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Conserved domains on  [gi|1906334857|ref|WP_189103692|]
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sugar ABC transporter substrate-binding protein [Deinococcus knuensis]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 10194401)

ABC transporter substrate-binding protein functions as the initial receptor in the active transport of one or more from a variety of substrates including sugars and contains type 2 periplasmic binding fold

CATH:  3.40.190.10
Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
PubMed:  26517916|24638992|25750732
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 23-405 6.32e-73

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: 233.07  E-value: 6.32e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  23 LEFWTISlAPLFNDEMNRLVTQFEKENPTVDLKWVDVPATAIEQKLLAAVAAGRPPAAVNLSSDMSVKLVQQGALEPLTL 102
Cdd:cd13585     2 LTFWDWG-QPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 103 T---DAQKKLYFASPLSTFTFDGKVMGVPWYWSPKVVAYNTEIFRKAGLDPAnPPRTIQTLIAAAKQIKD-RTGLYGFMP 178
Cdd:cd13585    81 YiekDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPK-PPWTWDELLEAAKKLTDkKGGQYGFAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 179 NINGIN---MLYLFQEAGLPVLDKSGSRAVFNSPEHVQLLTTYVDLYKKGYIPEDTMrRGFTAATELYSAGKLAMLITGP 255
Cdd:cd13585   160 RGGSGGqtqWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGVAPSSAT-TGGDEAVDLFASGKVAMMIDGP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 256 QFILRVENDNksIYGVTKVAPYPIN-IAGNVIHTGLMGFMVPKGVKDKALAQKLALFLTNDANQLQFSRVTKTTFPSTvk 334
Cdd:cd13585   239 WALGTLKDSK--VKFKWGVAPLPAGpGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAA-- 314

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906334857 335 ASTDKFFKQGGADAVSQGRLVASTELKKAkdltLIYPDASKLNKVFKDNIESAMAGQ--KTPKQALDDIVKAW 405
Cdd:cd13585   315 AAASAAAPDAKPALALAAAADALAAAVPP----PVPPPWPEVYPILSEALQEALLGAlgKSPEEALKEAAKEI 383
 
Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 23-405 6.32e-73

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: 233.07  E-value: 6.32e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  23 LEFWTISlAPLFNDEMNRLVTQFEKENPTVDLKWVDVPATAIEQKLLAAVAAGRPPAAVNLSSDMSVKLVQQGALEPLTL 102
Cdd:cd13585     2 LTFWDWG-QPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 103 T---DAQKKLYFASPLSTFTFDGKVMGVPWYWSPKVVAYNTEIFRKAGLDPAnPPRTIQTLIAAAKQIKD-RTGLYGFMP 178
Cdd:cd13585    81 YiekDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPK-PPWTWDELLEAAKKLTDkKGGQYGFAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 179 NINGIN---MLYLFQEAGLPVLDKSGSRAVFNSPEHVQLLTTYVDLYKKGYIPEDTMrRGFTAATELYSAGKLAMLITGP 255
Cdd:cd13585   160 RGGSGGqtqWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGVAPSSAT-TGGDEAVDLFASGKVAMMIDGP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 256 QFILRVENDNksIYGVTKVAPYPIN-IAGNVIHTGLMGFMVPKGVKDKALAQKLALFLTNDANQLQFSRVTKTTFPSTvk 334
Cdd:cd13585   239 WALGTLKDSK--VKFKWGVAPLPAGpGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAA-- 314

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906334857 335 ASTDKFFKQGGADAVSQGRLVASTELKKAkdltLIYPDASKLNKVFKDNIESAMAGQ--KTPKQALDDIVKAW 405
Cdd:cd13585   315 AAASAAAPDAKPALALAAAADALAAAVPP----PVPPPWPEVYPILSEALQEALLGAlgKSPEEALKEAAKEI 383
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 19-409 1.68e-68

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 221.07  E-value: 1.68e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  19 QKTQLEFWTISlaPLFNDEMNRLVTQFEKENPTVDLKWVDVPATAIEQKLLAAVAAGRPPAAVNLSSDMSVKLVQQGALE 98
Cdd:COG1653    31 GKVTLTVWHTG--GGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALV 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  99 PLT----LTDAQKKLYFASPLSTFTFDGKVMGVPWYWSPKVVAYNTEIFRKAGLDpanPPRTIQTLIAAAKQIKDRTGLY 174
Cdd:COG1653   109 PLDdlldDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLD---PPKTWDELLAAAKKLKAKDGVY 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 175 GF-MPNINGINMLYLFQEAGLPVLDKSGsRAVFNSPEHVQLLTTYVDLYKKGYIPEDTMRRGFTAATELYSAGKLAMLIT 253
Cdd:COG1653   186 GFaLGGKDGAAWLDLLLSAGGDLYDEDG-KPAFDSPEAVEALEFLKDLVKDGYVPPGALGTDWDDARAAFASGKAAMMIN 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 254 GPQFILRVENDNKSI-YGvtkVAPYPINIAGNVIHT--GLMGFMVPKGVKDKALAQKLALFLTNDANQLQFsrvtkttfp 330
Cdd:COG1653   265 GSWALGALKDAAPDFdVG---VAPLPGGPGGKKPASvlGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQAKW--------- 332

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906334857 331 stvkastdkffkqggadavsqgrlvastelkkakdltliypdasklnkvfkDNIESAMAGQKTPKQALDDIVKAWNASL 409
Cdd:COG1653   333 ---------------------------------------------------DALQAVLLGQKTPEEALDAAQAAANAAL 360
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 38-318 2.71e-28

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: 112.89  E-value: 2.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  38 MNRLVTQFEKENPTVDLKWVDVPATAIEQKLLAAVAAGRPPAAV-NLSSDMSVKLVQQGALEPLTlTDAQKKLYFaspls 116
Cdd:pfam01547  10 LQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPADVfASDNDWIAELAKAGLLLPLD-DYVANYLVL----- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 117 tftFDGKVMGVPWYWSPKVVAYNTEIFRKAGLDpanPPRTIQTLIAAAKQIKDRTGLY-----GFMPNINGINMLYLFQE 191
Cdd:pfam01547  84 ---GVPKLYGVPLAAETLGLIYNKDLFKKAGLD---PPKTWDELLEAAKKLKEKGKSPggaggGDASGTLGYFTLALLAS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 192 AGLPVLDKSGsrAVFNSPEHVQLLTTYVDLY-----KKGYIPEDTMRRGFTAATELYSAGKLAMLITGPQFILRV----- 261
Cdd:pfam01547 158 LGGPLFDKDG--GGLDNPEAVDAITYYVDLYakvllLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAAnkvkl 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1906334857 262 -ENDNKSIYGVTKVAPYPINIAGNVIHTGLMGFMVPKGVKDKALAQKLALFLTNDANQ 318
Cdd:pfam01547 236 kVAFAAPAPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQ 293
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
21-409 3.58e-17

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 82.93  E-value: 3.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  21 TQLEFWTiSLAPLFNDEMNRLVTQFEKENPtvDLKWVDVPATAIEQKLLAAVAA---GRPPAAVNLSSDMSVKLVQQGAL 97
Cdd:PRK10974   26 TEIPFWH-SMEGELGKEVDSLAQRFNASQP--DYKIVPVYKGNYEQSLAAGIAAfrsGNAPAILQVYEVGTATMMASKAI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  98 EPLT--LTDAQKKL---YFASPLSTFTFDGK---VMGVPWYWSPKVVAYNTEIFRKAGLDPANPPRTIQTLIAAAKQIKD 169
Cdd:PRK10974  103 KPVYdvFKDAGIPFdesQFVPTVAGYYSDAKtghLLSQPFNSSTPVLYYNKDAFKKAGLDPEQPPKTWQDLAAYAAKLRA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 170 RTGLYGFMPNINGINMLYLFQE-AGLPVLDKS----GSRAV--FNSPE---HVQLLTtyvDLYKKGyipedtmrrGFT-- 237
Cdd:PRK10974  183 AGMKCGYASGWQGWIQLENFSAwHGLPFASKNngfdGTDAVleFNKPEqvkHIALLE---EMNKKG---------DFTyv 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 238 ----AATELYSAGKLAMLITGPQFILRVENDNKSIYGVTkVAPYPINIAG---NVIhTGLMGFMVPKGvKDKA----LAQ 306
Cdd:PRK10974  251 grkdESTEKFYNGDCAITTASSGSLANIRKYAKFNYGVG-MMPYDADVKGapqNAI-IGGASLWVMQG-KDKEtykgVAK 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 307 KLAlFLTNDANQLQFSRvtKTTFPSTVKASTDKFFKQG------GAD-AVSQgrLVASTELKKAKDLTLiyPDASKLNKV 379
Cdd:PRK10974  328 FLD-FLAKPENAAEWHQ--KTGYLPITTAAYDLTREQGfyeknpGADtATRQ--MLNKPPLPFTKGLRL--GNMPQIRTI 400

                         410       420       430
                  ....*....|....*....|....*....|
gi 1906334857 380 FKDNIESAMAGQKTPKQALDDIVKAWNASL 409
Cdd:PRK10974  401 VDEELESVWTGKKTPQQALDSAVERGNQLL 430
 
Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 23-405 6.32e-73

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: 233.07  E-value: 6.32e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  23 LEFWTISlAPLFNDEMNRLVTQFEKENPTVDLKWVDVPATAIEQKLLAAVAAGRPPAAVNLSSDMSVKLVQQGALEPLTL 102
Cdd:cd13585     2 LTFWDWG-QPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 103 T---DAQKKLYFASPLSTFTFDGKVMGVPWYWSPKVVAYNTEIFRKAGLDPAnPPRTIQTLIAAAKQIKD-RTGLYGFMP 178
Cdd:cd13585    81 YiekDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPK-PPWTWDELLEAAKKLTDkKGGQYGFAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 179 NINGIN---MLYLFQEAGLPVLDKSGSRAVFNSPEHVQLLTTYVDLYKKGYIPEDTMrRGFTAATELYSAGKLAMLITGP 255
Cdd:cd13585   160 RGGSGGqtqWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGVAPSSAT-TGGDEAVDLFASGKVAMMIDGP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 256 QFILRVENDNksIYGVTKVAPYPIN-IAGNVIHTGLMGFMVPKGVKDKALAQKLALFLTNDANQLQFSRVTKTTFPSTvk 334
Cdd:cd13585   239 WALGTLKDSK--VKFKWGVAPLPAGpGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAA-- 314

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906334857 335 ASTDKFFKQGGADAVSQGRLVASTELKKAkdltLIYPDASKLNKVFKDNIESAMAGQ--KTPKQALDDIVKAW 405
Cdd:cd13585   315 AAASAAAPDAKPALALAAAADALAAAVPP----PVPPPWPEVYPILSEALQEALLGAlgKSPEEALKEAAKEI 383
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 19-409 1.68e-68

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 221.07  E-value: 1.68e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  19 QKTQLEFWTISlaPLFNDEMNRLVTQFEKENPTVDLKWVDVPATAIEQKLLAAVAAGRPPAAVNLSSDMSVKLVQQGALE 98
Cdd:COG1653    31 GKVTLTVWHTG--GGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALV 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  99 PLT----LTDAQKKLYFASPLSTFTFDGKVMGVPWYWSPKVVAYNTEIFRKAGLDpanPPRTIQTLIAAAKQIKDRTGLY 174
Cdd:COG1653   109 PLDdlldDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLD---PPKTWDELLAAAKKLKAKDGVY 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 175 GF-MPNINGINMLYLFQEAGLPVLDKSGsRAVFNSPEHVQLLTTYVDLYKKGYIPEDTMRRGFTAATELYSAGKLAMLIT 253
Cdd:COG1653   186 GFaLGGKDGAAWLDLLLSAGGDLYDEDG-KPAFDSPEAVEALEFLKDLVKDGYVPPGALGTDWDDARAAFASGKAAMMIN 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 254 GPQFILRVENDNKSI-YGvtkVAPYPINIAGNVIHT--GLMGFMVPKGVKDKALAQKLALFLTNDANQLQFsrvtkttfp 330
Cdd:COG1653   265 GSWALGALKDAAPDFdVG---VAPLPGGPGGKKPASvlGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQAKW--------- 332

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906334857 331 stvkastdkffkqggadavsqgrlvastelkkakdltliypdasklnkvfkDNIESAMAGQKTPKQALDDIVKAWNASL 409
Cdd:COG1653   333 ---------------------------------------------------DALQAVLLGQKTPEEALDAAQAAANAAL 360
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 22-404 3.02e-60

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: 200.21  E-value: 3.02e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  22 QLEFWTiSLAPLFNDEMNRLVTQFEKENPTVDLKWVDVP-ATAIEQKLLAAVAAGRPPAAVNLSSDMSVKLVQQGALEPL 100
Cdd:cd14748     1 EITFWH-GMSGPDGKALEELVDEFNKSHPDIKVKAVYQGsYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 101 T-LTDAQK---KLYFASPLSTFTFDGKVMGVPWYWSPKVVAYNTEIFRKAGLDPANPPRTIQTLIAAAKQIKD---RTGL 173
Cdd:cd14748    80 DdYIDKDGvddDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKDkggKTGR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 174 YGFMPNINGINMLY--LFQEAGLPVLDKSGSRAVFNSPEHVQLLTTYVDLY-KKGYIPEDTMrrgfTAATELYSAGKLAM 250
Cdd:cd14748   160 YGFALPPGDGGWTFqaLLWQNGGDLLDEDGGKVTFNSPEGVEALEFLVDLVgKDGVSPLNDW----GDAQDAFISGKVAM 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 251 LITGPQFILRVENDNKSI-YGVTKVaPYPINIAGNVIHTGlMGFMVPKGV-KDKALAQKLALFLTNDANQLQFSrvTKTT 328
Cdd:cd14748   236 TINGTWSLAGIRDKGAGFeYGVAPL-PAGKGKKGATPAGG-ASLVIPKGSsKKKEAAWEFIKFLTSPENQAKWA--KATG 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906334857 329 FPSTVKASTDKFFKQGGADAVSQgrlVASTELKKAKDLTLIYPDASKLNKVFKDNIESAMAGQKTPKQALDDIVKA 404
Cdd:cd14748   312 YLPVRKSAAEDPEEFLAENPNYK---VAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEK 384
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
38-409 2.27e-48

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 169.36  E-value: 2.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  38 MNRLVTQFEKEnPTVDLKWVDVPATAIEQKLLAAVAAGRPPAAVNLSSDMSVKLVQQGALEPLTLTDAQKKLYFASPLST 117
Cdd:COG2182    53 LEEAAAAFEEE-PGIKVKVVEVPWDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLADKDDFLPAALDA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 118 FTFDGKVMGVPWYWSPKVVAYNTEIFrkagldPANPPRTIQTLIAAAKQIKDrTGLYGFMPNINGINMLYLFQEA-GLPV 196
Cdd:COG2182   132 VTYDGKLYGVPYAVETLALYYNKDLV------KAEPPKTWDELIAAAKKLTA-AGKYGLAYDAGDAYYFYPFLAAfGGYL 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 197 LDKSGSRA---VFNSPEHVQLLTTYVDLYKKGYIPEDTmrrGFTAATELYSAGKLAMLITGPQFILRVENDNKSIYGvtk 273
Cdd:COG2182   205 FGKDGDDPkdvGLNSPGAVAALEYLKDLIKDGVLPADA---DYDAADALFAEGKAAMIINGPWAAADLKKALGIDYG--- 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 274 VAPYPINIAGNVIHT--GLMGFMVPKGVKDKALAQKLALFLTNDANQLQFSRVTKTTfPSTVKASTDKFFK-----QGGA 346
Cdd:COG2182   279 VAPLPTLAGGKPAKPfvGVKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALFEATGRI-PANKAAAEDAEVKadpliAAFA 357

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906334857 347 DAVSQGRLVASTelkkakdltliyPDASKLNKVFKDNIESAMAGQKTPKQALDDIVKAWNASL 409
Cdd:COG2182   358 EQAEYAVPMPNI------------PEMGAVWTPLGTALQAIASGKADPAEALDAAQKQIEAAI 408
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 36-349 5.30e-43

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: 154.78  E-value: 5.30e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  36 DEMNRLVTQFEKENPTVDLKWVDVPATAIEQKLLAAVAAGRPPAAVNLSSDMSVKLVQQGALEPLT---LTDAQKKLYFA 112
Cdd:cd14747    14 ELLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMGALEDLTpylEDLGGDKDLFP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 113 SPLSTFTFDGKVMGVPWYWSPKVVAYNTEIFRKAGldPANPPRTIQTLIAAAKQIKDRTG-LYGFMPNINGIN----MLY 187
Cdd:cd14747    94 GLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAG--GDEAPKTWDELEAAAKKIKADGPdVSGFAIPGKNDVwhnaLPF 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 188 LFQeAGLPVLDKSGSRAVFNSPEHVQLLTTYVDLYKKGYIPEDTMRRGfTAATELYSAGKLAMLITGPQFILRVENDNKS 267
Cdd:cd14747   172 VWG-AGGDLATKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENS-ADVEQAFANGKVAMIISGPWEIGAIREAGPD 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 268 IYGVTKVAPYPiniAGN-VIHTGLMG---FMVPKGVKDKALAQKLALFLTNDANQLQFSRVTKtTFPSTVKASTDKFFKQ 343
Cdd:cd14747   250 LAGKWGVAPLP---GGPgGGSPSFAGgsnLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATG-MLPANTSAWDDPSLAN 325


                  ....*.
gi 1906334857 344 GGADAV 349
Cdd:cd14747   326 DPLLAV 331
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 23-406 1.73e-40

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: 147.53  E-value: 1.73e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  23 LEFWTIslaplFNDE----MNRLVTQFEKENPTVDLKWVDVPATAIEQKLLAAVAAGRPPAAVNLSSDMSVKLVQQGALE 98
Cdd:cd14751     2 ITFWHT-----SSDEekvlYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  99 PL--TLTDAQKKLYFASPLSTFTFDGKVMGVPWYWSPKVVAYNTEIFRKAGLDpanPPRTIQTLIAAAKQIKDRTGLYGF 176
Cdd:cd14751    77 PLdgTPAFDDIVDYLPGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTE---VPKTMDELVAAAKAIKKKKGRYGL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 177 M-PNINGINMLYLFQEAGLPVLDKSGSRAVFNSPEHVQLLTTYVDLYKKGYIpEDTMRRGFTAATELYSAGKLAMLITGP 255
Cdd:cd14751   154 YiSGDGPYWLLPFLWSFGGDLTDEKKATGYLNSPESVRALETIVDLYDEGAI-TPCASGGYPNMQDGFKSGRYAMIVNGP 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 256 QFILRV----ENDNKSIYGvtkVAPYPINIAGNVIHTGLMGFMVPKGVKDKALAQKLALFLTNDANQLQFSRVTKtTFPs 331
Cdd:cd14751   233 WAYADIlggkEFKDPDNLG---IAPVPAGPGGSGSPVGGEDLVIFKGSKNKDAAWKFVKFMSSAEAQALTAAKLG-LLP- 307

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906334857 332 TVKASTDkffkqggADAVSQGRLVAS--TELKKAKDLTLIyPDASKLNKVFKDNIESAMAGQKTPKQALDDIVKAWN 406
Cdd:cd14751   308 TRTSAYE-------SPEVANNPMVAAfkPALETAVPRPPI-PEWGELFEPLTLAFAKVLRGEKSPREALDEAAKQWD 376
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 23-407 3.04e-40

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: 147.14  E-value: 3.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  23 LEFWTISLAPLFNDEMNRLVTQFEKENPTVDLKWVDVPATAIEQKLLAAVAAGRPPAAVNL-SSDMSVKLVQQGALEPLT 101
Cdd:cd14749     2 ITYWQYFTGDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLwPGGWLAEFVKAGLLLPLT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 102 LT---DAQKKLYFASPLSTFTFDGKVMGVPWYWSPKVVAYNTEIFRKAGldPANPPRTIQTLIAAAKQIKDRT------G 172
Cdd:cd14749    82 DYldpNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAG--GVKPPKTWDELIEAAKKDKFKAkgqtgfG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 173 LYGFMPNINGINMLYLFQEAGLPVLDKSGSRAVFNSPEHVQLLTTYVDLYKKGYIPEDTMRRGFTAATELYSAGKLAMLI 252
Cdd:cd14749   160 LLLGAQGGHWYFQYLVRQAGGGPLSDDGSGKATFNDPAFVQALQKLQDLVKAGAFQEGFEGIDYDDAGQAFAQGKAAMNI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 253 TGPQFI--LRVENDNKSIygvtKVAPYPINIAGNVIHT---GLMGFMVPKGVKDKALAQKLALFLTNDANQLQFSrVTKT 327
Cdd:cd14749   240 GGSWDLgaIKAGEPGGKI----GVFPFPTVGKGAQTSTiggSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQYL-EDVG 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 328 TFPSTVKASTDKffkqGGADAVSQGRLVASteLKKAKDLTLIYPDASKLNKVFKDNIESAMAGQKTPKQALDDIVKAWNA 407
Cdd:cd14749   315 LLPAKEVVAKDE----DPDPVAILGPFADV--LNAAGSTPFLDEYWPAAAQVHKDAVQKLLTGKIDPEQVVKQAQSAAAK 388
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 35-405 3.08e-32

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: 125.10  E-value: 3.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  35 NDEMNRLVTQFEKENPtVDLKWVDVPATAIEQKLLAAVAAGRPPAAVNLSSDMSVKLVQQGALEPLTLTDAQKKLYFASP 114
Cdd:cd13586    12 LEYLKELAEEFEKKYG-IKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLAVKIKNLPVA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 115 LSTFTFDGKVMGVPwyWSPKVVA--YNTEIFrkagldpANPPRTIQTLIAAAKQIKDRTG-LYGFMPNINGINMLY-LFQ 190
Cdd:cd13586    91 LAAVTYNGKLYGVP--VSVETIAlfYNKDLV-------PEPPKTWEELIALAKKFNDKAGgKYGFAYDQTNPYFSYpFLA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 191 EAGLPVLDKSGSRAV---FNSPEHVQLLTTYVDLYKK-GYIPEDTmrrGFTAATELYSAGKLAMLITGPQFI--LRVEND 264
Cdd:cd13586   162 AFGGYVFGENGGDPTdigLNNEGAVKGLKFIKDLKKKyKVLPPDL---DYDIADALFKEGKAAMIINGPWDLadYKDAGI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 265 NksiYGvtkVAPYPiNIAGNV---IHTGLMGFMVPKGVKDKALAQKLALFLTNDANQLQFSRVTKtTFPSTVKASTDKFF 341
Cdd:cd13586   239 N---FG---VAPLP-TLPGGKqaaPFVGVQGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTG-RIPALKDALNDAAV 310

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906334857 342 KqggadavSQGRLVASTELKKAKDLTLIYPDASKLNKVFKDNIESAMAGQKTPKQALDDIVKAW 405
Cdd:cd13586   311 K-------NDPLVKAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEEAAKDAVAAI 367
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 27-404 4.27e-31

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: 122.40  E-value: 4.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  27 TISLA----PLFNDEMNRLVTQFEKENPTVDLKWVDVPATAIEQ--KLLAAVAAGRPPAAVnLSSDM--SVKLVQQGALE 98
Cdd:cd14750     1 TITFAagsdGQEGELLKKAIAAFEKKHPDIKVEIEELPASSDDQrqQLVTALAAGSSAPDV-LGLDViwIPEFAEAGWLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  99 PLTLTDAQKKL--YFASPLSTFTFDGKVMGVPWYWSPKVVAYNTEIFRKAGldpANPPRTIQTLIAAAKQIKdrtglyGF 176
Cdd:cd14750    80 PLTEYLKEEEDddFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYG---PEPPKTWDELLEAAKKRK------AG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 177 MPNINGINMlYLFQEAGLP-------------VLDKSGSRAVFNSPEHVQLLTTYVDLYKKGYIPEDTMRRGFTAATELY 243
Cdd:cd14750   151 EPGIWGYVF-QGKQYEGLVcnflellwsnggdIFDDDSGKVTVDSPEALEALQFLRDLIGEGISPKGVLTYGEEEARAAF 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 244 SAGKLAMLITGPqFILRVENDNKS-IYGVTKVAPYPINIAGNviHTGLMG---FMVPKGVKDKALAQKLALFLTNDANQL 319
Cdd:cd14750   230 QAGKAAFMRNWP-YAYALLQGPESaVAGKVGVAPLPAGPGGG--SASTLGgwnLAISANSKHKEAAWEFVKFLTSPEVQK 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 320 QFsRVTKTTFPSTVKASTDKFFKqggADAVSQGRLVASTELKKAKDLTLIYPDASKlnkVFKDNIESAMAGQKTPKQALD 399
Cdd:cd14750   307 RR-AINGGLPPTRRALYDDPEVL---EAYPFLPALLEALENAVPRPVTPKYPEVST---AIQIALSAALSGQATPEEALK 379


                  ....*
gi 1906334857 400 DIVKA 404
Cdd:cd14750   380 QAQEK 384
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 38-318 2.71e-28

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: 112.89  E-value: 2.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  38 MNRLVTQFEKENPTVDLKWVDVPATAIEQKLLAAVAAGRPPAAV-NLSSDMSVKLVQQGALEPLTlTDAQKKLYFaspls 116
Cdd:pfam01547  10 LQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPADVfASDNDWIAELAKAGLLLPLD-DYVANYLVL----- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 117 tftFDGKVMGVPWYWSPKVVAYNTEIFRKAGLDpanPPRTIQTLIAAAKQIKDRTGLY-----GFMPNINGINMLYLFQE 191
Cdd:pfam01547  84 ---GVPKLYGVPLAAETLGLIYNKDLFKKAGLD---PPKTWDELLEAAKKLKEKGKSPggaggGDASGTLGYFTLALLAS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 192 AGLPVLDKSGsrAVFNSPEHVQLLTTYVDLY-----KKGYIPEDTMRRGFTAATELYSAGKLAMLITGPQFILRV----- 261
Cdd:pfam01547 158 LGGPLFDKDG--GGLDNPEAVDAITYYVDLYakvllLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAAnkvkl 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1906334857 262 -ENDNKSIYGVTKVAPYPINIAGNVIHTGLMGFMVPKGVKDKALAQKLALFLTNDANQ 318
Cdd:pfam01547 236 kVAFAAPAPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQ 293
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 41-346 1.44e-26

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 107.49  E-value: 1.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  41 LVTQFEKENPtVDLKWVDVPATAIEQKLLAAVAAGRPPAA--VNLSSDMSVKLVQQGALEPLTLTDAQKKLYFAspLSTF 118
Cdd:pfam13416   2 LAKAFEKKTG-VTVEVEPQASNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLADLSDVDNLDDLPDA--LDAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 119 TFDGKVMGVPWYWS-PKVVAYNTEIFRKAGLDPAnpprTIQTLIAAAKQIKDRTGLYGfmpniNGINMLYLFQEAGLPVL 197
Cdd:pfam13416  79 GYDGKLYGVPYAAStPTVLYYNKDLLKKAGEDPK----TWDELLAAAAKLKGKTGLTD-----PATGWLLWALLADGVDL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 198 DKSGSRAvfnsPEHVQLLTTYVDLYKKGYIPEDtmrrgFTAATELYSAGKLAMLITGPQFILRVENDNKsiygvtkvaPY 277
Cdd:pfam13416 150 TDDGKGV----EALDEALAYLKKLKDNGKVYNT-----GADAVQLFANGEVAMTVNGTWAAAAAKKAGK---------KL 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 278 PINIAGNVIHTGLMGFMVPKGVKDKAL-AQKLALFLTNDANQLQFSRVTKtTFPSTVKASTDKFFKQGGA 346
Cdd:pfam13416 212 GAVVPKDGSFLGGKGLVVPAGAKDPRLaALDFIKFLTSPENQAALAEDTG-YIPANKSAALSDEVKADPA 280
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 42-403 1.69e-25

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: 106.41  E-value: 1.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  42 VTQFEKENpTVDLKWVDVPATAIEQKLLAAVAAGRPPAAVNLSSDMSVKLVQQGALEPLTLTDAQKKLYFASPLSTFTFD 121
Cdd:cd13658    19 AKQYTKKT-GVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSKDKKKGFTDQALKALTYD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 122 GKVMGVPWYWSPKVVAYNTEIFRkagldpaNPPRTIQTLIAAAKQIKDRTG-LYGFMPNINGINMLY-LFQEAGLPVLDK 199
Cdd:cd13658    98 GKLYGLPAAVETLALYYNKDLVK-------NAPKTFDELEALAKDLTKEKGkQYGFLADATNFYYSYgLLAGNGGYIFKK 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 200 SGSRAV-----FNSPEHVQLLTTYVDLYKKGYIPE----DTMRrgftaatELYSAGKLAMLITGPQFILRVEnDNKSIYG 270
Cdd:cd13658   171 NGSDLDindigLNSPGAVKAVKFLKKWYTEGYLPKgmtgDVIQ-------GLFKEGKAAAVIDGPWAIQEYQ-EAGVNYG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 271 vtkVAPYPINIAGNVIHT--GLMGFMVPKGVKDKALAQKLALFLTNDANqlQFSRVTKTT-FPSTVKASTDKFFKQGGad 347
Cdd:cd13658   243 ---VAPLPTLPNGKPMAPflGVKGWYLSAYSKHKEWAQKFMEFLTSKEN--LKKRYDETNeIPPRKDVRSDPEIKNNP-- 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1906334857 348 avsqgrlVASTELKKAKDlTLIYPDASKLNKVF---KDNIESAMAGQKTPKQALDDIVK 403
Cdd:cd13658   316 -------LTSAFAKQASR-AVPMPNIPEMGAVWepaNNALFFILSGKKTPKQALNDAVN 366
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 25-404 3.55e-20

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: 91.32  E-value: 3.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  25 FWtISLAPLFNDEMNRLVTQFEKENPTVDLKWVDVPATAIEQKLLAAVAAGRPPAAVNLSSDMSVKLVQQGALEPLTLTD 104
Cdd:cd13522     4 VW-HQYDTGENQAVNELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDEYV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 105 AQKKLYFASPLSTFTFDGKVMGVPWYWSPKVVAYNTEIFrkagldPANPPRTIQTLIAAAKQIKDRtGLYGFMPNINGIN 184
Cdd:cd13522    83 SKSGKYAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLV------PKNPPKTWQELIALAQGLKAK-NVWGLVYNQNEPY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 185 MLYLFQEA-GLPVLDKSGSRAV--FNSPEHVQLLTTYVDL-YKKGYIPEDTmrrGFTAATELYSAGKLAMLITGPQFILR 260
Cdd:cd13522   156 FFAAWIGGfGGQVFKANNGKNNptLDTPGAVEALQFLVDLkSKYKIMPPET---DYSIADALFKAGKAAMIINGPWDLGD 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 261 VENDNKSIYGvtkVAPYPI--NIAGNVIHTGLMGFMVPKGVKDKALAQKLALFLTNDANQLQFSRVTKtTFPSTVKASTd 338
Cdd:cd13522   233 YRQALKINLG---VAPLPTfsGTKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAG-DIPANLQAYE- 307

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906334857 339 kffkqggaDAVSQGRLVASTELKKAKDLTL--IYPDASKLNKVFKDNIESAMAGQKTPKQALDDIVKA 404
Cdd:cd13522   308 --------SPAVQNKPAQKASAEQAAYGVPmpNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQQE 367
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
21-409 3.58e-17

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 82.93  E-value: 3.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  21 TQLEFWTiSLAPLFNDEMNRLVTQFEKENPtvDLKWVDVPATAIEQKLLAAVAA---GRPPAAVNLSSDMSVKLVQQGAL 97
Cdd:PRK10974   26 TEIPFWH-SMEGELGKEVDSLAQRFNASQP--DYKIVPVYKGNYEQSLAAGIAAfrsGNAPAILQVYEVGTATMMASKAI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  98 EPLT--LTDAQKKL---YFASPLSTFTFDGK---VMGVPWYWSPKVVAYNTEIFRKAGLDPANPPRTIQTLIAAAKQIKD 169
Cdd:PRK10974  103 KPVYdvFKDAGIPFdesQFVPTVAGYYSDAKtghLLSQPFNSSTPVLYYNKDAFKKAGLDPEQPPKTWQDLAAYAAKLRA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 170 RTGLYGFMPNINGINMLYLFQE-AGLPVLDKS----GSRAV--FNSPE---HVQLLTtyvDLYKKGyipedtmrrGFT-- 237
Cdd:PRK10974  183 AGMKCGYASGWQGWIQLENFSAwHGLPFASKNngfdGTDAVleFNKPEqvkHIALLE---EMNKKG---------DFTyv 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 238 ----AATELYSAGKLAMLITGPQFILRVENDNKSIYGVTkVAPYPINIAG---NVIhTGLMGFMVPKGvKDKA----LAQ 306
Cdd:PRK10974  251 grkdESTEKFYNGDCAITTASSGSLANIRKYAKFNYGVG-MMPYDADVKGapqNAI-IGGASLWVMQG-KDKEtykgVAK 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 307 KLAlFLTNDANQLQFSRvtKTTFPSTVKASTDKFFKQG------GAD-AVSQgrLVASTELKKAKDLTLiyPDASKLNKV 379
Cdd:PRK10974  328 FLD-FLAKPENAAEWHQ--KTGYLPITTAAYDLTREQGfyeknpGADtATRQ--MLNKPPLPFTKGLRL--GNMPQIRTI 400

                         410       420       430
                  ....*....|....*....|....*....|
gi 1906334857 380 FKDNIESAMAGQKTPKQALDDIVKAWNASL 409
Cdd:PRK10974  401 VDEELESVWTGKKTPQQALDSAVERGNQLL 430
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 46-322 1.31e-16

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: 81.22  E-value: 1.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  46 EKENPTVDLKWVdvPATAIEQKLLAAVAAGRPPAAVNLSSDM-SVKLVQQGALEPLT-----LTDAQKKLYFASPLSTFT 119
Cdd:cd13580    30 EKTNIDVKVKWV--PDSSYDEKLNLALASGDLPDIVVVNDPQlSITLVKQGALWDLTdyldkYYPNLKKIIEQEGWDSAS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 120 FDGKVMGVPWYWSPKvvAYNTEIFRKAGLDPAN--PPRTIQTLIAAAKQIKD-------RTGLYGFM-PNINGINMLYLF 189
Cdd:cd13580   108 VDGKIYGIPRKRPLI--GRNGLWIRKDWLDKLGleVPKTLDELYEVAKAFTEkdpdgngKKDTYGLTdTKDLIGSGFTGL 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 190 QEA-----GLPVLDKSGS-RAVFNSPEHVQLLTTYVDLYKKGYIPEDTMRRGFTAATELYSAGKLAMLITGPQFILRVEN 263
Cdd:cd13580   186 FGAfgappNNWWKDEDGKlVPGSIQPEMKEALKFLKKLYKEGLIDPEFAVNDGTKANEKFISGKAGIFVGNWWDPAWPQA 265

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906334857 264 DNKSIYGVTKVAPYPINI-----AGNVIHTGLMGF-MVPKGVKDKALAQKLALFLTNDANQLQFS 322
Cdd:cd13580   266 SLKKNDPDAEWVAVPIPSgpdgkYGVWAESGVNGFfVIPKKSKKPEAILKLLDFLSDPEVQKLLD 330
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 44-313 2.65e-16

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: 79.73  E-value: 2.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  44 QFEKENPTVDLKWVDVPATAIEQKLLAAVAAGRPPAAVNLSSDMSVKLVQQGALEPLT--LTDAQKKLYFASPLSTFTFD 121
Cdd:cd13657    22 EFEAKYPVPNVKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISdyLSEDDFENYLPTAVEAVTYK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 122 GKVMGVPWYWSPKVVAYNTEIFrkagldpANPPRTIQTLIAAAKQIKDR-TGLYGFMPNINGINMLYLFQEA-GLPVLDK 199
Cdd:cd13657   102 GKVYGLPEAYETVALIYNKALV-------DQPPETTDELLAIMKDHTDPaAGSYGLAYQVSDAYFVSAWIFGfGGYYFDD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 200 SGSRAVFNSPEHVQLLTTYVDlYKKGYIPEDTmrrGFTAATELYSAGKLAMLITGPQFILRVeNDNKSIYGvtkVAPYPI 279
Cdd:cd13657   175 ETDKPGLDTPETIKGIQFLKD-FSWPYMPSDP---SYNTQTSLFNEGKAAMIINGPWFIGGI-KAAGIDLG---VAPLPT 246

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1906334857 280 NIAGNVI--HTGLMGFMVPKGV--KDKALAQKLALFLT 313
Cdd:cd13657   247 VDGTNPPrpYSGVEGIYVTKYAerKNKEAALDFAKFFT 284
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 36-320 1.77e-13

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: 71.72  E-value: 1.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  36 DEMNRLVTQFEKENPTVDLKWVDVPATAIEQKLLAAVAAGRPPAAVNLS--SDMSVKLVQQGALEPLT-LTD------AQ 106
Cdd:cd13521    16 DDENWPVAKEIEKLTNVKLEIVAVTAATSQQKLNLMLASGDLPDIVGADylKDKFIAYGMEGAFLPLSkYIDqypnlkAF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 107 KKLYFASPLSTFTFDGKVMGVPwYWSPKVVAYNTEIFRKAGLDPAN--PPRTIQTLIAAAKQIKDRTglygfmPNING-- 182
Cdd:cd13521    96 FKQHPDVLRASTASDGKIYLIP-YEPPKDVPNQGYFIRKDWLDKLNlkTPKTLDELYNVLKAFKEKD------PNGNGka 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 183 -----INM-----LYLFQEAGLPVLDKSGS-----------RAVFNSPEHVQLLTTYVDLYKKGYIPEDTMRRGFTAATE 241
Cdd:cd13521   169 deipfIDRdplygAFRLINSWGARSAGGSTdsdwyedngkfKHPFASEEYKDGMKYMNKLYTEGLIDKESFTQKDDQAEQ 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 242 LYSAGKLAMLITGPQFILRVEND----NKSIYGvtkvaPYPINIAGNVI---------HTGLMGFMVPKGVKDKALAQKL 308
Cdd:cd13521   249 KFSNGKLGGFTHNWFASDNLFTAqlgkEKPMYI-----LLPIAPAGNVKgrreedspgYTGPDGVAISKKAKNPVAALKF 323

                         330
                  ....*....|..
gi 1906334857 309 ALFLTNDANQLQ 320
Cdd:cd13521   324 FDWLASEEGREL 335
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 65-400 3.55e-09

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: 57.99  E-value: 3.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  65 EQKLLAAVAAGRPPAAVNLSSDMSVKLVQQGALEPLTLTDAQKKLYFASPLSTFTFDGKVMGVPWYWSPKVVAYNTEIFR 144
Cdd:cd13656    40 EEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 145 kagldpaNPPRTIQTLIAAAKQIKDRtGLYGFMPNINGINMLYlfqeaglPVLDKSGSRAV-------------FNSPEH 211
Cdd:cd13656   120 -------NPPKTWEEIPALDKELKAK-GKSALMFNLQEPYFTW-------PLIAADGGYAFkyengkydikdvgVDNAGA 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 212 VQLLTTYVDLYKKGYIPEDTmrrGFTAATELYSAGKLAMLITGPQFILRVENdNKSIYGVTkvaPYPiNIAGNVIH--TG 289
Cdd:cd13656   185 KAGLTFLVDLIKNKHMNADT---DYSIAEAAFNKGETAMTINGPWAWSNIDT-SKVNYGVT---VLP-TFKGQPSKpfVG 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 290 LMGFMVPKGVKDKALAQKlalFLTNDANQLQFSRVTKTTFPSTVKASTdKFFKQGGADAvsqgrLVASTELKKAKDLTLI 369
Cdd:cd13656   257 VLSAGINAASPNKELAKE---FLENYLLTDEGLEAVNKDKPLGAVALK-SYEEELAKDP-----RIAATMENAQKGEIMP 327

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1906334857 370 -YPDASKLNKVFKDNIESAMAGQKTPKQALDD 400
Cdd:cd13656   328 nIPQMSAFWYAVRTAVINAASGRQTVDEALKD 359
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 42-146 3.04e-07

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: 51.53  E-value: 3.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  42 VTQFEKENP-TVDLKWVdvpatAIEQKLLAAV-AAGRPPAAVNLSSDMSVKLVQQGALEPL--TLTDAQKKLY--FASPL 115
Cdd:cd13588    16 VTAFEEATGcKVVVKFF-----GSEDEMVAKLrSGGGDYDVVTPSGDALLRLIAAGLVQPIdtSKIPNYANIDprLRNLP 90

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1906334857 116 StFTFDGKVMGVPWYWSPKVVAYNTEIFRKA 146
Cdd:cd13588    91 W-LTVDGKVYGVPYDWGANGLAYNTKKVKTP 120
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 38-338 2.76e-06

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: 48.88  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  38 MNRLVTQFEKENPTVDLKW---VDVPATAIEqKLLAAVAAGrppAAV-NLSSDMSVKLVQQGALEPLTLTDAQKKLYFAS 113
Cdd:cd13655    14 LKEMVDAFKEKHPEWKITItigVVGEADAKD-EVLKDPSAA---ADVfAFANDQLGELVDAGAIYPLTGSAVDKIKNTNS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 114 P--LSTFTFDGKVMGVPWYWSPKVVAYNTEIFRkagldpANPPRTIQTLIAAAKQIKDRTGlygfMPNINGINMLYLFQE 191
Cdd:cd13655    90 EatVDAVTYNGKLYGYPFTANTWFMYYDKSKLT------EDDVKSLDTMLAKAPDAKGKVS----FDLSNSWYLYAFFFG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 192 AGLPVLDKSGSRAV---FNSPEHVQLLTTYVDLYK-KGYIPEDTmrrgfTAATELYSAGKLAMLITGP---QFILRVEND 264
Cdd:cd13655   160 AGCKLFGNNGGDTAgcdFNNEKGVAVTNYLVDLVAnPKFVNDAD-----GDAISGLKDGTLGAGVSGPwdaANLKKALGD 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906334857 265 NksiYGVTKvapYP-INIAGNVIH----TGLMGFMVPKGVKDKALAQKLALFLTNDANQLQFSRVTKTTfPSTVKASTD 338
Cdd:cd13655   235 N---YAVAK---LPtYTLGGKDVQmksfAGYKAIGVNSNTKNPEAAMALADYLTNEESQLTRFEKRGIG-PTNKEAAES 306
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 47-302 5.30e-06

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: 48.51  E-value: 5.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  47 KENPTVDLKWVDVPATAIEQKLLAAVAAGRPPAAVN-LSSDMSVKLVQQGALEPLT--------LTDAQKKLYFASPLST 117
Cdd:cd13583    27 EEKTNVKFKRTPIPSSDYETKRSLLIASGDAPDIIPvLYPGEENEFVASGALLPISdyldympnYKKYVEKWGLGKELAT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 118 FTF-DGKVMGVPWYWSPKVV----AYNTEIFRKAGLDpanPPRTIQTLIAAAKQIKDRTG-LYGFMPNINGINML-YLFQ 190
Cdd:cd13583   107 GRQsDGKYYSLPGLHEDPGVqysfLYRKDIFEKAGIK---IPTTWDEFYAALKKLKEKYPdSYPYSDRWNSNALLlIAAP 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 191 EAGLP--------VLDKSGSRAVF--NSPEHVQLLTTYVDLYKKGYIPEDTMRRGFTAATELYSAGKLAMLITGPQFIL- 259
Cdd:cd13583   184 AFGTTagwgfsnyTYDPDTDKFVYgaTTDEYKDMLQYFNKLYAEGLLDPESFTQTDDQAKAKFLNGKSFVITTNPQTVDe 263

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1906334857 260 ---RVENDNKSIYGVTKVAPyPINIAGNVIHTGLM--GFMVPKGVKDK 302
Cdd:cd13583   264 lqrNLRAADGGNYEVVSITP-PAGPAGKAINGSRLenGFMISSKAKDS 310
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
41-146 3.30e-05

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 45.67  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  41 LVTQFEKE-NPTVDLKWVDVPATaieqkLLAAVAAGRPPA-AVNLSSDMSVKLVQQGALEPLTLTDAQ--KKLYfaSPLS 116
Cdd:COG0687    44 VLEPFEKEtGIKVVYDTYDSNEE-----MLAKLRAGGSGYdVVVPSDYFVARLIKAGLLQPLDKSKLPnlANLD--PRFK 116

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1906334857 117 TFTFD-GKVMGVPWYWSPKVVAYNTEIFRKA 146
Cdd:COG0687   117 DPPFDpGNVYGVPYTWGTTGIAYNTDKVKEP 147
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 32-312 4.25e-05

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


Pssm-ID: 270299 [Multi-domain]  Cd Length: 490  Bit Score: 45.39  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  32 PLFNDEMNRLVTQFEKENPTVDLKWVDVPATAIEQKLLAAVAAGRPPAAV---NLSSDMSVKLVQQGALEPLT-LTDAQ- 106
Cdd:cd13581    12 PLVEDYNENLFFKRLEEKTGIKIEWETVPEDAWAEKKNLMLASGDLPDAFlgaGASDADLMTYGKQGLFLPLEdLIDKYa 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 107 ---KKLYFASP----LSTFTfDGKVMGVPWY------WSPKVVAYNTEIFRKAGLDpanPPRTIQTLIAAAKQIKDRTgl 173
Cdd:cd13581    92 pnlKALFDENPdikaAITAP-DGHIYALPSVnecyhcSYGQRMWINKKWLDKLGLE---MPTTTDELYEVLKAFKEQD-- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 174 ygfmPNINGIN----------------MLYLFQEAGLPVLDKSGSRAV---------FNSPEHVQLLTTYVDLYKKGYIP 228
Cdd:cd13581   166 ----PNGNGKAdeiplsfsglnggtddPAFLLNSFGINDGGYGGYGFVvkdgkviytATDPEYKEALAYLNKLYKEGLID 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857 229 EDTmrrgFTAATELYSA-GKLAMLITGPQF----ILRVENDNKSIY----------GVTKV-APYPINIAGNvihtglmG 292
Cdd:cd13581   242 PEA----FTQDYDQLAAkGKASTAKVGVFFgwdpGLFFGEERYEQYvplpplkgpnGDQLAwVGNSSGYGRG-------G 310

                         330       340
                  ....*....|....*....|
gi 1906334857 293 FMVPKGVKDKALAQKLALFL 312
Cdd:cd13581   311 FVITSKNKNPEAAIRWADFL 330
PBP2_Fbp_like_2 cd13547
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 39-179 1.68e-04

Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270265 [Multi-domain]  Cd Length: 259  Bit Score: 42.98  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  39 NRLVTQFEKENPTVDLKWVDVPATAIEQKLLAAVAAGRPPAAVNLSSDMS--VKLVQQGALEPLTLTDAQKKLYFASPls 116
Cdd:cd13547    14 NALVEAFEKKYPGVKVEVFRAGTGKLMAKLAAEAEAGNPQADVLWVADPPtaEALKKEGLLLPYKSPEADAIPAPFYD-- 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906334857 117 tftFDGkvmgvPWYW---SPKVVAYNTEIFrkagldPANPPRTIQTLIAAAKqiKDRTGlygfMPN 179
Cdd:cd13547    92 ---KDG-----YYYGtrlSAMGIAYNTDKV------PEEAPKSWADLTKPKY--KGQIV----MPD 137
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 45-147 5.09e-03

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: 38.36  E-value: 5.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906334857  45 FEKENPTvdlKWVDVPATAIEQKLLAAVAAGRPPA-AVNLSSDMSVKLVQQGALEPLTltdaQKKLYFASPLSTFTFDGK 123
Cdd:cd13589    23 FEKETGI---KVVYDTGTSADRLAKLQAQAGNPQWdVVDLDDGDAARAIAEGLLEPLD----YSKIPNAAKDKAPAALKT 95

                          90       100
                  ....*....|....*....|....
gi 1906334857 124 VMGVPWYWSPKVVAYNTEIFRKAG 147
Cdd:cd13589    96 GYGVGYTLYSTGIAYNTDKFKEPP 119
 
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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