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Conserved domains on  [gi|516728843|ref|WP_018069624|]
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ABC transporter substrate-binding protein [Rhizobium ruizarguesonis]

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 ...
 36-354 5.92e-51

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 176.00  E-value: 5.92e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  36 TVVKWLHLelDPKYVAAWEDIVKKYEAQHPDVDIQMQFLENEAFKAKLPTLLQSDDVPDFFFSWGGGVlKQQSETGALQD 115
Cdd:COG1653   33 VTLTVWHT--GGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAPDVVQVDSGWL-AEFAAAGALVP 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 116 VTPALDADgGKLRGAYSPASVSGLTFEGKTWAIPYKVGLVSFFYNKALFAKAGVKAEdiKNWTDFLGTVKKIKA-AGIVP 194
Cdd:COG1653  110 LDDLLDDD-GLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPP--KTWDELLAAAKKLKAkDGVYG 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 195 IAGGGGEKWpihfYWSYLVMREGGQkVFEAAKTGQgegFLDPSIIKAGDDLAELGKLEPFQPGYLGSTWPQALGVFGDGK 274
Cdd:COG1653  187 FALGGKDGA----AWLDLLLSAGGD-LYDEDGKPA---FDSPEAVEALEFLKDLVKDGYVPPGALGTDWDDARAAFASGK 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 275 AAIILGFENTEANQRKNAGDgkglapDNIGRFAFPAVDGGaGKPTDTLGGlNGWAVTKKAS--KEAIDFLAFLTSADNER 352
Cdd:COG1653  259 AAMMINGSWALGALKDAAPD------FDVGVAPLPGGPGG-KKPASVLGG-SGLAIPKGSKnpEAAWKFLKFLTSPEAQA 330


                 ..
gi 516728843 353 AM 354
Cdd:COG1653  331 KW 332
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 36-354 5.92e-51

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 176.00  E-value: 5.92e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  36 TVVKWLHLelDPKYVAAWEDIVKKYEAQHPDVDIQMQFLENEAFKAKLPTLLQSDDVPDFFFSWGGGVlKQQSETGALQD 115
Cdd:COG1653   33 VTLTVWHT--GGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAPDVVQVDSGWL-AEFAAAGALVP 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 116 VTPALDADgGKLRGAYSPASVSGLTFEGKTWAIPYKVGLVSFFYNKALFAKAGVKAEdiKNWTDFLGTVKKIKA-AGIVP 194
Cdd:COG1653  110 LDDLLDDD-GLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPP--KTWDELLAAAKKLKAkDGVYG 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 195 IAGGGGEKWpihfYWSYLVMREGGQkVFEAAKTGQgegFLDPSIIKAGDDLAELGKLEPFQPGYLGSTWPQALGVFGDGK 274
Cdd:COG1653  187 FALGGKDGA----AWLDLLLSAGGD-LYDEDGKPA---FDSPEAVEALEFLKDLVKDGYVPPGALGTDWDDARAAFASGK 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 275 AAIILGFENTEANQRKNAGDgkglapDNIGRFAFPAVDGGaGKPTDTLGGlNGWAVTKKAS--KEAIDFLAFLTSADNER 352
Cdd:COG1653  259 AAMMINGSWALGALKDAAPD------FDVGVAPLPGGPGG-KKPASVLGG-SGLAIPKGSKnpEAAWKFLKFLTSPEAQA 330


                 ..
gi 516728843 353 AM 354
Cdd:COG1653  331 KW 332
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 46-431 3.45e-49

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: 171.79  E-value: 3.45e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  46 DPKYVAAWEDIVKKYEAQHPDVDIQMQFLENEAFKAKLPTLLQSDDVPDFFFSWGGGVLKQQSETGALQDVTPALDADGg 125
Cdd:cd14749   10 GDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPGGWLAEFVKAGLLLPLTDYLDPNG- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 126 kLRGAYSPASVSGLTFEGKTWAIPYKVGLVSFFYNKALFAKAGVKaEDIKNWTDFLGTVKKIKAAGIVPIAGGGGEKWPI 205
Cdd:cd14749   89 -VDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGV-KPPKTWDELIEAAKKDKFKAKGQTGFGLLLGAQG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 206 HFYW-SYLVMREGGqkVFEAAKTGQGEGFLDPSIIKAGDDLAELGKLEPFQPGYLGSTWPQALGVFGDGKAAIILG--FE 282
Cdd:cd14749  167 GHWYfQYLVRQAGG--GPLSDDGSGKATFNDPAFVQALQKLQDLVKAGAFQEGFEGIDYDDAGQAFAQGKAAMNIGgsWD 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 283 NTEANQrknagdgkGLAPDNIGRFAFPAVDGGAGKptdTLGGLNGWAVTKKAS----KEAIDFLAFLTSADNERAMAKAG 358
Cdd:cd14749  245 LGAIKA--------GEPGGKIGVFPFPTVGKGAQT---STIGGSDWAIAISANgkkkEAAVKFLKYLTSPEVMKQYLEDV 313

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516728843 359 MLLPVAVGAGDGVTNPLLAESAKQLAA--STWHQNYFDQDLGAAvGRVVNDVSVEIVSGQMNSKDGAQMIQDAFE 431
Cdd:cd14749  314 GLLPAKEVVAKDEDPDPVAILGPFADVlnAAGSTPFLDEYWPAA-AQVHKDAVQKLLTGKIDPEQVVKQAQSAAA 387
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 51-350 4.89e-23

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: 98.64  E-value: 4.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843   51 AAWEDIVKKYEAQHPDVDIQMQFLENEAFKAKLPTLLQSDDVPDFFFSWGGGVLKQQSETGALQDVTPALDADggklrga 130
Cdd:pfam01547   8 AALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANY------- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  131 yspasvsGLTFEGKTWAIPYKVGLVSFFYNKALFAKAGVKAedIKNWTDFLGTVKKIKAAGIVPIAGGGGEKWPIHFYWS 210
Cdd:pfam01547  81 -------LVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDP--PKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGYFT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  211 YLVMREGGQKVFEAAKTGQGEGFLDPSIIKAGDDLAELGKLE-PFQPGYLGSTWPQALGVFGDGKAAIILGFENTEANQR 289
Cdd:pfam01547 152 LALLASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKkLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAAN 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516728843  290 KNAGDG-----KGLAPDNIGRFAFPAVDGGAgkptdtlGGLNGWAVTKKAS--KEAIDFLAFLTSADN 350
Cdd:pfam01547 232 KVKLKVafaapAPDPKGDVGYAPLPAGKGGK-------GGGYGLAIPKGSKnkEAAKKFLDFLTSPEA 292
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
59-191 5.01e-03

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 38.84  E-value: 5.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  59 KYEAQHPDvdiqmqfleneAFKAKLPTLLQSDDVPDFFFsWGGGVLKQQSETGALQDVTPAldadgGKLRGAYSPASVSG 138
Cdd:PRK09474  60 KVTVEHPD-----------KLEEKFPQVAATGDGPDIIF-WAHDRFGGYAQSGLLAEVTPS-----KAFKDKLVPFTWDA 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516728843 139 LTFEGKTWAIPYKVGLVSFFYNKALfakagVKaEDIKNWTDFLGTVKKIKAAG 191
Cdd:PRK09474 123 VRYNGKLIGYPIAVEALSLIYNKDL-----VP-TPPKTWEEIPALDKELKAKG 169
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 36-354 5.92e-51

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 176.00  E-value: 5.92e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  36 TVVKWLHLelDPKYVAAWEDIVKKYEAQHPDVDIQMQFLENEAFKAKLPTLLQSDDVPDFFFSWGGGVlKQQSETGALQD 115
Cdd:COG1653   33 VTLTVWHT--GGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAPDVVQVDSGWL-AEFAAAGALVP 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 116 VTPALDADgGKLRGAYSPASVSGLTFEGKTWAIPYKVGLVSFFYNKALFAKAGVKAEdiKNWTDFLGTVKKIKA-AGIVP 194
Cdd:COG1653  110 LDDLLDDD-GLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPP--KTWDELLAAAKKLKAkDGVYG 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 195 IAGGGGEKWpihfYWSYLVMREGGQkVFEAAKTGQgegFLDPSIIKAGDDLAELGKLEPFQPGYLGSTWPQALGVFGDGK 274
Cdd:COG1653  187 FALGGKDGA----AWLDLLLSAGGD-LYDEDGKPA---FDSPEAVEALEFLKDLVKDGYVPPGALGTDWDDARAAFASGK 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 275 AAIILGFENTEANQRKNAGDgkglapDNIGRFAFPAVDGGaGKPTDTLGGlNGWAVTKKAS--KEAIDFLAFLTSADNER 352
Cdd:COG1653  259 AAMMINGSWALGALKDAAPD------FDVGVAPLPGGPGG-KKPASVLGG-SGLAIPKGSKnpEAAWKFLKFLTSPEAQA 330


                 ..
gi 516728843 353 AM 354
Cdd:COG1653  331 KW 332
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 46-431 3.45e-49

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: 171.79  E-value: 3.45e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  46 DPKYVAAWEDIVKKYEAQHPDVDIQMQFLENEAFKAKLPTLLQSDDVPDFFFSWGGGVLKQQSETGALQDVTPALDADGg 125
Cdd:cd14749   10 GDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPGGWLAEFVKAGLLLPLTDYLDPNG- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 126 kLRGAYSPASVSGLTFEGKTWAIPYKVGLVSFFYNKALFAKAGVKaEDIKNWTDFLGTVKKIKAAGIVPIAGGGGEKWPI 205
Cdd:cd14749   89 -VDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGV-KPPKTWDELIEAAKKDKFKAKGQTGFGLLLGAQG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 206 HFYW-SYLVMREGGqkVFEAAKTGQGEGFLDPSIIKAGDDLAELGKLEPFQPGYLGSTWPQALGVFGDGKAAIILG--FE 282
Cdd:cd14749  167 GHWYfQYLVRQAGG--GPLSDDGSGKATFNDPAFVQALQKLQDLVKAGAFQEGFEGIDYDDAGQAFAQGKAAMNIGgsWD 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 283 NTEANQrknagdgkGLAPDNIGRFAFPAVDGGAGKptdTLGGLNGWAVTKKAS----KEAIDFLAFLTSADNERAMAKAG 358
Cdd:cd14749  245 LGAIKA--------GEPGGKIGVFPFPTVGKGAQT---STIGGSDWAIAISANgkkkEAAVKFLKYLTSPEVMKQYLEDV 313

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516728843 359 MLLPVAVGAGDGVTNPLLAESAKQLAA--STWHQNYFDQDLGAAvGRVVNDVSVEIVSGQMNSKDGAQMIQDAFE 431
Cdd:cd14749  314 GLLPAKEVVAKDEDPDPVAILGPFADVlnAAGSTPFLDEYWPAA-AQVHKDAVQKLLTGKIDPEQVVKQAQSAAA 387
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
46-431 8.40e-33

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 128.14  E-value: 8.40e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  46 DPKYVAAWEDIVKKYEAQhPDVDIQMQFLENEAFKAKLPTLLQSDDVPDFFFsWGGGVLKQQSETGALQDVTPALDAdgg 125
Cdd:COG2182   46 DDDEAEALEEAAAAFEEE-PGIKVKVVEVPWDDLREKLTTAAPAGKGPDVFV-GAHDWLGELAEAGLLAPLDDDLAD--- 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 126 klRGAYSPASVSGLTFEGKTWAIPYKVGLVSFFYNKALfakagVKAEDIKNWTDFLGTVKKIKAAGIVPIAGGGGEkwpi 205
Cdd:COG2182  121 --KDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDL-----VKAEPPKTWDELIAAAKKLTAAGKYGLAYDAGD---- 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 206 hFYWSYLVMREGGQKVFEAAKTGQGE-GFLDPSIIKAGDDLAELGKlEPFQPGylGSTWPQALGVFGDGKAAIILGFENT 284
Cdd:COG2182  190 -AYYFYPFLAAFGGYLFGKDGDDPKDvGLNSPGAVAALEYLKDLIK-DGVLPA--DADYDAADALFAEGKAAMIINGPWA 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 285 EANQRKNAGDGKGLAPdnigrfaFPAVDGgaGKPTDTLGGLNGWAVTKKAS--KEAIDFLAFLTSADNERAMAKAGMLLP 362
Cdd:COG2182  266 AADLKKALGIDYGVAP-------LPTLAG--GKPAKPFVGVKGFGVSAYSKnkEAAQEFAEYLTSPEAQKALFEATGRIP 336

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516728843 363 VAVGAGDGVT---NPLLAESAKQLAAST-------WhqNYFDQDLGAAVGrvvndvsvEIVSGQMNSKDGAQMIQDAFE 431
Cdd:COG2182  337 ANKAAAEDAEvkaDPLIAAFAEQAEYAVpmpnipeM--GAVWTPLGTALQ--------AIASGKADPAEALDAAQKQIE 405
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 46-358 1.39e-32

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: 126.75  E-value: 1.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  46 DPKYVAAWEDIVKKYEAQHPDVDIQMQFLENEAFKAKLPTLLQSDDVPDFFFSWGGGVLkQQSETGALQDVTPALDADGG 125
Cdd:cd13585    9 QPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVP-EFASNGALLDLDDYIEKDGL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 126 KlrGAYSPASVSGLTFEGKTWAIPYKVGLVSFFYNKALFAKAGVKAEDIKNWTDFLGTVKKIK--AAGIVPIAGGGGEKW 203
Cdd:cd13585   88 D--DDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTdkKGGQYGFALRGGSGG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 204 PihFYWSYLVMREGGQKVFEAAKTGqgeGFLDPSIIKAGDDLAELGKlEPFQPGYLGSTWPQALGVFGDGKAAIILGFEN 283
Cdd:cd13585  166 Q--TQWYPFLWSNGGDLLDEDDGKA---TLNSPEAVEALQFYVDLYK-DGVAPSSATTGGDEAVDLFASGKVAMMIDGPW 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516728843 284 TEANQRKNAGDGK-GLAPdnigrfaFPAVDGGAGKptdTLGGLNGWAVTKKaSK---EAIDFLAFLTSADNERAMAKAG 358
Cdd:cd13585  240 ALGTLKDSKVKFKwGVAP-------LPAGPGGKRA---SVLGGWGLAISKN-SKhpeAAWKFIKFLTSKENQLKLGGAA 307
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 51-429 6.89e-32

The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold; This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270451 [Multi-domain]  Cd Length: 385  Bit Score: 125.10  E-value: 6.89e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  51 AAWEDIVKKYEAQHPDVDIQMQFLEN-EAFKAKLPTLLQSDDVPDFFFSWGGGVlKQQSETGALQDVTPALDADGGKLrG 129
Cdd:cd14748   14 KALEELVDEFNKSHPDIKVKAVYQGSyDDTLTKLLAALAAGTAPDVAQVDASWV-AQLADSGALEPLDDYIDKDGVDD-D 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 130 AYSPASVSGLTFEGKTWAIPYKVGLVSFFYNKALFAKAGVKAED-IKNWTDFLGTVKKIKaagivpIAGGGGEKWPI--- 205
Cdd:cd14748   92 DFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKpPKTWDELEEAAKKLK------DKGGKTGRYGFalp 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 206 ----HFYWSYLVMREGGQKVFEAAKTGQgegFLDPSIIKAGDDLAELGKLEPFQPGYlgsTWPQALGVFGDGKAAIILgf 281
Cdd:cd14748  166 pgdgGWTFQALLWQNGGDLLDEDGGKVT---FNSPEGVEALEFLVDLVGKDGVSPLN---DWGDAQDAFISGKVAMTI-- 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 282 eNTEANQRKNAGDGKGLapdNIGRFAFPAVDGGAGKptdTLGGLNGWAVTKKASKE---AIDFLAFLTSADNERAMAKAG 358
Cdd:cd14748  238 -NGTWSLAGIRDKGAGF---EYGVAPLPAGKGKKGA---TPAGGASLVIPKGSSKKkeaAWEFIKFLTSPENQAKWAKAT 310

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516728843 359 MLLPVAVGA-----GDGVTNPLLAESAKQLAASTWHQNYFDQdlGAAVGRVVNDVSVEIVSGQMNSKDGAQMIQDA 429
Cdd:cd14748  311 GYLPVRKSAaedpeEFLAENPNYKVAVDQLDYAKPWGPPVPN--GAEIRDELNEALEAALLGKKTPEEALKEAQEK 384
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 54-386 1.00e-23

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: 102.01  E-value: 1.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  54 EDIVKKYEAQHPDVDIQMQFLENEAFKAKLPTLLQSDDVPD---FFFSWGGGVlkqqSETGALQDVTPALDADGGklRGA 130
Cdd:cd14747   17 KELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDvvqLGNTWVAEF----AAMGALEDLTPYLEDLGG--DKD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 131 YSPASVSGLTFEGKTWAIPYKVGLVSFFYNKALFAKAGVkAEDIKNWTDFLGTVKKIKAAG--IVPIAGGGGEKWPIHFY 208
Cdd:cd14747   91 LFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGG-DEAPKTWDELEAAAKKIKADGpdVSGFAIPGKNDVWHNAL 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 209 ---WSYlvmreGGQKVFEAAKTGQgegFLDPSIIKAgddLAELGKLepFQPGY----LGSTWPQALGVFGDGKAAIILGf 281
Cdd:cd14747  170 pfvWGA-----GGDLATKDKWKAT---LDSPEAVAG---LEFYTSL--YQKGLspksTLENSADVEQAFANGKVAMIIS- 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 282 enTEANQRKNAGDGKGLApDNIGRFAFPAVDGGAGkpTDTLGGLNgWAVTKKASK--EAIDFLAFLTSADNERAMAKAGM 359
Cdd:cd14747  236 --GPWEIGAIREAGPDLA-GKWGVAPLPGGPGGGS--PSFAGGSN-LAVFKGSKNkdLAWKFIEFLSSPENQAAYAKATG 309

                        330       340       350
                 ....*....|....*....|....*....|
gi 516728843 360 LLPVAVGAGDGV---TNPLLAESAKQLAAS 386
Cdd:cd14747  310 MLPANTSAWDDPslaNDPLLAVFAEQLKTG 339
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 51-350 4.89e-23

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: 98.64  E-value: 4.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843   51 AAWEDIVKKYEAQHPDVDIQMQFLENEAFKAKLPTLLQSDDVPDFFFSWGGGVLKQQSETGALQDVTPALDADggklrga 130
Cdd:pfam01547   8 AALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANY------- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  131 yspasvsGLTFEGKTWAIPYKVGLVSFFYNKALFAKAGVKAedIKNWTDFLGTVKKIKAAGIVPIAGGGGEKWPIHFYWS 210
Cdd:pfam01547  81 -------LVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDP--PKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGYFT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  211 YLVMREGGQKVFEAAKTGQGEGFLDPSIIKAGDDLAELGKLE-PFQPGYLGSTWPQALGVFGDGKAAIILGFENTEANQR 289
Cdd:pfam01547 152 LALLASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKkLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAAN 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516728843  290 KNAGDG-----KGLAPDNIGRFAFPAVDGGAgkptdtlGGLNGWAVTKKAS--KEAIDFLAFLTSADN 350
Cdd:pfam01547 232 KVKLKVafaapAPDPKGDVGYAPLPAGKGGK-------GGGYGLAIPKGSKnkEAAKKFLDFLTSPEA 292
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 46-363 2.64e-20

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: 91.97  E-value: 2.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  46 DPKYVAAWEDIVKKYEAQHPDVDIQMQFLENEA--FKAKLPTLLQS-DDVPDFFFS---WgggvLKQQSETGALQDVTPA 119
Cdd:cd14750    9 DGQEGELLKKAIAAFEKKHPDIKVEIEELPASSddQRQQLVTALAAgSSAPDVLGLdviW----IPEFAEAGWLLPLTEY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 120 LDADGgklRGAYSPASVSGLTFEGKTWAIPY--KVGLvsFFYNKALFAKAGVKAEdiKNWTDFLGTVKKIKAA--GIVPI 195
Cdd:cd14750   85 LKEEE---DDDFLPATVEANTYDGKLYALPWftDAGL--LYYRKDLLEKYGPEPP--KTWDELLEAAKKRKAGepGIWGY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 196 AGGGGEKWP-----IHFYWSYlvmreGGQkVFEaaKTGQGEGFLDPSIIKAGDDLAEL--GKLEPfqPGYLGSTWPQALG 268
Cdd:cd14750  158 VFQGKQYEGlvcnfLELLWSN-----GGD-IFD--DDSGKVTVDSPEALEALQFLRDLigEGISP--KGVLTYGEEEARA 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 269 VFGDGKAAIILG--FENTEANQRKNAGDGK-GLAPDnigrfafPAVDGGagKPTDTLGGLNgWAVTKKASK--EAIDFLA 343
Cdd:cd14750  228 AFQAGKAAFMRNwpYAYALLQGPESAVAGKvGVAPL-------PAGPGG--GSASTLGGWN-LAISANSKHkeAAWEFVK 297

                        330       340
                 ....*....|....*....|
gi 516728843 344 FLTSADNERAMAKAGMLLPV 363
Cdd:cd14750  298 FLTSPEVQKRRAINGGLPPT 317
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 54-383 5.80e-20

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: 90.90  E-value: 5.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  54 EDIVKKYEAQHPDVDIQMQFLENEAFKAKLPTLLQSDDVPDFF---FSWgggvLKQQSETGALQDV--TPALDADGGKLR 128
Cdd:cd14751   17 EKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMradIAW----VPEFAKLGYLQPLdgTPAFDDIVDYLP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 129 GAYSPASvsgltFEGKTWAIPYKVGLVSFFYNKALFAKAGVKAEdiKNWTDFLGTVKKIKAAGIVPIAG--GGGEKWPIH 206
Cdd:cd14751   93 GPMETNR-----YNGHYYGVPQVTNTLALFYNKRLLEEAGTEVP--KTMDELVAAAKAIKKKKGRYGLYisGDGPYWLLP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 207 FYWSYlvmreGGQKVFEAAKTGQgegFLDPSIIKAGD---DLAELGKLEPFQPGylgsTWPQALGVFGDGKAAIILGFEN 283
Cdd:cd14751  166 FLWSF-----GGDLTDEKKATGY---LNSPESVRALEtivDLYDEGAITPCASG----GYPNMQDGFKSGRYAMIVNGPW 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 284 TEANQRKNAGDGkglAPDNIGRFAFPAVDGGAGKPtdtLGGLNgWAV--TKKASKEAIDFLAFLTSADNERAMAKAGMLL 361
Cdd:cd14751  234 AYADILGGKEFK---DPDNLGIAPVPAGPGGSGSP---VGGED-LVIfkGSKNKDAAWKFVKFMSSAEAQALTAAKLGLL 306

                        330       340
                 ....*....|....*....|....*
gi 516728843 362 PVAVGAGDG---VTNPLLAESAKQL 383
Cdd:cd14751  307 PTRTSAYESpevANNPMVAAFKPAL 331
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 36-367 3.60e-18

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: 85.51  E-value: 3.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  36 TVVKWlHlELDPKYVAAWEDIVKKYEAQHPDVDIQMQFLENEAFKAKLPTLLQSDDVPDFFFsWGGGVLKQQSETGALQD 115
Cdd:cd13657    1 TITIW-H-ALTGAEEDALQQIIDEFEAKYPVPNVKVPFEKKPDLQNKLLTAIPAGEGPDLFI-WAHDWIGQFAEAGLLVP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 116 VTPALDADGGKlrgAYSPASVSGLTFEGKTWAIPYKVGLVSFFYNKALFAKAGVKAEDIKNWTDFLgtvkKIKAAGIVPI 195
Cdd:cd13657   78 ISDYLSEDDFE---NYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQPPETTDELLAIMKDH----TDPAAGSYGL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 196 AGGGGEkwPIHFYWSYlvmreggqkvfeaakTGQGEGFLDPSIIKAGDDLAELGK----LEPFQPGYLGSTWPQAL--GV 269
Cdd:cd13657  151 AYQVSD--AYFVSAWI---------------FGFGGYYFDDETDKPGLDTPETIKgiqfLKDFSWPYMPSDPSYNTqtSL 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 270 FGDGKAA-IILGfeNTEANQRKNAGDGKGLAPdnigrfaFPAVDGgaGKPTDTLGGLNGWAVTK----KASKEAIDFLAF 344
Cdd:cd13657  214 FNEGKAAmIING--PWFIGGIKAAGIDLGVAP-------LPTVDG--TNPPRPYSGVEGIYVTKyaerKNKEAALDFAKF 282

                        330       340
                 ....*....|....*....|...
gi 516728843 345 LTSADNERAMAKAGMLLPVAVGA 367
Cdd:cd13657  283 FTTAEASKILADENGYVPAATNA 305
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 36-387 1.07e-17

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: 84.27  E-value: 1.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  36 TVVKWLHLEldpKYVAAWEDIVKKYEAQHpDVDIQMQFLENEAFKAKLPTLLQSDDVPDFFFS---WGGgvlkQQSETGA 112
Cdd:cd13586    1 TITVWTDED---GELEYLKELAEEFEKKY-GIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGphdWLG----ELAAAGL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 113 LQDVTPALDADGGklrgaYSPASVSGLTFEGKTWAIPYKVGLVSFFYNKALFakagvkAEDIKNWTDFLGTVKKikaagi 192
Cdd:cd13586   73 LAPIPEYLAVKIK-----NLPVALAAVTYNGKLYGVPVSVETIALFYNKDLV------PEPPKTWEELIALAKK------ 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 193 vpIAGGGGEKWPI-----HFYWSYLVMREGGQKVFeaAKTGQGE---GFLDPSIIKAGDDLAELGKLEPFQPGylGSTWP 264
Cdd:cd13586  136 --FNDKAGGKYGFaydqtNPYFSYPFLAAFGGYVF--GENGGDPtdiGLNNEGAVKGLKFIKDLKKKYKVLPP--DLDYD 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 265 QALGVFGDGKAAIIL-GFENTEAnqRKNAGDGKGLAPdnigrfaFPAVDGgaGKPTDTLGGLNGWAVTKKAS--KEAIDF 341
Cdd:cd13586  210 IADALFKEGKAAMIInGPWDLAD--YKDAGINFGVAP-------LPTLPG--GKQAAPFVGVQGAFVSAYSKnkEAAVEF 278

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 516728843 342 LAFLTSADNERAMAKAGMLLPV---AVGAGDGVTNPLLAESAKQLAAST 387
Cdd:cd13586  279 AEYLTSDEAQLLLFEKTGRIPAlkdALNDAAVKNDPLVKAFAEQAQYGV 327
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 55-369 3.63e-17

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 81.30  E-value: 3.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843   55 DIVKKYEAQHpDVDIQMQFLENEAFKAKLPTLLQSDDVPDFF-FSWGGGVLKQQSETGALQDVTPALDADggklrgaYSP 133
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDLDvVWIAADQLATLAEAGLLADLSDVDNLD-------DLP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  134 ASVSGLTFEGKTWAIPYKVG-LVSFFYNKALFAKAGvkaEDIKNWTDFLGTVKKIKAAGIVPIAGGGgekwpihfyWSYL 212
Cdd:pfam13416  73 DALDAAGYDGKLYGVPYAAStPTVLYYNKDLLKKAG---EDPKTWDELLAAAAKLKGKTGLTDPATG---------WLLW 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  213 VMREGGQKVFEAAKTGQGEgfldpsiIKAGDDLAELGKlepfqPGYLGSTWPQALGVFGDGKAAIILGFENTEANQRKNA 292
Cdd:pfam13416 141 ALLADGVDLTDDGKGVEAL-------DEALAYLKKLKD-----NGKVYNTGADAVQLFANGEVAMTVNGTWAAAAAKKAG 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  293 gdgkglapDNIGrFAFPavdggagKPTDTLGGlNGWAVTKKASKE---AIDFLAFLTSADNERAMAKAGMLLPVAVGAGD 369
Cdd:pfam13416 209 --------KKLG-AVVP-------KDGSFLGG-KGLVVPAGAKDPrlaALDFIKFLTSPENQAALAEDTGYIPANKSAAL 271
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 52-384 4.81e-13

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: 70.13  E-value: 4.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  52 AWEDIVKKYEAQHPDVDIQMQFLENEAFKAKLPTLLQSDDVPDFFFS---WGGgvlkQQSETGALQDVTPALDADGgklr 128
Cdd:cd13522   15 AVNELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGpsdSLG----PFAAAGLLAPLDEYVSKSG---- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 129 gAYSPASVSGLTFEGKTWAIPYKVGLVSFFYNKALFAKagvkaEDIKNWTDFLGTVKKIKAAGIVPIAGGGGEKwpihFY 208
Cdd:cd13522   87 -KYAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVPK-----NPPKTWQELIALAQGLKAKNVWGLVYNQNEP----YF 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 209 WSYLVMREGGQkVFEAaktgqGEGFLDPSIIKAG--DDLAELGKLEpFQPGYLGST--WPQALGVFGDGKAAIILGFENT 284
Cdd:cd13522  157 FAAWIGGFGGQ-VFKA-----NNGKNNPTLDTPGavEALQFLVDLK-SKYKIMPPEtdYSIADALFKAGKAAMIINGPWD 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 285 EANQRKNAGDGKGLAPdnigrfaFPAVDGGAgKPTDTLGGLnGWAVTKKASKEAID--FLAFLTSADNERAMAKAGMLLP 362
Cdd:cd13522  230 LGDYRQALKINLGVAP-------LPTFSGTK-HAAPFVGGK-GFGINKESQNKAAAveFVKYLTSYQAQLVLFDDAGDIP 300

                        330       340
                 ....*....|....*....|....*
gi 516728843 363 VAVGAGDG---VTNPLLAESAKQLA 384
Cdd:cd13522  301 ANLQAYESpavQNKPAQKASAEQAA 325
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 46-428 9.67e-13

The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold; This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270376 [Multi-domain]  Cd Length: 372  Bit Score: 69.05  E-value: 9.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  46 DPKYVAAW-EDIVKKYEAQHpdvDIQMQFLENEAFKA--KLPTLLQSDDVPDFFFsWGGGVLKQQSETGALQDVTPalda 122
Cdd:cd13658    7 DEDKKMAFiKKIAKQYTKKT---GVKVKLVEVDQLDQleKLSLDGPAGKGPDVMV-APHDRIGSAVLQGLLSPIKL---- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 123 DGGKLRGaYSPASVSGLTFEGKTWAIPYKVGLVSFFYNKALFAKAGVKAEDIKNWTDFLGTVKKiKAAGIVPIAGgggek 202
Cdd:cd13658   79 SKDKKKG-FTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKDLTKEKG-KQYGFLADAT----- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 203 wpiHFYWSYLVMREGGQKVFeaaktGQGEGFLDPSIIKAGDDLAELGkLEPFQPGYLGSTWPQAL------GVFGDGK-A 275
Cdd:cd13658  152 ---NFYYSYGLLAGNGGYIF-----KKNGSDLDINDIGLNSPGAVKA-VKFLKKWYTEGYLPKGMtgdviqGLFKEGKaA 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 276 AIILGFENteANQRKNAGDGKGLAPdnigrfaFPAVDGgaGKPTDTLGGLNGWAVTK--KASKEAIDFLAFLTSADNERA 353
Cdd:cd13658  223 AVIDGPWA--IQEYQEAGVNYGVAP-------LPTLPN--GKPMAPFLGVKGWYLSAysKHKEWAQKFMEFLTSKENLKK 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 354 MAKAGMLLPVAVGA---GDGVTNPLLAESAKQLAASTWHQNYFDQdlgAAVGRVVNDVSVEIVSGQMNSK----DGAQMI 426
Cdd:cd13658  292 RYDETNEIPPRKDVrsdPEIKNNPLTSAFAKQASRAVPMPNIPEM---GAVWEPANNALFFILSGKKTPKqalnDAVNDI 368


                 ..
gi 516728843 427 QD 428
Cdd:cd13658  369 KE 370
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 67-151 1.62e-07

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


Pssm-ID: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 53.49  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  67 VDIQMQFLENEAFKAKLPTLLQSDDVPDFFFSWGGGVLKQQSETGALQDVTPALDADGGKLRGAYSPASVSGLTFEGKTW 146
Cdd:cd13580   34 IDVKVKWVPDSSYDEKLNLALASGDLPDIVVVNDPQLSITLVKQGALWDLTDYLDKYYPNLKKIIEQEGWDSASVDGKIY 113


                 ....*
gi 516728843 147 AIPYK 151
Cdd:cd13580  114 GIPRK 118
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 55-351 2.48e-05

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


Pssm-ID: 270373 [Multi-domain]  Cd Length: 363  Bit Score: 46.18  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  55 DIVKKYEAQHPDVDIQMQFLENEAFKAKlpTLLQSD-----DVpdffFSWGGGVLKQQSETGALQDVTPALDAdggKLRG 129
Cdd:cd13655   16 EMVDAFKEKHPEWKITITIGVVGEADAK--DEVLKDpsaaaDV----FAFANDQLGELVDAGAIYPLTGSAVD---KIKN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 130 AYSPASVSGLTFEGKTWAIPYKVGLVSFFYNKALFakagvKAEDIKNWTDFLGTVKKIKAAGIVPIAGGggekwpihfYW 209
Cdd:cd13655   87 TNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKL-----TEDDVKSLDTMLAKAPDAKGKVSFDLSNS---------WY 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 210 SYLVMREGGQKVFEAAKTG-QGEGFLDPSIIKAGDDLAELGKlepfQPGYLGSTWPQALGVFGDGKA-AIILGFENTeAN 287
Cdd:cd13655  153 LYAFFFGAGCKLFGNNGGDtAGCDFNNEKGVAVTNYLVDLVA----NPKFVNDADGDAISGLKDGTLgAGVSGPWDA-AN 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516728843 288 QRKNAGDGKGLAPdnigrfaFPAVD-GGAGKPTDTLGGLNGWAV--TKKASKEAIDFLAFLTSADNE 351
Cdd:cd13655  228 LKKALGDNYAVAK-------LPTYTlGGKDVQMKSFAGYKAIGVnsNTKNPEAAMALADYLTNEESQ 287
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 54-337 1.01e-04

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


Pssm-ID: 270374 [Multi-domain]  Cd Length: 364  Bit Score: 44.12  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  54 EDIVKKYEAqhpDVDIQMQFLENEAFKAKLPTLLQSDDVPDFFFsWGGGVLKQQSETGALQDVTPaldadGGKLRGAYSP 133
Cdd:cd13656   17 AEVGKKFEK---DTGIKVTVEHPDKLEEKFPQVAATGDGPDIIF-WAHDRFGGYAQSGLLAEITP-----DKAFQDKLYP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 134 ASVSGLTFEGKTWAIPYKVGLVSFFYNKALFAKAGvkaediKNWTDFLGTVKKIKAAGIVPIAGGGGEKwpihfYWSYLV 213
Cdd:cd13656   88 FTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPP------KTWEEIPALDKELKAKGKSALMFNLQEP-----YFTWPL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 214 MREGGQKVFeaaKTGQGEGFL-DPSIIKAGDDLAELGKLEPFQPGYL--GSTWPQALGVFGDGKAAIILGFENTEANQRK 290
Cdd:cd13656  157 IAADGGYAF---KYENGKYDIkDVGVDNAGAKAGLTFLVDLIKNKHMnaDTDYSIAEAAFNKGETAMTINGPWAWSNIDT 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 516728843 291 NAGDgKGLAPdnigrfaFPAVDGGAGKP-TDTLG-GLNGWAVTKKASKE 337
Cdd:cd13656  234 SKVN-YGVTV-------LPTFKGQPSKPfVGVLSaGINAASPNKELAKE 274
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
49-408 1.62e-03

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 40.28  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  49 YVAAW-----EDIVKKYEAQHpDVDIQMQFLE-NEAFKAKLptlLQSDDVPDFFFSWGGGVLKQQSEtGALQdvtpALDA 122
Cdd:COG0687   32 NVYNWggyidPDVLEPFEKET-GIKVVYDTYDsNEEMLAKL---RAGGSGYDVVVPSDYFVARLIKA-GLLQ----PLDK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 123 DggKLRGA--YSPASVSGLTFEGKTWAIPYKVGLVSFFYNKALFakagvkAEDIKNWTDFLgtvkKIKAAGIVpiagggg 200
Cdd:COG0687  103 S--KLPNLanLDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKV------KEPPTSWADLW----DPEYKGKV------- 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 201 ekwpihfywsylVMREGGQKVFEAA--KTGQGEGFLDPSIIKAGddLAELGKLEPFQPGYlGSTWPQALGVFGDGKAAII 278
Cdd:COG0687  164 ------------ALLDDPREVLGAAllYLGYDPNSTDPADLDAA--FELLIELKPNVRAF-WSDGAEYIQLLASGEVDLA 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843 279 LGFeNTEANQRKNAGdgkglapDNIgRFAFPAvDGgagkptdTLGGLNGWAVTKKASK--EAIDFLAFLTSADNERAMAK 356
Cdd:COG0687  229 VGW-SGDALALRAEG-------PPI-AYVIPK-EG-------ALLWFDNMAIPKGAPNpdLAYAFINFMLSPEVAAALAE 291

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516728843 357 AGMLLPVAVGAGDGVT-----NPLLAESAKQLAASTWhQNYFDQDLGAAVGRVVNDV 408
Cdd:COG0687  292 YVGYAPPNKAARELLPpelaaNPAIYPPEEVLDKLEF-WNPLPPENRELYTRRWTEI 347
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
59-191 5.01e-03

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 38.84  E-value: 5.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516728843  59 KYEAQHPDvdiqmqfleneAFKAKLPTLLQSDDVPDFFFsWGGGVLKQQSETGALQDVTPAldadgGKLRGAYSPASVSG 138
Cdd:PRK09474  60 KVTVEHPD-----------KLEEKFPQVAATGDGPDIIF-WAHDRFGGYAQSGLLAEVTPS-----KAFKDKLVPFTWDA 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516728843 139 LTFEGKTWAIPYKVGLVSFFYNKALfakagVKaEDIKNWTDFLGTVKKIKAAG 191
Cdd:PRK09474 123 VRYNGKLIGYPIAVEALSLIYNKDL-----VP-TPPKTWEEIPALDKELKAKG 169
 
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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