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Conserved domains on  [gi|2525772005|ref|WP_287544090|]
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extracellular solute-binding protein [Bifidobacterium sp.]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Periplasmic_Binding_Protein_Type_2 super family cl21456
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 52-422 2.96e-97

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


The actual alignment was detected with superfamily member cd14747:

Pssm-ID: 473866 [Multi-domain]  Cd Length: 386  Bit Score: 296.15  E-value: 2.96e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  52 LTVWAMGN--EGDLLGDFVDGFKEENPDVNITVTAIPWASAHDKIQTAIAAGTVPDVIQMGTTWMADFA--DAFAPV-PE 126
Cdd:cd14747     2 LTVWAMGNsaEAELLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAamGALEDLtPY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 127 NFDLSDFS---AGPLEAGQVNGEQLGVPWYVDSHVLYYRTDIAEQAGWDHAPETLDELKQMAEDVKQVDGVENGMYIsPS 203
Cdd:cd14747    82 LEDLGGDKdlfPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGDEAPKTWDELEAAAKKIKADGPDVSGFAI-PG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 204 GADSWQGTLWAFFSSGVSLMDDeDNW--TLDTPEMHEATEYIDGFFKDGITGTNLDVTPGVSITQFVNGETPIMTGGPTT 281
Cdd:cd14747   161 KNDVWHNALPFVWGAGGDLATK-DKWkaTLDSPEAVAGLEFYTSLYQKGLSPKSTLENSADVEQAFANGKVAMIISGPWE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 282 ISQIADQGGDPDT-YATAVIPKG--VSSTSFVGGADFVVMDEAANPEAGWKFIQWMTEPETQVEWYKTATVLPSSQSAWE 358
Cdd:cd14747   240 IGAIREAGPDLAGkWGVAPLPGGpgGGSPSFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGMLPANTSAWD 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525772005 359 DEVLAGDEKLVAYGEQLESTQAPPAVPTWAQVSAAGD-RIMEQIYKGQLSVDEGLKNLQTEAESI 422
Cdd:cd14747   320 DPSLANDPLLAVFAEQLKTGKATPATPEWGEIEAELVlVLEEVWIGVGADVEDALDKAAAEINEI 384
 
Name Accession Description Interval E-value
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 52-422 2.96e-97

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: 296.15  E-value: 2.96e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  52 LTVWAMGN--EGDLLGDFVDGFKEENPDVNITVTAIPWASAHDKIQTAIAAGTVPDVIQMGTTWMADFA--DAFAPV-PE 126
Cdd:cd14747     2 LTVWAMGNsaEAELLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAamGALEDLtPY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 127 NFDLSDFS---AGPLEAGQVNGEQLGVPWYVDSHVLYYRTDIAEQAGWDHAPETLDELKQMAEDVKQVDGVENGMYIsPS 203
Cdd:cd14747    82 LEDLGGDKdlfPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGDEAPKTWDELEAAAKKIKADGPDVSGFAI-PG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 204 GADSWQGTLWAFFSSGVSLMDDeDNW--TLDTPEMHEATEYIDGFFKDGITGTNLDVTPGVSITQFVNGETPIMTGGPTT 281
Cdd:cd14747   161 KNDVWHNALPFVWGAGGDLATK-DKWkaTLDSPEAVAGLEFYTSLYQKGLSPKSTLENSADVEQAFANGKVAMIISGPWE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 282 ISQIADQGGDPDT-YATAVIPKG--VSSTSFVGGADFVVMDEAANPEAGWKFIQWMTEPETQVEWYKTATVLPSSQSAWE 358
Cdd:cd14747   240 IGAIREAGPDLAGkWGVAPLPGGpgGGSPSFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGMLPANTSAWD 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525772005 359 DEVLAGDEKLVAYGEQLESTQAPPAVPTWAQVSAAGD-RIMEQIYKGQLSVDEGLKNLQTEAESI 422
Cdd:cd14747   320 DPSLANDPLLAVFAEQLKTGKATPATPEWGEIEAELVlVLEEVWIGVGADVEDALDKAAAEINEI 384
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-422 1.09e-78

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 249.10  E-value: 1.09e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005   1 MKRtpwKTAVALFAGASMLFGMNACGRTDDTADGVDdnavtsidSEPATGDLTVWAMGNEGDLLGDFVDGFKEEnPDVNI 80
Cdd:COG2182     1 MKR---RLLAALALALALALALAACGSGSSSSGSSS--------AAGAGGTLTVWVDDDEAEALEEAAAAFEEE-PGIKV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  81 TVTAIPWASAHDKIQTAIAAGTVPDVIQMGTTWMADFADA--FAPVPENF-DLSDFSAGPLEAGQVNGEQLGVPWYVDSH 157
Cdd:COG2182    69 KVVEVPWDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAglLAPLDDDLaDKDDFLPAALDAVTYDGKLYGVPYAVETL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 158 VLYYRTDIAEQAgwdhAPETLDELKQMAEDVKQvDGVENGMYispSGADSWQgtLWAFFSS-GVSL----MDDEDNWTLD 232
Cdd:COG2182   149 ALYYNKDLVKAE----PPKTWDELIAAAKKLTA-AGKYGLAY---DAGDAYY--FYPFLAAfGGYLfgkdGDDPKDVGLN 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 233 TPEMHEATEYIDGFFKDGITGTNLDvtPGVSITQFVNGETPIMTGGPTTISQIADQGGDPdtYATAVIPK---GVSSTSF 309
Cdd:COG2182   219 SPGAVAALEYLKDLIKDGVLPADAD--YDAADALFAEGKAAMIINGPWAAADLKKALGID--YGVAPLPTlagGKPAKPF 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 310 VGGADFVVMDEAANPEAGWKFIQWMTEPETQVEWYKTATVLPSSQSAWEDEVLAGDEKLVAYGEQLESTQAPPAVPTWAQ 389
Cdd:COG2182   295 VGVKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAAAEDAEVKADPLIAAFAEQAEYAVPMPNIPEMGA 374

                         410       420       430
                  ....*....|....*....|....*....|...
gi 2525772005 390 VSAAGDRIMEQIYKGQLSVDEGLKNLQTEAESI 422
Cdd:COG2182   375 VWTPLGTALQAIASGKADPAEALDAAQKQIEAA 407
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 66-368 7.92e-31

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 119.43  E-value: 7.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  66 DFVDGFKEENpDVNITVTAIPWASAHDKIQTAIAAGTVPD--VIQMGTTWMADFA--DAFAPVPENFDLSDFSAGpLEAG 141
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDldVVWIAADQLATLAeaGLLADLSDVDNLDDLPDA-LDAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 142 QVNGEQLGVPW-YVDSHVLYYRTDIAEQAGWDhaPETLDELKQMAEDVKqvdgvenGMYISPSGADSWQgtLWAFFSSGV 220
Cdd:pfam13416  79 GYDGKLYGVPYaASTPTVLYYNKDLLKKAGED--PKTWDELLAAAAKLK-------GKTGLTDPATGWL--LWALLADGV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 221 SLMDDEDNWtldtPEMHEATEYIDGFFKDGITGTNLDVTPGVsitqFVNGETPIMTGGPTTISQIADQGGDpdtyATAVI 300
Cdd:pfam13416 148 DLTDDGKGV----EALDEALAYLKKLKDNGKVYNTGADAVQL----FANGEVAMTVNGTWAAAAAKKAGKK----LGAVV 215

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772005 301 PKgvsSTSFVGGADFVVMDEAANPE-AGWKFIQWMTEPETQVEWYKTATVLPSSQSAWEDEVLAGDEKL 368
Cdd:pfam13416 216 PK---DGSFLGGKGLVVPAGAKDPRlAALDFIKFLTSPENQAALAEDTGYIPANKSAALSDEVKADPAL 281
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
48-358 3.41e-08

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 55.19  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  48 ATGDLTVW-AMGNE-GDLLGDFVDGFKEENPDVNITVTaipWASAHDKIQTA-IAA---GTVPDVIQM---GT-TWMADF 117
Cdd:PRK10974   24 AVTEIPFWhSMEGElGKEVDSLAQRFNASQPDYKIVPV---YKGNYEQSLAAgIAAfrsGNAPAILQVyevGTaTMMASK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 118 A-----DAFAPVPENFDLSDFSagPLEAG----QVNGEQLGVPWYVDSHVLYYRTDIAEQAGWD--HAPETLDELKQMAE 186
Cdd:PRK10974  101 AikpvyDVFKDAGIPFDESQFV--PTVAGyysdAKTGHLLSQPFNSSTPVLYYNKDAFKKAGLDpeQPPKTWQDLAAYAA 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 187 DVKQvdgveNGMyiSPSGADSWQG-------TLW--AFFSSGVSLMDDED-NWTLDTPEMHEATEYIDGFFKDGitgtnl 256
Cdd:PRK10974  179 KLRA-----AGM--KCGYASGWQGwiqlenfSAWhgLPFASKNNGFDGTDaVLEFNKPEQVKHIALLEEMNKKG------ 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 257 DVT----PGVSITQFVNGETPIMT---GGPTTISQIADQggdpdTYATAVIP-----KGVSSTSFVGGADFVVMD--EAA 322
Cdd:PRK10974  246 DFTyvgrKDESTEKFYNGDCAITTassGSLANIRKYAKF-----NYGVGMMPydadvKGAPQNAIIGGASLWVMQgkDKE 320

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2525772005 323 NPEAGWKFIQWMTEPETQVEWYKTATVLPSSQSAWE 358
Cdd:PRK10974  321 TYKGVAKFLDFLAKPENAAEWHQKTGYLPITTAAYD 356
 
Name Accession Description Interval E-value
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 52-422 2.96e-97

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: 296.15  E-value: 2.96e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  52 LTVWAMGN--EGDLLGDFVDGFKEENPDVNITVTAIPWASAHDKIQTAIAAGTVPDVIQMGTTWMADFA--DAFAPV-PE 126
Cdd:cd14747     2 LTVWAMGNsaEAELLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAamGALEDLtPY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 127 NFDLSDFS---AGPLEAGQVNGEQLGVPWYVDSHVLYYRTDIAEQAGWDHAPETLDELKQMAEDVKQVDGVENGMYIsPS 203
Cdd:cd14747    82 LEDLGGDKdlfPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGDEAPKTWDELEAAAKKIKADGPDVSGFAI-PG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 204 GADSWQGTLWAFFSSGVSLMDDeDNW--TLDTPEMHEATEYIDGFFKDGITGTNLDVTPGVSITQFVNGETPIMTGGPTT 281
Cdd:cd14747   161 KNDVWHNALPFVWGAGGDLATK-DKWkaTLDSPEAVAGLEFYTSLYQKGLSPKSTLENSADVEQAFANGKVAMIISGPWE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 282 ISQIADQGGDPDT-YATAVIPKG--VSSTSFVGGADFVVMDEAANPEAGWKFIQWMTEPETQVEWYKTATVLPSSQSAWE 358
Cdd:cd14747   240 IGAIREAGPDLAGkWGVAPLPGGpgGGSPSFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGMLPANTSAWD 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525772005 359 DEVLAGDEKLVAYGEQLESTQAPPAVPTWAQVSAAGD-RIMEQIYKGQLSVDEGLKNLQTEAESI 422
Cdd:cd14747   320 DPSLANDPLLAVFAEQLKTGKATPATPEWGEIEAELVlVLEEVWIGVGADVEDALDKAAAEINEI 384
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-422 1.09e-78

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 249.10  E-value: 1.09e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005   1 MKRtpwKTAVALFAGASMLFGMNACGRTDDTADGVDdnavtsidSEPATGDLTVWAMGNEGDLLGDFVDGFKEEnPDVNI 80
Cdd:COG2182     1 MKR---RLLAALALALALALALAACGSGSSSSGSSS--------AAGAGGTLTVWVDDDEAEALEEAAAAFEEE-PGIKV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  81 TVTAIPWASAHDKIQTAIAAGTVPDVIQMGTTWMADFADA--FAPVPENF-DLSDFSAGPLEAGQVNGEQLGVPWYVDSH 157
Cdd:COG2182    69 KVVEVPWDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAglLAPLDDDLaDKDDFLPAALDAVTYDGKLYGVPYAVETL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 158 VLYYRTDIAEQAgwdhAPETLDELKQMAEDVKQvDGVENGMYispSGADSWQgtLWAFFSS-GVSL----MDDEDNWTLD 232
Cdd:COG2182   149 ALYYNKDLVKAE----PPKTWDELIAAAKKLTA-AGKYGLAY---DAGDAYY--FYPFLAAfGGYLfgkdGDDPKDVGLN 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 233 TPEMHEATEYIDGFFKDGITGTNLDvtPGVSITQFVNGETPIMTGGPTTISQIADQGGDPdtYATAVIPK---GVSSTSF 309
Cdd:COG2182   219 SPGAVAALEYLKDLIKDGVLPADAD--YDAADALFAEGKAAMIINGPWAAADLKKALGID--YGVAPLPTlagGKPAKPF 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 310 VGGADFVVMDEAANPEAGWKFIQWMTEPETQVEWYKTATVLPSSQSAWEDEVLAGDEKLVAYGEQLESTQAPPAVPTWAQ 389
Cdd:COG2182   295 VGVKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAAAEDAEVKADPLIAAFAEQAEYAVPMPNIPEMGA 374

                         410       420       430
                  ....*....|....*....|....*....|...
gi 2525772005 390 VSAAGDRIMEQIYKGQLSVDEGLKNLQTEAESI 422
Cdd:COG2182   375 VWTPLGTALQAIASGKADPAEALDAAQKQIEAA 407
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-343 5.56e-70

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 225.31  E-value: 5.56e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005   1 MKRtpwktaVALFAGASMLFGMNACGrTDDTADGVDDNAVTsidsepatgdLTVWAM-GNEGDLLGDFVDGFKEENPDVN 79
Cdd:COG1653     1 MRR------LALALAAALALALAACG-GGGSGAAAAAGKVT----------LTVWHTgGGEAAALEALIKEFEAEHPGIK 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  80 ITVTAIPWASAHDKIQTAIAAGTVPDVIQMGTTWMADFADA--FAPVPE-----NFDLSDFSAGPLEAGQVNGEQLGVPW 152
Cdd:COG1653    64 VEVESVPYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAgaLVPLDDlldddGLDKDDFLPGALDAGTYDGKLYGVPF 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 153 YVDSHVLYYRTDIAEQAGWDhAPETLDELKQMAEDVKQVDGVeNGMYISPSGADSWQGTLWAFfssGVSLMDDEDNWTLD 232
Cdd:COG1653   144 NTDTLGLYYNKDLFEKAGLD-PPKTWDELLAAAKKLKAKDGV-YGFALGGKDGAAWLDLLLSA---GGDLYDEDGKPAFD 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 233 TPEMHEATEYIDGFFKDGITGTN-LDVTPGVSITQFVNGETPIMTGGPTTISQIADQGGDPDtYATAVIPK---GVSSTS 308
Cdd:COG1653   219 SPEAVEALEFLKDLVKDGYVPPGaLGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDFD-VGVAPLPGgpgGKKPAS 297

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 2525772005 309 FVGGADFVVMDEAANPEAGWKFIQWMTEPETQVEW 343
Cdd:COG1653   298 VLGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQAKW 332
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 52-419 4.29e-68

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: 221.12  E-value: 4.29e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  52 LTVWAMGN--EGDLLGDFVDGFKEENPDVNITVTAIPWASAHDKIQTAIAAGTVPDVIQMGTTWMADFADAFAPVP---- 125
Cdd:cd13585     2 LTFWDWGQpaETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDlddy 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 126 --ENFDLSDFSAGPLEAGQVNGEQLGVPWYVDSHVLYYRTDIAEQAGW-DHAPETLDELKQMAEDVKQVDGVENGMYISP 202
Cdd:cd13585    82 ieKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPgPKPPWTWDELLEAAKKLTDKKGGQYGFALRG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 203 SGADSWQGTLWaFFSSGVSLMDDED-NWTLDTPEMHEATEYIDGFFKDGITGTNLDVTPGVSITQFVNGETPIMTGGPTT 281
Cdd:cd13585   162 GSGGQTQWYPF-LWSNGGDLLDEDDgKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFASGKVAMMIDGPWA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 282 ISQIADQGGDpDTYATAVIPKGVS--STSFVGGADFVVMDEAANPEAGWKFIQWMTEPETQVEWYKTATVLPSSQSAWED 359
Cdd:cd13585   241 LGTLKDSKVK-FKWGVAPLPAGPGgkRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAASA 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772005 360 EVLAGDEKLVAYG--EQLESTQAPPAVPTWAQVSAAGDRIMEQIYKGQL--SVDEGLKNLQTEA 419
Cdd:cd13585   320 AAPDAKPALALAAaaDALAAAVPPPVPPPWPEVYPILSEALQEALLGALgkSPEEALKEAAKEI 383
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 52-419 7.36e-68

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: 220.63  E-value: 7.36e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  52 LTVWAM--GNEGDLLGDFVDGFKEENPDVNITVTAIPWAS-AHDKIQTAIAAGTVPDVIQMGTTWMADFAD--AFAPVPE 126
Cdd:cd14748     2 ITFWHGmsGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDdTLTKLLAALAAGTAPDVAQVDASWVAQLADsgALEPLDD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 127 -----NFDLSDFSAGPLEAGQVNGEQLGVPWYVDSHVLYYRTDIAEQAGWD--HAPETLDELKQMAEDVKQVDGVEN--G 197
Cdd:cd14748    82 yidkdGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDpeKPPKTWDELEEAAKKLKDKGGKTGryG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 198 MYISPSGADSWQGTLwaFFSSGVSLMDDED-NWTLDTPEMHEATEYI-DGFFKDGITGTNLDVTPGvsiTQFVNGETPIM 275
Cdd:cd14748   162 FALPPGDGGWTFQAL--LWQNGGDLLDEDGgKVTFNSPEGVEALEFLvDLVGKDGVSPLNDWGDAQ---DAFISGKVAMT 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 276 TGGPTTISQIADQGGDpDTYATAVIPKGVSST--SFVGGADFVVM-DEAANPEAGWKFIQWMTEPETQVEWYKTATVLPS 352
Cdd:cd14748   237 INGTWSLAGIRDKGAG-FEYGVAPLPAGKGKKgaTPAGGASLVIPkGSSKKKEAAWEFIKFLTSPENQAKWAKATGYLPV 315

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 353 SQSAWEDEV--LAGD-EKLVAYGEQLESTQAPPAVPTWAQVSAAGDRIMEQIYKGQLSVDEGLKNLQTEA 419
Cdd:cd14748   316 RKSAAEDPEefLAENpNYKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 60-418 2.76e-59

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: 197.99  E-value: 2.76e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  60 EGDLLGDFVDGFKEENPDVNITVTAIPWASAHDKIQTAIAAGTVPDVIQMGTTWMADFA--DAFAPV---PENFDLSDFS 134
Cdd:cd14751    12 EKVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAklGYLQPLdgtPAFDDIVDYL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 135 AGPLEAGQVNGEQLGVPWYVDSHVLYYRTDIAEQAGWDhAPETLDELKQMAEDVKQVDGVEnGMYISPSGADSWQGTLWA 214
Cdd:cd14751    92 PGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTE-VPKTMDELVAAAKAIKKKKGRY-GLYISGDGPYWLLPFLWS 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 215 FfssGVSLMDDED-NWTLDTPEMHEATEYI-DGFFKDGITGTNLDVTPGVSiTQFVNGETPIMTGGPTTISQIADQGG-- 290
Cdd:cd14751   170 F---GGDLTDEKKaTGYLNSPESVRALETIvDLYDEGAITPCASGGYPNMQ-DGFKSGRYAMIVNGPWAYADILGGKEfk 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 291 DPDTYATAVIPKG-VSSTSFVGGADFVVMDEAANPEAGWKFIQWMTEPETQVEWYKTATVLPSSQSAWEDEVLAGDEKLV 369
Cdd:cd14751   246 DPDNLGIAPVPAGpGGSGSPVGGEDLVIFKGSKNKDAAWKFVKFMSSAEAQALTAAKLGLLPTRTSAYESPEVANNPMVA 325

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2525772005 370 AYGEQLESTQAPPAVPTWAQVSAAGDRIMEQIYKGQLSVDEGLKNLQTE 418
Cdd:cd14751   326 AFKPALETAVPRPPIPEWGELFEPLTLAFAKVLRGEKSPREALDEAAKQ 374
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 54-418 2.07e-43

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: 156.30  E-value: 2.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  54 VWAMGNEG---DLLGDFVDGFKEENPDVNITVTAIPWAS--AHDKIQTAIAAG-TVPDVIQMGTTWMADFADAF--APVP 125
Cdd:cd14750     3 TFAAGSDGqegELLKKAIAAFEKKHPDIKVEIEELPASSddQRQQLVTALAAGsSAPDVLGLDVIWIPEFAEAGwlLPLT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 126 ENF---DLSDFSAGPLEAGQVNGEQLGVPWYVDSHVLYYRTDIAEQAGwDHAPETLDELKQMAEDVKQVDGVENGMyisp 202
Cdd:cd14750    83 EYLkeeEDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYG-PEPPKTWDELLEAAKKRKAGEPGIWGY---- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 203 sgadSWQGTLWA---------FFSSGVSLMDDED-NWTLDTPEMHEATEYIDGFFKDGITGTNLDVTPGVSITQ-FVNGE 271
Cdd:cd14750   158 ----VFQGKQYEglvcnflelLWSNGGDIFDDDSgKVTVDSPEALEALQFLRDLIGEGISPKGVLTYGEEEARAaFQAGK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 272 TPIMTGGPT-------TISQIADQGGdpdtYATAVIPKGVSSTSFVGGADFVVMDEAANPEAGWKFIQWMTEPETQVEWY 344
Cdd:cd14750   234 AAFMRNWPYayallqgPESAVAGKVG----VAPLPAGPGGGSASTLGGWNLAISANSKHKEAAWEFVKFLTSPEVQKRRA 309

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525772005 345 KTATVLPSSQSAWED-EVLAGDEKLVAYGEQLESTQAPPAVPTWAQVSAAGDRIMEQIYKGQLSVDEGLKNLQTE 418
Cdd:cd14750   310 INGGLPPTRRALYDDpEVLEAYPFLPALLEALENAVPRPVTPKYPEVSTAIQIALSAALSGQATPEEALKQAQEK 384
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 51-421 6.98e-42

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: 152.15  E-value: 6.98e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  51 DLTVWAMGNEGD---LLGDFVDGFKEENPDVNITVTAIPWASAHDKIQTAIAAGTVPDVIQM-GTTWMADFADA--FAPV 124
Cdd:cd14749     1 TITYWQYFTGDTkkkYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLwPGGWLAEFVKAglLLPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 125 PENFDLSD----FSAGPLEAGQVNGEQLGVPWYVDSHVLYYRTDIAEQAGWDHAPETLDELKQMAEDVKQVDGVENGMYI 200
Cdd:cd14749    81 TDYLDPNGvdkrFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGVKPPKTWDELIEAAKKDKFKAKGQTGFGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 201 SPSGAD-SWQGTLWAFFSSGVSLMDDEDN-WTLDTPEMHEATEYIDGFFKDGITGTN-LDVTPGVSITQFVNGETpIMTG 277
Cdd:cd14749   161 LLGAQGgHWYFQYLVRQAGGGPLSDDGSGkATFNDPAFVQALQKLQDLVKAGAFQEGfEGIDYDDAGQAFAQGKA-AMNI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 278 GPTTISQIADQGGDPDTYATAVIPKGVSS--TSFVGGADFVVMDEA--ANPEAGWKFIQWMTEPETQVEWYKTATVLPSS 353
Cdd:cd14749   240 GGSWDLGAIKAGEPGGKIGVFPFPTVGKGaqTSTIGGSDWAIAISAngKKKEAAVKFLKYLTSPEVMKQYLEDVGLLPAK 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772005 354 QSAWEDEVLAGDEKLVAYGEQLESTQAPPAV-PTWAQVSAAGDRIMEQIYKGQLSVDEGLKNLQTEAES 421
Cdd:cd14749   320 EVVAKDEDPDPVAILGPFADVLNAAGSTPFLdEYWPAAAQVHKDAVQKLLTGKIDPEQVVKQAQSAAAK 388
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 51-419 8.47e-39

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: 143.20  E-value: 8.47e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  51 DLTVW-AMGNEGDLLGDFVDGFKEENpDVNITVTAIPWASAHDKIQTAIAAGTVPDVIQMGTTWMADFADA--FAPVPEN 127
Cdd:cd13586     1 TITVWtDEDGELEYLKELAEEFEKKY-GIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAglLAPIPEY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 128 FDLSDFSAG-PLEAGQVNGEQLGVPWYVDSHVLYYRTDIAEQAgwdhaPETLDELKQMAEdvKQVDGVENGMYISPSGAD 206
Cdd:cd13586    80 LAVKIKNLPvALAAVTYNGKLYGVPVSVETIALFYNKDLVPEP-----PKTWEELIALAK--KFNDKAGGKYGFAYDQTN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 207 SWQgtLWAFFSS-GVSLMDDEDNWT----LDTPEMHEATEYI-DGFFKDGITGTNLDvtPGVSITQFVNGETPIMTGGPT 280
Cdd:cd13586   153 PYF--SYPFLAAfGGYVFGENGGDPtdigLNNEGAVKGLKFIkDLKKKYKVLPPDLD--YDIADALFKEGKAAMIINGPW 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 281 TISQIADQGgdpDTYATAVIPK---GVSSTSFVGGADFVVMDEAANPEAGWKFIQWMTEPETQVEWYKTATVLPSSQSAW 357
Cdd:cd13586   229 DLADYKDAG---INFGVAPLPTlpgGKQAAPFVGVQGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALKDAL 305

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525772005 358 EDEVLAGDEKLVAYGEQLESTQAPPAVPTWAQVSAAGDRIMEQIYKGQLSVDEGLKNLQTEA 419
Cdd:cd13586   306 NDAAVKNDPLVKAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEEAAKDAVAAI 367
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 52-419 4.61e-33

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: 127.88  E-value: 4.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  52 LTVWA--MGNEGDLLGDFVDGFKEENPDVNITVTAIPWASAHDKIQTAIAAGTVPDVIQMGTTWMADFADAFAPVPEN-- 127
Cdd:cd13657     2 ITIWHalTGAEEDALQQIIDEFEAKYPVPNVKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISdy 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 128 ---FDLSDFSAGPLEAGQVNGEQLGVPWYVDSHVLYYRTDIaeqagWDHAPETLDELKQMAEDVKQVDgveNGMY-ISPS 203
Cdd:cd13657    82 lseDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKAL-----VDQPPETTDELLAIMKDHTDPA---AGSYgLAYQ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 204 GADSWQGTLWaFFSSGVSLMDDE-DNWTLDTPEMHEATEYIDGFFKDGITGTNLDVTpgvSITQFVNGETPIMTGGPTTI 282
Cdd:cd13657   154 VSDAYFVSAW-IFGFGGYYFDDEtDKPGLDTPETIKGIQFLKDFSWPYMPSDPSYNT---QTSLFNEGKAAMIINGPWFI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 283 SQIADQGGDpdtYATAVIPKgVSSTS----FVG--GADFVVMDEAANPEAGWKFIQWMTEPETQVEWYKTATVLPSSQSA 356
Cdd:cd13657   230 GGIKAAGID---LGVAPLPT-VDGTNpprpYSGveGIYVTKYAERKNKEAALDFAKFFTTAEASKILADENGYVPAATNA 305

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525772005 357 WEDEVLAGDEKLVAYGEQLESTQAPPAVPTWAQVSAAGDRIMEQIYKGQLSVDEGLKNLQTEA 419
Cdd:cd13657   306 YDDAEVAADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQEALAAAQQEI 368
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 66-368 7.92e-31

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 119.43  E-value: 7.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  66 DFVDGFKEENpDVNITVTAIPWASAHDKIQTAIAAGTVPD--VIQMGTTWMADFA--DAFAPVPENFDLSDFSAGpLEAG 141
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDldVVWIAADQLATLAeaGLLADLSDVDNLDDLPDA-LDAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 142 QVNGEQLGVPW-YVDSHVLYYRTDIAEQAGWDhaPETLDELKQMAEDVKqvdgvenGMYISPSGADSWQgtLWAFFSSGV 220
Cdd:pfam13416  79 GYDGKLYGVPYaASTPTVLYYNKDLLKKAGED--PKTWDELLAAAAKLK-------GKTGLTDPATGWL--LWALLADGV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 221 SLMDDEDNWtldtPEMHEATEYIDGFFKDGITGTNLDVTPGVsitqFVNGETPIMTGGPTTISQIADQGGDpdtyATAVI 300
Cdd:pfam13416 148 DLTDDGKGV----EALDEALAYLKKLKDNGKVYNTGADAVQL----FANGEVAMTVNGTWAAAAAKKAGKK----LGAVV 215

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772005 301 PKgvsSTSFVGGADFVVMDEAANPE-AGWKFIQWMTEPETQVEWYKTATVLPSSQSAWEDEVLAGDEKL 368
Cdd:pfam13416 216 PK---DGSFLGGKGLVVPAGAKDPRlAALDFIKFLTSPENQAALAEDTGYIPANKSAALSDEVKADPAL 281
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 52-419 2.99e-30

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: 119.82  E-value: 2.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  52 LTVWAMGNEGDL--LGDFVDGFKEENPDVNITVTAIPWASAHDKIQTAIAAGTVPDVIQMGTTWMADFADA--FAPVPEN 127
Cdd:cd13522     2 ITVWHQYDTGENqaVNELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAglLAPLDEY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 128 FDLSDFSAG-PLEAGQVNGEQLGVPWYVDSHVLYYRTDIAEqagwDHAPETLDELKQMAedvkQVDGVENGMYISpsgad 206
Cdd:cd13522    82 VSKSGKYAPnTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVP----KNPPKTWQELIALA----QGLKAKNVWGLV----- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 207 sWQGTL----WAFFSS-GVSLMDDED---NWTLDTPEMHEATEYI-DGFFKDGITGTNLDvtPGVSITQFVNGETPIMTG 277
Cdd:cd13522   149 -YNQNEpyffAAWIGGfGGQVFKANNgknNPTLDTPGAVEALQFLvDLKSKYKIMPPETD--YSIADALFKAGKAAMIIN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 278 GPTTISQIADQGGDpdTYATAVIP---KGVSSTSFVGGADFVVMDEAANPEAGWKFIQWMTEPETQVEWYKTATVLPSSQ 354
Cdd:cd13522   226 GPWDLGDYRQALKI--NLGVAPLPtfsGTKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDIPANL 303

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525772005 355 SAWEDEVLAGDEKLVAYGEQLESTQAPPAVPTWAQVSAAGDRIMEQIYKGQLSVDEGLKNLQTEA 419
Cdd:cd13522   304 QAYESPAVQNKPAQKASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQQEA 368
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 67-340 4.09e-26

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: 107.12  E-value: 4.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  67 FVDGFKEENPDVNITVTAIPWASAHDKIQTAIAAGTVP-DVIQMGTTWMADFADAFAPVPENFDLSDfsagplEAGQVNG 145
Cdd:pfam01547  13 LVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVAN------YLVLGVP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 146 EQLGVPWYVDSHVLYYRTDIAEQAGWDhAPETLDELKQMAEDVKqvdGVENGMYISPSGADSWQGTLW--AFFSSGVSLM 223
Cdd:pfam01547  87 KLYGVPLAAETLGLIYNKDLFKKAGLD-PPKTWDELLEAAKKLK---EKGKSPGGAGGGDASGTLGYFtlALLASLGGPL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 224 DDEDNWTLDTPEMHEATEYIDGFFKDGITGTNLDVTPGVS------ITQFVNGETPIMTGGPTTISQ----------IAD 287
Cdd:pfam01547 163 FDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGadgreaLALFEQGKAAMGIVGPWAALAankvklkvafAAP 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2525772005 288 QGGDPDTYATAVIPKGvsSTSFVGGADFVVMDEAANPEAGWKFIQWMTEPETQ 340
Cdd:pfam01547 243 APDPKGDVGYAPLPAG--KGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQ 293
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 52-414 2.94e-24

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: 103.33  E-value: 2.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  52 LTVWA-MGNEGDLLGDFVDGFKEENpDVNITVTAIPWASAHDKIQTAIAAGTVPDVI-----QMGTTWMADFAdafAPVP 125
Cdd:cd13658     2 LTVWVdEDKKMAFIKKIAKQYTKKT-GVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMvaphdRIGSAVLQGLL---SPIK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 126 E-NFDLSDFSAGPLEAGQVNGEQLGVPWYVDSHVLYYRTDIAEQAgwdhaPETLDELKQMAEDVKQVDGVENGM------ 198
Cdd:cd13658    78 LsKDKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNA-----PKTFDELEALAKDLTKEKGKQYGFladatn 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 199 ------YISPSGAdswqgtlWAFFSSGVSLmdDEDNWTLDTPEMHEATEYIDGFFKDGI--TGTNLDVTpgvsITQFVNG 270
Cdd:cd13658   153 fyysygLLAGNGG-------YIFKKNGSDL--DINDIGLNSPGAVKAVKFLKKWYTEGYlpKGMTGDVI----QGLFKEG 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 271 ETPIMTGGPTTISQIADQGGDpdtYATAVIPK---GVSSTSFVGGADFVVMDEAANPEAGWKFIQWMTEPETQVEWYKTA 347
Cdd:cd13658   220 KAAAVIDGPWAIQEYQEAGVN---YGVAPLPTlpnGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTSKENLKKRYDET 296

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772005 348 TVLPSSQSAWEDEVLAGDEKLVAYGEQLESTQAPPAVPTWAQVSAAGDRIMEQIYKGQLSVDEGLKN 414
Cdd:cd13658   297 NEIPPRKDVRSDPEIKNNPLTSAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKTPKQALND 363
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 73-340 2.01e-18

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: 87.00  E-value: 2.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  73 EENPDVNITVTAIPWASAHDKIQTAIAAGTVPDVIQ-MGTTWMADFA--DAFAPVPENFD------LSDFSAGPLEAGQV 143
Cdd:cd13580    29 EEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVvNDPQLSITLVkqGALWDLTDYLDkyypnlKKIIEQEGWDSASV 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 144 NGEQLGVPWYVDS---HVLYYRTDIAEQAGWDhAPETLDELKQMAEDVKQVDGVENG------MYISPSGADSWQGTLWA 214
Cdd:cd13580   109 DGKIYGIPRKRPLigrNGLWIRKDWLDKLGLE-VPKTLDELYEVAKAFTEKDPDGNGkkdtygLTDTKDLIGSGFTGLFG 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 215 FFSSGVSLMDDEDNWTL----DTPEMHEATEYIDGFFKDGITGTNLDVTPGVSITQ-FVNGETPIMTGGPTTISQI--AD 287
Cdd:cd13580   188 AFGAPPNNWWKDEDGKLvpgsIQPEMKEALKFLKKLYKEGLIDPEFAVNDGTKANEkFISGKAGIFVGNWWDPAWPqaSL 267

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 288 QGGDPDT----YATAVIPKG---VSSTSFVGGAdFVVMDEAANPEAGWKFIQWMTEPETQ 340
Cdd:cd13580   268 KKNDPDAewvaVPIPSGPDGkygVWAESGVNGF-FVIPKKSKKPEAILKLLDFLSDPEVQ 326
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 51-378 2.63e-14

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: 73.92  E-value: 2.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  51 DLTVWAMGNEGDLLGDFVDGFKEENPDVNITVT--AIPWASAHDKIQTAIAAGtvPDVIQMGTTWMADFADA--FAPVPE 126
Cdd:cd13655     1 TLTVWGPQEDQEWLKEMVDAFKEKHPEWKITITigVVGEADAKDEVLKDPSAA--ADVFAFANDQLGELVDAgaIYPLTG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 127 NFDL---SDFSAGPLEAGQVNGEQLGVPWYVDSHVLYYrtdiaeqagwdhapetlDELKQMAEDVKQVDGV-----ENGM 198
Cdd:cd13655    79 SAVDkikNTNSEATVDAVTYNGKLYGYPFTANTWFMYY-----------------DKSKLTEDDVKSLDTMlakapDAKG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 199 YISPSGADSWQgtLWAFFSS-GVSLMDDED------NWTLDTPEmhEATEYIDGFFKDGITGTNLDvtpGVSITQFVNGE 271
Cdd:cd13655   142 KVSFDLSNSWY--LYAFFFGaGCKLFGNNGgdtagcDFNNEKGV--AVTNYLVDLVANPKFVNDAD---GDAISGLKDGT 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 272 TPIMTGGPTTISQIADQGGdpDTYATAVIP------KGVSSTSFVGGADFVVMDEAANPEAGWKFIQWMTEPETQVEWYK 345
Cdd:cd13655   215 LGAGVSGPWDAANLKKALG--DNYAVAKLPtytlggKDVQMKSFAGYKAIGVNSNTKNPEAAMALADYLTNEESQLTRFE 292

                         330       340       350
                  ....*....|....*....|....*....|...
gi 2525772005 346 TATVLPSSQSAWEDEVLAGDEKLVAYGEQLEST 378
Cdd:cd13655   293 KRGIGPTNKEAAESDAVKADPAAKALIAQSNEA 325
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 73-340 8.45e-09

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: 57.37  E-value: 8.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  73 EENPDVNITVTAIPWASAHDKIQTAIAAGTVPDVIQM-----GTTWMAdfADAFAPVPENFD-LSDFSA-------GPL- 138
Cdd:cd13583    27 EEKTNVKFKRTPIPSSDYETKRSLLIASGDAPDIIPVlypgeENEFVA--SGALLPISDYLDyMPNYKKyvekwglGKEl 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 139 -EAGQVNGE------QLGVPWYvdSHVLYYRTDIAEQAGWDhAPETLDELKQMAEDVKQVDGV------ENGMYISPSGA 205
Cdd:cd13583   105 aTGRQSDGKyyslpgLHEDPGV--QYSFLYRKDIFEKAGIK-IPTTWDEFYAALKKLKEKYPDsypysdRWNSNALLLIA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 206 DSWQGTlWAFFSSGVSLMDDEDN---WTLDTPEMHEATEYIDGFFKDGI------TGTNLDVTpgvsiTQFVNGETPIMT 276
Cdd:cd13583   182 APAFGT-TAGWGFSNYTYDPDTDkfvYGATTDEYKDMLQYFNKLYAEGLldpesfTQTDDQAK-----AKFLNGKSFVIT 255

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772005 277 ---GGPTTISQIADQGGDPDTYATAVIP------KGVSSTSFVGGADFVV-MDEAANPEAGWKFIQWMTEPETQ 340
Cdd:cd13583   256 tnpQTVDELQRNLRAADGGNYEVVSITPpagpagKAINGSRLENGFMISSkAKDSKNFEALLQFLDWLYSDEGQ 329
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
48-358 3.41e-08

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 55.19  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  48 ATGDLTVW-AMGNE-GDLLGDFVDGFKEENPDVNITVTaipWASAHDKIQTA-IAA---GTVPDVIQM---GT-TWMADF 117
Cdd:PRK10974   24 AVTEIPFWhSMEGElGKEVDSLAQRFNASQPDYKIVPV---YKGNYEQSLAAgIAAfrsGNAPAILQVyevGTaTMMASK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 118 A-----DAFAPVPENFDLSDFSagPLEAG----QVNGEQLGVPWYVDSHVLYYRTDIAEQAGWD--HAPETLDELKQMAE 186
Cdd:PRK10974  101 AikpvyDVFKDAGIPFDESQFV--PTVAGyysdAKTGHLLSQPFNSSTPVLYYNKDAFKKAGLDpeQPPKTWQDLAAYAA 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 187 DVKQvdgveNGMyiSPSGADSWQG-------TLW--AFFSSGVSLMDDED-NWTLDTPEMHEATEYIDGFFKDGitgtnl 256
Cdd:PRK10974  179 KLRA-----AGM--KCGYASGWQGwiqlenfSAWhgLPFASKNNGFDGTDaVLEFNKPEQVKHIALLEEMNKKG------ 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 257 DVT----PGVSITQFVNGETPIMT---GGPTTISQIADQggdpdTYATAVIP-----KGVSSTSFVGGADFVVMD--EAA 322
Cdd:PRK10974  246 DFTyvgrKDESTEKFYNGDCAITTassGSLANIRKYAKF-----NYGVGMMPydadvKGAPQNAIIGGASLWVMQgkDKE 320

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2525772005 323 NPEAGWKFIQWMTEPETQVEWYKTATVLPSSQSAWE 358
Cdd:PRK10974  321 TYKGVAKFLDFLAKPENAAEWHQKTGYLPITTAAYD 356
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
66-389 3.68e-08

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 54.92  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  66 DFVDGFKEENpdvNITVTAIPWASAHDKIQTAIAAGTVPDVIQMGTTWMADF--ADAFAPVP----ENFD--LSDFSAGP 137
Cdd:COG0687    43 DVLEPFEKET---GIKVVYDTYDSNEEMLAKLRAGGSGYDVVVPSDYFVARLikAGLLQPLDksklPNLAnlDPRFKDPP 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 138 LEAGQVNGeqlgVPWYVDSHVLYYRTDIAEQAgwdhaPETLDEL--KQMAEDVkqvdgvenGMYispsgaDSWQGTLWAf 215
Cdd:COG0687   120 FDPGNVYG----VPYTWGTTGIAYNTDKVKEP-----PTSWADLwdPEYKGKV--------ALL------DDPREVLGA- 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 216 fssgVSLMDDEDNWTLDTPEMHEATE-------YIDGFFKDGITGTNLdvtpgvsitqFVNGETPIMTGGPTTISQIADQ 288
Cdd:COG0687   176 ----ALLYLGYDPNSTDPADLDAAFEllielkpNVRAFWSDGAEYIQL----------LASGEVDLAVGWSGDALALRAE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 289 GGDpdtyATAVIPK-GvsSTSFVGGadFVVMDEAANPEAGWKFIQWMTEPETQVEWYKTATVLPSSQSAWE--DEVLAGD 365
Cdd:COG0687   242 GPP----IAYVIPKeG--ALLWFDN--MAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAAREllPPELAAN 313

                         330       340
                  ....*....|....*....|....
gi 2525772005 366 EKLVAYGEQLESTQAPPAVPTWAQ 389
Cdd:COG0687   314 PAIYPPEEVLDKLEFWNPLPPENR 337
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 73-341 1.63e-05

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


Pssm-ID: 270239 [Multi-domain]  Cd Length: 483  Bit Score: 47.07  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  73 EENPDVNITVTAIPWASAHDKIQTAIAAGTVPDVIQMG---TTWMADF-ADAFAPVPENFDL--------SDFSAGPLEA 140
Cdd:cd13521    27 EKLTNVKLEIVAVTAATSQQKLNLMLASGDLPDIVGADylkDKFIAYGmEGAFLPLSKYIDQypnlkaffKQHPDVLRAS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 141 GQVNGEQLGVPWY----VDSHVLYYRTDIAEQAGWdHAPETLDELKQMAEDVKQVDGVENG-----MYISPSGADSWQGT 211
Cdd:cd13521   107 TASDGKIYLIPYEppkdVPNQGYFIRKDWLDKLNL-KTPKTLDELYNVLKAFKEKDPNGNGkadeiPFIDRDPLYGAFRL 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 212 L--WAFFSS-GVSLMD-DEDNWTLDTPEMHEAteyidgfFKDGITGTNLDVTPGV----SITQ--------FVNGETPIM 275
Cdd:cd13521   186 InsWGARSAgGSTDSDwYEDNGKFKHPFASEE-------YKDGMKYMNKLYTEGLidkeSFTQkddqaeqkFSNGKLGGF 258

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772005 276 TGGPTTISQIADQ--GGDPDTYAT--AVIPKGVS------STSFVGGADFVVMDEAANPEAGWKFIQWMTEPETQV 341
Cdd:cd13521   259 THNWFASDNLFTAqlGKEKPMYILlpIAPAGNVKgrreedSPGYTGPDGVAISKKAKNPVAALKFFDWLASEEGRE 334
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 67-343 1.34e-04

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


Pssm-ID: 270307 [Multi-domain]  Cd Length: 268  Bit Score: 43.37  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  67 FVDGFKEENpdvNITVTAIPWASAHDKIQTAIAAGTVP-DVIQM--GTTWMADFADAFAPVPENfDLSDFSAGPLEAGQV 143
Cdd:cd13589    19 VIEPFEKET---GIKVVYDTGTSADRLAKLQAQAGNPQwDVVDLddGDAARAIAEGLLEPLDYS-KIPNAAKDKAPAALK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 144 NGEqlGVPWYVDSHVLYYRTDIAEQAGWdhaPETLDELKqmaeDVKQVDGvengmyisPSGADSWQGTLWAFFSsgvsLM 223
Cdd:cd13589    95 TGY--GVGYTLYSTGIAYNTDKFKEPPT---SWWLADFW----DVGKFPG--------PRILNTSGLALLEAAL----LA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 224 DDEDNWTLDtpemheateyIDGFF------KDGITGTnlDVTPGVSITQFVNGETPIMTGGPTTISQIADQGGDPDTyat 297
Cdd:cd13589   154 DGVDPYPLD----------VDRAFaklkelKPNVVTW--WTSGAQLAQLLQSGEVDMAPAWNGRAQALIDAGAPVAF--- 218

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2525772005 298 aVIPKGvssTSFVGGADFVVMDEAANPEAGWKFIQWMTEPETQVEW 343
Cdd:cd13589   219 -VWPKE---GAILGPDTLAIVKGAPNKELAMKFINFALSPEVQAAL 260
PBP2_Thiaminase_I cd13524
Thiaminase-I has high structural homology to the type 2 periplasmic binding proteins of active ...
 105-392 7.68e-04

Thiaminase-I has high structural homology to the type 2 periplasmic binding proteins of active transport systems; Thiaminase-I, a thiamin-(vitamin B1) degrading enzyme, is a monomer in its biologically active form, with two distinct globular domains (N- and C-domains) separated by a deep groove. It has a structural topology similar to the periplasmic substrate-domains of ABC-type transport systems, such as thiamin-binding protein (TbpA), that possess the type 2 periplasmic binding protein fold. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea.


Pssm-ID: 270242  Cd Length: 363  Bit Score: 41.37  E-value: 7.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 105 DVIQMGTTWMADF--ADAFAPVPENFDlSDFSAGPLEAGQVNGEQLGVPWYVDSHVLYYRTDIAEQAgwdhapETLDELK 182
Cdd:cd13524    62 DVVEIDTIFLGHLvdAGYLLPFGIDQA-RDYLPFALQAVSRNGEVYGVPQLLCTNLLFYRSPDLGQA------TDIASLY 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 183 QMAEDVkQVDGVenGMYISPSGadSWqgTLWAFFSSgvSLMDDEDNWTLDT---PEMHEATEYIDGF-------FKDGIT 252
Cdd:cd13524   135 KKIGTS-HPSGK--GLLINLAG--SW--TLASMYLD--ALIDVTGQYTLYDalpDLEPLDAKVIASLrqlvnscLMAGVN 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 253 GTnLDVTPGVS---ITQFVNGETPIMTGGPTTISQIADQGGDPDTYATAVIPKGVSSTSFVGGADFVVMDEAAN--PEAG 327
Cdd:cd13524   206 PC-QYGTDGDSyvrVEWFAKGSARAFIGYSERLMRMRKAGDYVEQLRVKSIPLGTGDIPLFFTDALVVNSKCAGtcPELA 284

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772005 328 WKFIQWMTEPETQVEWYKTATV---------LPSSQSAWEDEVLAGDEKLVAYGEQLEST-----QAPPAVPTWAQVSA 392
Cdd:cd13524   285 KKLANFMASDDVVEQALRARDDgdgavprylLPATHSVFEAEPAADDPLYSELRQLVSGArpypfRLGPEVRTWLQDAK 363
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 73-338 2.84e-03

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


Pssm-ID: 270299 [Multi-domain]  Cd Length: 490  Bit Score: 40.00  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005  73 EENPDVNITVTAIPWASAHDKIQTAIAAGTVPDVIQMGTTWMA---------------DFADAFAP-VPENFDLSDFSAG 136
Cdd:cd13581    27 EEKTGIKIEWETVPEDAWAEKKNLMLASGDLPDAFLGAGASDAdlmtygkqglflpleDLIDKYAPnLKALFDENPDIKA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 137 PLEAgqVNGEQLGVPWY------VDSHVLYYRTDIAEQAGWDhAPETLDELKQMAEDVKQVDGVENG------MYISPsG 204
Cdd:cd13581   107 AITA--PDGHIYALPSVnecyhcSYGQRMWINKKWLDKLGLE-MPTTTDELYEVLKAFKEQDPNGNGkadeipLSFSG-L 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 205 ADSWQGTLWAFFSSGVSLMDDEDN----------WTLDTPEMHEATEYIDGFFKDGItgtnLDvtPGvSITQ-------F 267
Cdd:cd13581   183 NGGTDDPAFLLNSFGINDGGYGGYgfvvkdgkviYTATDPEYKEALAYLNKLYKEGL----ID--PE-AFTQdydqlaaK 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772005 268 VNGETPImTGGPTTISQIADQGGDP-DTYATAVIPKG--------VSSTSFVGGADFVVMDEAANPEAGWKFIQWMTEPE 338
Cdd:cd13581   256 GKASTAK-VGVFFGWDPGLFFGEERyEQYVPLPPLKGpngdqlawVGNSSGYGRGGFVITSKNKNPEAAIRWADFLYSPE 334
 
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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