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Conserved domains on  [gi|1765992889|gb|KAB6762557|]
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sugar ABC transporter substrate-binding protein [Bifidobacterium longum]

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 ...
 1-310 1.35e-54

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 186.02  E-value: 1.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889   1 MTAILSVSLASCG-----QATDDNRTEISVWSWEPS----MGEVIRRFEKANPDIRVKWTNISG---YGNLNTAIQDGyG 68
Cdd:COG1653     8 LAAALALALAACGgggsgAAAAAGKVTLTVWHTGGGeaaaLEALIKEFEAEHPGIKVEVESVPYddyRTKLLTALAAG-N 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  69 TPDVAQIEYYALLQYAVSGQLLDLTDKI---GSDYSNFFTlGTWSSVQLAGRTYGLPMDSGPMGFFYNEDVFRQAGVDAT 145
Cdd:COG1653    87 APDVVQVDSGWLAEFAAAGALVPLDDLLdddGLDKDDFLP-GALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 146 kiKTWDDYYEAAEKLKEI-GAY-IAADSGDGSFYDAMVWLAGGQPFhtSADGKtvtIDLDEDAGTQRFtEFWQKMIDEGL 223
Cdd:COG1653   166 --KTWDELLAAAKKLKAKdGVYgFALGGKDGAAWLDLLLSAGGDLY--DEDGK---PAFDSPEAVEAL-EFLKDLVKDGY 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 224 VDTTSATWS-DRWKSRVGTGTIASVFSGAWMPSLLLSNVPGAAglWRVAPMPTY-GGQPANAENGGSALTVLQLTRKPDA 301
Cdd:COG1653   238 VPPGALGTDwDDARAAFASGKAAMMINGSWALGALKDAAPDFD--VGVAPLPGGpGGKKPASVLGGSGLAIPKGSKNPEA 315


                  ....*....
gi 1765992889 302 AYRFVDFVA 310
Cdd:COG1653   316 AWKFLKFLT 324
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-310 1.35e-54

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 186.02  E-value: 1.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889   1 MTAILSVSLASCG-----QATDDNRTEISVWSWEPS----MGEVIRRFEKANPDIRVKWTNISG---YGNLNTAIQDGyG 68
Cdd:COG1653     8 LAAALALALAACGgggsgAAAAAGKVTLTVWHTGGGeaaaLEALIKEFEAEHPGIKVEVESVPYddyRTKLLTALAAG-N 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  69 TPDVAQIEYYALLQYAVSGQLLDLTDKI---GSDYSNFFTlGTWSSVQLAGRTYGLPMDSGPMGFFYNEDVFRQAGVDAT 145
Cdd:COG1653    87 APDVVQVDSGWLAEFAAAGALVPLDDLLdddGLDKDDFLP-GALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 146 kiKTWDDYYEAAEKLKEI-GAY-IAADSGDGSFYDAMVWLAGGQPFhtSADGKtvtIDLDEDAGTQRFtEFWQKMIDEGL 223
Cdd:COG1653   166 --KTWDELLAAAKKLKAKdGVYgFALGGKDGAAWLDLLLSAGGDLY--DEDGK---PAFDSPEAVEAL-EFLKDLVKDGY 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 224 VDTTSATWS-DRWKSRVGTGTIASVFSGAWMPSLLLSNVPGAAglWRVAPMPTY-GGQPANAENGGSALTVLQLTRKPDA 301
Cdd:COG1653   238 VPPGALGTDwDDARAAFASGKAAMMINGSWALGALKDAAPDFD--VGVAPLPGGpGGKKPASVLGGSGLAIPKGSKNPEA 315


                  ....*....
gi 1765992889 302 AYRFVDFVA 310
Cdd:COG1653   316 AWKFLKFLT 324
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 22-336 2.13e-53

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: 183.38  E-value: 2.13e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  22 EISVWSW-----EPSMGEVIRRFEKANPDIRVKWTNIsGYGN----LNTAIQDGyGTPDVAQIEYYALLQYAVSGQLLDL 92
Cdd:cd13585     1 TLTFWDWgqpaeTAALKKLIDAFEKENPGVKVEVVPV-PYDDywtkLTTAAAAG-TAPDVFYVDGPWVPEFASNGALLDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  93 TDKIGSD-YSNFFTLGTWSSVQLAGRTYGLPMDSGPMGFFYNEDVFRQAGVDATKIKTWDDYYEAAEKLK--EIGAY--- 166
Cdd:cd13585    79 DDYIEKDgLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTdkKGGQYgfa 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 167 IAADSGDGSFYDAMVWLAGGQPFhtSADGKTVTIDldeDAGTQRFTEFWQKMIDEGLVDTTSATWSDRWKSRVGTGTIAS 246
Cdd:cd13585   159 LRGGSGGQTQWYPFLWSNGGDLL--DEDDGKATLN---SPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFASGKVAM 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 247 VFSGAWMPSLLlsNVPGAAGLWRVAPMPTYGGQPANAENGGSALTVLQLTRKPDAAYRFVDFVAHDAQGISARVDGGAFP 326
Cdd:cd13585   234 MIDGPWALGTL--KDSKVKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAA 311

                         330
                  ....*....|
gi 1765992889 327 ADYATLNSAD 336
Cdd:cd13585   312 LAAAAASAAA 321
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 34-310 1.31e-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: 105.96  E-value: 1.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  34 EVIRRFEKANPDIRVKWTNI---SGYGNLNTAIQDGYGTPDVAQIEYYALLQYAVSGQLLDLTDKIGSDYsnfftlgtws 110
Cdd:pfam01547  12 ALVKEFEKEHPGIKVEVESVgsgSLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYL---------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 111 sVQLAGRTYGLPMDSGPMGFFYNEDVFRQAGVDAtkIKTWDDYYEAAEKLKE-----IGAYIAADSGDGS-FYDAMVWLA 184
Cdd:pfam01547  82 -VLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDP--PKTWDELLEAAKKLKEkgkspGGAGGGDASGTLGyFTLALLASL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 185 GGQPFHtsADGKTVTIDLDEDAGTQRFTEFWQKMIDEGL--VDTTSATWSDRWKSrVGTGTIASVFSGAWMPSLLLS--- 259
Cdd:pfam01547 159 GGPLFD--KDGGGLDNPEAVDAITYYVDLYAKVLLLKKLknPGVAGADGREALAL-FEQGKAAMGIVGPWAALAANKvkl 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1765992889 260 ------NVPGAAGLWRVAPMPTyggqPANAENGGSALTVLQLTRKPDAAYRFVDFVA 310
Cdd:pfam01547 236 kvafaaPAPDPKGDVGYAPLPA----GKGGKGGGYGLAIPKGSKNKEAAKKFLDFLT 288
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
1-310 1.05e-03

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 41.32  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889   1 MTAILSVSLASCGQATddnrTEISVW-SWEPSMGE----VIRRFEKANPDIRVkwtnISGY-GNLNTAIQDGYGT----- 69
Cdd:PRK10974   10 LGLALGLALSGNAQAV----TEIPFWhSMEGELGKevdsLAQRFNASQPDYKI----VPVYkGNYEQSLAAGIAAfrsgn 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  70 -PDVAQIEYYALLQYAVSGQLLDLTD-----KIGSDYSNFF-TLGTWSSVQLAGRTYGLPMDSGPMGFFYNEDVFRQAGV 142
Cdd:PRK10974   82 aPAILQVYEVGTATMMASKAIKPVYDvfkdaGIPFDESQFVpTVAGYYSDAKTGHLLSQPFNSSTPVLYYNKDAFKKAGL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 143 DATKI-KTWDDYYEAAEKLKEIGAYIAADSGDGSF-----YDAmvWlaGGQPFHTSA---DGKTVTIDLDEDAGTqRFTE 213
Cdd:PRK10974  162 DPEQPpKTWQDLAAYAAKLRAAGMKCGYASGWQGWiqlenFSA--W--HGLPFASKNngfDGTDAVLEFNKPEQV-KHIA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 214 FWQKMIDEGlvDTTSATWSDRWKSRVGTG--TIASVFSGAwmpsllLSNVPGAAGL-WRVAPMP---TYGGQPANAENGG 287
Cdd:PRK10974  237 LLEEMNKKG--DFTYVGRKDESTEKFYNGdcAITTASSGS------LANIRKYAKFnYGVGMMPydaDVKGAPQNAIIGG 308

                         330       340
                  ....*....|....*....|....*..
gi 1765992889 288 SALTVLQltRKPDAAYR----FVDFVA 310
Cdd:PRK10974  309 ASLWVMQ--GKDKETYKgvakFLDFLA 333
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-310 1.35e-54

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 186.02  E-value: 1.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889   1 MTAILSVSLASCG-----QATDDNRTEISVWSWEPS----MGEVIRRFEKANPDIRVKWTNISG---YGNLNTAIQDGyG 68
Cdd:COG1653     8 LAAALALALAACGgggsgAAAAAGKVTLTVWHTGGGeaaaLEALIKEFEAEHPGIKVEVESVPYddyRTKLLTALAAG-N 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  69 TPDVAQIEYYALLQYAVSGQLLDLTDKI---GSDYSNFFTlGTWSSVQLAGRTYGLPMDSGPMGFFYNEDVFRQAGVDAT 145
Cdd:COG1653    87 APDVVQVDSGWLAEFAAAGALVPLDDLLdddGLDKDDFLP-GALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 146 kiKTWDDYYEAAEKLKEI-GAY-IAADSGDGSFYDAMVWLAGGQPFhtSADGKtvtIDLDEDAGTQRFtEFWQKMIDEGL 223
Cdd:COG1653   166 --KTWDELLAAAKKLKAKdGVYgFALGGKDGAAWLDLLLSAGGDLY--DEDGK---PAFDSPEAVEAL-EFLKDLVKDGY 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 224 VDTTSATWS-DRWKSRVGTGTIASVFSGAWMPSLLLSNVPGAAglWRVAPMPTY-GGQPANAENGGSALTVLQLTRKPDA 301
Cdd:COG1653   238 VPPGALGTDwDDARAAFASGKAAMMINGSWALGALKDAAPDFD--VGVAPLPGGpGGKKPASVLGGSGLAIPKGSKNPEA 315


                  ....*....
gi 1765992889 302 AYRFVDFVA 310
Cdd:COG1653   316 AWKFLKFLT 324
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 22-336 2.13e-53

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: 183.38  E-value: 2.13e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  22 EISVWSW-----EPSMGEVIRRFEKANPDIRVKWTNIsGYGN----LNTAIQDGyGTPDVAQIEYYALLQYAVSGQLLDL 92
Cdd:cd13585     1 TLTFWDWgqpaeTAALKKLIDAFEKENPGVKVEVVPV-PYDDywtkLTTAAAAG-TAPDVFYVDGPWVPEFASNGALLDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  93 TDKIGSD-YSNFFTLGTWSSVQLAGRTYGLPMDSGPMGFFYNEDVFRQAGVDATKIKTWDDYYEAAEKLK--EIGAY--- 166
Cdd:cd13585    79 DDYIEKDgLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTdkKGGQYgfa 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 167 IAADSGDGSFYDAMVWLAGGQPFhtSADGKTVTIDldeDAGTQRFTEFWQKMIDEGLVDTTSATWSDRWKSRVGTGTIAS 246
Cdd:cd13585   159 LRGGSGGQTQWYPFLWSNGGDLL--DEDDGKATLN---SPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFASGKVAM 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 247 VFSGAWMPSLLlsNVPGAAGLWRVAPMPTYGGQPANAENGGSALTVLQLTRKPDAAYRFVDFVAHDAQGISARVDGGAFP 326
Cdd:cd13585   234 MIDGPWALGTL--KDSKVKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAA 311

                         330
                  ....*....|
gi 1765992889 327 ADYATLNSAD 336
Cdd:cd13585   312 LAAAAASAAA 321
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 22-327 2.13e-42

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: 154.37  E-value: 2.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  22 EISVWS-----WEPSMGEVIRRFEKANPDIRVKWTNISGYGN----LNTAIQDGyGTPDVAQIEYYALLQYAVSGQLLDL 92
Cdd:cd14748     1 EITFWHgmsgpDGKALEELVDEFNKSHPDIKVKAVYQGSYDDtltkLLAALAAG-TAPDVAQVDASWVAQLADSGALEPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  93 TDKIGSDYSNFFTL--GTWSSVQLAGRTYGLPMDSGPMGFFYNEDVFRQAGVDATK-IKTWDDYYEAAEKLKEIGA---- 165
Cdd:cd14748    80 DDYIDKDGVDDDDFypAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKpPKTWDELEEAAKKLKDKGGktgr 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 166 --YIAADSGDGSFYDAMVWLAGGQPFhtSADGKTVTIDLDEdagTQRFTEFWQKMI-DEGLVDTTSATWSDrwkSRVGTG 242
Cdd:cd14748   160 ygFALPPGDGGWTFQALLWQNGGDLL--DEDGGKVTFNSPE---GVEALEFLVDLVgKDGVSPLNDWGDAQ---DAFISG 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 243 TIASVFSGAWMPSLLLSNVPGAAglWRVAPMPTYGGQPANAENGGSALTVL-QLTRKPDAAYRFVDFVAHDAQGISARVD 321
Cdd:cd14748   232 KVAMTINGTWSLAGIRDKGAGFE--YGVAPLPAGKGKKGATPAGGASLVIPkGSSKKKEAAWEFIKFLTSPENQAKWAKA 309


                  ....*.
gi 1765992889 322 GGAFPA 327
Cdd:cd14748   310 TGYLPV 315
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 22-339 3.84e-41

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: 150.93  E-value: 3.84e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  22 EISVW-----SWEPSMGEVIRRFEKANPDIRVKWTNI---SGYGNLNTAIQDGyGTPDVAQIEYYALLQYAVSGQLLDLT 93
Cdd:cd14747     1 TLTVWamgnsAEAELLKELADEFEKENPGIEVKVQVLpwgDAHTKITTAAASG-DGPDVVQLGNTWVAEFAAMGALEDLT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  94 DKIGSDYSNF-FTLGTWSSVQLAGRTYGLPMDSGPMGFFYNEDVFRQAGVDATKiKTWDDYYEAAEKLKE-----IGAYI 167
Cdd:cd14747    80 PYLEDLGGDKdLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGDEAP-KTWDELEAAAKKIKAdgpdvSGFAI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 168 AADSGDGSFYDAMVWLAGGQPFhtSADGKTVTIDldeDAGTQRFTEFWQKMIDEGLVDTTSATWSDRWKSRVGTGTIASV 247
Cdd:cd14747   159 PGKNDVWHNALPFVWGAGGDLA--TKDKWKATLD---SPEAVAGLEFYTSLYQKGLSPKSTLENSADVEQAFANGKVAMI 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 248 FSGAWMPSLLLSNVPGAAGLWRVAPMP--TYGGQPANAenGGSALTVLQLTRKPDAAYRFVDFVAHDAQGISARVDGGAF 325
Cdd:cd14747   234 ISGPWEIGAIREAGPDLAGKWGVAPLPggPGGGSPSFA--GGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGML 311

                         330
                  ....*....|....
gi 1765992889 326 PADYATLNSADFLD 339
Cdd:cd14747   312 PANTSAWDDPSLAN 325
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-310 3.39e-38

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 143.55  E-value: 3.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889   1 MTAILSVSLASCGQATDDNRT--------EISVWSWE---PSMGEVIRRFEKAnPDIRVKWTNISG---YGNLNTAIQDG 66
Cdd:COG2182    11 LALALALALAACGSGSSSSGSssaagaggTLTVWVDDdeaEALEEAAAAFEEE-PGIKVKVVEVPWddlREKLTTAAPAG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  67 YGtPDVAQIEYYALLQYAVSGQLLDLTDKIgSDYSNFFTlGTWSSVQLAGRTYGLPMDSGPMGFFYNEDVfrqagVDATK 146
Cdd:COG2182    90 KG-PDVFVGAHDWLGELAEAGLLAPLDDDL-ADKDDFLP-AALDAVTYDGKLYGVPYAVETLALYYNKDL-----VKAEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 147 IKTWDDYYEAAEKLKEIGAY-IAADSGDGSFYDAMVWLAGGQPF-HTSADGKTVTIDldeDAGTQRFTEFWQKMIDEGLV 224
Cdd:COG2182   162 PKTWDELIAAAKKLTAAGKYgLAYDAGDAYYFYPFLAAFGGYLFgKDGDDPKDVGLN---SPGAVAALEYLKDLIKDGVL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 225 DtTSATWSDrWKSRVGTGTIASVFSGAWMpsllLSNVPGAAGL-WRVAPMPTY-GGQPANAENGGSALTVLQLTRKPDAA 302
Cdd:COG2182   239 P-ADADYDA-ADALFAEGKAAMIINGPWA----AADLKKALGIdYGVAPLPTLaGGKPAKPFVGVKGFGVSAYSKNKEAA 312


                  ....*...
gi 1765992889 303 YRFVDFVA 310
Cdd:COG2182   313 QEFAEYLT 320
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 22-327 5.13e-35

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: 134.04  E-value: 5.13e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  22 EISVWSW------EPSMGEVIRRFEKANPDIRVKWTNI--SGYGN-LNTAIQDGYGtPDVAQIEYYALLQ-YAVSGQLLD 91
Cdd:cd14749     1 TITYWQYftgdtkKKYMDELIADFEKENPNIKVKVVVFpyDNYKTkLKTAVAAGEG-PDVFNLWPGGWLAeFVKAGLLLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  92 LTDKIGSD-YSNFFTLGTWSSVQLAGRTYGLPMDSGPMGFFYNEDVFRQAGVDaTKIKTWDDYYEAAEKLKeIGAYIAA- 169
Cdd:cd14749    80 LTDYLDPNgVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGV-KPPKTWDELIEAAKKDK-FKAKGQTg 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 170 ------DSGDGSFYDAMVWLAGGQPFHTSADGKtVTIdlDEDAGTQRFtEFWQKMIDEGLV--DTTSATWSDRWKSrVGT 241
Cdd:cd14749   158 fglllgAQGGHWYFQYLVRQAGGGPLSDDGSGK-ATF--NDPAFVQAL-QKLQDLVKAGAFqeGFEGIDYDDAGQA-FAQ 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 242 GTIASVFSGAW-MPSLLLSNVPGAaglWRVAPMPTYGGQPANAENGGS--ALTVLQLTRKPDAAYRFVDFVAHDAQGISA 318
Cdd:cd14749   233 GKAAMNIGGSWdLGAIKAGEPGGK---IGVFPFPTVGKGAQTSTIGGSdwAIAISANGKKKEAAVKFLKYLTSPEVMKQY 309


                  ....*....
gi 1765992889 319 RVDGGAFPA 327
Cdd:cd14749   310 LEDVGLLPA 318
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 23-327 8.71e-29

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: 116.63  E-value: 8.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  23 ISVWSWEPSMGEVIRRFEKANPDIRVKWTNISGYGN-----LNTAIQDGYGTPDVAQIEYYALLQYAVSGQLLDLTDKIG 97
Cdd:cd14750     7 GSDGQEGELLKKAIAAFEKKHPDIKVEIEELPASSDdqrqqLVTALAAGSSAPDVLGLDVIWIPEFAEAGWLLPLTEYLK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  98 SDYSNFFTLGTWSSVQLAGRTYGLP--MDSGpmGFFYNEDVFRQAGVDATKikTWDDYYEAAEKLKE----IGAYIA-AD 170
Cdd:cd14750    87 EEEDDDFLPATVEANTYDGKLYALPwfTDAG--LLYYRKDLLEKYGPEPPK--TWDELLEAAKKRKAgepgIWGYVFqGK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 171 SGDGSFYDAM--VWLAGGQPFhtSADGKTVTIDldEDAGTQRFtEFWQKMIDEGLVDTTSATWSDRwKSRVGTGTIASVF 248
Cdd:cd14750   163 QYEGLVCNFLelLWSNGGDIF--DDDSGKVTVD--SPEALEAL-QFLRDLIGEGISPKGVLTYGEE-EARAAFQAGKAAF 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 249 SGAW--MPSLLLSNVPGAAGLWRVAPMPTYGGQPANAENGGSALTVLQLTRKPDAAYRFVDFVAHDAQGISARVDGGAFP 326
Cdd:cd14750   237 MRNWpyAYALLQGPESAVAGKVGVAPLPAGPGGGSASTLGGWNLAISANSKHKEAAWEFVKFLTSPEVQKRRAINGGLPP 316


                  .
gi 1765992889 327 A 327
Cdd:cd14750   317 T 317
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 29-308 1.68e-27

The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold; This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270454 [Multi-domain]  Cd Length: 376  Bit Score: 112.86  E-value: 1.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  29 EPSMGEVIRRFEKANPDIRVKWTNISGYGNLN---TAIQDGYGtPDVAQIEYYALLQYAVSGQLLDLTDKIGSDYSNFFT 105
Cdd:cd14751    13 KVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHNqikTAAAGGQA-PDVMRADIAWVPEFAKLGYLQPLDGTPAFDDIVDYL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 106 LGTWSSVQLAGRTYGLPMDSGPMGFFYNEDVFRQAGVDATkiKTWDDYYEAAEKLKEI-GAYIAADSGDGSFYDA-MVWL 183
Cdd:cd14751    92 PGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEVP--KTMDELVAAAKAIKKKkGRYGLYISGDGPYWLLpFLWS 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 184 AGGQpfHTSADGKTVTIDldeDAGTQRFTEFWQKMIDEGLVDTTSATWSDRWKSRVGTGTIASVFSGAWMPSLLLSNV-- 261
Cdd:cd14751   170 FGGD--LTDEKKATGYLN---SPESVRALETIVDLYDEGAITPCASGGYPNMQDGFKSGRYAMIVNGPWAYADILGGKef 244

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1765992889 262 --PGAAGlwrVAPMPT-YGGQPanAENGGSALTVLQLTRKPDAAYRFVDF 308
Cdd:cd14751   245 kdPDNLG---IAPVPAgPGGSG--SPVGGEDLVIFKGSKNKDAAWKFVKF 289
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 34-310 1.31e-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: 105.96  E-value: 1.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  34 EVIRRFEKANPDIRVKWTNI---SGYGNLNTAIQDGYGTPDVAQIEYYALLQYAVSGQLLDLTDKIGSDYsnfftlgtws 110
Cdd:pfam01547  12 ALVKEFEKEHPGIKVEVESVgsgSLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDDYVANYL---------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 111 sVQLAGRTYGLPMDSGPMGFFYNEDVFRQAGVDAtkIKTWDDYYEAAEKLKE-----IGAYIAADSGDGS-FYDAMVWLA 184
Cdd:pfam01547  82 -VLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDP--PKTWDELLEAAKKLKEkgkspGGAGGGDASGTLGyFTLALLASL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 185 GGQPFHtsADGKTVTIDLDEDAGTQRFTEFWQKMIDEGL--VDTTSATWSDRWKSrVGTGTIASVFSGAWMPSLLLS--- 259
Cdd:pfam01547 159 GGPLFD--KDGGGLDNPEAVDAITYYVDLYAKVLLLKKLknPGVAGADGREALAL-FEQGKAAMGIVGPWAALAANKvkl 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1765992889 260 ------NVPGAAGLWRVAPMPTyggqPANAENGGSALTVLQLTRKPDAAYRFVDFVA 310
Cdd:pfam01547 236 kvafaaPAPDPKGDVGYAPLPA----GKGGKGGGYGLAIPKGSKNKEAAKKFLDFLT 288
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 34-252 1.28e-19

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 88.62  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  34 EVIRRFEKANpDIRVKWTNIS--GYGN-LNTAIQDG-YGTPDVAQIEYYALLQYAVSGQLLDLTDKIGSDYSNfftlGTW 109
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQAsnDLQAkLLAAAAAGnAPDLDVVWIAADQLATLAEAGLLADLSDVDNLDDLP----DAL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 110 SSVQLAGRTYGLPMD-SGPMGFFYNEDVFRQAGVDatkIKTWDDYYEAAEKLKeiGAYIAADSGDGSFYDAMVwlaggqp 188
Cdd:pfam13416  76 DAAGYDGKLYGVPYAaSTPTVLYYNKDLLKKAGED---PKTWDELLAAAAKLK--GKTGLTDPATGWLLWALL------- 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1765992889 189 fhtsADGKTVTIDLDEDAGTQRFTEFWQKMIDEGlvdTTSATWSDrWKSRVGTGTIASVFSGAW 252
Cdd:pfam13416 144 ----ADGVDLTDDGKGVEALDEALAYLKKLKDNG---KVYNTGAD-AVQLFANGEVAMTVNGTW 199
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 22-346 6.55e-16

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: 78.88  E-value: 6.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  22 EISVWSWEPS----MGEVIRRFEKANpDIRVKWTNI---SGYGNLNTAIQDGYGtPDVAQIEYYALLQYAVSGQLLDLTD 94
Cdd:cd13586     1 TITVWTDEDGeleyLKELAEEFEKKY-GIKVEVVYVdsgDTREKFITAGPAGKG-PDVFFGPHDWLGELAAAGLLAPIPE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  95 KIGSDYsnFFTLGTWSSVQLAGRTYGLPMDSGPMGFFYNEDVFRQAGvdatkiKTWDDYYEAAEKLKEIGA---YIAADS 171
Cdd:cd13586    79 YLAVKI--KNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPEPP------KTWEELIALAKKFNDKAGgkyGFAYDQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 172 GDgsFYDAMVWLA--GGQPFHTSADGKTvTIDLDEDAGTQRFtEFWQKMIDEGLVDTTSATWsDRWKSRVGTGTIASVFS 249
Cdd:cd13586   151 TN--PYFSYPFLAafGGYVFGENGGDPT-DIGLNNEGAVKGL-KFIKDLKKKYKVLPPDLDY-DIADALFKEGKAAMIIN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 250 GAWmpslllsNVPG--AAGL-WRVAPMPTY-GGQPANAENGGSALTVLQLTRKPDAAYRFVDFVAHDAQGISARVDGGAF 325
Cdd:cd13586   226 GPW-------DLADykDAGInFGVAPLPTLpGGKQAAPFVGVQGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRI 298

                         330       340
                  ....*....|....*....|.
gi 1765992889 326 PAdyatLNSAdfLDKTTITND 346
Cdd:cd13586   299 PA----LKDA--LNDAAVKND 313
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 40-310 2.30e-15

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: 78.14  E-value: 2.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  40 EKANPDIRVKWTNISGYGN-LNTAIQDGyGTPDVAQI-EYYALLQYAVSGQLLDLTDKI---GSDYSNFFTLGTWSSVQL 114
Cdd:cd13580    30 EKTNIDVKVKWVPDSSYDEkLNLALASG-DLPDIVVVnDPQLSITLVKQGALWDLTDYLdkyYPNLKKIIEQEGWDSASV 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 115 AGRTYGLP---MDSGPMGFFYNEDVFRQAGVDATKikTWDDYYEAAEKLKE-----------IGAYIAADSGDGSFYDAM 180
Cdd:cd13580   109 DGKIYGIPrkrPLIGRNGLWIRKDWLDKLGLEVPK--TLDELYEVAKAFTEkdpdgngkkdtYGLTDTKDLIGSGFTGLF 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 181 VWL-AGGQPFHTSADGKTV-TIDLDEdagTQRFTEFWQKMIDEGLVD-----TTSATWSDRWKSrvgtGTIASVFSGAWM 253
Cdd:cd13580   187 GAFgAPPNNWWKDEDGKLVpGSIQPE---MKEALKFLKKLYKEGLIDpefavNDGTKANEKFIS----GKAGIFVGNWWD 259

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1765992889 254 P----SLLLSNVPGAAGLWRVAPMPTYGGQPANAENGGSALTVLQLT-RKPDAAYRFVDFVA 310
Cdd:cd13580   260 PawpqASLKKNDPDAEWVAVPIPSGPDGKYGVWAESGVNGFFVIPKKsKKPEAILKLLDFLS 321
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 23-335 1.93e-14

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: 74.37  E-value: 1.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  23 ISVWSWEPSMG-----EVIRRFEKANPDIRVKWTNISGYG---NLNTAIQDGYGtPDVAQIEYYALLQYAVSGQLLDLTD 94
Cdd:cd13522     2 ITVWHQYDTGEnqavnELIAKFEKAYPGITVEVTYQDTEArrqFFSTAAAGGKG-PDVVFGPSDSLGPFAAAGLLAPLDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  95 KIGSDYSNFFTlgTWSSVQLAGRTYGLPMDSGPMGFFYNEDVfrqagVDATKIKTWDDYYEAAEKLKEIGAY-IAADSGD 173
Cdd:cd13522    81 YVSKSGKYAPN--TIAAMKLNGKLYGVPVSVGAHLMYYNKKL-----VPKNPPKTWQELIALAQGLKAKNVWgLVYNQNE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 174 GSFYDAMVWLAGGQPFhtSADGKTVTIDLDEDAGTQRFTeFWQKMIDEGLVdTTSATWSDRWKSRVGTGTIASVFSGAWM 253
Cdd:cd13522   154 PYFFAAWIGGFGGQVF--KANNGKNNPTLDTPGAVEALQ-FLVDLKSKYKI-MPPETDYSIADALFKAGKAAMIINGPWD 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 254 PSLLLSNVPGAAGlwrVAPMPTY-GGQPANAENGGSALTVLQLTRKPDAAYRFVDFVAHDAQGISARVDGGAFPADYATL 332
Cdd:cd13522   230 LGDYRQALKINLG---VAPLPTFsGTKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDIPANLQAY 306


                  ...
gi 1765992889 333 NSA 335
Cdd:cd13522   307 ESP 309
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 59-313 1.69e-12

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: 69.02  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  59 LNTAIQDGyGTPDVAQIEYYA--LLQYAVSGQLLDLTDKIgSDYSNF------FTLGTWSSVQLAGRTYGLPmdSGPMGF 130
Cdd:cd13521    48 LNLMLASG-DLPDIVGADYLKdkFIAYGMEGAFLPLSKYI-DQYPNLkaffkqHPDVLRASTASDGKIYLIP--YEPPKD 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 131 FYNEDVF-RQAGVDATK---IKTWDDYYEAAEKLKE-----------IGAYIAADSGDG----SFYDAMvWLAGGQPFHT 191
Cdd:cd13521   124 VPNQGYFiRKDWLDKLNlktPKTLDELYNVLKAFKEkdpngngkadeIPFIDRDPLYGAfrliNSWGAR-SAGGSTDSDW 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 192 SADGKTVTIDLDEDAGTQRFtEFWQKMIDEGLVDTTSATWSDRW-KSRVGTGTIAsVFSGAWMPSLLLSNvPGAAGLWR- 269
Cdd:cd13521   203 YEDNGKFKHPFASEEYKDGM-KYMNKLYTEGLIDKESFTQKDDQaEQKFSNGKLG-GFTHNWFASDNLFT-AQLGKEKPm 279

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1765992889 270 -----VAPMPTYGGQPANAENGGSALTVLQLTRK---PDAAYRFVDFVAHDA 313
Cdd:cd13521   280 yillpIAPAGNVKGRREEDSPGYTGPDGVAISKKaknPVAALKFFDWLASEE 331
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 22-336 1.38e-11

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: 65.86  E-value: 1.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  22 EISVW-SWEPS----MGEVIRRFEKANP--DIRVKWTNISGYGN-LNTAIQDGYGtPDVAQIEYYALLQYAVSGQLLDLT 93
Cdd:cd13657     1 TITIWhALTGAeedaLQQIIDEFEAKYPvpNVKVPFEKKPDLQNkLLTAIPAGEG-PDLFIWAHDWIGQFAEAGLLVPIS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  94 DKIGSDYSNFFTLGTWSSVQLAGRTYGLPMDSGPMGFFYNEDVFRQAGvdatkiKTWDDYYEAAEKL--KEIGAY-IAAD 170
Cdd:cd13657    80 DYLSEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQPP------ETTDELLAIMKDHtdPAAGSYgLAYQ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 171 SGDGSFYDAMVWLAGGQPFhtSADGKTVTIDLDE--DAGTQRFTEFWQKMIDEGLVDTTSATWSDrwksrvgtGTIASVF 248
Cdd:cd13657   154 VSDAYFVSAWIFGFGGYYF--DDETDKPGLDTPEtiKGIQFLKDFSWPYMPSDPSYNTQTSLFNE--------GKAAMII 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 249 SGAWmpslLLSNVPGAAGLWRVAPMPTYGGQPANAENGGSALTVLQLT---RKPDAAYRFVDFVAHDAQGISARVDGGAF 325
Cdd:cd13657   224 NGPW----FIGGIKAAGIDLGVAPLPTVDGTNPPRPYSGVEGIYVTKYaerKNKEAALDFAKFFTTAEASKILADENGYV 299

                         330
                  ....*....|.
gi 1765992889 326 PADYATLNSAD 336
Cdd:cd13657   300 PAATNAYDDAE 310
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 41-308 6.72e-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: 54.67  E-value: 6.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  41 KANPDIRVKWTNI--SGYGN-LNTAIQDGyGTPDVAQIEYYALL-QYAVSGQLLDLTDKIG--SDYSNFFTLGTW----- 109
Cdd:cd13583    27 EEKTNVKFKRTPIpsSDYETkRSLLIASG-DAPDIIPVLYPGEEnEFVASGALLPISDYLDymPNYKKYVEKWGLgkela 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 110 SSVQLAGRTY---GLPMDSGP-MGFFYNEDVFRQAGVDATKikTWDDYYEAAEKLKEIGA---YIAADSGDGSFYDAMVW 182
Cdd:cd13583   106 TGRQSDGKYYslpGLHEDPGVqYSFLYRKDIFEKAGIKIPT--TWDEFYAALKKLKEKYPdsyPYSDRWNSNALLLIAAP 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 183 LAGGQPFhtsADGKTVTIDLDED----AGTQ----RFTEFWQKMIDEGLVDTTSATWS-DRWKSRVGTGTIASVFSGAWM 253
Cdd:cd13583   184 AFGTTAG---WGFSNYTYDPDTDkfvyGATTdeykDMLQYFNKLYAEGLLDPESFTQTdDQAKAKFLNGKSFVITTNPQT 260

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1765992889 254 PSLLLSNVPGAAGL-WRVAPMPTYGGQPANAENG-----GSALTV-LQLTRKPDAAYRFVDF 308
Cdd:cd13583   261 VDELQRNLRAADGGnYEVVSITPPAGPAGKAINGsrlenGFMISSkAKDSKNFEALLQFLDW 322
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-152 5.68e-07

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 51.45  E-value: 5.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889   1 MTAILSVSLASCGQATDDNRTeISVWSWEPSMGE-VIRRFEKANpDIRVkwtNISGYGNLNTA---IQDGYGTPDVAQIE 76
Cdd:COG0687    10 AAAALAAALAGGAPAAAAEGT-LNVYNWGGYIDPdVLEPFEKET-GIKV---VYDTYDSNEEMlakLRAGGSGYDVVVPS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  77 YYALLQYAVSGQLLDL-TDKIgSDYSN---FFTLGTWSsvqlAGRTYGLPMDSGPMGFFYNEDVFRQAgvdatkIKTWDD 152
Cdd:COG0687    85 DYFVARLIKAGLLQPLdKSKL-PNLANldpRFKDPPFD----PGNVYGVPYTWGTTGIAYNTDKVKEP------PTSWAD 153
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 34-337 1.28e-06

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


Pssm-ID: 270376 [Multi-domain]  Cd Length: 372  Bit Score: 50.17  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  34 EVIRRFEKANpDIRVKWTNISGYGNLNTAIQDGYG--TPDVAQIEYYALLQYAVSGQLLDLtdKIGSDYSNFFTLGTWSS 111
Cdd:cd13658    17 KIAKQYTKKT-GVKVKLVEVDQLDQLEKLSLDGPAgkGPDVMVAPHDRIGSAVLQGLLSPI--KLSKDKKKGFTDQALKA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 112 VQLAGRTYGLPMDSGPMGFFYNEDVFRQAgvdatkIKTWDDYYEAAEKL---KEIGAYIAADSGDgsFYDAMVWLA--GG 186
Cdd:cd13658    94 LTYDGKLYGLPAAVETLALYYNKDLVKNA------PKTFDELEALAKDLtkeKGKQYGFLADATN--FYYSYGLLAgnGG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 187 QPF-HTSADGKTVTIDLDEDaGTQRFTEFWQKMIDEGLVdtTSATWSDRWKSRVGTGTIASVFSGAWMpslllSNVPGAA 265
Cdd:cd13658   166 YIFkKNGSDLDINDIGLNSP-GAVKAVKFLKKWYTEGYL--PKGMTGDVIQGLFKEGKAAAVIDGPWA-----IQEYQEA 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1765992889 266 GL-WRVAPMPTY-GGQPANAENGGSALTVLQLTRKPDAAYRFVDFVAHDAQGISARVDGGAFPADYATLNSADF 337
Cdd:cd13658   238 GVnYGVAPLPTLpNGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTSKENLKKRYDETNEIPPRKDVRSDPEI 311
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 32-281 1.13e-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: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  32 MGEVIRRFEKaNPDIRVKWTNISGY-GNLNTAIQDGYGtPDVAQIEYYALLQYAVSGQLLDLT-DKIGSD-YSNFftlgT 108
Cdd:cd13656    16 LAEVGKKFEK-DTGIKVTVEHPDKLeEKFPQVAATGDG-PDIIFWAHDRFGGYAQSGLLAEITpDKAFQDkLYPF----T 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 109 WSSVQLAGRTYGLPMDSGPMGFFYNEDVFRqagvdaTKIKTWDDYYEAAEKLKEIG-AYIAADSGDGSFYDAMVWLAGGQ 187
Cdd:cd13656    90 WDAVRYNGKLIAYPIAVEALSLIYNKDLLP------NPPKTWEEIPALDKELKAKGkSALMFNLQEPYFTWPLIAADGGY 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 188 PFHTSADG---KTVTIDldeDAGTQRFTEFWQKMIDEGLVDTTSATwsDRWKSRVGTGTIASVFSGAWMpsllLSNVPGA 264
Cdd:cd13656   164 AFKYENGKydiKDVGVD---NAGAKAGLTFLVDLIKNKHMNADTDY--SIAEAAFNKGETAMTINGPWA----WSNIDTS 234

                         250
                  ....*....|....*..
gi 1765992889 265 AGLWRVAPMPTYGGQPA 281
Cdd:cd13656   235 KVNYGVTVLPTFKGQPS 251
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 35-194 3.48e-04

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


Pssm-ID: 270306 [Multi-domain]  Cd Length: 279  Bit Score: 42.28  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  35 VIRRFEKANPdIRVKWTNISGYGNLNTAIQDGYGTPDVAQIEYYALLQYAVSG--QLLDlTDKIgSDYSNF---FTLGTW 109
Cdd:cd13588    15 WVTAFEEATG-CKVVVKFFGSEDEMVAKLRSGGGDYDVVTPSGDALLRLIAAGlvQPID-TSKI-PNYANIdprLRNLPW 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 110 SSVQlaGRTYGLPMDSGPMGFFYNEDVFRQAgvDATKIKT-WDDYYEAaeklkEIGAYiaaDSGDGSFYDAMVWLAGGQP 188
Cdd:cd13588    92 LTVD--GKVYGVPYDWGANGLAYNTKKVKTP--PTSWLALlWDPKYKG-----RVAAR---DDPIDAIADAALYLGQDPP 159


                  ....*.
gi 1765992889 189 FHTSAD 194
Cdd:cd13588   160 FNLTDE 165
PBP2_AlgQ_like_3 cd13582
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 102-345 4.98e-04

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


Pssm-ID: 270300 [Multi-domain]  Cd Length: 504  Bit Score: 42.31  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 102 NFFTLGTWssvqlagRTYGLPMDSGPmGFFYNEDVFRQAGVDatKIKTWDDYYEAAEKLKE----------IGAYIAADS 171
Cdd:cd13582   107 HIYYLPNY-------RVEDAPWYPNG-GFWLQHDVLKELGYP--KIKTLDDYENLIKDYKKkyptingqptIGFTALTDD 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 172 -------GDGSFY----DAMVWLaggqpfhtsADGKTVTIDL-DEDAGTQRFTEFWQKMIDEGLVDTTSATWS-DRWKSR 238
Cdd:cd13582   177 wrflisvTNPAFLagypNDGEVY---------VDPKTLKAKFhYTRPYYKEYYKWLNELWNEGLLDKESFTQKyDQYLAK 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 239 VGTGTIASVFSGAWM---PSLLLSNVPGAAGLWRVAP-------------MPTYGGqpanaeNGGSALTVlqLTRKPDAA 302
Cdd:cd13582   248 IASGRVLGFYDAGWDignAITALKAKGKDERLYAYYPvavgvddkdynygDPGYLG------GDGIAITK--SCKDPERA 319

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1765992889 303 YRFVDFVA-HDAQ-----GISAR----VDGGAF---PADYATLNSADFLDKTTITN 345
Cdd:cd13582   320 FKFLDWLAsEEAQklinwGIEGVdydvDDGKRVyltEEMAAKNKDPDYTKKTGIGK 375
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 23-276 8.98e-04

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: 41.18  E-value: 8.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  23 ISVWSWEPS---MGEVIRRFEKANPDIRVKWT-NISGYGNLNTAI-QDGYGTPDVAQIEYYALLQYAVSGQLLDLTDKIG 97
Cdd:cd13655     2 LTVWGPQEDqewLKEMVDAFKEKHPEWKITITiGVVGEADAKDEVlKDPSAAADVFAFANDQLGELVDAGAIYPLTGSAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  98 SDYSNFFTLGTWSSVQLAGRTYGLPMDSGPMGFFYNEDVFRQAGVdatkiKTWDdyyEAAEKLKEIGAYIAADSgDGSFY 177
Cdd:cd13655    82 DKIKNTNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLTEDDV-----KSLD---TMLAKAPDAKGKVSFDL-SNSWY 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 178 DAMVWLAGGQPFHTSADGKTVTIDLDEDAGTQrFTEFWQKMID-EGLVDTTSATWsdrwKSRVGTGTIASVFSGAWMpsl 256
Cdd:cd13655   153 LYAFFFGAGCKLFGNNGGDTAGCDFNNEKGVA-VTNYLVDLVAnPKFVNDADGDA----ISGLKDGTLGAGVSGPWD--- 224

                         250       260
                  ....*....|....*....|.
gi 1765992889 257 lLSNVPGAAGL-WRVAPMPTY 276
Cdd:cd13655   225 -AANLKKALGDnYAVAKLPTY 244
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
1-310 1.05e-03

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 41.32  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889   1 MTAILSVSLASCGQATddnrTEISVW-SWEPSMGE----VIRRFEKANPDIRVkwtnISGY-GNLNTAIQDGYGT----- 69
Cdd:PRK10974   10 LGLALGLALSGNAQAV----TEIPFWhSMEGELGKevdsLAQRFNASQPDYKI----VPVYkGNYEQSLAAGIAAfrsgn 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  70 -PDVAQIEYYALLQYAVSGQLLDLTD-----KIGSDYSNFF-TLGTWSSVQLAGRTYGLPMDSGPMGFFYNEDVFRQAGV 142
Cdd:PRK10974   82 aPAILQVYEVGTATMMASKAIKPVYDvfkdaGIPFDESQFVpTVAGYYSDAKTGHLLSQPFNSSTPVLYYNKDAFKKAGL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 143 DATKI-KTWDDYYEAAEKLKEIGAYIAADSGDGSF-----YDAmvWlaGGQPFHTSA---DGKTVTIDLDEDAGTqRFTE 213
Cdd:PRK10974  162 DPEQPpKTWQDLAAYAAKLRAAGMKCGYASGWQGWiqlenFSA--W--HGLPFASKNngfDGTDAVLEFNKPEQV-KHIA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 214 FWQKMIDEGlvDTTSATWSDRWKSRVGTG--TIASVFSGAwmpsllLSNVPGAAGL-WRVAPMP---TYGGQPANAENGG 287
Cdd:PRK10974  237 LLEEMNKKG--DFTYVGRKDESTEKFYNGdcAITTASSGS------LANIRKYAKFnYGVGMMPydaDVKGAPQNAIIGG 308

                         330       340
                  ....*....|....*....|....*..
gi 1765992889 288 SALTVLQltRKPDAAYR----FVDFVA 310
Cdd:PRK10974  309 ASLWVMQ--GKDKETYKgvakFLDFLA 333
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 40-308 3.21e-03

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


Pssm-ID: 270299 [Multi-domain]  Cd Length: 490  Bit Score: 40.00  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889  40 EKANpdIRVKWTNISGYG-----NLNTAIQDgygTPDV---AQIEYYALLQYAVSGQLLDLTDKI---GSDYSNFF---- 104
Cdd:cd13581    28 EKTG--IKIEWETVPEDAwaekkNLMLASGD---LPDAflgAGASDADLMTYGKQGLFLPLEDLIdkyAPNLKALFdenp 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 105 -TLGTWSSvqLAGRTYGLP-------MDSGPMGFFyNEDVFRQAGVDATKikTWDDYYEAAEKLKEIGA--YIAAD---- 170
Cdd:cd13581   103 dIKAAITA--PDGHIYALPsvnecyhCSYGQRMWI-NKKWLDKLGLEMPT--TTDELYEVLKAFKEQDPngNGKADeipl 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765992889 171 --SGDGSFYDAMVWLAGGqpFHTSADGKTVTIDLDEDaGTQRFT----------EFWQKMIDEGLVDTTSATWSDRWKSR 238
Cdd:cd13581   178 sfSGLNGGTDDPAFLLNS--FGINDGGYGGYGFVVKD-GKVIYTatdpeykealAYLNKLYKEGLIDPEAFTQDYDQLAA 254

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1765992889 239 VGTGTIASVFSGAWMPSLLLsnvpGAAGLWR----VAPMPTYGGQPANAENGGSALTV--LQLTRK---PDAAYRFVDF 308
Cdd:cd13581   255 KGKASTAKVGVFFGWDPGLF----FGEERYEqyvpLPPLKGPNGDQLAWVGNSSGYGRggFVITSKnknPEAAIRWADF 329
 
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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