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Conserved domains on  [gi|495648618|ref|WP_008373197|]
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MULTISPECIES: ABC transporter substrate-binding protein [Coprococcus]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 10600506)

ABC transporter substrate-binding protein functions as the initial receptor in the transport of substrates like fatty acids, hydrophobic amino acids, or amino acid amides, including the branched-chain amino acids leucine, isoleucine, and valine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 59-379 5.17e-44

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


:

Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 155.26  E-value: 5.17e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618   59 QLAKDYTKETGVDVTVVTAASGNYETTLMSEMGKSGAPTL---FQVNGPVGLANWKDYCYDLSDSDIYKELTSDDYALKD 135
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQASNDLQAKLLAAAAAGNAPDLdvvWIAADQLATLAEAGLLADLSDVDNLDDLPDALDAAGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  136 GDSVAGIGYVIET-YGIITNKTLLKEAGytpDDIKSFADLKKVAEDITNRTselgfsaftsAGMDGSSDWRFKTHLAnlp 214
Cdd:pfam13416  81 DGKLYGVPYAASTpTVLYYNKDLLKKAG---EDPKTWDELLAAAAKLKGKT----------GLTDPATGWLLWALLA--- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  215 iyfeyqdEGINTTDAIKGT-YLDNYRDMWDLYINNSTCdpkdlaAKTGDDARNEFLNKKAVFYQNGTWEYTQLIDGGltd 293
Cdd:pfam13416 145 -------DGVDLTDDGKGVeALDEALAYLKKLKDNGKV------YNTGADAVQLFANGEVAMTVNGTWAAAAAKKAG--- 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  294 DDMTMLPIyfgvgdeaNQGLCTGTENyWCVNKDADEADiQATLDFMDWcVTSDEGTKCMADDMGFNIPFKKAQESQNlfI 373
Cdd:pfam13416 209 KKLGAVVP--------KDGSFLGGKG-LVVPAGAKDPR-LAALDFIKF-LTSPENQAALAEDTGYIPANKSAALSDE--V 275


                  ....*.
gi 495648618  374 KEDKQM 379
Cdd:pfam13416 276 KADPAL 281
 
Name Accession Description Interval E-value
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 59-379 5.17e-44

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 155.26  E-value: 5.17e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618   59 QLAKDYTKETGVDVTVVTAASGNYETTLMSEMGKSGAPTL---FQVNGPVGLANWKDYCYDLSDSDIYKELTSDDYALKD 135
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQASNDLQAKLLAAAAAGNAPDLdvvWIAADQLATLAEAGLLADLSDVDNLDDLPDALDAAGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  136 GDSVAGIGYVIET-YGIITNKTLLKEAGytpDDIKSFADLKKVAEDITNRTselgfsaftsAGMDGSSDWRFKTHLAnlp 214
Cdd:pfam13416  81 DGKLYGVPYAASTpTVLYYNKDLLKKAG---EDPKTWDELLAAAAKLKGKT----------GLTDPATGWLLWALLA--- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  215 iyfeyqdEGINTTDAIKGT-YLDNYRDMWDLYINNSTCdpkdlaAKTGDDARNEFLNKKAVFYQNGTWEYTQLIDGGltd 293
Cdd:pfam13416 145 -------DGVDLTDDGKGVeALDEALAYLKKLKDNGKV------YNTGADAVQLFANGEVAMTVNGTWAAAAAKKAG--- 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  294 DDMTMLPIyfgvgdeaNQGLCTGTENyWCVNKDADEADiQATLDFMDWcVTSDEGTKCMADDMGFNIPFKKAQESQNlfI 373
Cdd:pfam13416 209 KKLGAVVP--------KDGSFLGGKG-LVVPAGAKDPR-LAALDFIKF-LTSPENQAALAEDTGYIPANKSAALSDE--V 275


                  ....*.
gi 495648618  374 KEDKQM 379
Cdd:pfam13416 276 KADPAL 281
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 4-350 3.40e-36

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 136.33  E-value: 3.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618   4 KKRWLALGLVGIMTLgcfAGCGSKSDGKSADGkgdsSKGSVYYLNFKPEQDEQWQQLAKDYTKET-GVDVTVVTAASGNY 82
Cdd:COG1653    2 RRLALALAAALALAL---AACGGGGSGAAAAA----GKVTLTVWHTGGGEAAALEALIKEFEAEHpGIKVEVESVPYDDY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  83 ETTLMSEMGKSGAPTLFQVNGPvGLANW--KDYCYDLSDSDIYKELTSDDY------ALKDGDSVAGIGYVIETYGIITN 154
Cdd:COG1653   75 RTKLLTALAAGNAPDVVQVDSG-WLAEFaaAGALVPLDDLLDDDGLDKDDFlpgaldAGTYDGKLYGVPFNTDTLGLYYN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 155 KTLLKEAGYTPDdiKSFADLKKVAEDITNRTSELGFsaftsaGMDGSSDWRFKTHLANL--PIYFEYQDEGINTTDAIKG 232
Cdd:COG1653  154 KDLFEKAGLDPP--KTWDELLAAAKKLKAKDGVYGF------ALGGKDGAAWLDLLLSAggDLYDEDGKPAFDSPEAVEA 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 233 tyLDNYRDMWDLYINnstcdPKDLAAKTGDDARNEFLNKKAVFYQNGTWEYTQLIDGGlTDDDMTMLPIYFGVGDEANQG 312
Cdd:COG1653  226 --LEFLKDLVKDGYV-----PPGALGTDWDDARAAFASGKAAMMINGSWALGALKDAA-PDFDVGVAPLPGGPGGKKPAS 297

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 495648618 313 LCTGTenYWCVNKDADeaDIQATLDFMDWcVTSDEGTK 350
Cdd:COG1653  298 VLGGS--GLAIPKGSK--NPEAAWKFLKF-LTSPEAQA 330
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 51-418 2.10e-17

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: 83.61  E-value: 2.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  51 PEQDEQWQQLAKDYTKE-TGVDVTVVTAASGNYETTLMSEMGKSGAPTLFQVNGP-VGLANWKDYCYDLsDSDIYKELTS 128
Cdd:cd13585   10 PAETAALKKLIDAFEKEnPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPwVPEFASNGALLDL-DDYIEKDGLD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 129 DDY------ALKDGDSVAGIGYVIETYGIITNKTLLKEAGYTPDDIKSFADLKKVAEDITNRTSEL-GFSAFTSAGmdGS 201
Cdd:cd13585   89 DDFppglldAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTDKKGGQyGFALRGGSG--GQ 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 202 SDWRFKTHLANLPIYFEYQDE-GINTTDAIKGtyLDNYRDMWDLYINnstcdPKDLAAkTGDDARNEFLNKKAVFYQNGT 280
Cdd:cd13585  167 TQWYPFLWSNGGDLLDEDDGKaTLNSPEAVEA--LQFYVDLYKDGVA-----PSSATT-GGDEAVDLFASGKVAMMIDGP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 281 WEYTQLIDGGLTDD-DMTMLPiyfgVGDEANQGLCTGTENyWCVNKDADEADiqATLDFMDWcVTSDEGTKCMADDMGFN 359
Cdd:cd13585  239 WALGTLKDSKVKFKwGVAPLP----AGPGGKRASVLGGWG-LAISKNSKHPE--AAWKFIKF-LTSKENQLKLGGAAGPA 310

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495648618 360 IPFKKAQESQNLFIKED--KQMTEDGKTPVAWNFSTMPSEEWKNGVGSALTAYAADQTDAN 418
Cdd:cd13585  311 ALAAAAASAAAPDAKPAlaLAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGALGKS 371
 
Name Accession Description Interval E-value
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 59-379 5.17e-44

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 155.26  E-value: 5.17e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618   59 QLAKDYTKETGVDVTVVTAASGNYETTLMSEMGKSGAPTL---FQVNGPVGLANWKDYCYDLSDSDIYKELTSDDYALKD 135
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQASNDLQAKLLAAAAAGNAPDLdvvWIAADQLATLAEAGLLADLSDVDNLDDLPDALDAAGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  136 GDSVAGIGYVIET-YGIITNKTLLKEAGytpDDIKSFADLKKVAEDITNRTselgfsaftsAGMDGSSDWRFKTHLAnlp 214
Cdd:pfam13416  81 DGKLYGVPYAASTpTVLYYNKDLLKKAG---EDPKTWDELLAAAAKLKGKT----------GLTDPATGWLLWALLA--- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  215 iyfeyqdEGINTTDAIKGT-YLDNYRDMWDLYINNSTCdpkdlaAKTGDDARNEFLNKKAVFYQNGTWEYTQLIDGGltd 293
Cdd:pfam13416 145 -------DGVDLTDDGKGVeALDEALAYLKKLKDNGKV------YNTGADAVQLFANGEVAMTVNGTWAAAAAKKAG--- 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  294 DDMTMLPIyfgvgdeaNQGLCTGTENyWCVNKDADEADiQATLDFMDWcVTSDEGTKCMADDMGFNIPFKKAQESQNlfI 373
Cdd:pfam13416 209 KKLGAVVP--------KDGSFLGGKG-LVVPAGAKDPR-LAALDFIKF-LTSPENQAALAEDTGYIPANKSAALSDE--V 275


                  ....*.
gi 495648618  374 KEDKQM 379
Cdd:pfam13416 276 KADPAL 281
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 4-350 3.40e-36

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 136.33  E-value: 3.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618   4 KKRWLALGLVGIMTLgcfAGCGSKSDGKSADGkgdsSKGSVYYLNFKPEQDEQWQQLAKDYTKET-GVDVTVVTAASGNY 82
Cdd:COG1653    2 RRLALALAAALALAL---AACGGGGSGAAAAA----GKVTLTVWHTGGGEAAALEALIKEFEAEHpGIKVEVESVPYDDY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  83 ETTLMSEMGKSGAPTLFQVNGPvGLANW--KDYCYDLSDSDIYKELTSDDY------ALKDGDSVAGIGYVIETYGIITN 154
Cdd:COG1653   75 RTKLLTALAAGNAPDVVQVDSG-WLAEFaaAGALVPLDDLLDDDGLDKDDFlpgaldAGTYDGKLYGVPFNTDTLGLYYN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 155 KTLLKEAGYTPDdiKSFADLKKVAEDITNRTSELGFsaftsaGMDGSSDWRFKTHLANL--PIYFEYQDEGINTTDAIKG 232
Cdd:COG1653  154 KDLFEKAGLDPP--KTWDELLAAAKKLKAKDGVYGF------ALGGKDGAAWLDLLLSAggDLYDEDGKPAFDSPEAVEA 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 233 tyLDNYRDMWDLYINnstcdPKDLAAKTGDDARNEFLNKKAVFYQNGTWEYTQLIDGGlTDDDMTMLPIYFGVGDEANQG 312
Cdd:COG1653  226 --LEFLKDLVKDGYV-----PPGALGTDWDDARAAFASGKAAMMINGSWALGALKDAA-PDFDVGVAPLPGGPGGKKPAS 297

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 495648618 313 LCTGTenYWCVNKDADeaDIQATLDFMDWcVTSDEGTK 350
Cdd:COG1653  298 VLGGS--GLAIPKGSK--NPEAAWKFLKF-LTSPEAQA 330
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
4-432 3.29e-19

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 89.24  E-value: 3.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618   4 KKRWLALGLVGIMTLGCFAGCGSKSDGKSADGKGDSSKGSVYYLNfkPEQDEQWQQLAKDYTKETGVDVTVVTAASGNYE 83
Cdd:COG2182    2 KRRLLAALALALALALALAACGSGSSSSGSSSAAGAGGTLTVWVD--DDEAEALEEAAAAFEEEPGIKVKVVEVPWDDLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  84 TTLMSEMGKSGAPTLFqVNGPVGLANWKD--YCYDLSDSDIYKELTSDDY--ALKDGDSVAGIGYVIETYGIITNKTLLK 159
Cdd:COG2182   80 EKLTTAAPAGKGPDVF-VGAHDWLGELAEagLLAPLDDDLADKDDFLPAAldAVTYDGKLYGVPYAVETLALYYNKDLVK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 160 EagytpDDIKSFADLKKVAEDITNRTsELGFSA------FTSAGMDGSSDWRFKTHLANLpiyfeyQDEGINTTDAIKGT 233
Cdd:COG2182  159 A-----EPPKTWDELIAAAKKLTAAG-KYGLAYdagdayYFYPFLAAFGGYLFGKDGDDP------KDVGLNSPGAVAAL 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 234 YLdnYRDMwdlyINNSTCDPkdlaAKTGDDARNEFLNKKAVFYQNGTWEYTQLIDGglTDDDMTMLPIYFGVGDEANQGL 313
Cdd:COG2182  227 EY--LKDL----IKDGVLPA----DADYDAADALFAEGKAAMIINGPWAAADLKKA--LGIDYGVAPLPTLAGGKPAKPF 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 314 cTGTENyWCVNKDADEADiqATLDFMdWCVTSDEGTKCMADDMGfNIP-FKKAQESqnLFIKEDK------QMTEDGK-T 385
Cdd:COG2182  295 -VGVKG-FGVSAYSKNKE--AAQEFA-EYLTSPEAQKALFEATG-RIPaNKAAAED--AEVKADPliaafaEQAEYAVpM 366

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 495648618 386 PvawNFSTMpSEEWkNGVGSALTAYAADQTDAN--WDAVVSAFVDGWAS 432
Cdd:COG2182  367 P---NIPEM-GAVW-TPLGTALQAIASGKADPAeaLDAAQKQIEAAIAQ 410
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 51-418 2.10e-17

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: 83.61  E-value: 2.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  51 PEQDEQWQQLAKDYTKE-TGVDVTVVTAASGNYETTLMSEMGKSGAPTLFQVNGP-VGLANWKDYCYDLsDSDIYKELTS 128
Cdd:cd13585   10 PAETAALKKLIDAFEKEnPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPwVPEFASNGALLDL-DDYIEKDGLD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 129 DDY------ALKDGDSVAGIGYVIETYGIITNKTLLKEAGYTPDDIKSFADLKKVAEDITNRTSEL-GFSAFTSAGmdGS 201
Cdd:cd13585   89 DDFppglldAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTDKKGGQyGFALRGGSG--GQ 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 202 SDWRFKTHLANLPIYFEYQDE-GINTTDAIKGtyLDNYRDMWDLYINnstcdPKDLAAkTGDDARNEFLNKKAVFYQNGT 280
Cdd:cd13585  167 TQWYPFLWSNGGDLLDEDDGKaTLNSPEAVEA--LQFYVDLYKDGVA-----PSSATT-GGDEAVDLFASGKVAMMIDGP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 281 WEYTQLIDGGLTDD-DMTMLPiyfgVGDEANQGLCTGTENyWCVNKDADEADiqATLDFMDWcVTSDEGTKCMADDMGFN 359
Cdd:cd13585  239 WALGTLKDSKVKFKwGVAPLP----AGPGGKRASVLGGWG-LAISKNSKHPE--AAWKFIKF-LTSKENQLKLGGAAGPA 310

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495648618 360 IPFKKAQESQNLFIKED--KQMTEDGKTPVAWNFSTMPSEEWKNGVGSALTAYAADQTDAN 418
Cdd:cd13585  311 ALAAAAASAAAPDAKPAlaLAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGALGKS 371
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 52-350 2.60e-13

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: 70.14  E-value: 2.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618   52 EQDEQWQQLAKDYTKE-TGVDVTVVTAASGNYETTLMSEMGKSGAPT-LFQVNGpvglanwkDYCYDLSDSDIYKELTSD 129
Cdd:pfam01547   5 TEAAALQALVKEFEKEhPGIKVEVESVGSGSLAQKLTTAIAAGDGPAdVFASDN--------DWIAELAKAGLLLPLDDY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  130 --DYALKDGDSVAGIGYVIETYGIITNKTLLKEAGYTPddIKSFADLKKVAEDITNRTSELGFSAFTSAGmdGSSDWRFK 207
Cdd:pfam01547  77 vaNYLVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDP--PKTWDELLEAAKKLKEKGKSPGGAGGGDAS--GTLGYFTL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  208 THLANLPIYFEYQDEGINTTDAIKGTyLDNYRDMWDLYINNSTCDPKDLAAKTGDDARNEFLNKKAVFYQNGTWEYTQLI 287
Cdd:pfam01547 153 ALLASLGGPLFDKDGGGLDNPEAVDA-ITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAAN 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495648618  288 DGGL---TDDDMTMLPIYFGVGDEANQGLCTGTENYWCVNKDADEADiqATLDFMDWcVTSDEGTK 350
Cdd:pfam01547 232 KVKLkvaFAAPAPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGSKNKE--AAKKFLDF-LTSPEAQA 294
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 55-417 3.57e-13

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: 70.78  E-value: 3.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  55 EQWQQLAKDYTKE-TGVDVTVVTAASGNYETT-LMSEMgKSG-APTLFQVngpvGLANWKDYC--------------YDL 117
Cdd:cd14748   14 KALEELVDEFNKShPDIKVKAVYQGSYDDTLTkLLAAL-AAGtAPDVAQV----DASWVAQLAdsgaleplddyidkDGV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 118 SDSDIYKELTsdDYALKDGdSVAGIGYVIETYGIITNKTLLKEAGYTPDD-IKSFADLKKVAE---DITNRTSELGFSAF 193
Cdd:cd14748   89 DDDDFYPAAL--DAGTYDG-KLYGLPFDTSTPVLYYNKDLFEEAGLDPEKpPKTWDELEEAAKklkDKGGKTGRYGFALP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 194 TSAGmdgssDWRFKTHL--ANLPIYFEYQDE-GINTTDAIKgtYLDNYRDMWDlyinnstcDPKDLAAKTGDDARNEFLN 270
Cdd:cd14748  166 PGDG-----GWTFQALLwqNGGDLLDEDGGKvTFNSPEGVE--ALEFLVDLVG--------KDGVSPLNDWGDAQDAFIS 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 271 KKAVFYQNGTWEYTQLIDGGLTDDDMTMLPIYFGVGDEANQglcTGTENYWcVNKDADEaDIQATLDFMDWcVTSDEGTK 350
Cdd:cd14748  231 GKVAMTINGTWSLAGIRDKGAGFEYGVAPLPAGKGKKGATP---AGGASLV-IPKGSSK-KKEAAWEFIKF-LTSPENQA 304

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 351 CMADDMGFNIPFKKAQESQNLFIKEDKQMT---EDGKTPVAWNFSTMPSEEWKNGVGSALTAYAADQTDA 417
Cdd:cd14748  305 KWAKATGYLPVRKSAAEDPEEFLAENPNYKvavDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTP 374
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 52-368 2.04e-08

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: 55.76  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  52 EQDEQWQQLAKDYTKETGVDVTVVTAASGNYETTLMSEMGKSGAPTLFQvnGP---VGLANWKDYCYDLSDSDIYKELTS 128
Cdd:cd13586   10 GELEYLKELAEEFEKKYGIKVEVVYVDSGDTREKFITAGPAGKGPDVFF--GPhdwLGELAAAGLLAPIPEYLAVKIKNL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 129 DDY--ALKDGDSVAGIGYVIETYGIITNKTLLKEAgytPddiKSFADLKKVAEDITNRTSEL-GFSA-----------FT 194
Cdd:cd13586   88 PVAlaAVTYNGKLYGVPVSVETIALFYNKDLVPEP---P---KTWEELIALAKKFNDKAGGKyGFAYdqtnpyfsypfLA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 195 SAGMdgssdWRFKthlanlPIYFEYQDEGINTTDAIKGtyLDNYRDMWDLY-INNSTCDPkdlaaktgDDARNEFLNKKA 273
Cdd:cd13586  162 AFGG-----YVFG------ENGGDPTDIGLNNEGAVKG--LKFIKDLKKKYkVLPPDLDY--------DIADALFKEGKA 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 274 VFYQNGTWEYTQLIDGGLtDDDMTMLPIYFGvgdeANQGLCTGTENYWCVNkdADEADIQATLDFMDWcVTSDEGTKCMA 353
Cdd:cd13586  221 AMIINGPWDLADYKDAGI-NFGVAPLPTLPG----GKQAAPFVGVQGAFVS--AYSKNKEAAVEFAEY-LTSDEAQLLLF 292

                        330
                 ....*....|....*
gi 495648618 354 DDMGFNIPFKKAQES 368
Cdd:cd13586  293 EKTGRIPALKDALND 307
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 43-347 2.68e-08

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: 55.46  E-value: 2.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  43 SVYYLNFKPEQDEQWQQLAKDYTKET-GVDVTVVTAASGNYETTLMSEMGKSGAPTLFQVNGPVGLANWKD--YCYDLSD 119
Cdd:cd14749    3 TYWQYFTGDTKKKYMDELIADFEKENpNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPGGWLAEFVKagLLLPLTD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 120 sDIYKE-------LTSDDYALKDGDsVAGIGYVIETYGIITNKTLLKEAGytPDDI-KSFADLKKVAEDITNRTseLGFS 191
Cdd:cd14749   83 -YLDPNgvdkrflPGLADAVTFNGK-VYGIPFAARALALFYNKDLFEEAG--GVKPpKTWDELIEAAKKDKFKA--KGQT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 192 AFTSAGMDGSSDWRFKTHLANL--PIYFEYQDEGINTTDAIKGTYLDNYRDMwdlyINNSTCDPKDLAAKTgDDARNEFL 269
Cdd:cd14749  157 GFGLLLGAQGGHWYFQYLVRQAggGPLSDDGSGKATFNDPAFVQALQKLQDL----VKAGAFQEGFEGIDY-DDAGQAFA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 270 NKKAVFYQNGTWEYTQlIDGGLTDDDM--TMLPiyfgVGDEANQGLCTGTeNYWCVNKDADEADIQATLDFMDWcVTSDE 347
Cdd:cd14749  232 QGKAAMNIGGSWDLGA-IKAGEPGGKIgvFPFP----TVGKGAQTSTIGG-SDWAIAISANGKKKEAAVKFLKY-LTSPE 304
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 51-365 1.06e-07

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: 53.53  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  51 PEQDEQWQQLAKDYTKETGVD-VTVVTAASGNYETTLMSEMGKSGAPTLFQVN----GPVGLANWKDYCYDLSDSDIYKE 125
Cdd:cd13657   10 GAEEDALQQIIDEFEAKYPVPnVKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAhdwiGQFAEAGLLVPISDYLSEDDFEN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 126 LTsdDYALKDG---DSVAGIGYVIETYGIITNKTLLKEAgytPddiKSFADLKKVAEDITNRTSE---LGFSA----FTS 195
Cdd:cd13657   90 YL--PTAVEAVtykGKVYGLPEAYETVALIYNKALVDQP---P---ETTDELLAIMKDHTDPAAGsygLAYQVsdayFVS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 196 A---GMDGSsdwrfkthlanlpiYF--EYQDEGINTTDAIKGtyLDNYRDMWDLYInnstcdPKDLaakTGDDARNEFLN 270
Cdd:cd13657  162 AwifGFGGY--------------YFddETDKPGLDTPETIKG--IQFLKDFSWPYM------PSDP---SYNTQTSLFNE 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 271 KKAVFYQNGTWEYTQLIDGGltdDDMTMLPIyfGVGDEANQGLCTGTENYWCVNKDADEADIQATLDFMDWcVTSDEGTK 350
Cdd:cd13657  217 GKAAMIINGPWFIGGIKAAG---IDLGVAPL--PTVDGTNPPRPYSGVEGIYVTKYAERKNKEAALDFAKF-FTTAEASK 290

                        330
                 ....*....|....*
gi 495648618 351 CMADDMGFnIPFKKA 365
Cdd:cd13657  291 ILADENGY-VPAATN 304
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 53-178 1.08e-07

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: 53.00  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  53 QDEQWQQLAKDYTKETGVDVTVVTAASGNYETTLMSEMGKSGAPTLFQVNGPVGLANWKDYCYDLSDSDIYKELtsDDYA 132
Cdd:cd13589   12 EDAQRKAVIEPFEKETGIKVVYDTGTSADRLAKLQAQAGNPQWDVVDLDDGDAARAIAEGLLEPLDYSKIPNAA--KDKA 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 495648618 133 LKDGDSVAGIGYVIETYGIITNKTLLKEAGyTPDDIKSFADLKKVA 178
Cdd:cd13589   90 PAALKTGYGVGYTLYSTGIAYNTDKFKEPP-TSWWLADFWDVGKFP 134
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 53-417 1.90e-07

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: 52.87  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  53 QDEQWQQLAKDYTKETGVDVTVVT--AASGNYETTLMSEMGKsGAPTLFQVNGPVGLANWKDYCYDLSDSDIyKELTSDD 130
Cdd:cd13658   11 KMAFIKKIAKQYTKKTGVKVKLVEvdQLDQLEKLSLDGPAGK-GPDVMVAPHDRIGSAVLQGLLSPIKLSKD-KKKGFTD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 131 YALKD---GDSVAGIGYVIETYGIITNKTLLKEAgytpddIKSFADLKKVAEDITNRT-SELGFSA------FTSAGMDG 200
Cdd:cd13658   89 QALKAltyDGKLYGLPAAVETLALYYNKDLVKNA------PKTFDELEALAKDLTKEKgKQYGFLAdatnfyYSYGLLAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 201 SSDWRFKTHLANLPIyfeyQDEGINTTDAIKG-TYLDNYRDmwdlyinnSTCDPKDLaakTGDDARNEFLNKKAVFYQNG 279
Cdd:cd13658  163 NGGYIFKKNGSDLDI----NDIGLNSPGAVKAvKFLKKWYT--------EGYLPKGM---TGDVIQGLFKEGKAAAVIDG 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 280 TWEYTQLIDGGL--------TDDDMTMLPIYFGVgdeanQGlctgtenyWCVNKDADeaDIQATLDFMDWcVTSDEGTKC 351
Cdd:cd13658  228 PWAIQEYQEAGVnygvaplpTLPNGKPMAPFLGV-----KG--------WYLSAYSK--HKEWAQKFMEF-LTSKENLKK 291

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495648618 352 MADDMGfNIPFKKAQESQNLfIKEDKQMtedgkTPVAWNFST---MPS-----EEWkNGVGSALTAYAADQTDA 417
Cdd:cd13658  292 RYDETN-EIPPRKDVRSDPE-IKNNPLT-----SAFAKQASRavpMPNipemgAVW-EPANNALFFILSGKKTP 357
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
3-174 1.38e-03

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 40.66  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618   3 NKKRWLALGLVGIMTLGCFAGCGSKSDGKsadgkgdsskgsVYYLNFKPEQDEQWqqlAKDYTKETGVDVTVVTAASGny 82
Cdd:COG0687    2 SRRSLLGLAAAALAAALAGGAPAAAAEGT------------LNVYNWGGYIDPDV---LEPFEKETGIKVVYDTYDSN-- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  83 eTTLMSEMgKSGAPT--LFQVNGP-VGLANWKDYCYDLSDSDI--YKELtsDDYALK---DGDSVAGIGYVIETYGIITN 154
Cdd:COG0687   65 -EEMLAKL-RAGGSGydVVVPSDYfVARLIKAGLLQPLDKSKLpnLANL--DPRFKDppfDPGNVYGVPYTWGTTGIAYN 140

                        170       180
                 ....*....|....*....|
gi 495648618 155 KTLLKEagytpdDIKSFADL 174
Cdd:COG0687  141 TDKVKE------PPTSWADL 154
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 44-399 2.40e-03

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: 40.06  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  44 VYYLNFKPEQDEQWQQLAKDYTKET-GVDVTVV------------TAASGNYETTLM-------SEMGKSGAptLFQVNG 103
Cdd:cd14751    3 TFWHTSSDEEKVLYEKLIPAFEKEYpKIKVKAVrvpfdglhnqikTAAAGGQAPDVMradiawvPEFAKLGY--LQPLDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 104 PVGLANWKDYcydlsdsdiykeLTSD-DYALKDGDSVaGIGYVIETYGIITNKTLLKEAGYTPDdiKSFADLKKVAEDIT 182
Cdd:cd14751   81 TPAFDDIVDY------------LPGPmETNRYNGHYY-GVPQVTNTLALFYNKRLLEEAGTEVP--KTMDELVAAAKAIK 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 183 NRTSELGFsaftsaGMDGSSDWRFkthlanLPiYF-----EYQDEG-----INTTDAIKGtyldnYRDMWDLYinnstcd 252
Cdd:cd14751  146 KKKGRYGL------YISGDGPYWL------LP-FLwsfggDLTDEKkatgyLNSPESVRA-----LETIVDLY------- 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 253 PKDLAAKTGDD----ARNEFLNKKAVFYQNGTWEYTQlIDGGLTDDDMTMLPIYFGVGDEANQGLCTGTENYwCVNKDAD 328
Cdd:cd14751  201 DEGAITPCASGgypnMQDGFKSGRYAMIVNGPWAYAD-ILGGKEFKDPDNLGIAPVPAGPGGSGSPVGGEDL-VIFKGSK 278

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495648618 329 EADiqATLDFMDWcVTSDEGTKCMADDMGFnIPFKKA-----QESQNLFIKEDKQMTEdgktpVAWNFSTMPseEW 399
Cdd:cd14751  279 NKD--AAWKFVKF-MSSAEAQALTAAKLGL-LPTRTSayespEVANNPMVAAFKPALE-----TAVPRPPIP--EW 343
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 62-341 3.91e-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: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618  62 KDYTKETGVDVTVVTAASGNYETTLMSEMGKSGAPTLFQVNGPVGLANWKDY--CYDLSD-----SDIYK---ELTSDDY 131
Cdd:cd13580   26 KYLEEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVVNDPQLSITLVKQgaLWDLTDyldkyYPNLKkiiEQEGWDS 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 132 ALKDGD--SVAGIGYVIETYGIITNKTLLKEAGYTPDdiKSFADLKKVAEditnrtselgfsAFTSAGMDG--------- 200
Cdd:cd13580  106 ASVDGKiyGIPRKRPLIGRNGLWIRKDWLDKLGLEVP--KTLDELYEVAK------------AFTEKDPDGngkkdtygl 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495648618 201 -----SSDWRFKTHLANLPIYFEYQDEGINTTDaIKGTYLDNYRDMW----DLY----INnstcdpKDLAAKTGDDARNE 267
Cdd:cd13580  172 tdtkdLIGSGFTGLFGAFGAPPNNWWKDEDGKL-VPGSIQPEMKEALkflkKLYkeglID------PEFAVNDGTKANEK 244

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495648618 268 FLNKKAVFYQnGTWEYTQLIDGGLT----DDDMTMLPIYFGVGDEANQGLCTGTENYWCVNKDADEADiqATLDFMDW 341
Cdd:cd13580  245 FISGKAGIFV-GNWWDPAWPQASLKkndpDAEWVAVPIPSGPDGKYGVWAESGVNGFFVIPKKSKKPE--AILKLLDF 319
 
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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