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Conserved domains on  [gi|1811729725|dbj|GFH41525|]
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ABC transporter substrate-binding protein [Lactococcus hodotermopsidis]

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 ...
 5-376 7.64e-62

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 204.51  E-value: 7.64e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725   5 KKLLIGAAVAAlgvSALLTGCGGkkADDASGDKDGKVKISMaWWGSQVRHDATVKVIEMYEKENPKVDIEYEFYDMDGYL 84
Cdd:COG1653     2 RRLALALAAAL---ALALAACGG--GGSGAAAAAGKVTLTV-WHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  85 TKLNTLAASKTVWDVFQM-GGNFPAFIDS--IEPLDQYIKDGLIDTSNISEGYLATTQQDGKQWGISNGVGAYGIAYDPA 161
Cdd:COG1653    76 TKLLTALAAGNAPDVVQVdSGWLAEFAAAgaLVPLDDLLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 162 MFKKAGLDEPtpdWTWADFEEMCLKIHDKTGQFGFSNFDDFKTATMAITQTGGGNNFfsteTNSKTMGFKDPKlLVPYLE 241
Cdd:COG1653   156 LFEKAGLDPP---KTWDELLAAAKKLKAKDGVYGFALGGKDGAAWLDLLLSAGGDLY----DEDGKPAFDSPE-AVEALE 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 242 MRKNLVDAGAYPDPGAIKEIKDIeGDYLVTGEAAMTWVAANQLQALRTAA-GREIKMMTLPKTKADVPGGGMMSSQMLSM 320
Cdd:COG1653   228 FLKDLVKDGYVPPGALGTDWDDA-RAAFASGKAAMMINGSWALGALKDAApDFDVGVAPLPGGPGGKKPASVLGGSGLAI 306

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1811729725 321 AKNSKHKEEAAKFISYFeTNIEANKILNGERGVPIDDKVREELTKTADENMQEVYN 376
Cdd:COG1653   307 PKGSKNPEAAWKFLKFL-TSPEAQAKWDALQAVLLGQKTPEEALDAAQAAANAALA 361
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 5-376 7.64e-62

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 204.51  E-value: 7.64e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725   5 KKLLIGAAVAAlgvSALLTGCGGkkADDASGDKDGKVKISMaWWGSQVRHDATVKVIEMYEKENPKVDIEYEFYDMDGYL 84
Cdd:COG1653     2 RRLALALAAAL---ALALAACGG--GGSGAAAAAGKVTLTV-WHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  85 TKLNTLAASKTVWDVFQM-GGNFPAFIDS--IEPLDQYIKDGLIDTSNISEGYLATTQQDGKQWGISNGVGAYGIAYDPA 161
Cdd:COG1653    76 TKLLTALAAGNAPDVVQVdSGWLAEFAAAgaLVPLDDLLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 162 MFKKAGLDEPtpdWTWADFEEMCLKIHDKTGQFGFSNFDDFKTATMAITQTGGGNNFfsteTNSKTMGFKDPKlLVPYLE 241
Cdd:COG1653   156 LFEKAGLDPP---KTWDELLAAAKKLKAKDGVYGFALGGKDGAAWLDLLLSAGGDLY----DEDGKPAFDSPE-AVEALE 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 242 MRKNLVDAGAYPDPGAIKEIKDIeGDYLVTGEAAMTWVAANQLQALRTAA-GREIKMMTLPKTKADVPGGGMMSSQMLSM 320
Cdd:COG1653   228 FLKDLVKDGYVPPGALGTDWDDA-RAAFASGKAAMMINGSWALGALKDAApDFDVGVAPLPGGPGGKKPASVLGGSGLAI 306

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1811729725 321 AKNSKHKEEAAKFISYFeTNIEANKILNGERGVPIDDKVREELTKTADENMQEVYN 376
Cdd:COG1653   307 PKGSKNPEAAWKFLKFL-TSPEAQAKWDALQAVLLGQKTPEEALDAAQAAANAALA 361
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 42-425 9.56e-49

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: 170.66  E-value: 9.56e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  42 KISMAWWGSQVRHDATVKVIEMYEKENPKVDIEYEFYDMDGYLTKLNTLAASKTVWDVFQMGG-NFPAFIDS--IEPLDQ 118
Cdd:cd13585     1 TLTFWDWGQPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGpWVPEFASNgaLLDLDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 119 YIKDGLIDTsNISEGYLATTQQDGKQWGISNGVGAYGIAYDPAMFKKAGlDEPTPDWTWADFEEMCLKIHD-KTGQFGFS 197
Cdd:cd13585    81 YIEKDGLDD-DFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAG-PGPKPPWTWDELLEAAKKLTDkKGGQYGFA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 198 ---NFDDFKTATMAITQTGGgnNFFSTETnsKTMGFKDPKlLVPYLEMRKNLVDAGAypDPGAIKEIKDIEGDYLVTGEA 274
Cdd:cd13585   159 lrgGSGGQTQWYPFLWSNGG--DLLDEDD--GKATLNSPE-AVEALQFYVDLYKDGV--APSSATTGGDEAVDLFASGKV 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 275 AMTWVAANQLQALRTAAGR-EIKMMTLPKTKADvPGGGMMSSQMLSMAKNSKHKEEAAKFISYFeTNIEANKILNGERGV 353
Cdd:cd13585   232 AMMIDGPWALGTLKDSKVKfKWGVAPLPAGPGG-KRASVLGGWGLAISKNSKHPEAAWKFIKFL-TSKENQLKLGGAAGP 309

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1811729725 354 PIDDKVREELTKTADENMQEVYNYIDLVGEFDKGEGNPIESPANAAIEDQYKLLLEQVLydQTTPAKAAKDL 425
Cdd:cd13585   310 AALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGAL--GKSPEEALKEA 379
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 48-340 4.61e-20

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: 90.17  E-value: 4.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  48 WGSQVRHDATVKVIEMYEKENPKVDIEYEFYDMDGYLTKLNT-LAASKTVWDVFQMGGNFPAFIDS---IEPLDQYIKDG 123
Cdd:pfam01547   1 AASLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTaIAAGDGPADVFASDNDWIAELAKaglLLPLDDYVANY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 124 LIDtsnisegylattqQDGKQWGISNGVGAYGIAYDPAMFKKAGLDEPtpdWTWADFEEMCLKIHDKT----GQFGFSNF 199
Cdd:pfam01547  81 LVL-------------GVPKLYGVPLAAETLGLIYNKDLFKKAGLDPP---KTWDELLEAAKKLKEKGkspgGAGGGDAS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 200 DDFKTATMAITQTGGGNNFFSTETNSKTMGFKDPKLLVPYLEMRKNLVDAGAYPDPGAIKEikDIEGDYLVTGEAAMTWV 279
Cdd:pfam01547 145 GTLGYFTLALLASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADG--REALALFEQGKAAMGIV 222

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811729725 280 AANQLQALRTAAGREIKMMTLPKTKADV-------PGGGMMSSQMLSMAKNSKHKEEAAKFISYFETN 340
Cdd:pfam01547 223 GPWAALAANKVKLKVAFAAPAPDPKGDVgyaplpaGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSP 290
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 5-376 7.64e-62

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 204.51  E-value: 7.64e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725   5 KKLLIGAAVAAlgvSALLTGCGGkkADDASGDKDGKVKISMaWWGSQVRHDATVKVIEMYEKENPKVDIEYEFYDMDGYL 84
Cdd:COG1653     2 RRLALALAAAL---ALALAACGG--GGSGAAAAAGKVTLTV-WHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  85 TKLNTLAASKTVWDVFQM-GGNFPAFIDS--IEPLDQYIKDGLIDTSNISEGYLATTQQDGKQWGISNGVGAYGIAYDPA 161
Cdd:COG1653    76 TKLLTALAAGNAPDVVQVdSGWLAEFAAAgaLVPLDDLLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 162 MFKKAGLDEPtpdWTWADFEEMCLKIHDKTGQFGFSNFDDFKTATMAITQTGGGNNFfsteTNSKTMGFKDPKlLVPYLE 241
Cdd:COG1653   156 LFEKAGLDPP---KTWDELLAAAKKLKAKDGVYGFALGGKDGAAWLDLLLSAGGDLY----DEDGKPAFDSPE-AVEALE 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 242 MRKNLVDAGAYPDPGAIKEIKDIeGDYLVTGEAAMTWVAANQLQALRTAA-GREIKMMTLPKTKADVPGGGMMSSQMLSM 320
Cdd:COG1653   228 FLKDLVKDGYVPPGALGTDWDDA-RAAFASGKAAMMINGSWALGALKDAApDFDVGVAPLPGGPGGKKPASVLGGSGLAI 306

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1811729725 321 AKNSKHKEEAAKFISYFeTNIEANKILNGERGVPIDDKVREELTKTADENMQEVYN 376
Cdd:COG1653   307 PKGSKNPEAAWKFLKFL-TSPEAQAKWDALQAVLLGQKTPEEALDAAQAAANAALA 361
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 42-425 9.56e-49

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: 170.66  E-value: 9.56e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  42 KISMAWWGSQVRHDATVKVIEMYEKENPKVDIEYEFYDMDGYLTKLNTLAASKTVWDVFQMGG-NFPAFIDS--IEPLDQ 118
Cdd:cd13585     1 TLTFWDWGQPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGpWVPEFASNgaLLDLDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 119 YIKDGLIDTsNISEGYLATTQQDGKQWGISNGVGAYGIAYDPAMFKKAGlDEPTPDWTWADFEEMCLKIHD-KTGQFGFS 197
Cdd:cd13585    81 YIEKDGLDD-DFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAG-PGPKPPWTWDELLEAAKKLTDkKGGQYGFA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 198 ---NFDDFKTATMAITQTGGgnNFFSTETnsKTMGFKDPKlLVPYLEMRKNLVDAGAypDPGAIKEIKDIEGDYLVTGEA 274
Cdd:cd13585   159 lrgGSGGQTQWYPFLWSNGG--DLLDEDD--GKATLNSPE-AVEALQFYVDLYKDGV--APSSATTGGDEAVDLFASGKV 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 275 AMTWVAANQLQALRTAAGR-EIKMMTLPKTKADvPGGGMMSSQMLSMAKNSKHKEEAAKFISYFeTNIEANKILNGERGV 353
Cdd:cd13585   232 AMMIDGPWALGTLKDSKVKfKWGVAPLPAGPGG-KRASVLGGWGLAISKNSKHPEAAWKFIKFL-TSKENQLKLGGAAGP 309

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1811729725 354 PIDDKVREELTKTADENMQEVYNYIDLVGEFDKGEGNPIESPANAAIEDQYKLLLEQVLydQTTPAKAAKDL 425
Cdd:cd13585   310 AALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGAL--GKSPEEALKEA 379
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 55-427 1.15e-39

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: 146.28  E-value: 1.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  55 DATVKVIEMYEKENPKVDIEYEFY-DMDGYLTKLNTLAASKTVWDVFQMGGNF-PAFIDS--IEPLDQYIKDGLIDTSNI 130
Cdd:cd14748    14 KALEELVDEFNKSHPDIKVKAVYQgSYDDTLTKLLAALAAGTAPDVAQVDASWvAQLADSgaLEPLDDYIDKDGVDDDDF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 131 SEGYLATTQQDGKQWGISNGVGAYGIAYDPAMFKKAGLDEPTPDWTWADFEEMCLKIHD---KTGQFGFSNFDDFKTAT- 206
Cdd:cd14748    94 YPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKDkggKTGRYGFALPPGDGGWTf 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 207 -MAITQTGGGnnfFSTETNSKTMgFKDPKlLVPYLEMRKNLVDAGAYPDPGAIKEIkdieGDYLVTGEAAMTWVAANQLQ 285
Cdd:cd14748   174 qALLWQNGGD---LLDEDGGKVT-FNSPE-GVEALEFLVDLVGKDGVSPLNDWGDA----QDAFISGKVAMTINGTWSLA 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 286 ALR-TAAGREIKMMTLPKTKaDVPGGGMMSSQMLSMAKN-SKHKEEAAKFISYFETNiEANKILNGERGVPIddkVREEL 363
Cdd:cd14748   245 GIRdKGAGFEYGVAPLPAGK-GKKGATPAGGASLVIPKGsSKKKEAAWEFIKFLTSP-ENQAKWAKATGYLP---VRKSA 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1811729725 364 TKTADENMQEVYNYIDLVGEFDKGEGNPIESPANAAIEDQYKLLLEQVLYDQTTPAKAAKDLYA 427
Cdd:cd14748   320 AEDPEEFLAENPNYKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQE 383
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
3-435 6.09e-36

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 136.62  E-value: 6.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725   3 KRKKLLIGAAVAALGVSalLTGCGGKKAD-DASGDKDGKVKISMawWGSQVRHDATVKVIEMYEKEnPKVDIEYEFYDMD 81
Cdd:COG2182     2 KRRLLAALALALALALA--LAACGSGSSSsGSSSAAGAGGTLTV--WVDDDEAEALEEAAAAFEEE-PGIKVKVVEVPWD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  82 GYLTKLNTLAASKTVWDVFQMGG-NFPAFIDS--IEPLDQYIKDglidTSNISEGYLATTQQDGKQWGISNGVGAYGIAY 158
Cdd:COG2182    77 DLREKLTTAAPAGKGPDVFVGAHdWLGELAEAglLAPLDDDLAD----KDDFLPAALDAVTYDGKLYGVPYAVETLALYY 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 159 DPAMFKKaglDEPTpdwTWADFEEMCLKIHDKtGQFGFS-NFDDFKTATMAITQTGGGnnFFSTET-NSKTMGFKDPKLl 236
Cdd:COG2182   153 NKDLVKA---EPPK---TWDELIAAAKKLTAA-GKYGLAyDAGDAYYFYPFLAAFGGY--LFGKDGdDPKDVGLNSPGA- 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 237 VPYLEMRKNLVDAGAYPDPGAikeiKDIEGDYLVTGEAAMT----WVAANqlqaLRTAAGREIKMMTLPKTKADVPGGGM 312
Cdd:COG2182   223 VAALEYLKDLIKDGVLPADAD----YDAADALFAEGKAAMIingpWAAAD----LKKALGIDYGVAPLPTLAGGKPAKPF 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 313 MSSQMLSMAKNSKHKEEAAKFISYFeTNIEANKILNGERG-VPIDDKVREELTKTADENMQEVYNYIdlvgefDKGEGNP 391
Cdd:COG2182   295 VGVKGFGVSAYSKNKEAAQEFAEYL-TSPEAQKALFEATGrIPANKAAAEDAEVKADPLIAAFAEQA------EYAVPMP 367

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1811729725 392 IeSPANAAIEDQYKLLLEQVLYDQTTPAKAAKDLYAFAKEQLGE 435
Cdd:COG2182   368 N-IPEMGAVWTPLGTALQAIASGKADPAEALDAAQKQIEAAIAQ 410
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 59-425 2.24e-24

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: 104.00  E-value: 2.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  59 KVIEMYEKENPKVDIEYEFYDMDGYLTKLNTLAASKTVWDVFQM--GGNFPAFIDS--IEPLDQYIKDGLIDTSNISeGY 134
Cdd:cd14749    19 ELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLwpGGWLAEFVKAglLLPLTDYLDPNGVDKRFLP-GL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 135 LATTQQDGKQWGISNGVGAYGIAYDPAMFKKAGLDEPtPDwTWADFEEMCLKI-HDKTGQFGFSNFDDFKTA----TMAI 209
Cdd:cd14749    98 ADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGVKP-PK-TWDELIEAAKKDkFKAKGQTGFGLLLGAQGGhwyfQYLV 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 210 TQTGGGnnfFSTETNSKTMGFKDPKlLVPYLEMRKNLVDAGAYPDPGAIKEIKDIEGDYlVTGEAAMTWVAANQLQALRT 289
Cdd:cd14749   176 RQAGGG---PLSDDGSGKATFNDPA-FVQALQKLQDLVKAGAFQEGFEGIDYDDAGQAF-AQGKAAMNIGGSWDLGAIKA 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 290 A-AGREIKMMTLP-KTKADVPGGGMMSSQMLSMAKNSKHKEEAAKFISYFETNiEANKILngergvpidDKVREELTKTA 367
Cdd:cd14749   251 GePGGKIGVFPFPtVGKGAQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSP-EVMKQY---------LEDVGLLPAKE 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1811729725 368 DENMQEVYNYIDLVGEFDKGEGNPIESPA----NAAIEDQYKLLLEQVLYDQTTPAKAAKDL 425
Cdd:cd14749   321 VVAKDEDPDPVAILGPFADVLNAAGSTPFldeyWPAAAQVHKDAVQKLLTGKIDPEQVVKQA 382
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 59-433 8.48e-22

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: 96.61  E-value: 8.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  59 KVIEMYEKENPKVDIEYEFYDMDGYLTKLNTLAASKTVWDVFQMGGNF-PAFIDS--IEPLDQYIKDgLIDTSNISEGYL 135
Cdd:cd14747    18 ELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWvAEFAAMgaLEDLTPYLED-LGGDKDLFPGLV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 136 ATTQQDGKQWGISNGVGAYGIAYDPAMFKKAGLDEPtPDwTWADFEEMCLKI-HDKTGQFGFS---NFDDFKTATMAITQ 211
Cdd:cd14747    97 DTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGDEA-PK-TWDELEAAAKKIkADGPDVSGFAipgKNDVWHNALPFVWG 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 212 TGGgnNFFSTETNSKTmgFKDPKlLVPYLEMRKNLVDAGAYPDPGAIKEIkDIEGDYlVTGEAAM----TWVAANQLQAL 287
Cdd:cd14747   175 AGG--DLATKDKWKAT--LDSPE-AVAGLEFYTSLYQKGLSPKSTLENSA-DVEQAF-ANGKVAMiisgPWEIGAIREAG 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 288 RTAAGReIKMMTLPKTkadvPGGGMMSS---QMLSMAKNSKHKEEAAKFISYFeTNIEANKILNGERGV-PIDDKVREEL 363
Cdd:cd14747   248 PDLAGK-WGVAPLPGG----PGGGSPSFaggSNLAVFKGSKNKDLAWKFIEFL-SSPENQAAYAKATGMlPANTSAWDDP 321

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1811729725 364 TKTADENMQEVYNYIdlvgefDKGEGNPIeSPANAAIEDQYKLLLEQVLYDQT-TPAKAAKDLYAFAKEQL 433
Cdd:cd14747   322 SLANDPLLAVFAEQL------KTGKATPA-TPEWGEIEAELVLVLEEVWIGVGaDVEDALDKAAAEINEIL 385
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 48-340 4.61e-20

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: 90.17  E-value: 4.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  48 WGSQVRHDATVKVIEMYEKENPKVDIEYEFYDMDGYLTKLNT-LAASKTVWDVFQMGGNFPAFIDS---IEPLDQYIKDG 123
Cdd:pfam01547   1 AASLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTaIAAGDGPADVFASDNDWIAELAKaglLLPLDDYVANY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 124 LIDtsnisegylattqQDGKQWGISNGVGAYGIAYDPAMFKKAGLDEPtpdWTWADFEEMCLKIHDKT----GQFGFSNF 199
Cdd:pfam01547  81 LVL-------------GVPKLYGVPLAAETLGLIYNKDLFKKAGLDPP---KTWDELLEAAKKLKEKGkspgGAGGGDAS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 200 DDFKTATMAITQTGGGNNFFSTETNSKTMGFKDPKLLVPYLEMRKNLVDAGAYPDPGAIKEikDIEGDYLVTGEAAMTWV 279
Cdd:pfam01547 145 GTLGYFTLALLASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADG--REALALFEQGKAAMGIV 222

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811729725 280 AANQLQALRTAAGREIKMMTLPKTKADV-------PGGGMMSSQMLSMAKNSKHKEEAAKFISYFETN 340
Cdd:pfam01547 223 GPWAALAANKVKLKVAFAAPAPDPKGDVgyaplpaGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSP 290
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 42-425 2.28e-19

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: 89.28  E-value: 2.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  42 KISMAWWGSQVRHDATVKVIEMYEKENP--KVDIEYEFYDMDGYLTKLNTLAASK-TVWDVFQMGGNFPA-FIDS--IEP 115
Cdd:cd14750     1 TITFAAGSDGQEGELLKKAIAAFEKKHPdiKVEIEELPASSDDQRQQLVTALAAGsSAPDVLGLDVIWIPeFAEAgwLLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 116 LDQYIKDGliDTSNISEGYLATTQQDGKQWGISNGVGAYGIAYDPAMFKKAGLDEPTpdwTWADFEEMCLK-IHDKTGQF 194
Cdd:cd14750    81 LTEYLKEE--EDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPEPPK---TWDELLEAAKKrKAGEPGIW 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 195 GFS-NFDDFKTAT----MAITQTGGGnnFFSTEtnSKTMGFKDPKLLVPyLEMRKNLVDAGAypDPGAIKEIKDIE-GDY 268
Cdd:cd14750   156 GYVfQGKQYEGLVcnflELLWSNGGD--IFDDD--SGKVTVDSPEALEA-LQFLRDLIGEGI--SPKGVLTYGEEEaRAA 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 269 LVTGEAAM--TWVAANQL-QALRTAAGREIKMMTLPKTKaDVPGGGMMSSQMLSMAKNSKHKEEAAKFISYFeTNIEANK 345
Cdd:cd14750   229 FQAGKAAFmrNWPYAYALlQGPESAVAGKVGVAPLPAGP-GGGSASTLGGWNLAISANSKHKEAAWEFVKFL-TSPEVQK 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 346 ILNGERGVPiddKVREELTKtaDENMQEVYNYI-DLVGEFDKGEGNPIeSPANAAIEDQYKLLLEQVLYDQTTPAKAAKD 424
Cdd:cd14750   307 RRAINGGLP---PTRRALYD--DPEVLEAYPFLpALLEALENAVPRPV-TPKYPEVSTAIQIALSAALSGQATPEEALKQ 380


                  .
gi 1811729725 425 L 425
Cdd:cd14750   381 A 381
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 59-425 3.96e-15

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: 76.65  E-value: 3.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  59 KVIEMYEKENPKVDIEYEFYDMDGYLTKLNTLAASKTVWDVFQMG-GNFPAF--IDSIEPLDQYikDGLIDTSNISEGYL 135
Cdd:cd14751    18 KLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADiAWVPEFakLGYLQPLDGT--PAFDDIVDYLPGPM 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 136 ATTQQDGKQWGISNGVGAYGIAYDPAMFKKAGLDEPTpdwTWADFEEMCLKIHDKTGQFGFS-NFDDFKTATMAITQTGG 214
Cdd:cd14751    96 ETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEVPK---TMDELVAAAKAIKKKKGRYGLYiSGDGPYWLLPFLWSFGG 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 215 GnnffSTETNSKTMGFKDPKLlVPYLEMRKNLVDAGAypdpgAIKEIKDIEGDY---LVTGEAAMT----WVAANQLQAL 287
Cdd:cd14751   173 D----LTDEKKATGYLNSPES-VRALETIVDLYDEGA-----ITPCASGGYPNMqdgFKSGRYAMIvngpWAYADILGGK 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 288 RTAAGREIKMMTLP--KTKADVPGGGmmssQMLSMAKNSKHKEEAAKFISYFeTNIEANKILNGERG-VPIDDKVREELT 364
Cdd:cd14751   243 EFKDPDNLGIAPVPagPGGSGSPVGG----EDLVIFKGSKNKDAAWKFVKFM-SSAEAQALTAAKLGlLPTRTSAYESPE 317

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1811729725 365 KTADENMQEvynYIDLVgefDKGEGNPIeSPANAAIEDQYKLLLEQVLYDQTTPAKAAKDL 425
Cdd:cd14751   318 VANNPMVAA---FKPAL---ETAVPRPP-IPEWGELFEPLTLAFAKVLRGEKSPREALDEA 371
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
2-336 1.67e-14

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 74.18  E-value: 1.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725   2 LKRKKLLigaAVAALGVSALLTGCGgkkaddASGDKDGKVKISMawWGSQVRHDatvkVIEMYEKENpKVDIEYEFYD-M 80
Cdd:COG0687     1 MSRRSLL---GLAAAALAAALAGGA------PAAAAEGTLNVYN--WGGYIDPD----VLEPFEKET-GIKVVYDTYDsN 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  81 DGYLTKLntlAASKTVWDVFQMGGNFpafidsiepLDQYIKDGL---IDTS------NISEGYLATTQQDGKQWGISNGV 151
Cdd:COG0687    65 EEMLAKL---RAGGSGYDVVVPSDYF---------VARLIKAGLlqpLDKSklpnlaNLDPRFKDPPFDPGNVYGVPYTW 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 152 GAYGIAYDPAMFKKagldEPTpdwTWADF--EEMclkihdkTGQFGFsnFDDFKTATMAITQTGGGNNFFSTETNSKTMG 229
Cdd:COG0687   133 GTTGIAYNTDKVKE----PPT---SWADLwdPEY-------KGKVAL--LDDPREVLGAALLYLGYDPNSTDPADLDAAF 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 230 fkdpKLLvpyLEMRKNLvdAGAYPDPGAIKeikdiegDYLVTGEAAMTWVAANQLQALRtAAGREIKmMTLPKTkadvpg 309
Cdd:COG0687   197 ----ELL---IELKPNV--RAFWSDGAEYI-------QLLASGEVDLAVGWSGDALALR-AEGPPIA-YVIPKE------ 252

                         330       340
                  ....*....|....*....|....*..
gi 1811729725 310 GGMMSSQMLSMAKNSKHKEEAAKFISY 336
Cdd:COG0687   253 GALLWFDNMAIPKGAPNPDLAYAFINF 279
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 42-336 1.16e-13

The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270307 [Multi-domain]  Cd Length: 268  Bit Score: 70.72  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  42 KISMAWWGSQVRHDATVKVIEMYEKENPkVDIEYEFYDMDGYLTKLntLAASKTV-WDVFQMGGNFpafidsiepLDQYI 120
Cdd:cd13589     1 TLVVATWGGSYEDAQRKAVIEPFEKETG-IKVVYDTGTSADRLAKL--QAQAGNPqWDVVDLDDGD---------AARAI 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 121 KDGL---IDTSNI-SEGYLATTQQDGKQWGISNGVGAYGIAYDPAMFKkagldEPTPDWTWADFEemclkihdKTGQFGF 196
Cdd:cd13589    69 AEGLlepLDYSKIpNAAKDKAPAALKTGYGVGYTLYSTGIAYNTDKFK-----EPPTSWWLADFW--------DVGKFPG 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 197 SNFDDfKTATMAITQTGGGNNFFSTETNSKTmGFKdpKLlvpyLEMRKNLVdagAYPDPGAikeikDIEgDYLVTGEAAM 276
Cdd:cd13589   136 PRILN-TSGLALLEAALLADGVDPYPLDVDR-AFA--KL----KELKPNVV---TWWTSGA-----QLA-QLLQSGEVDM 198

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 277 TWVAANQLQALRtAAGREIKmMTLPKtkadvpGGGMMSSQMLSMAKNSKHKEEAAKFISY 336
Cdd:cd13589   199 APAWNGRAQALI-DAGAPVA-FVWPK------EGAILGPDTLAIVKGAPNKELAMKFINF 250
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 47-424 3.77e-11

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: 64.24  E-value: 3.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  47 WWGSQVRHDATVKVIEMYEKENPkVDIEYEFYDMDGYLTKLNTLAASKTVWDVF-----QMGGNFPAfiDSIEPLDQYik 121
Cdd:cd13586     5 WTDEDGELEYLKELAEEFEKKYG-IKVEVVYVDSGDTREKFITAGPAGKGPDVFfgphdWLGELAAA--GLLAPIPEY-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 122 dgLIDTSNISEGYLATTQQDGKQWGISNGVGAYGIAYDPAMFkkagldePTPDWTWADFEEMCLKIHDKTG-QFGF-SNF 199
Cdd:cd13586    80 --LAVKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLV-------PEPPKTWEELIALAKKFNDKAGgKYGFaYDQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 200 DDFkTATMAITQTGGGNNFFSTETNSKTMGFKDPKLlVPYLEMRKNLVDAGAYPDPGAIKeikDIEGDYLVTGEAAMT-- 277
Cdd:cd13586   151 TNP-YFSYPFLAAFGGYVFGENGGDPTDIGLNNEGA-VKGLKFIKDLKKKYKVLPPDLDY---DIADALFKEGKAAMIin 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 278 --WVAANQLqalrtAAGREIKMMTLPKTKADVPGGGMMSSQMLSMAKNSKHKEEAAKFISYFETNIEANKILNGERGVPi 355
Cdd:cd13586   226 gpWDLADYK-----DAGINFGVAPLPTLPGGKQAAPFVGVQGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIP- 299

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1811729725 356 ddkvreelTKTADENMQEVYNYIDLVGEFDKGE-GNPIES-PANAAIEDQYKLLLEQVLYDQTTPAKAAKD 424
Cdd:cd13586   300 --------ALKDALNDAAVKNDPLVKAFAEQAQyGVPMPNiPEMAAVWDAMGNALNLVASGKATPEEAAKD 362
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 59-337 1.27e-10

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 62.04  E-value: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  59 KVIEMYEKENpKVDIEYEFYDMDGYLTKLNTLAASKTV--WDVFQM-GGNFPAFIDS--IEPLDQYikdgliDTSNISEG 133
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNApdLDVVWIaADQLATLAEAglLADLSDV------DNLDDLPD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 134 YLATTQQDGKQWGISNGVGA-YGIAYDPAMFKKAGLDeptpDWTWADFEEMCLKIHDKTGQFGFSNFddfktaTMAITQT 212
Cdd:pfam13416  74 ALDAAGYDGKLYGVPYAASTpTVLYYNKDLLKKAGED----PKTWDELLAAAAKLKGKTGLTDPATG------WLLWALL 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 213 GGGNNFfsTETNSKTMGFKDpkllvpYLEMRKNLVDAGAYPDPGAikeikDIEGDYLvTGEAAMTWVAANQLQALRTAAg 292
Cdd:pfam13416 144 ADGVDL--TDDGKGVEALDE------ALAYLKKLKDNGKVYNTGA-----DAVQLFA-NGEVAMTVNGTWAAAAAKKAG- 208

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1811729725 293 reikmmtlPKTKADVPGGGMMS-SQMLSMAKNSKHKEEAA-KFISYF 337
Cdd:pfam13416 209 --------KKLGAVVPKDGSFLgGKGLVVPAGAKDPRLAAlDFIKFL 247
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 42-424 2.20e-10

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: 62.04  E-value: 2.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  42 KISMAWWGSQVRHDATVKVIEMYEKENPKVDIEYEFYDMDGYLTKLNTLAASKT----VWDVFQMGGNFPAfIDSIEPLD 117
Cdd:cd13522     1 TITVWHQYDTGENQAVNELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKgpdvVFGPSDSLGPFAA-AGLLAPLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 118 QYIKDGLIDTSNisegYLATTQQDGKQWGISNGVGAYgiaydpAMFKKAGLDEPTPDWTWADFEEMC--LKIHDKTGqFG 195
Cdd:cd13522    80 EYVSKSGKYAPN----TIAAMKLNGKLYGVPVSVGAH------LMYYNKKLVPKNPPKTWQELIALAqgLKAKNVWG-LV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 196 FSNFDDFKTATMaitQTGGGNNFFSTETNSKTMGFkDPKLLVPYLEMRKNLVDAGAYPDPGAIKEIKDIEgdyLVTGEAA 275
Cdd:cd13522   149 YNQNEPYFFAAW---IGGFGGQVFKANNGKNNPTL-DTPGAVEALQFLVDLKSKYKIMPPETDYSIADAL---FKAGKAA 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 276 MT----WVAANQLQALRTAAGreikMMTLPKTKADVPGGGMMSSQMLSMAKNSKHKEEAAKFISYFeTNIEANKILNGER 351
Cdd:cd13522   222 MIingpWDLGDYRQALKINLG----VAPLPTFSGTKHAAPFVGGKGFGINKESQNKAAAVEFVKYL-TSYQAQLVLFDDA 296

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1811729725 352 G-VPIDDKVREELTKTADENMQEVynyidlVGEFDKGEGNPIeSPANAAIEDQYKLLLEQVLYDQTTPAKAAKD 424
Cdd:cd13522   297 GdIPANLQAYESPAVQNKPAQKAS------AEQAAYGVPMPN-IPEMRAVWDAFRIAVNSVLAGKVTPEAAAKD 363
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 40-359 1.45e-06

The periplasmic binding component of ABC transport system specific for maltodextrin; This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270375 [Multi-domain]  Cd Length: 368  Bit Score: 50.07  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  40 KVKISMAWWGSQvrHDATVKVIEMYEKENPKVDIEYEFYDMDGYLTKLNTLAASKTVWDVFQMG----GNFpAFIDSIEP 115
Cdd:cd13657     1 TITIWHALTGAE--EDALQQIIDEFEAKYPVPNVKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAhdwiGQF-AEAGLLVP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 116 LDQYIkdglidTSNISEGYLATTQQ----DGKQWGISNGVGAYGIAYDPAMFkkagldePTPDWTWADFEEMCLKIHDK- 190
Cdd:cd13657    78 ISDYL------SEDDFENYLPTAVEavtyKGKVYGLPEAYETVALIYNKALV-------DQPPETTDELLAIMKDHTDPa 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 191 TGQFGFSNFDDFKTATMAITQTGGGNNFfstetnsktmgfkDPKLLVPYLEmrknlvdagaypDPGAIKEIK-------- 262
Cdd:cd13657   145 AGSYGLAYQVSDAYFVSAWIFGFGGYYF-------------DDETDKPGLD------------TPETIKGIQflkdfswp 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 263 ----DIEGDYLVT----GEAAMTWVAANQLQALRtAAGREIKMMTLPK---TKADVPGGGmMSSQMLSMAKNSKHKEEAA 331
Cdd:cd13657   200 ympsDPSYNTQTSlfneGKAAMIINGPWFIGGIK-AAGIDLGVAPLPTvdgTNPPRPYSG-VEGIYVTKYAERKNKEAAL 277

                         330       340
                  ....*....|....*....|....*....
gi 1811729725 332 KFISYFETNiEANKILNGERG-VPIDDKV 359
Cdd:cd13657   278 DFAKFFTTA-EASKILADENGyVPAATNA 305
PBP2_polyamines cd13523
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 48-336 2.32e-06

The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding proteins that function as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as 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: 270241 [Multi-domain]  Cd Length: 268  Bit Score: 48.97  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  48 WGSQVRHDatvkVIEMYEKENpKVDIEYEFYDMDGYLTKLNTlAASKTVWDVFQMGGNF-PAFIDS--IEPLDqyiKDGL 124
Cdd:cd13523     7 WGGYLPQD----IIDPFEKET-GIKVVVDTAANSERMIKKLS-AGGSGGFDLVTPSDSYtSRQLGVglMQPID---KSLL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 125 IDTSNISEGY--LATTQQDGKQWGISNGVGAYGIAYDPAMFKkagldePTPDWTWADfeeMCLKihDKTGQFGFSNfDDF 202
Cdd:cd13523    78 PSWATLDPHLtlAAVLTVPGKKYGVPYQWGATGLVYNTDKVK------APPKSYAAD---LDDP--KYKGRVSFSD-IPR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 203 KTATMAitqtggGNNFFSTETNSKTMGFKDPKLlvPYLEMRKNLVdaGAYPDPGAikEIKDIegdyLVTGE--AAMTWVA 280
Cdd:cd13523   146 ETFAMA------LANLGADGNEELYPDFTDAAA--ALLKELKPNV--KKYWSNAS--QPANL----LLNGEvvLAMAWLG 209

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1811729725 281 -ANQLQAlrtaAGREIKMmTLPKtkadvpGGGMMSSQMLSMAKNSKHKEEAAKFISY 336
Cdd:cd13523   210 sGFKLKQ----AGAPIEF-VVPK------EGAVGWLDTFAVPANAPNKDGAYKLLNA 255
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 40-336 1.59e-05

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


Pssm-ID: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 46.97  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  40 KVKISMAWW---GSQVRHDatvKVIEMYEKENPKVDIEYEFYDMDGYLTKLNTLAASKTVWDVFQM--GGNFPAFIDS-- 112
Cdd:cd13583     1 PLTLSMMYRdhpNYPVKDD---WLIWKEIEEKTNVKFKRTPIPSSDYETKRSLLIASGDAPDIIPVlyPGEENEFVASga 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 113 IEPLDQYIK-----DGLIDTSNISEGYLATTQQDGK-----QWGISNGVGaYGIAYDPAMFKKAGLDEPTpdwTWADFEE 182
Cdd:cd13583    78 LLPISDYLDympnyKKYVEKWGLGKELATGRQSDGKyyslpGLHEDPGVQ-YSFLYRKDIFEKAGIKIPT---TWDEFYA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 183 MCLKIHDKTG-------QFGFSNFDDFkTATMAITQTGGGNNFFSTETNSK-------TMGFKDpkllvpYLEMRKNLVD 248
Cdd:cd13583   154 ALKKLKEKYPdsypysdRWNSNALLLI-AAPAFGTTAGWGFSNYTYDPDTDkfvygatTDEYKD------MLQYFNKLYA 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 249 AGAYpDPGAIKEIKDIEGDYLVTGEAAMTW------VAANQLQALRTAAGREIKMMTLPKTKA------DVPGGGMMSSq 316
Cdd:cd13583   227 EGLL-DPESFTQTDDQAKAKFLNGKSFVITtnpqtvDELQRNLRAADGGNYEVVSITPPAGPAgkaingSRLENGFMIS- 304

                         330       340
                  ....*....|....*....|
gi 1811729725 317 mlSMAKNSKHKEEAAKFISY 336
Cdd:cd13583   305 --SKAKDSKNFEALLQFLDW 322
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 39-183 2.70e-05

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


Pssm-ID: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  39 GKVKIS-MAWWGSQVRHDATVKVIEMYEKENPKVDIEYEFYDMDGYLTKLNTLAASKTVWDVFQMGG--NFPAFIDS--I 113
Cdd:cd13580     1 EPVTITiVANLGGNPKPDPDDNPYTKYLEEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVVNDpqLSITLVKQgaL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811729725 114 EPLDQYIKDGLID-TSNISEGYLATTQQDGKQWGISngvGAYGIAYDPAMF------KKAGLDEPTpdwTWADFEEM 183
Cdd:cd13580    81 WDLTDYLDKYYPNlKKIIEQEGWDSASVDGKIYGIP---RKRPLIGRNGLWirkdwlDKLGLEVPK---TLDELYEV 151
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 40-431 6.10e-05

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: 45.14  E-value: 6.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  40 KVKISMAWWGSQVRHDATVKVIEMYEKENpkVDIEYEFYDMDGYLTKLNTLAASKTVWDVFQMGG---NFPAFIDS--IE 114
Cdd:cd13521     3 TLSVLMAFNDNWVDDENWPVAKEIEKLTN--VKLEIVAVTAATSQQKLNLMLASGDLPDIVGADYlkdKFIAYGMEgaFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 115 PLDQYIKDG-----LIDTSNisEGYLATTQQDGKQWGISN----GVGAYGIAYDPAMFKKAGLdePTPDwTWADFEEMCL 185
Cdd:cd13521    81 PLSKYIDQYpnlkaFFKQHP--DVLRASTASDGKIYLIPYeppkDVPNQGYFIRKDWLDKLNL--KTPK-TLDELYNVLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 186 KIHDK----TGQ---FGFSNFDDFKTATMAITQTGGGNNFFSTETNSKTMG--FKDPKLLVPYLEMRK---NLVDAGaYP 253
Cdd:cd13521   156 AFKEKdpngNGKadeIPFIDRDPLYGAFRLINSWGARSAGGSTDSDWYEDNgkFKHPFASEEYKDGMKymnKLYTEG-LI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 254 DPGAIKEIKDIEGDYLVTGEAAMTWVAANQLQALRTAAGREIKMMTL-----------PKTKADVPGGGMMSSQMLSmaK 322
Cdd:cd13521   235 DKESFTQKDDQAEQKFSNGKLGGFTHNWFASDNLFTAQLGKEKPMYIllpiapagnvkGRREEDSPGYTGPDGVAIS--K 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 323 NSKHKEEAAKFISYFETniEANKILN--GERGVPIDDKVREELTKTADENM-QEVYNYIDLVGEFDKGegnpiespanaA 399
Cdd:cd13521   313 KAKNPVAALKFFDWLAS--EEGRELAnfGIEGVHYNKDNGKKRTKDPVKKSdQPGDNQLYDLPAFIKG-----------G 379

                         410       420       430
                  ....*....|....*....|....*....|..
gi 1811729725 400 IEDQYKLLLEQVLYDQTTPAKAAKDLYAFAKE 431
Cdd:cd13521   380 FWNEYTYPRPQWGVLTGDSARLPIDMYIKPKY 411
PBP2_PotF cd13659
The periplasmic substrate-binding component of an ABC putrescine transport system and related ...
 60-337 3.08e-04

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


Pssm-ID: 270377 [Multi-domain]  Cd Length: 331  Bit Score: 42.71  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  60 VIEMYEKENpKVDIEYEFYDMDGYLTKlnTLAASKTVWDVFQMGGNF-PAFIDS--IEPLDqyiKDGLIDTSNISEGYLA 136
Cdd:cd13659    15 TLEDFEKET-GIKVVYDTYDSNEELEA--KLLAGGSGYDLVVPSANFlGRQIKAgaLQKLD---KSKLPNWKNLDPLLLK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 137 TTQQ--DGKQWGISNGVGAYGIAYDPAMFKKAGLDEPTPDWTWA-DFEEMclkihDKTGQFGFSnFDDFKTATMAITQTG 213
Cdd:cd13659    89 LLAAvdPGNRYAVPYMWGTTGIAYNVDKVKAALGDDLPDSWDLVfDPENL-----SKLKSCGVS-VLDSPEEVFPAALNY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 214 GGNNFFSTETNSKTMGFKDPKLLVPYLEMrknlVDAGAYpdpgaikeIKDIEGdylvtGE--AAMTWvAANQLQALRTA- 290
Cdd:cd13659   163 LGLDPNSTDPEDIKAAEDLLKKVRPYVRY----FHSSKY--------INDLAN-----GEicVAIGW-SGDAVQAAQRAk 224

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1811729725 291 -AGREIKMM-TLPKTkadvpgGGMMSSQMLSMAKNSKHKEEAAKFISYF 337
Cdd:cd13659   225 eAGNGVTLEyVIPKE------GANLWFDMFAIPADAKNPDNAYRFINYL 267
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 62-186 2.47e-03

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


Pssm-ID: 270299 [Multi-domain]  Cd Length: 490  Bit Score: 40.00  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  62 EMYEKENpkVDIEYEFYDMDGYLTKLNTLAASKTVWDVFqMGGNF-PAFIDS------IEPLDQYIKDGLIDTSNISEGY 134
Cdd:cd13581    25 RLEEKTG--IKIEWETVPEDAWAEKKNLMLASGDLPDAF-LGAGAsDADLMTygkqglFLPLEDLIDKYAPNLKALFDEN 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1811729725 135 L----ATTQQDGKQWGISNGVGAYGIAYDPAMF------KKAGLDEPTpdwTWADFEEMCLK 186
Cdd:cd13581   102 PdikaAITAPDGHIYALPSVNECYHCSYGQRMWinkkwlDKLGLEMPT---TTDELYEVLKA 160
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 64-336 2.95e-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: 39.20  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725  64 YEKENP-KVDIEYeFYDMDGYLTKLNTlaaSKTVWDVFQMGGNFpafidsiepLDQYIKDGL---IDTSNIsEGYLATTQ 139
Cdd:cd13588    19 FEEATGcKVVVKF-FGSEDEMVAKLRS---GGGDYDVVTPSGDA---------LLRLIAAGLvqpIDTSKI-PNYANIDP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 140 Q---------DGKQWGISNGVGAYGIAYDPAMFKKAgldeptPDWTWADFEemclkihDK--TGQFGFSN--FDDFKTAT 206
Cdd:cd13588    85 RlrnlpwltvDGKVYGVPYDWGANGLAYNTKKVKTP------PTSWLALLW-------DPkyKGRVAARDdpIDAIADAA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811729725 207 MAITQTGGGNNffsteTNSKTMGFKDpKLlvpyLEMRKNLvdaGAYPDPGAikEIKDIegdyLVTGE--AAMTW-VAANQ 283
Cdd:cd13588   152 LYLGQDPPFNL-----TDEQLDAVKA-KL----REQRPLV---RKYWSDGA--ELVQL----FANGEvvAATAWsGQVNA 212

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1811729725 284 LQalrtAAGREIKMMtlpktkadVPGGGMMS-SQMLSMAKNSKHKEEAAKFISY 336
Cdd:cd13588   213 LQ----KAGKPVAYV--------IPKEGATGwVDTWMILKDAKNPDCAYKWLNY 254
 
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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