLYISGDGPYWLLPFLWS 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 258 FfegygaapghwngkfsliekdgkvvwGGALPDEMKK--------GLTALQAM---YNEGSLAK--NFGTMDLTainKDL 324
Cdd:cd14751  170 F--------------------------GGDLTDEKKAtgylnspeSVRALETIvdlYDEGAITPcaSGGYPNMQ---DGF 220

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 686540696 325 GSGKAGIFFAPMWgAMTSIMDAIKSDPNAHFTSARIPDGNGEGSSkaymPTLPESYfVISSKAKNPEALIKLI 397
Cdd:cd14751  221 KSGRYAMIVNGPW-AYADILGGKEFKDPDNLGIAPVPAGPGGSGS----PVGGEDL-VIFKGSKNKDAAWKFV 287
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 111-479 5.02e-09

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


Pssm-ID: 270240 [Multi-domain]  Cd Length: 368  Bit Score: 58.19  E-value: 5.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 111 QGETKLSTAIASGSYPDVFTVSASELVKYAQTNVIADISEVYEKyatpelneyLNVDEGASLASAKVDGKLYAIPKMSsg 190
Cdd:cd13522   41 ARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDEYVSK---------SGKYAPNTIAAMKLNGKLYGVPVSV-- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 191 fdGVMMMFVRQdwlDNLGLKMPATMDELVEVASaftkndpdGNGKADTYGLALNGKEGFamlsglqaFFEGYGAAPGHWN 270
Cdd:cd13522  110 --GAHLMYYNK---KLVPKNPPKTWQELIALAQ--------GLKAKNVWGLVYNQNEPY--------FFAAWIGGFGGQV 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 271 GKFslieKDGKVVWGGALPdEMKKGLTALQAMYNEGSLakNFGTMDLTAINKDLGSGKAGIFFAPMWgamtsIMDAIKSD 350
Cdd:cd13522  169 FKA----NNGKNNPTLDTP-GAVEALQFLVDLKSKYKI--MPPETDYSIADALFKAGKAAMIINGPW-----DLGDYRQA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 351 PNAHFTSARIPDGNGEGSSKaymPTLPESYFVISSKAKNPEALIKLinlsVQKLIHPSNEDEFNKyygqtdvYSGWKFSL 430
Cdd:cd13522  237 LKINLGVAPLPTFSGTKHAA---PFVGGKGFGINKESQNKAAAVEF----VKYLTSYQAQLVLFD-------DAGDIPAN 302

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 686540696 431 TQTLN--PLKNLENYYKESQALQTGDTSELNVEQKGDYDKMKYYLDAVEAG 479
Cdd:cd13522  303 LQAYEspAVQNKPAQKASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAG 353
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 95-297 6.78e-08

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 54.33  E-value: 6.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696   95 KENGYNITPMYSvDASQGETKLSTAIASGSYPDVFTVSASE--LVKYAQTNVIADISEVYEKYATPELneylnvdegasL 172
Cdd:pfam13416   8 KKTGVTVEVEPQ-ASNDLQAKLLAAAAAGNAPDLDVVWIAAdqLATLAEAGLLADLSDVDNLDDLPDA-----------L 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  173 ASAKVDGKLYAIPKMSSgfdGVMMMFVRQDWLDNLGLKmPATMDELVEVASAFTK-----NDPDGNG----------KAD 237
Cdd:pfam13416  76 DAAGYDGKLYGVPYAAS---TPTVLYYNKDLLKKAGED-PKTWDELLAAAAKLKGktgltDPATGWLlwalladgvdLTD 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 686540696  238 TYGLALNGKEGFAMLSGLQAffegYGAAPGHWNGKFSLIeKDGKVV----WGGALPDEMKKGLT 297
Cdd:pfam13416 152 DGKGVEALDEALAYLKKLKD----NGKVYNTGADAVQLF-ANGEVAmtvnGTWAAAAAKKAGKK 210
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 113-302 7.09e-08

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: 54.69  E-value: 7.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 113 ETKLSTAIASGSYPDVFTVSASELVKYAQTNVIADISEVyekyatpELNEYLNVDEGASLASAKVDGKLYAIPKMSSGfd 192
Cdd:cd13657   43 QNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISDY-------LSEDDFENYLPTAVEAVTYKGKVYGLPEAYET-- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 193 gvMMMFVRQDWLDNLglkmPATMDELVEVASAFTKNDPdgngkaDTYGLALNGKEGFAmlsgLQAFFEGYGAapghwngk 272
Cdd:cd13657  114 --VALIYNKALVDQP----PETTDELLAIMKDHTDPAA------GSYGLAYQVSDAYF----VSAWIFGFGG-------- 169

                        170       180       190
                 ....*....|....*....|....*....|
gi 686540696 273 fSLIEKDGKVVwgGALPDEMKKGLTALQAM 302
Cdd:cd13657  170 -YYFDDETDKP--GLDTPETIKGIQFLKDF 196
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 81-422 1.36e-06

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: 50.94  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696  81 GQETESQNTWMDLY-KENGYNITpMYSVDASQGETKLSTAIASGSYPDVFTVSASELVKYAQTNVIADISEvyEKYATPE 159
Cdd:cd13658    9 DKKMAFIKKIAKQYtKKTGVKVK-LVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKL--SKDKKKG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 160 LNEylnvdegASLASAKVDGKLYAIPKMSSgfdgVMMMFVRQDWLDNlglkMPATMDELVEVASAFTKndPDGNgkadTY 239
Cdd:cd13658   86 FTD-------QALKALTYDGKLYGLPAAVE----TLALYYNKDLVKN----APKTFDELEALAKDLTK--EKGK----QY 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 240 GLALNGKEgFAMLSGlqaFFEGYGAAPGHWNGKFSLIEKDgkvvwgGALPDEMKKGLTALQAMYNEGSLAKNfgtMDLTA 319
Cdd:cd13658  145 GFLADATN-FYYSYG---LLAGNGGYIFKKNGSDLDINDI------GLNSPGAVKAVKFLKKWYTEGYLPKG---MTGDV 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686540696 320 INKDLGSGKAGIFFAPMWGAmtsimdAIKSDPNAHFTSARIP-DGNGegssKAYMPTLPESYFVISSKAKNPEALIKLIN 398
Cdd:cd13658  212 IQGLFKEGKAAAVIDGPWAI------QEYQEAGVNYGVAPLPtLPNG----KPMAPFLGVKGWYLSAYSKHKEWAQKFME 281

                        330       340
                 ....*....|....*....|....
gi 686540696 399 LSVQKLIHPSNEDEFNKYYGQTDV 422
Cdd:cd13658  282 FLTSKENLKKRYDETNEIPPRKDV 305
 
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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