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Conserved domains on  [gi|499271023|ref|WP_010968416|]
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MULTISPECIES: ABC transporter substrate-binding protein [Sinorhizobium]

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 ...
 1-332 7.84e-56

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 188.33  E-value: 7.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023   1 MTRTTMKGLLLASSIL------GSAGLAQAQDATLTIESWRNDDLAIWQEkLIPAFEAKNPGIKVVFAPSAPTEYNAALN 74
Cdd:COG1653    1 MRRLALALAAALALALaacgggGSGAAAAAGKVTLTVWHTGGGEAAALEA-LIKEFEAEHPGIKVEVESVPYDDYRTKLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  75 AKLDAGSAGDLITCRPFDASlELYNKKHLADLTGLSGMENF--SDVAKSAW--TTDDGKaTFCVPMASVIHGFIYNKDAF 150
Cdd:COG1653   80 TALAAGNAPDVVQVDSGWLA-EFAAAGALVPLDDLLDDDGLdkDDFLPGALdaGTYDGK-LYGVPFNTDTLGLYYNKDLF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 151 DQLGLSVPATEEEFFAVLEKIKADGNYIPMAMGTKDLWEAATMGYQNiGPNYWKGEegrlallkGEQKLTDEPWVEPFRV 230
Cdd:COG1653  158 EKAGLDPPKTWDELLAAAKKLKAKDGVYGFALGGKDGAAWLDLLLSA-GGDLYDED--------GKPAFDSPEAVEALEF 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 231 LAKW--KDYLGDGFEAQTYPDSQNLFTLGRAAIYPAGSWEISGFNTQA-EFKMGAFPPPVKKAGDTCYISDHNDiGIGLN 307
Cdd:COG1653  229 LKDLvkDGYVPPGALGTDWDDARAAFASGKAAMMINGSWALGALKDAApDFDVGVAPLPGGPGGKKPASVLGGS-GLAIP 307

                        330       340
                 ....*....|....*....|....*
gi 499271023 308 AKSKNADAAKTFLTWVASPEFAEIY 332
Cdd:COG1653  308 KGSKNPEAAWKFLKFLTSPEAQAKW 332
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-332 7.84e-56

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 188.33  E-value: 7.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023   1 MTRTTMKGLLLASSIL------GSAGLAQAQDATLTIESWRNDDLAIWQEkLIPAFEAKNPGIKVVFAPSAPTEYNAALN 74
Cdd:COG1653    1 MRRLALALAAALALALaacgggGSGAAAAAGKVTLTVWHTGGGEAAALEA-LIKEFEAEHPGIKVEVESVPYDDYRTKLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  75 AKLDAGSAGDLITCRPFDASlELYNKKHLADLTGLSGMENF--SDVAKSAW--TTDDGKaTFCVPMASVIHGFIYNKDAF 150
Cdd:COG1653   80 TALAAGNAPDVVQVDSGWLA-EFAAAGALVPLDDLLDDDGLdkDDFLPGALdaGTYDGK-LYGVPFNTDTLGLYYNKDLF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 151 DQLGLSVPATEEEFFAVLEKIKADGNYIPMAMGTKDLWEAATMGYQNiGPNYWKGEegrlallkGEQKLTDEPWVEPFRV 230
Cdd:COG1653  158 EKAGLDPPKTWDELLAAAKKLKAKDGVYGFALGGKDGAAWLDLLLSA-GGDLYDED--------GKPAFDSPEAVEALEF 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 231 LAKW--KDYLGDGFEAQTYPDSQNLFTLGRAAIYPAGSWEISGFNTQA-EFKMGAFPPPVKKAGDTCYISDHNDiGIGLN 307
Cdd:COG1653  229 LKDLvkDGYVPPGALGTDWDDARAAFASGKAAMMINGSWALGALKDAApDFDVGVAPLPGGPGGKKPASVLGGS-GLAIP 307

                        330       340
                 ....*....|....*....|....*
gi 499271023 308 AKSKNADAAKTFLTWVASPEFAEIY 332
Cdd:COG1653  308 KGSKNPEAAWKFLKFLTSPEAQAKW 332
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 28-409 5.87e-43

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: 154.85  E-value: 5.87e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  28 TLTIESWR-NDDLAIWQEKLIPAFEAKNPGIKVVFAPSAPTEYNAALNAKLDAGSAGDLITCRPFDASLELYNKKHLADL 106
Cdd:cd14749    1 TITYWQYFtGDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPGGWLAEFVKAGLLLPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 107 T------GLSGmeNFSDVAKSAwTTDDGKAtFCVPMASVIHGFIYNKDAFDQLG-LSVPATEEEFFAVLEKIKADGNYI- 178
Cdd:cd14749   81 TdyldpnGVDK--RFLPGLADA-VTFNGKV-YGIPFAARALALFYNKDLFEEAGgVKPPKTWDELIEAAKKDKFKAKGQt 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 179 PMAMGTKDL---WEAATMGYQNiGPNYWKgeegrlALLKGEQKLTDEPWVEPFRVLA--KWKDYLGDGFEAQTYPDSQNL 253
Cdd:cd14749  157 GFGLLLGAQgghWYFQYLVRQA-GGGPLS------DDGSGKATFNDPAFVQALQKLQdlVKAGAFQEGFEGIDYDDAGQA 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 254 FTLGRAAIYPAGSWEISGFNTQ-AEFKMGAFPPPVKKAGDTCYISDHNDIGIGLNAKSKNADAAKTFLTWVASPEFAEIY 332
Cdd:cd14749  230 FAQGKAAMNIGGSWDLGAIKAGePGGKIGVFPFPTVGKGAQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQY 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 333 ANA---LPGFFSLNSTAVKMSDPLAQEFVSWREKCKPTIRSTYqilsrgTPNLENETWV-MSANVINGTDTPEAAAKKLQ 408
Cdd:cd14749  310 LEDvglLPAKEVVAKDEDPDPVAILGPFADVLNAAGSTPFLDE------YWPAAAQVHKdAVQKLLTGKIDPEQVVKQAQ 383


                 .
gi 499271023 409 D 409
Cdd:cd14749  384 S 384
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 38-327 2.25e-25

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: 104.81  E-value: 2.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023   38 DLAIWQEkLIPAFEAKNPGIKVVFAPSAPTEYNAALNAKLDAGSA-GDLITCRPFDASlELYNKKHLADLTGLSGMENFS 116
Cdd:pfam01547   6 EAAALQA-LVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGpADVFASDNDWIA-ELAKAGLLLPLDDYVANYLVL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  117 DVAKsawttddgkaTFCVPMASVIHGFIYNKDAFDQLGLSVPATEEEFFAVLEKIKADGNYIPMAMGTKDLWEAA--TMG 194
Cdd:pfam01547  84 GVPK----------LYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGyfTLA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  195 YQNIGPNYWKGEEGRlALLKGEQKLTDEPWVEPFRVLAKWKDYLGDGFEAQTYPDSQNLFTLGRAAIYPAGSWEISGFNT 274
Cdd:pfam01547 154 LLASLGGPLFDKDGG-GLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAANK 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499271023  275 Q------------AEFKMGAFPPPVKKAGdtcyisDHNDIGIGLNAKSKNADAAKTFLTWVASPE 327
Cdd:pfam01547 233 VklkvafaapapdPKGDVGYAPLPAGKGG------KGGGYGLAIPKGSKNKEAAKKFLDFLTSPE 291
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-332 7.84e-56

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 188.33  E-value: 7.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023   1 MTRTTMKGLLLASSIL------GSAGLAQAQDATLTIESWRNDDLAIWQEkLIPAFEAKNPGIKVVFAPSAPTEYNAALN 74
Cdd:COG1653    1 MRRLALALAAALALALaacgggGSGAAAAAGKVTLTVWHTGGGEAAALEA-LIKEFEAEHPGIKVEVESVPYDDYRTKLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  75 AKLDAGSAGDLITCRPFDASlELYNKKHLADLTGLSGMENF--SDVAKSAW--TTDDGKaTFCVPMASVIHGFIYNKDAF 150
Cdd:COG1653   80 TALAAGNAPDVVQVDSGWLA-EFAAAGALVPLDDLLDDDGLdkDDFLPGALdaGTYDGK-LYGVPFNTDTLGLYYNKDLF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 151 DQLGLSVPATEEEFFAVLEKIKADGNYIPMAMGTKDLWEAATMGYQNiGPNYWKGEegrlallkGEQKLTDEPWVEPFRV 230
Cdd:COG1653  158 EKAGLDPPKTWDELLAAAKKLKAKDGVYGFALGGKDGAAWLDLLLSA-GGDLYDED--------GKPAFDSPEAVEALEF 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 231 LAKW--KDYLGDGFEAQTYPDSQNLFTLGRAAIYPAGSWEISGFNTQA-EFKMGAFPPPVKKAGDTCYISDHNDiGIGLN 307
Cdd:COG1653  229 LKDLvkDGYVPPGALGTDWDDARAAFASGKAAMMINGSWALGALKDAApDFDVGVAPLPGGPGGKKPASVLGGS-GLAIP 307

                        330       340
                 ....*....|....*....|....*
gi 499271023 308 AKSKNADAAKTFLTWVASPEFAEIY 332
Cdd:COG1653  308 KGSKNPEAAWKFLKFLTSPEAQAKW 332
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 28-409 5.87e-43

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: 154.85  E-value: 5.87e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  28 TLTIESWR-NDDLAIWQEKLIPAFEAKNPGIKVVFAPSAPTEYNAALNAKLDAGSAGDLITCRPFDASLELYNKKHLADL 106
Cdd:cd14749    1 TITYWQYFtGDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPGGWLAEFVKAGLLLPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 107 T------GLSGmeNFSDVAKSAwTTDDGKAtFCVPMASVIHGFIYNKDAFDQLG-LSVPATEEEFFAVLEKIKADGNYI- 178
Cdd:cd14749   81 TdyldpnGVDK--RFLPGLADA-VTFNGKV-YGIPFAARALALFYNKDLFEEAGgVKPPKTWDELIEAAKKDKFKAKGQt 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 179 PMAMGTKDL---WEAATMGYQNiGPNYWKgeegrlALLKGEQKLTDEPWVEPFRVLA--KWKDYLGDGFEAQTYPDSQNL 253
Cdd:cd14749  157 GFGLLLGAQgghWYFQYLVRQA-GGGPLS------DDGSGKATFNDPAFVQALQKLQdlVKAGAFQEGFEGIDYDDAGQA 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 254 FTLGRAAIYPAGSWEISGFNTQ-AEFKMGAFPPPVKKAGDTCYISDHNDIGIGLNAKSKNADAAKTFLTWVASPEFAEIY 332
Cdd:cd14749  230 FAQGKAAMNIGGSWDLGAIKAGePGGKIGVFPFPTVGKGAQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQY 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 333 ANA---LPGFFSLNSTAVKMSDPLAQEFVSWREKCKPTIRSTYqilsrgTPNLENETWV-MSANVINGTDTPEAAAKKLQ 408
Cdd:cd14749  310 LEDvglLPAKEVVAKDEDPDPVAILGPFADVLNAAGSTPFLDE------YWPAAAQVHKdAVQKLLTGKIDPEQVVKQAQ 383


                 .
gi 499271023 409 D 409
Cdd:cd14749  384 S 384
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 28-409 1.32e-38

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: 142.93  E-value: 1.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  28 TLTIESWRNDDLAIWQEKLIPAFEAKNPGIKVVFAPSAPTEYNAALNAKLDAGSAGDLITCRPFDASlELYNKKHLADLT 107
Cdd:cd13585    1 TLTFWDWGQPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVP-EFASNGALLDLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 108 GL---SGMENFSDVAKSAWTTDDGKaTFCVPMASVIHGFIYNKDAFDQLG--LSVPATEEEFFAVLEKIK--ADGNY-IP 179
Cdd:cd13585   80 DYiekDGLDDDFPPGLLDAGTYDGK-LYGLPFDADTLVLFYNKDLFDKAGpgPKPPWTWDELLEAAKKLTdkKGGQYgFA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 180 MAMGTKDLWEAATMGYQNiGPNYWKGEEGRLAllkgeqkLTDEPWVEPFRVLAK-WKDYLGDGFEAQTYPDSQNLFTLGR 258
Cdd:cd13585  159 LRGGSGGQTQWYPFLWSN-GGDLLDEDDGKAT-------LNSPEAVEALQFYVDlYKDGVAPSSATTGGDEAVDLFASGK 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 259 AAIYPAGSWEISGFNT-QAEFKMGAFPPPVKKAGDTCYISdhNDIGIGLNAKSKNADAAKTFLTWVASPEFAEIYANALP 337
Cdd:cd13585  231 VAMMIDGPWALGTLKDsKVKFKWGVAPLPAGPGGKRASVL--GGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAG 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499271023 338 GFFSLNSTAVKMSDPLAQEFVSWREKcKPTIRSTYQILSRGTPNLENETWVMSANVING--TDTPEAAAKKLQD 409
Cdd:cd13585  309 PAALAAAAASAAAPDAKPALALAAAA-DALAAAVPPPVPPPWPEVYPILSEALQEALLGalGKSPEEALKEAAK 381
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-413 6.58e-30

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 119.67  E-value: 6.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023   1 MTRTTMKGLLLA------------SSILGSAGLAQAQDATLTIesWRNDDLAIWQEKLIPAFEAKnPGIKVVFAPSAPTE 68
Cdd:COG2182    1 MKRRLLAALALAlalalalaacgsGSSSSGSSSAAGAGGTLTV--WVDDDEAEALEEAAAAFEEE-PGIKVKVVEVPWDD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  69 YNAALNAKLDAGSAGDLITCrPFDASLELYNKKHLADLT-GLSGMENFSDVAKSAWTTDDgkATFCVPMASVIHGFIYNK 147
Cdd:COG2182   78 LREKLTTAAPAGKGPDVFVG-AHDWLGELAEAGLLAPLDdDLADKDDFLPAALDAVTYDG--KLYGVPYAVETLALYYNK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 148 DAFDQlglSVPATEEEFFAVLEKIKADGNYiPMAMGTKDLWEAATMGYQNIGpnYWKGEEGRLAllkGEQKLTDEPWVEp 227
Cdd:COG2182  155 DLVKA---EPPKTWDELIAAAKKLTAAGKY-GLAYDAGDAYYFYPFLAAFGG--YLFGKDGDDP---KDVGLNSPGAVA- 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 228 frVLAKWKDYLGDGF--EAQTYPDSQNLFTLGRAAIYPAGSWEISGFNTQAEFKMGAFPPPVKKAGDT--CYISDHndiG 303
Cdd:COG2182  225 --ALEYLKDLIKDGVlpADADYDAADALFAEGKAAMIINGPWAAADLKKALGIDYGVAPLPTLAGGKPakPFVGVK---G 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 304 IGLNAKSKNADAAKTFLTWVASPEFAEIYA---NALPGFFSLNSTAVKMSDPLAQefvswrekckpTIRSTYQIlSRGTP 380
Cdd:COG2182  300 FGVSAYSKNKEAAQEFAEYLTSPEAQKALFeatGRIPANKAAAEDAEVKADPLIA-----------AFAEQAEY-AVPMP 367

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 499271023 381 NLE--NETWV----MSANVINGTDTPEAAAKKLQDGLDS 413
Cdd:COG2182  368 NIPemGAVWTplgtALQAIASGKADPAEALDAAQKQIEA 406
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 44-409 1.22e-28

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: 115.85  E-value: 1.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  44 EKLIPAFEAKNPGIKV--VFAPSApTEYNAALNAKLDAGSAGDLITCRPFDAsLELYNKKHLADLTGLSGMENFSDVA-- 119
Cdd:cd14748   17 EELVDEFNKSHPDIKVkaVYQGSY-DDTLTKLLAALAAGTAPDVAQVDASWV-AQLADSGALEPLDDYIDKDGVDDDDfy 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 120 KSAW--TTDDGKaTFCVPMASVIHGFIYNKDAFDQLGL---SVPATEEEFFAVLEKIKADG---NYIPMAMGTKDL-WEA 190
Cdd:cd14748   95 PAALdaGTYDGK-LYGLPFDTSTPVLYYNKDLFEEAGLdpeKPPKTWDELEEAAKKLKDKGgktGRYGFALPPGDGgWTF 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 191 ATMGYQNiGPNYWKGEEGRLALlkgeqklTDEPWVEpfrVLAKWKDYLGD-GFEA-QTYPDSQNLFTLGRAAIYPAGSWE 268
Cdd:cd14748  174 QALLWQN-GGDLLDEDGGKVTF-------NSPEGVE---ALEFLVDLVGKdGVSPlNDWGDAQDAFISGKVAMTINGTWS 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 269 ISGF-NTQAEFKMG-AFPPPVKKAGDTCYISDHNdIGIgLNAKSKNADAAKTFLTWVASPEFAEIYANALpGFFSLNSTA 346
Cdd:cd14748  243 LAGIrDKGAGFEYGvAPLPAGKGKKGATPAGGAS-LVI-PKGSSKKKEAAWEFIKFLTSPENQAKWAKAT-GYLPVRKSA 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499271023 347 ------VKMSDPLAQEFVSWREKCKPTIRSTYQilsrgTPNLENETWVMSANVINGTDTPEAAAKKLQD 409
Cdd:cd14748  320 aedpeeFLAENPNYKVAVDQLDYAKPWGPPVPN-----GAEIRDELNEALEAALLGKKTPEEALKEAQE 383
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 38-327 2.25e-25

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: 104.81  E-value: 2.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023   38 DLAIWQEkLIPAFEAKNPGIKVVFAPSAPTEYNAALNAKLDAGSA-GDLITCRPFDASlELYNKKHLADLTGLSGMENFS 116
Cdd:pfam01547   6 EAAALQA-LVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGpADVFASDNDWIA-ELAKAGLLLPLDDYVANYLVL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  117 DVAKsawttddgkaTFCVPMASVIHGFIYNKDAFDQLGLSVPATEEEFFAVLEKIKADGNYIPMAMGTKDLWEAA--TMG 194
Cdd:pfam01547  84 GVPK----------LYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGyfTLA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  195 YQNIGPNYWKGEEGRlALLKGEQKLTDEPWVEPFRVLAKWKDYLGDGFEAQTYPDSQNLFTLGRAAIYPAGSWEISGFNT 274
Cdd:pfam01547 154 LLASLGGPLFDKDGG-GLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAANK 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499271023  275 Q------------AEFKMGAFPPPVKKAGdtcyisDHNDIGIGLNAKSKNADAAKTFLTWVASPE 327
Cdd:pfam01547 233 VklkvafaapapdPKGDVGYAPLPAGKGG------KGGGYGLAIPKGSKNKEAAKKFLDFLTSPE 291
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 45-347 3.36e-24

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 101.33  E-value: 3.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023   45 KLIPAFEAKNpGIKVVFAPSAPTEYNAALNAKLDAGSAGDL-ITCRPFDASLELYNKKHLADLTGLSGMENFSDVAKSAw 123
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDLdVVWIAADQLATLAEAGLLADLSDVDNLDDLPDALDAA- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  124 tTDDGKaTFCVP-MASVIHGFIYNKDAFDQLGlSVPATEEEFFAVLEKIKAdgnyipmamgtKDLWEAATMGYqnigpny 202
Cdd:pfam13416  79 -GYDGK-LYGVPyAASTPTVLYYNKDLLKKAG-EDPKTWDELLAAAAKLKG-----------KTGLTDPATGW------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  203 wkgeeGRLALLKGEQKLTDEPWVEPF--RVLAKWKDYLGDGFEAQTYPDSQNLFTLGRAAIYPAGSWEISGFNtQAEFKM 280
Cdd:pfam13416 138 -----LLWALLADGVDLTDDGKGVEAldEALAYLKKLKDNGKVYNTGADAVQLFANGEVAMTVNGTWAAAAAK-KAGKKL 211

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499271023  281 GAFPPPVKkagdtcYISDHNDIGIglNAKSKNAD-AAKTFLTWVASPEFAEIYANALpGFFSLNSTAV 347
Cdd:pfam13416 212 GAVVPKDG------SFLGGKGLVV--PAGAKDPRlAALDFIKFLTSPENQAALAEDT-GYIPANKSAA 270
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 30-412 1.63e-22

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: 98.22  E-value: 1.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  30 TIESWR--NDDLAIWQEKLIPAFEAKNPGIKVVfAPSAPteYNAALNAKLDAGSAGDL-------ITCRPFDASLELynk 100
Cdd:cd14751    1 TITFWHtsSDEEKVLYEKLIPAFEKEYPKIKVK-AVRVP--FDGLHNQIKTAAAGGQApdvmradIAWVPEFAKLGY--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 101 khLADLTGLSGMENFSDVAKSAWTTD--DGKaTFCVPMASVIHGFIYNKDAFDQLGLSVPATEEEFFAVLEKIKAdgnyi 178
Cdd:cd14751   75 --LQPLDGTPAFDDIVDYLPGPMETNryNGH-YYGVPQVTNTLALFYNKRLLEEAGTEVPKTMDELVAAAKAIKK----- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 179 pmAMGTKDLWEAATMGYqNIGPNYWkGEEGRLA-LLKGEQKLTDEPWVEPFRVLAKWKD-YLGDGFEAQTYPDSQNLFTL 256
Cdd:cd14751  147 --KKGRYGLYISGDGPY-WLLPFLW-SFGGDLTdEKKATGYLNSPESVRALETIVDLYDeGAITPCASGGYPNMQDGFKS 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 257 GRAAIYPAGSWEISGFNTQAEF----KMGAFPPPVKKAGDTCYISDHNdigIGLNAKSKNADAAKTFLTWVASPEFAEIY 332
Cdd:cd14751  223 GRYAMIVNGPWAYADILGGKEFkdpdNLGIAPVPAGPGGSGSPVGGED---LVIFKGSKNKDAAWKFVKFMSSAEAQALT 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 333 A---NALPGFFSLNSTAVKMSDPLAQEFVSWREKCK--PTIRSTYQILSRGTPNLEnetwvmsaNVINGTDTPEAAAKKL 407
Cdd:cd14751  300 AaklGLLPTRTSAYESPEVANNPMVAAFKPALETAVprPPIPEWGELFEPLTLAFA--------KVLRGEKSPREALDEA 371


                 ....*
gi 499271023 408 QDGLD 412
Cdd:cd14751  372 AKQWD 376
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 28-357 6.01e-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: 90.84  E-value: 6.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  28 TLTIESWRNDDLAIWQEKLIPAFEAKNPGIKVVFAPSAPTEYNAALNAKLDAGSAGDLI----TCRPFDASLELynkkhL 103
Cdd:cd14747    1 TLTVWAMGNSAEAELLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVqlgnTWVAEFAAMGA-----L 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 104 ADLTG-LSGMENFSDVAKSAW--TTDDGKaTFCVPMASVIHGFIYNKDAFDQLGLS-VPATEEEFFAVLEKIKADG-NYI 178
Cdd:cd14747   76 EDLTPyLEDLGGDKDLFPGLVdtGTVDGK-YYGVPWYADTRALFYRTDLLKKAGGDeAPKTWDELEAAAKKIKADGpDVS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 179 PMAMGTKDLWeaatmgYQNIGPNYWkGEEGRLAL-LKGEQKLTDEPWVEPfrvLAKWKDYLGDGF-EAQTYPDSQN---L 253
Cdd:cd14747  155 GFAIPGKNDV------WHNALPFVW-GAGGDLATkDKWKATLDSPEAVAG---LEFYTSLYQKGLsPKSTLENSADveqA 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 254 FTLGRAAIYPAGSWEISGF---NTQAEFKMGAFPPPVKKAGDTCYISDHNDIGIglNAKSKNADAAKTFLTWVASPEFAE 330
Cdd:cd14747  225 FANGKVAMIISGPWEIGAIreaGPDLAGKWGVAPLPGGPGGGSPSFAGGSNLAV--FKGSKNKDLAWKFIEFLSSPENQA 302

                        330       340       350
                 ....*....|....*....|....*....|
gi 499271023 331 IYA---NALPGFFSLNSTAVKMSDPLAQEF 357
Cdd:cd14747  303 AYAkatGMLPANTSAWDDPSLANDPLLAVF 332
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 28-409 3.22e-14

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: 73.48  E-value: 3.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  28 TLTIesWRNDDLAI-WQEKLIPAFEAKNpGIKVVFAPSAPTEYNAALNAKLDAGSAGDLITCrPFDASLELYNKKHLADL 106
Cdd:cd13586    1 TITV--WTDEDGELeYLKELAEEFEKKY-GIKVEVVYVDSGDTREKFITAGPAGKGPDVFFG-PHDWLGELAAAGLLAPI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 107 TGLSGMENF-SDVAKSAWTTDdGKAtFCVPMASVIHGFIYNKDAFDQlglsVPATEEEFFAVLEKI-KADGNYIPMAMGT 184
Cdd:cd13586   77 PEYLAVKIKnLPVALAAVTYN-GKL-YGVPVSVETIALFYNKDLVPE----PPKTWEELIALAKKFnDKAGGKYGFAYDQ 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 185 KDLWEAAT---------MGYQNIGPN--YWKGEEGrlallkgeqkltdepwVEPFRVLAKWKDYLGDGFEAQTYPDSQNL 253
Cdd:cd13586  151 TNPYFSYPflaafggyvFGENGGDPTdiGLNNEGA----------------VKGLKFIKDLKKKYKVLPPDLDYDIADAL 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 254 FTLGRAAIYPAGSWEISGFNTqAEFKMGAFPPPVKKAGD--TCYISDhndIGIGLNAKSKNADAAKTFLTWVASPEFAEI 331
Cdd:cd13586  215 FKEGKAAMIINGPWDLADYKD-AGINFGVAPLPTLPGGKqaAPFVGV---QGAFVSAYSKNKEAAVEFAEYLTSDEAQLL 290

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 332 Y---ANALPGFFS-LNSTAVKmSDPLAQEFVswrekckptirstyQILSRGT--PNLE--NETW----VMSANVINGTDT 399
Cdd:cd13586  291 LfekTGRIPALKDaLNDAAVK-NDPLVKAFA--------------EQAQYGVpmPNIPemAAVWdamgNALNLVASGKAT 355

                        410
                 ....*....|
gi 499271023 400 PEAAAKKLQD 409
Cdd:cd13586  356 PEEAAKDAVA 365
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 57-327 2.57e-13

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: 71.20  E-value: 2.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  57 IKVVFAPSAptEYNAALNAKLDAGSAGDLITCRPFDASLELYNKKHLADLTGLsgMENFSDVAKSAW-------TTDDGK 129
Cdd:cd13580   36 VKVKWVPDS--SYDEKLNLALASGDLPDIVVVNDPQLSITLVKQGALWDLTDY--LDKYYPNLKKIIeqegwdsASVDGK 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 130 --ATFCVPMASVIHGFIYNKDAFDQLGLSVPATEEEFFAVLEKIK---ADGNYI---PMAMGTKDLWEAAT---MGYQNI 198
Cdd:cd13580  112 iyGIPRKRPLIGRNGLWIRKDWLDKLGLEVPKTLDELYEVAKAFTekdPDGNGKkdtYGLTDTKDLIGSGFtglFGAFGA 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 199 GPNYWKGEEGRLALLKGEQKLTDEpwvepfrVLAKWKDYLGDG-----FEAQTYPDSQNLFTLGRAAIYPAGSWEISGFN 273
Cdd:cd13580  192 PPNNWWKDEDGKLVPGSIQPEMKE-------ALKFLKKLYKEGlidpeFAVNDGTKANEKFISGKAGIFVGNWWDPAWPQ 264

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 274 TQA-----EFKMGAFPPPVKKAGD-TCYISDHNDIGIGLNAKSKNADAAKTFLTWVASPE 327
Cdd:cd13580  265 ASLkkndpDAEWVAVPIPSGPDGKyGVWAESGVNGFFVIPKKSKKPEAILKLLDFLSDPE 324
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 44-408 3.69e-13

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: 70.48  E-value: 3.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  44 EKLIPAFEAKNPGIKVVFAPSAPTEYNAALNAKLDAGSAGDLITcRPFDASLELYNKKHLADLTGLSG---MENFSDVAK 120
Cdd:cd13657   17 QQIIDEFEAKYPVPNVKVPFEKKPDLQNKLLTAIPAGEGPDLFI-WAHDWIGQFAEAGLLVPISDYLSeddFENYLPTAV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 121 SAWTTDDGkaTFCVPMASVIHGFIYNKDAFDQLglsvPATEEEFFAVLEKI--KADGNYiPMAMGTKDLWEAATMgYQNI 198
Cdd:cd13657   96 EAVTYKGK--VYGLPEAYETVALIYNKALVDQP----PETTDELLAIMKDHtdPAAGSY-GLAYQVSDAYFVSAW-IFGF 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 199 GPNYWKGEEGRLALLKGEQKltdepwvEPFRVLAKW-KDYLgdgFEAQTYPDSQNLFTLGRAAIYPAGSWEISGFNtQAE 277
Cdd:cd13657  168 GGYYFDDETDKPGLDTPETI-------KGIQFLKDFsWPYM---PSDPSYNTQTSLFNEGKAAMIINGPWFIGGIK-AAG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 278 FKMGAFP-PPVKKAGDTCYISDHNDIGIGLNAKSKNADAAKTFLTWVASPEFAEIYANALpGFFSLNSTAvkMSDPLAQE 356
Cdd:cd13657  237 IDLGVAPlPTVDGTNPPRPYSGVEGIYVTKYAERKNKEAALDFAKFFTTAEASKILADEN-GYVPAATNA--YDDAEVAA 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 357 fvswrekcKPTIRSTYQILSRGT--PNLENETWVMS------ANVINGTDTPEAAAKKLQ 408
Cdd:cd13657  314 --------DPVIAAFKAQAEHGVpmPNSPEMASVWGpvtlalAAVYQGGQDPQEALAAAQ 365
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-352 4.41e-13

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 69.94  E-value: 4.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023   1 MTRTTMKGL--LLASSILGSAGLAQAQDATLTIESWRNDdlaiWQEKLIPAFEAKNpGIKVVFAPSaptEYNAALNAKLD 78
Cdd:COG0687    1 MSRRSLLGLaaAALAAALAGGAPAAAAEGTLNVYNWGGY----IDPDVLEPFEKET-GIKVVYDTY---DSNEEMLAKLR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  79 AGSAG-DLITcrPFDASLELYNKKHLA---DLTGLSGMENFSDVAKSAwTTDDGKaTFCVPMASVIHGFIYNKDAFDQlg 154
Cdd:COG0687   73 AGGSGyDVVV--PSDYFVARLIKAGLLqplDKSKLPNLANLDPRFKDP-PFDPGN-VYGVPYTWGTTGIAYNTDKVKE-- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 155 lsVPATEEEFFAvlEKIKA-----DGNYIPMAMGtkdlweAATMGYqniGPNywkgeegrlallkgeqKLTDEPWVEPFR 229
Cdd:COG0687  147 --PPTSWADLWD--PEYKGkvallDDPREVLGAA------LLYLGY---DPN----------------STDPADLDAAFE 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 230 VLAKWKDYLGdGFEAqTYPDSQNLFTLGRAAIYPAGSWEISGFNTQAEfKMGAFPPpvkKAGDTCYISdhndiGIGLNAK 309
Cdd:COG0687  198 LLIELKPNVR-AFWS-DGAEYIQLLASGEVDLAVGWSGDALALRAEGP-PIAYVIP---KEGALLWFD-----NMAIPKG 266

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 499271023 310 SKNADAAKTFLTWVASPEFAEIYANALpGFFSLNSTAVKMSDP 352
Cdd:COG0687  267 APNPDLAYAFINFMLSPEVAAALAEYV-GYAPPNKAARELLPP 308
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 44-409 2.01e-10

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: 61.93  E-value: 2.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  44 EKLIPAFEAKNPGIKV--VFAPSAPTEYNAALNAKLDAGSAG-DLITcrpFDASL--ELYNKKHLADLTGLSGMENFSDV 118
Cdd:cd14750   17 KKAIAAFEKKHPDIKVeiEELPASSDDQRQQLVTALAAGSSApDVLG---LDVIWipEFAEAGWLLPLTEYLKEEEDDDF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 119 AKSAW--TTDDGKaTFCVPMASVIHGFIYNKDAFDQLGLSVPATEEEFFAVLEKIKA-DGNYIPMAMGTKDlWEAATmgy 195
Cdd:cd14750   94 LPATVeaNTYDGK-LYALPWFTDAGLLYYRKDLLEKYGPEPPKTWDELLEAAKKRKAgEPGIWGYVFQGKQ-YEGLV--- 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 196 QNIGPNYW-------KGEEGRLALlkGEQKLTDepwvepfrVLAKWKDYLGDGF---EAQTY--PDSQNLFTLGRAAI-- 261
Cdd:cd14750  169 CNFLELLWsnggdifDDDSGKVTV--DSPEALE--------ALQFLRDLIGEGIspkGVLTYgeEEARAAFQAGKAAFmr 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 262 -YPAGSWEISGFNTQAEFKMGAFPPPVKKAGDTcyisdHNDIG---IGLNAKSKNADAAKTFLTWVASPE----FAEIYA 333
Cdd:cd14750  239 nWPYAYALLQGPESAVAGKVGVAPLPAGPGGGS-----ASTLGgwnLAISANSKHKEAAWEFVKFLTSPEvqkrRAINGG 313

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499271023 334 NALPGFFSLNSTAVKMSDPLAQEFVSWREKCKPTIRSTYQilsrgtPNLENETWVMSANVINGTDTPEAAAKKLQD 409
Cdd:cd14750  314 LPPTRRALYDDPEVLEAYPFLPALLEALENAVPRPVTPKY------PEVSTAIQIALSAALSGQATPEEALKQAQE 383
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 119-331 2.48e-09

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: 59.01  E-value: 2.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 119 AKSAWTTDDGKaTFCVP----MASVIHGFIYNKDAFDQLGLSVPATEEEFFAVLEKIKADGnyiPMAMGTKDLWEAATM- 193
Cdd:cd13521  102 VLRASTASDGK-IYLIPyeppKDVPNQGYFIRKDWLDKLNLKTPKTLDELYNVLKAFKEKD---PNGNGKADEIPFIDRd 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 194 -------------GYQNIGPNY--WKGEEGRLallkgEQKLTDEPWVEPFRVLAKWKD--YLGDGFEAQTYPDSQNLFTL 256
Cdd:cd13521  178 plygafrlinswgARSAGGSTDsdWYEDNGKF-----KHPFASEEYKDGMKYMNKLYTegLIDKESFTQKDDQAEQKFSN 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 257 GRAAIYPAGSWEISGFNTQ--AEFKMGAFP-PPVKKAGDTCYISD------HNDiGIGLNAKSKNADAAKTFLTWVASPE 327
Cdd:cd13521  253 GKLGGFTHNWFASDNLFTAqlGKEKPMYILlPIAPAGNVKGRREEdspgytGPD-GVAISKKAKNPVAALKFFDWLASEE 331


                 ....
gi 499271023 328 FAEI 331
Cdd:cd13521  332 GREL 335
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 56-338 1.84e-08

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: 56.17  E-value: 1.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  56 GIKVVFAPSAPTEYNAALNAKLDAGSAGDLI-TCRPFDASLELYNK------------KHLADLTGLsgMENFSDvAKSA 122
Cdd:cd13581   31 GIKIEWETVPEDAWAEKKNLMLASGDLPDAFlGAGASDADLMTYGKqglflpledlidKYAPNLKAL--FDENPD-IKAA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 123 WTTDDGK------ATFCVPMASVIHGFIyNKDAFDQLGLSVPATEEEFFAVLEKIK---ADGNY----IPMAmGTKDLWE 189
Cdd:cd13581  108 ITAPDGHiyalpsVNECYHCSYGQRMWI-NKKWLDKLGLEMPTTTDELYEVLKAFKeqdPNGNGkadeIPLS-FSGLNGG 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 190 ---------AATMGYQNIGPNYWKGEEGRLALLkgeqkLTDEPWVEPFRVLAK-WKDYLGDGfEAQTYPDSQNLfTLGRA 259
Cdd:cd13581  186 tddpafllnSFGINDGGYGGYGFVVKDGKVIYT-----ATDPEYKEALAYLNKlYKEGLIDP-EAFTQDYDQLA-AKGKA 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 260 AIYPAGS---WEISGFNTQAEFKMGAFPPPVKKAGDTCYISDHNDIGIG-----LNAKSKNADAAKTFLTWVASPEFAEI 331
Cdd:cd13581  259 STAKVGVffgWDPGLFFGEERYEQYVPLPPLKGPNGDQLAWVGNSSGYGrggfvITSKNKNPEAAIRWADFLYSPEGSLQ 338


                 ....*..
gi 499271023 332 YANALPG 338
Cdd:cd13581  339 ANFGPEG 345
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 44-405 2.36e-08

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: 55.57  E-value: 2.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  44 EKLIPAFEAKNpGIKVVFAPSAPTEYNAALNAKLDAGSAGDLITCrPFDASLELYNKKHLADLTGLSGMENFSDVAKSAW 123
Cdd:cd13658   16 KKIAKQYTKKT-GVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVA-PHDRIGSAVLQGLLSPIKLSKDKKKGFTDQALKA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 124 TTDDGKaTFCVPMASVIHGFIYNKDAFDQlglsVPATEEEFFAVLEKI-KADGNYIPMAMGTKDLWeaatMGYQNIGPN- 201
Cdd:cd13658   94 LTYDGK-LYGLPAAVETLALYYNKDLVKN----APKTFDELEALAKDLtKEKGKQYGFLADATNFY----YSYGLLAGNg 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 202 -YWKGEEGRlALLKGEQKLTDEPWVEPFRVLAKW--KDYLGDGFEAQTYpdsQNLFTLGRAAIYPAGSWEISGFNTqAEF 278
Cdd:cd13658  165 gYIFKKNGS-DLDINDIGLNSPGAVKAVKFLKKWytEGYLPKGMTGDVI---QGLFKEGKAAAVIDGPWAIQEYQE-AGV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 279 KMGAFPPPVKKAGDTCyisdHNDIGIG---LNAKSKNADAAKTFLTWVASPEFAEIY---ANALPGFFSLNSTAVKMSDP 352
Cdd:cd13658  240 NYGVAPLPTLPNGKPM----APFLGVKgwyLSAYSKHKEWAQKFMEFLTSKENLKKRydeTNEIPPRKDVRSDPEIKNNP 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499271023 353 LAQEFVSWREKCKPtirstyqilsrgTPNLEN--ETW----VMSANVINGTDTPEAAAK 405
Cdd:cd13658  316 LTSAFAKQASRAVP------------MPNIPEmgAVWepanNALFFILSGKKTPKQALN 362
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 141-330 7.28e-08

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: 54.28  E-value: 7.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 141 HGFIYNKDAFDQLGLSVPATEEEFFAVLEKIK----------------ADGNYIPMAMGTKDLWEAATMGYQNIGPNYWK 204
Cdd:cd13583  128 YSFLYRKDIFEKAGIKIPTTWDEFYAALKKLKekypdsypysdrwnsnALLLIAAPAFGTTAGWGFSNYTYDPDTDKFVY 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 205 G--EEGRLALLKGEQKLTDEPWVEP-----FRVLAKWKDYLGDGFEAQTYP-DSQNLFTLGRAAiypagsweisgfnTQA 276
Cdd:cd13583  208 GatTDEYKDMLQYFNKLYAEGLLDPesftqTDDQAKAKFLNGKSFVITTNPqTVDELQRNLRAA-------------DGG 274

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499271023 277 EFKMGAFPPPVKKAGDTcYISDHNDIGIGLNAK---SKNADAAKTFLTWVASPEFAE 330
Cdd:cd13583  275 NYEVVSITPPAGPAGKA-INGSRLENGFMISSKakdSKNFEALLQFLDWLYSDEGQE 330
PBP2_AlgQ1_2 cd13584
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 ...
 120-338 1.01e-06

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: 50.90  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 120 KSAWTTDDGKATFC--VP---MASVIHGFIYNKDAFDQLGLSVPATEEEFFAVLEKIK-ADGNYIPMAMGTKDLWEAATM 193
Cdd:cd13584  107 KKAITTDDGNIYGFpyLPdgdVAKEARGYFIRKDWLDKLGLKTPSTIDEWYTVLKAFKeRDPNGNGKADEVPLILTKPGY 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 194 GYQNIGPNYWkGEEGRLALLKGEQKLtdePWVEP-FR----VLAKW-KDYLGDG--FEAQTYPDSQNLFTLGRAAIYPAG 265
Cdd:cd13584  187 DETGRLINAW-GAYMDFYQENGKVKY---GPLEPgFKdflkTMNQWyKEGLIDPdfFTRKAKAREQNIMNGNIGGFTHDW 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 266 SWEISGFNTQA-----EFKMGAFPPPVKKAGDTCYISDH----NDIGIGLNAKSKNADAAKTFLTWVASPEFAEIYANAL 336
Cdd:cd13584  263 FASTGTFNLALlknvpDFKLVAVPPPVLNKGQTPYEEDSrqiaKGDGAAITASNKNPVLAIKWLDYAYSEEGRLLSNFGV 342


                 ..
gi 499271023 337 PG 338
Cdd:cd13584  343 EG 344
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 46-408 5.95e-06

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: 48.18  E-value: 5.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023  46 LIPAFEAKNPGIKV--VFAPSAPTE--YNAALnakldAGSAGDLITCRPFDASLELYNKKHLADLTglSGMENFSDVAKS 121
Cdd:cd13522   19 LIAKFEKAYPGITVevTYQDTEARRqfFSTAA-----AGGKGPDVVFGPSDSLGPFAAAGLLAPLD--EYVSKSGKYAPN 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 122 AWTTD--DGKaTFCVPMASVIHGFIYNKDafdQLGLSVPATEEEFFAvLEKIKADGNYIPMAMGtkdlweaATMGYQNIG 199
Cdd:cd13522   92 TIAAMklNGK-LYGVPVSVGAHLMYYNKK---LVPKNPPKTWQELIA-LAQGLKAKNVWGLVYN-------QNEPYFFAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 200 pnyWKGEEGRLALLKGEQK----LTDEPWVEPFRVLAKWKDYLGDGFEAQTYPDSQNLFTLGRAAIYPAGSWEISGFNTQ 275
Cdd:cd13522  160 ---WIGGFGGQVFKANNGKnnptLDTPGAVEALQFLVDLKSKYKIMPPETDYSIADALFKAGKAAMIINGPWDLGDYRQA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271023 276 AEFKMGAFPPPV--KKAGDTCYISDhndIGIGLNAKSKNADAAKTFLTWVASPEFAEIY---ANALPGFFSLNSTAVKMS 350
Cdd:cd13522  237 LKINLGVAPLPTfsGTKHAAPFVGG---KGFGINKESQNKAAAVEFVKYLTSYQAQLVLfddAGDIPANLQAYESPAVQN 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499271023 351 DPLAQEFVSWREKCKPTirstyqilsrgtPNLENETWVMSA------NVINGTDTPEAAAKKLQ 408
Cdd:cd13522  314 KPAQKASAEQAAYGVPM------------PNIPEMRAVWDAfriavnSVLAGKVTPEAAAKDAQ 365
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 303-335 5.94e-03

ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 38.38  E-value: 5.94e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 499271023 303 GIGLNAKSKNADAAKTFLTWVASPEFAEIYANA 335
Cdd:COG1840  208 GAAILKGAPNPEAAKLFIDFLLSDEGQELLAEE 240
 
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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