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Conserved domains on  [gi|2648730963|ref|WP_324621888|]
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extracellular solute-binding protein [Bifidobacterium breve]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 11447308)

ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of one or more from a variety of substrates including carbohydrates

Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
PubMed:  26517916|24638992|25750732|26517916
SCOP:  3000083
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 7-365 1.10e-52

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 181.01  E-value: 1.10e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963   7 KACSIISATALFLGVSACGSANTNSGGTAEGitaedvekaltddsktVELTFW---APSYNAMKASVEAFQKKYPHIKID 83
Cdd:COG1653     2 RRLALALAAALALALAACGGGGSGAAAAAGK----------------VTLTVWhtgGGEAAALEALIKEFEAEHPGIKVE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  84 FVNPGSSsDFNTKLQNAITAKKGvPEVVQFGYDSYGQFAMTGGLLNFkNDSLEKYW--GDKYLDAAWKGVHLAGGLYAIP 161
Cdd:COG1653    66 VESVPYD-DYRTKLLTALAAGNA-PDVVQVDSGWLAEFAAAGALVPL-DDLLDDDGldKDDFLPGALDAGTYDGKLYGVP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 162 QDIAPMVMYVRQDILDQYGLKTPTTWDEFYEIGKQLHEKNPDlYMSYLELGQSKYWSNYYREAGAKIWgvgsDTSLSLDF 241
Cdd:COG1653   143 FNTDTLGLYYNKDLFEKAGLDPPKTWDELLAAAKKLKAKDGV-YGFALGGKDGAAWLDLLLSAGGDLY----DEDGKPAF 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 242 DSDKAKSVDEFLTKCIRDGVLEP--VNSGTDEFNRDMNNGRYASWIDEEWRGNLIRSSFPSQsgKWKVYQLPSWEKGAKS 319
Cdd:COG1653   218 DSPEAVEALEFLKDLVKDGYVPPgaLGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDF--DVGVAPLPGGPGGKKP 295

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2648730963 320 VTTGAGSVLSVTAATDpsKRAAAIAFADWINSSE--ESIQAFQDSNNG 365
Cdd:COG1653   296 ASVLGGSGLAIPKGSK--NPEAAWKFLKFLTSPEaqAKWDALQAVLLG 341
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 7-365 1.10e-52

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 181.01  E-value: 1.10e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963   7 KACSIISATALFLGVSACGSANTNSGGTAEGitaedvekaltddsktVELTFW---APSYNAMKASVEAFQKKYPHIKID 83
Cdd:COG1653     2 RRLALALAAALALALAACGGGGSGAAAAAGK----------------VTLTVWhtgGGEAAALEALIKEFEAEHPGIKVE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  84 FVNPGSSsDFNTKLQNAITAKKGvPEVVQFGYDSYGQFAMTGGLLNFkNDSLEKYW--GDKYLDAAWKGVHLAGGLYAIP 161
Cdd:COG1653    66 VESVPYD-DYRTKLLTALAAGNA-PDVVQVDSGWLAEFAAAGALVPL-DDLLDDDGldKDDFLPGALDAGTYDGKLYGVP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 162 QDIAPMVMYVRQDILDQYGLKTPTTWDEFYEIGKQLHEKNPDlYMSYLELGQSKYWSNYYREAGAKIWgvgsDTSLSLDF 241
Cdd:COG1653   143 FNTDTLGLYYNKDLFEKAGLDPPKTWDELLAAAKKLKAKDGV-YGFALGGKDGAAWLDLLLSAGGDLY----DEDGKPAF 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 242 DSDKAKSVDEFLTKCIRDGVLEP--VNSGTDEFNRDMNNGRYASWIDEEWRGNLIRSSFPSQsgKWKVYQLPSWEKGAKS 319
Cdd:COG1653   218 DSPEAVEALEFLKDLVKDGYVPPgaLGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDF--DVGVAPLPGGPGGKKP 295

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2648730963 320 VTTGAGSVLSVTAATDpsKRAAAIAFADWINSSE--ESIQAFQDSNNG 365
Cdd:COG1653   296 ASVLGGSGLAIPKGSK--NPEAAWKFLKFLTSPEaqAKWDALQAVLLG 341
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 55-440 4.20e-41

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: 150.63  E-value: 4.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  55 ELTFW----APSYNAMKASVEAFQKKYPHIKIDFVnPGSSSDFNTKLQNAITAKKGvPEVVQFGYDSYGQFAMTGGLLN- 129
Cdd:cd13585     1 TLTFWdwgqPAETAALKKLIDAFEKENPGVKVEVV-PVPYDDYWTKLTTAAAAGTA-PDVFYVDGPWVPEFASNGALLDl 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 130 ---FKNDSLEKYWGDKYLDAAWKGvhlaGGLYAIPQDIAPMVMYVRQDILDQYG--LKTPTTWDEFYEIGKQLHEKNPDL 204
Cdd:cd13585    79 ddyIEKDGLDDDFPPGLLDAGTYD----GKLYGLPFDADTLVLFYNKDLFDKAGpgPKPPWTWDELLEAAKKLTDKKGGQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 205 Y---MSYLELGQSkYWSNYYREAGAKIWgvgSDTSLSLDFDSDKAKSVDEFLTKCIRDGVL-EPVNSGTDEFNRDMNNGR 280
Cdd:cd13585   155 YgfaLRGGSGGQT-QWYPFLWSNGGDLL---DEDDGKATLNSPEAVEALQFYVDLYKDGVApSSATTGGDEAVDLFASGK 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 281 YASWIDEEWRGNLIRSSFPsqSGKWKVYQLPSWeKGAKSVTTGAGSVLSVTAATDpsKRAAAIAFADWINSSEESIQAFQ 360
Cdd:cd13585   231 VAMMIDGPWALGTLKDSKV--KFKWGVAPLPAG-PGGKRASVLGGWGLAISKNSK--HPEAAWKFIKFLTSKENQLKLGG 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 361 DSNNGFFFMAAKSFRDNYGEGEEDPYFGQNVSKLYFEAADNINSDWEYLPFGVQLDTMFTDVMApglESKEDVATTASKY 440
Cdd:cd13585   306 AAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGALG---KSPEEALKEAAKE 382
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 61-353 1.19e-21

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: 94.79  E-value: 1.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  61 PSYNAMKASVEAFQKKYPHIKIDFvNPGSSSDFNTKLQNAITAKKGVPEVVQFGYDSYGQFAMTGGLLNFkNDSLEKYWG 140
Cdd:pfam01547   5 TEAAALQALVKEFEKEHPGIKVEV-ESVGSGSLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPL-DDYVANYLV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 141 DKYldaawkgvhlaGGLYAIPQDIAPMVMYVRQDILDQYGLKTPTTWDEFYEIGKQLHEKNPDLYMSY--LELGQSKYWS 218
Cdd:pfam01547  83 LGV-----------PKLYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAGggDASGTLGYFT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 219 NYY-REAGAKIWGVGSDTSLSLDFDSDKAKSVDEFLTKCIRDGVLEPVNSGTD-EFNRDM-NNGRYASWIDEEWRGNLIR 295
Cdd:pfam01547 152 LALlASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADgREALALfEQGKAAMGIVGPWAALAAN 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2648730963 296 S---------SFPSQSGKWKVYQLPSWEKGAKSVTTgagsvLSVTAATDpsKRAAAIAFADWINSSE 353
Cdd:pfam01547 232 KvklkvafaaPAPDPKGDVGYAPLPAGKGGKGGGYG-----LAIPKGSK--NKEAAKKFLDFLTSPE 291
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 7-365 1.10e-52

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 181.01  E-value: 1.10e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963   7 KACSIISATALFLGVSACGSANTNSGGTAEGitaedvekaltddsktVELTFW---APSYNAMKASVEAFQKKYPHIKID 83
Cdd:COG1653     2 RRLALALAAALALALAACGGGGSGAAAAAGK----------------VTLTVWhtgGGEAAALEALIKEFEAEHPGIKVE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  84 FVNPGSSsDFNTKLQNAITAKKGvPEVVQFGYDSYGQFAMTGGLLNFkNDSLEKYW--GDKYLDAAWKGVHLAGGLYAIP 161
Cdd:COG1653    66 VESVPYD-DYRTKLLTALAAGNA-PDVVQVDSGWLAEFAAAGALVPL-DDLLDDDGldKDDFLPGALDAGTYDGKLYGVP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 162 QDIAPMVMYVRQDILDQYGLKTPTTWDEFYEIGKQLHEKNPDlYMSYLELGQSKYWSNYYREAGAKIWgvgsDTSLSLDF 241
Cdd:COG1653   143 FNTDTLGLYYNKDLFEKAGLDPPKTWDELLAAAKKLKAKDGV-YGFALGGKDGAAWLDLLLSAGGDLY----DEDGKPAF 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 242 DSDKAKSVDEFLTKCIRDGVLEP--VNSGTDEFNRDMNNGRYASWIDEEWRGNLIRSSFPSQsgKWKVYQLPSWEKGAKS 319
Cdd:COG1653   218 DSPEAVEALEFLKDLVKDGYVPPgaLGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDF--DVGVAPLPGGPGGKKP 295

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2648730963 320 VTTGAGSVLSVTAATDpsKRAAAIAFADWINSSE--ESIQAFQDSNNG 365
Cdd:COG1653   296 ASVLGGSGLAIPKGSK--NPEAAWKFLKFLTSPEaqAKWDALQAVLLG 341
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 55-440 4.20e-41

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: 150.63  E-value: 4.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  55 ELTFW----APSYNAMKASVEAFQKKYPHIKIDFVnPGSSSDFNTKLQNAITAKKGvPEVVQFGYDSYGQFAMTGGLLN- 129
Cdd:cd13585     1 TLTFWdwgqPAETAALKKLIDAFEKENPGVKVEVV-PVPYDDYWTKLTTAAAAGTA-PDVFYVDGPWVPEFASNGALLDl 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 130 ---FKNDSLEKYWGDKYLDAAWKGvhlaGGLYAIPQDIAPMVMYVRQDILDQYG--LKTPTTWDEFYEIGKQLHEKNPDL 204
Cdd:cd13585    79 ddyIEKDGLDDDFPPGLLDAGTYD----GKLYGLPFDADTLVLFYNKDLFDKAGpgPKPPWTWDELLEAAKKLTDKKGGQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 205 Y---MSYLELGQSkYWSNYYREAGAKIWgvgSDTSLSLDFDSDKAKSVDEFLTKCIRDGVL-EPVNSGTDEFNRDMNNGR 280
Cdd:cd13585   155 YgfaLRGGSGGQT-QWYPFLWSNGGDLL---DEDDGKATLNSPEAVEALQFYVDLYKDGVApSSATTGGDEAVDLFASGK 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 281 YASWIDEEWRGNLIRSSFPsqSGKWKVYQLPSWeKGAKSVTTGAGSVLSVTAATDpsKRAAAIAFADWINSSEESIQAFQ 360
Cdd:cd13585   231 VAMMIDGPWALGTLKDSKV--KFKWGVAPLPAG-PGGKRASVLGGWGLAISKNSK--HPEAAWKFIKFLTSKENQLKLGG 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 361 DSNNGFFFMAAKSFRDNYGEGEEDPYFGQNVSKLYFEAADNINSDWEYLPFGVQLDTMFTDVMApglESKEDVATTASKY 440
Cdd:cd13585   306 AAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGALG---KSPEEALKEAAKE 382
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-364 3.16e-34

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 132.38  E-value: 3.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963   1 MVSKWAKACSIisATALFLGVSACGSANTNSGGTAEgitaedvekaltdDSKTVELTFWAPSY--NAMKASVEAFQKKyP 78
Cdd:COG2182     1 MKRRLLAALAL--ALALALALAACGSGSSSSGSSSA-------------AGAGGTLTVWVDDDeaEALEEAAAAFEEE-P 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  79 HIKIDFVNPGSSsDFNTKLQNAITAKKGvPEVVQFGYDSYGQFAmTGGLLNFKNDSLEKYwgDKYLDAAWKGVHLAGGLY 158
Cdd:COG2182    65 GIKVKVVEVPWD-DLREKLTTAAPAGKG-PDVFVGAHDWLGELA-EAGLLAPLDDDLADK--DDFLPAALDAVTYDGKLY 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 159 AIPQDIAPMVMYVRQDILDQyglKTPTTWDEFYEIGKQLHEknPDLYMSYLELGQSKYWSNYYREAGAKIWGVGSDTSLS 238
Cdd:COG2182   140 GVPYAVETLALYYNKDLVKA---EPPKTWDELIAAAKKLTA--AGKYGLAYDAGDAYYFYPFLAAFGGYLFGKDGDDPKD 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 239 LDFDSDKAKSVDEFLTKCIRDGVLePVNSGTDEFNRDMNNGRYASWIDEEWRGNLIRSSFPSqsgKWKVYQLPSWEKGAK 318
Cdd:COG2182   215 VGLNSPGAVAALEYLKDLIKDGVL-PADADYDAADALFAEGKAAMIINGPWAAADLKKALGI---DYGVAPLPTLAGGKP 290

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 2648730963 319 SVTTGAGSVLSVTAATDpsKRAAAIAFADWINsSEESIQAFQDSNN 364
Cdd:COG2182   291 AKPFVGVKGFGVSAYSK--NKEAAQEFAEYLT-SPEAQKALFEATG 333
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 55-450 6.80e-31

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: 122.79  E-value: 6.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  55 ELTFWAPSY----NAMKASVEAFQKKYPHIKIDFVNPGSSSDFNTKLQNAITAKKGvPEVVQFGYDSYGQFAMTGGLLNF 130
Cdd:cd14748     1 EITFWHGMSgpdgKALEELVDEFNKSHPDIKVKAVYQGSYDDTLTKLLAALAAGTA-PDVAQVDASWVAQLADSGALEPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 131 KND-SLEKYWGDKYLDAAWKGVHLAGGLYAIPQDIAPMVMYVRQDILDQYGL---KTPTTWDEFYEIGKQLHEKNPD--- 203
Cdd:cd14748    80 DDYiDKDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLdpeKPPKTWDELEEAAKKLKDKGGKtgr 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 204 --LYMSYLELGQskYWSNYYREAGAKIWgvgSDTSLSLDFDSDKAKSVDEFLTKCIRDGVLEPVNSGTDEFNrDMNNGRY 281
Cdd:cd14748   160 ygFALPPGDGGW--TFQALLWQNGGDLL---DEDGGKVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQD-AFISGKV 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 282 ASWIDEEWRGNLIRSSFPsqSGKWKVYQLPSWeKGAKSVTTGAGSVLSVTaATDPSKRAAAIAFADWINSSEESIQAFQD 361
Cdd:cd14748   234 AMTINGTWSLAGIRDKGA--GFEYGVAPLPAG-KGKKGATPAGGASLVIP-KGSSKKKEAAWEFIKFLTSPENQAKWAKA 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 362 SnnGFFFMAAKSFRDNYGEGEEDPYFgqnvsKLYFEAADNINSDWEYLPFGVQLDTMFTDVMAPGLESKEDVAttaskys 441
Cdd:cd14748   310 T--GYLPVRKSAAEDPEEFLAENPNY-----KVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPE------- 375


                  ....*....
gi 2648730963 442 DAIKNYAEK 450
Cdd:cd14748   376 EALKEAQEK 384
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 55-361 2.49e-28

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: 115.49  E-value: 2.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  55 ELTFWA----PSYNAMKASVEAFQKKYPHIKIDFVNPGSSsDFNTKLQNAITAKKGvPEVVQFGYDSYGQFAMTGGLLNF 130
Cdd:cd14747     1 TLTVWAmgnsAEAELLKELADEFEKENPGIEVKVQVLPWG-DAHTKITTAAASGDG-PDVVQLGNTWVAEFAAMGALEDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 131 KNDSLEKYWGDKYLDAAWKGVHLAGGLYAIPQDIAPMVMYVRQDILDQYGLKT-PTTWDEFYEIGKQLHEKNPDLYMSYL 209
Cdd:cd14747    79 TPYLEDLGGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGDEaPKTWDELEAAAKKIKADGPDVSGFAI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 210 ElGQSKYWSNYYreagAKIWGVGSDTSLSLD----FDSDKAKSVDEFLTKCIRDG-VLEPVNSGTDEFNRDMNNGRYASW 284
Cdd:cd14747   159 P-GKNDVWHNAL----PFVWGAGGDLATKDKwkatLDSPEAVAGLEFYTSLYQKGlSPKSTLENSADVEQAFANGKVAMI 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2648730963 285 IDEEWRGNLIRSSFPSQSGKWKVYQLPSWEKGaKSVTTGAGSVLSVTAATDpsKRAAAIAFADWInSSEESIQAFQD 361
Cdd:cd14747   234 ISGPWEIGAIREAGPDLAGKWGVAPLPGGPGG-GSPSFAGGSNLAVFKGSK--NKDLAWKFIEFL-SSPENQAAYAK 306
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 55-358 6.88e-27

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: 111.23  E-value: 6.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  55 ELTFWAPS----YNAMKASVEAFQKKYPHIKIDFV-NPGSSSDFNTKLQNAITAKKGVPEVVQFgyDSY--GQFAMTGGL 127
Cdd:cd14750     1 TITFAAGSdgqeGELLKKAIAAFEKKHPDIKVEIEeLPASSDDQRQQLVTALAAGSSAPDVLGL--DVIwiPEFAEAGWL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 128 LNFKNDSLEKYWGDkYLDAAWKGVHLAGGLYAIPQDIAPMVMYVRQDILDQYGLKTPTTWDEFYEIGKQLHEKNPDLY-- 205
Cdd:cd14750    79 LPLTEYLKEEEDDD-FLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPEPPKTWDELLEAAKKRKAGEPGIWgy 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 206 ----MSY-------LELgqskYWSNyyreaGAKIWGVGSDTSLsldFDSDKAKSVDEFLTKCIRDGVLEPVNS--GTDEF 272
Cdd:cd14750   158 vfqgKQYeglvcnfLEL----LWSN-----GGDIFDDDSGKVT---VDSPEALEALQFLRDLIGEGISPKGVLtyGEEEA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 273 NRDMNNGRYA---SWIDEEWRGNLIRSSFPsqsGKWKVYQLPSWEKGaKSVTTGAGSVLSVTAATDpsKRAAAIAFADWI 349
Cdd:cd14750   226 RAAFQAGKAAfmrNWPYAYALLQGPESAVA---GKVGVAPLPAGPGG-GSASTLGGWNLAISANSK--HKEAAWEFVKFL 299


                  ....*....
gi 2648730963 350 NSSEESIQA 358
Cdd:cd14750   300 TSPEVQKRR 308
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 55-364 3.48e-26

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: 109.39  E-value: 3.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  55 ELTFWAPSYN-----AMKASVEAFQKKYPHIKIDFVNPGSSsDFNTKLQNAITAKKGvPEVVQFGYdsYGQFA--MTGGL 127
Cdd:cd14749     1 TITYWQYFTGdtkkkYMDELIADFEKENPNIKVKVVVFPYD-NYKTKLKTAVAAGEG-PDVFNLWP--GGWLAefVKAGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 128 LNFKNDSLEKY-WGDKYLDAAWKGVHLAGGLYAIPQDIAPMVMYVRQDILDQYG-LKTPTTWDEFYEIGKQLHEKNPDLY 205
Cdd:cd14749    77 LLPLTDYLDPNgVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGgVKPPKTWDELIEAAKKDKFKAKGQT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 206 -MSYLELGQSKYWSNYY---REAGAKIWGVGSDTslsLDFDSDKAKSVDEFLTKCIRDGVLEPVNSGTDeFNRDMNN--- 278
Cdd:cd14749   157 gFGLLLGAQGGHWYFQYlvrQAGGGPLSDDGSGK---ATFNDPAFVQALQKLQDLVKAGAFQEGFEGID-YDDAGQAfaq 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 279 GRYASWIDEEWR-GNLIRSSFPsqsGKWKVYQLPSWEKGAKSVTTGaGSVLSVTAATDPSKRAAAIAFADWINsSEESIQ 357
Cdd:cd14749   233 GKAAMNIGGSWDlGAIKAGEPG---GKIGVFPFPTVGKGAQTSTIG-GSDWAIAISANGKKKEAAVKFLKYLT-SPEVMK 307


                  ....*..
gi 2648730963 358 AFQDSNN 364
Cdd:cd14749   308 QYLEDVG 314
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 61-353 1.19e-21

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: 94.79  E-value: 1.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  61 PSYNAMKASVEAFQKKYPHIKIDFvNPGSSSDFNTKLQNAITAKKGVPEVVQFGYDSYGQFAMTGGLLNFkNDSLEKYWG 140
Cdd:pfam01547   5 TEAAALQALVKEFEKEHPGIKVEV-ESVGSGSLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPL-DDYVANYLV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 141 DKYldaawkgvhlaGGLYAIPQDIAPMVMYVRQDILDQYGLKTPTTWDEFYEIGKQLHEKNPDLYMSY--LELGQSKYWS 218
Cdd:pfam01547  83 LGV-----------PKLYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAGggDASGTLGYFT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 219 NYY-REAGAKIWGVGSDTSLSLDFDSDKAKSVDEFLTKCIRDGVLEPVNSGTD-EFNRDM-NNGRYASWIDEEWRGNLIR 295
Cdd:pfam01547 152 LALlASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADgREALALfEQGKAAMGIVGPWAALAAN 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2648730963 296 S---------SFPSQSGKWKVYQLPSWEKGAKSVTTgagsvLSVTAATDpsKRAAAIAFADWINSSE 353
Cdd:pfam01547 232 KvklkvafaaPAPDPKGDVGYAPLPAGKGGKGGGYG-----LAIPKGSK--NKEAAKKFLDFLTSPE 291
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 52-353 1.30e-15

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


Pssm-ID: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 78.91  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  52 KTVELTFWAPSYNAMKAS------VEAFQKKYPhIKIDFVNPgSSSDFNTKLQNAITAKKgVPEVVqFGYDSY------- 118
Cdd:cd13580     1 EPVTITIVANLGGNPKPDpddnpyTKYLEEKTN-IDVKVKWV-PDSSYDEKLNLALASGD-LPDIV-VVNDPQlsitlvk 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 119 -GQFAMTGGLLNFKNDSLEKYWGDKYLDAAWKGvhlaGGLYAIPQ---DIAPMVMYVRQDILDQYGLKTPTTWDEFYEIG 194
Cdd:cd13580    77 qGALWDLTDYLDKYYPNLKKIIEQEGWDSASVD----GKIYGIPRkrpLIGRNGLWIRKDWLDKLGLEVPKTLDELYEVA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 195 KQLHEKNPDLY-------MSyleLGQSKYWSNYYREAGA-----KIWGVGSDTSLSLDFDSDKAKSVDEFLTKCIRDGVL 262
Cdd:cd13580   153 KAFTEKDPDGNgkkdtygLT---DTKDLIGSGFTGLFGAfgappNNWWKDEDGKLVPGSIQPEMKEALKFLKKLYKEGLI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 263 EP---VNSGTDeFNRDMNNGRYASWIDEEWRGNLIRSSFPS--QSGKWKVYQLPSWEKGAKSVTTGAGSVLSVTAATDPS 337
Cdd:cd13580   230 DPefaVNDGTK-ANEKFISGKAGIFVGNWWDPAWPQASLKKndPDAEWVAVPIPSGPDGKYGVWAESGVNGFFVIPKKSK 308

                         330
                  ....*....|....*.
gi 2648730963 338 KRAAAIAFADWINSSE 353
Cdd:cd13580   309 KPEAILKLLDFLSDPE 324
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 56-201 9.13e-15

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: 75.53  E-value: 9.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  56 LTFW----APSYNAMKASVEAFQKKYPHIKIDFVNPgSSSDFNTKLQNAITAKKGvPEVVQFGYDSYGQFAMTGGLLNfk 131
Cdd:cd13522     2 ITVWhqydTGENQAVNELIAKFEKAYPGITVEVTYQ-DTEARRQFFSTAAAGGKG-PDVVFGPSDSLGPFAAAGLLAP-- 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2648730963 132 ndsLEKYWGDKYLDA--AWKGVHLAGGLYAIPQDIAPMVMYVRQDILDQyglKTPTTWDEFYEIGKQLHEKN 201
Cdd:cd13522    78 ---LDEYVSKSGKYApnTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVPK---NPPKTWQELIALAQGLKAKN 143
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 55-356 1.28e-14

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: 75.11  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  55 ELTFW----APSYNAMKASVEAFQKKYPH--IKIDFVNPGsssDFNTKLQNAITAKKGvPEVVQFGYDSYGQFAMTGgLL 128
Cdd:cd13657     1 TITIWhaltGAEEDALQQIIDEFEAKYPVpnVKVPFEKKP---DLQNKLLTAIPAGEG-PDLFIWAHDWIGQFAEAG-LL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 129 NFKNDSLEKYWGDKYLDAAWKGVHLAGGLYAIPQDIAPMVMYVRQDILDQyglkTPTTWDEFYEIGKQLHEKNPDLYmsy 208
Cdd:cd13657    76 VPISDYLSEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQ----PPETTDELLAIMKDHTDPAAGSY--- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 209 lelGQSKYWSNYYREAgAKIWGVGS----DTSLSLDFDSDKAKSVDEFLTKCIRDGVlePVNSGTDEFNRDMNNGRYASW 284
Cdd:cd13657   149 ---GLAYQVSDAYFVS-AWIFGFGGyyfdDETDKPGLDTPETIKGIQFLKDFSWPYM--PSDPSYNTQTSLFNEGKAAMI 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2648730963 285 IDEEWRGNLIRssfpsQSG-KWKVYQLP--SWEKGAKSVTTGAGsvLSVTAATDPSKRAAAIAFADWINSSEESI 356
Cdd:cd13657   223 INGPWFIGGIK-----AAGiDLGVAPLPtvDGTNPPRPYSGVEG--IYVTKYAERKNKEAALDFAKFFTTAEASK 290
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 56-358 2.73e-14

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: 73.95  E-value: 2.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  56 LTFWApSYNA-----MKASVEAFQKKYPHIKIDFVnpgsSSDFNTKLQNAITAKKG--VPEVVQFGYDSYGQFAMTGGLL 128
Cdd:cd14751     2 ITFWH-TSSDeekvlYEKLIPAFEKEYPKIKVKAV----RVPFDGLHNQIKTAAAGgqAPDVMRADIAWVPEFAKLGYLQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 129 NFKNDSLEKYWGDkYLDAAWKGVHLAGGLYAIPQDIAPMVMYVRQDILDQYGLKTPTTWDEFYEIGKQLHEKNPDlyMSY 208
Cdd:cd14751    77 PLDGTPAFDDIVD-YLPGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEVPKTMDELVAAAKAIKKKKGR--YGL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 209 LELGQSKYWSNYYreagakIWGVGSDTSlsldfDSDKAK----SVD-----EFLTKCIRDGVLEPVNSGTD-EFNRDMNN 278
Cdd:cd14751   154 YISGDGPYWLLPF------LWSFGGDLT-----DEKKATgylnSPEsvralETIVDLYDEGAITPCASGGYpNMQDGFKS 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 279 GRYASWIDEEWR-GNLIRSSFPSQSGKWKVYQLPSWEKGAKSVTtgAGSVLSVTAATDPSKraAAIAFADWINSSEESIQ 357
Cdd:cd14751   223 GRYAMIVNGPWAyADILGGKEFKDPDNLGIAPVPAGPGGSGSPV--GGEDLVIFKGSKNKD--AAWKFVKFMSSAEAQAL 298


                  .
gi 2648730963 358 A 358
Cdd:cd14751   299 T 299
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 55-247 3.79e-14

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: 73.48  E-value: 3.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  55 ELTFWA---PSYNAMKASVEAFQKKYPhIKIDFVNPGSSsDFNTKLQNAITAKKGvPEVVQFGYDSYGQFAMTGGLLNFK 131
Cdd:cd13586     1 TITVWTdedGELEYLKELAEEFEKKYG-IKVEVVYVDSG-DTREKFITAGPAGKG-PDVFFGPHDWLGELAAAGLLAPIP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 132 NDSLEKYwgdKYLDAAWKGVHLAGGLYAIPQDIAPMVMYVRQDILDQyglkTPTTWDEFYEIGKQLHEKNPDLYMSYLEL 211
Cdd:cd13586    78 EYLAVKI---KNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPE----PPKTWEELIALAKKFNDKAGGKYGFAYDQ 150

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2648730963 212 GQSKYWSNYYREAGAKIWGVGSDTSLSLDFDSDKAK 247
Cdd:cd13586   151 TNPYFSYPFLAAFGGYVFGENGGDPTDIGLNNEGAV 186
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 99-359 3.14e-12

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


Pssm-ID: 270239 [Multi-domain]  Cd Length: 483  Bit Score: 68.25  E-value: 3.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  99 NAITAKKGVPEVV--QFGYDSYGQFAMTGGLLNFkNDSLEKYWGDKYLDAAWKGVHLA-----GGLYAIP----QDIAPM 167
Cdd:cd13521    49 NLMLASGDLPDIVgaDYLKDKFIAYGMEGAFLPL-SKYIDQYPNLKAFFKQHPDVLRAstasdGKIYLIPyeppKDVPNQ 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 168 VMYVRQDILDQYGLKTPTTWDEFYEIGKQLHEKNPDLYmsylelGQSKYWS--------NYYREAG--AKIWGVGSDTSl 237
Cdd:cd13521   128 GYFIRKDWLDKLNLKTPKTLDELYNVLKAFKEKDPNGN------GKADEIPfidrdplyGAFRLINswGARSAGGSTDS- 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 238 slDFDSDKAKSVDEFLTKCIRDGV-------------LEPVNSGTDEFNRDMNNGRYASWIDEEWRG-NLIRSSFPSQSG 303
Cdd:cd13521   201 --DWYEDNGKFKHPFASEEYKDGMkymnklyteglidKESFTQKDDQAEQKFSNGKLGGFTHNWFASdNLFTAQLGKEKP 278

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2648730963 304 KWKVYQLPS-------WEKGAKSVTTGAGSVLSVTAAtDPskrAAAIAFADWINSSEESIQAF 359
Cdd:cd13521   279 MYILLPIAPagnvkgrREEDSPGYTGPDGVAISKKAK-NP---VAALKFFDWLASEEGRELAN 337
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 80-353 7.52e-12

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: 67.00  E-value: 7.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  80 IKIDFvNPGSSSDFNTKLQNAITAKKgVPEVVQ-FGYDSYGQFAMTGGLLNFkNDSLEKY---------WGDKYLDAAWK 149
Cdd:cd13583    32 VKFKR-TPIPSSDYETKRSLLIASGD-APDIIPvLYPGEENEFVASGALLPI-SDYLDYMpnykkyvekWGLGKELATGR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 150 GVhlAGGLYAIP-QDIAPMVMY---VRQDILDQYGLKTPTTWDEFYEIGKQLHEKNPDLYmSYLELGQSKYWSNYYREA- 224
Cdd:cd13583   109 QS--DGKYYSLPgLHEDPGVQYsflYRKDIFEKAGIKIPTTWDEFYAALKKLKEKYPDSY-PYSDRWNSNALLLIAAPAf 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 225 -GAKIWGVGSDTslsLDFDSDK---------AKSVDEFLTKCIRDGVLEP--VNSGTDEFNRDMNNGR-YASWIDEEWRG 291
Cdd:cd13583   186 gTTAGWGFSNYT---YDPDTDKfvygattdeYKDMLQYFNKLYAEGLLDPesFTQTDDQAKAKFLNGKsFVITTNPQTVD 262

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2648730963 292 NLIRSSFPSQSGKWKVYQL--PSWEKGA--KSVTTGAGSVLSVTAATDPsKRAAAIAFADWINSSE 353
Cdd:cd13583   263 ELQRNLRAADGGNYEVVSItpPAGPAGKaiNGSRLENGFMISSKAKDSK-NFEALLQFLDWLYSDE 327
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 68-363 1.50e-09

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 58.57  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  68 ASVEAFQKKYpHIKIDFVnPGSSSDFNTKLQNAITAKKGVPEVVQFGYDSYGQFAMTGGLLnfknDSLEKYWGDKYLDAA 147
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVE-PQASNDLQAKLLAAAAAGNAPDLDVVWIAADQLATLAEAGLL----ADLSDVDNLDDLPDA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 148 WKGVHLAGGLYAIPQDI-APMVMYVRQDILDQYGlKTPTTWDEFYEIGKQLHEKNpdlymsylelGQSKYWSNYYrEAGA 226
Cdd:pfam13416  75 LDAAGYDGKLYGVPYAAsTPTVLYYNKDLLKKAG-EDPKTWDELLAAAAKLKGKT----------GLTDPATGWL-LWAL 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 227 KIWGVGSDTSLSLDFDSDKAKsvdEFLTKCIRDGVLepVNSGTDeFNRDMNNGRYASwideewrgnlirssfpSQSGKWk 306
Cdd:pfam13416 143 LADGVDLTDDGKGVEALDEAL---AYLKKLKDNGKV--YNTGAD-AVQLFANGEVAM----------------TVNGTW- 199

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2648730963 307 vyQLPSWEKGAKSVTTGA---GSVLSVTA----ATDPSKRAAAIAFADWINSSEESIQAFQDSN 363
Cdd:pfam13416 200 --AAAAAKKAGKKLGAVVpkdGSFLGGKGlvvpAGAKDPRLAALDFIKFLTSPENQAALAEDTG 261
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 56-365 1.67e-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: 50.04  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  56 LTFWAPS--YNAMKASVEAFQKKYPHIKIDF-VNPGSSSDFNTKLQNAITAkkgVPEVVQFGYDSYGQFAMTGGLLNFKN 132
Cdd:cd13655     2 LTVWGPQedQEWLKEMVDAFKEKHPEWKITItIGVVGEADAKDEVLKDPSA---AADVFAFANDQLGELVDAGAIYPLTG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 133 DSLEKYwGDKYLDAAWKGVHLAGGLYAIPQDIAPMVMYVRQDILDQYGLKtptTWDEFYEIGKQLHEKnpdLYMsylELG 212
Cdd:cd13655    79 SAVDKI-KNTNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLTEDDVK---SLDTMLAKAPDAKGK---VSF---DLS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 213 QSKYWSNYYREAGAKIWGVGSDTSLSLDFDSDKAKSVdeflTKCIRDGVLEP--VNSGTDEFNRDMNNGRYASWIDEEWR 290
Cdd:cd13655   149 NSWYLYAFFFGAGCKLFGNNGGDTAGCDFNNEKGVAV----TNYLVDLVANPkfVNDADGDAISGLKDGTLGAGVSGPWD 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2648730963 291 GNLIRSSFPSQSGkwkVYQLPSWEKGAKSVTTG--AGS-VLSVTAAT-DPskrAAAIAFADWINSSEESIQAFQDSNNG 365
Cdd:cd13655   225 AANLKKALGDNYA---VAKLPTYTLGGKDVQMKsfAGYkAIGVNSNTkNP---EAAMALADYLTNEESQLTRFEKRGIG 297
PBP2_AlgQ1_2 cd13584
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 ...
 55-204 2.23e-06

Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 periplasmic binding fold; This group represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria such as Sphingomonas sp. A1. 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 includes 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: 270302 [Multi-domain]  Cd Length: 481  Bit Score: 49.74  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  55 ELTFW--------APSYNAMKASVEAFQKKypHIKIDFVNPGSSSDFNTKLqNAITAKKGVPEVVqfGYDSYG------Q 120
Cdd:cd13584     1 ELTLWihmhfrdkWPNDNDLPVYKEMERKT--NVKLNFVANPVAQNSQEQF-NLMMASGQLPDII--GGDWLKdkggfeK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 121 FAMTGGLLNFkNDSLEKYWGD--KYLDA--AWKGVHLA--GGLYAIP----QDIAPM--VMYVRQDILDQYGLKTPTTWD 188
Cdd:cd13584    76 YGEDGAFLPL-NDLIDQYAPNlkKFLDEhpDVKKAITTddGNIYGFPylpdGDVAKEarGYFIRKDWLDKLGLKTPSTID 154

                         170
                  ....*....|....*.
gi 2648730963 189 EFYEIGKQLHEKNPDL 204
Cdd:cd13584   155 EWYTVLKAFKERDPNG 170
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 54-202 2.17e-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: 46.54  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  54 VELTFWAPSY-NAMKASVEAFQKKYPH---IKIDFVNPgSSSDFNTKLqNAITAKKGVPEVVQFGYDS------YGQfam 123
Cdd:cd13581     2 VTLTIFVRKSpLVEDYNENLFFKRLEEktgIKIEWETV-PEDAWAEKK-NLMLASGDLPDAFLGAGASdadlmtYGK--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 124 tGGLLNFKNDSLEKYWG------DKYLDAawKGVHLA--GGLYAIPQDI------APMVMYVRQDILDQYGLKTPTTWDE 189
Cdd:cd13581    77 -QGLFLPLEDLIDKYAPnlkalfDENPDI--KAAITApdGHIYALPSVNecyhcsYGQRMWINKKWLDKLGLEMPTTTDE 153

                         170
                  ....*....|...
gi 2648730963 190 FYEIGKQLHEKNP 202
Cdd:cd13581   154 LYEVLKAFKEQDP 166
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 55-208 5.59e-04

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: 42.09  E-value: 5.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  55 ELTFWA---PSYNAMKASVEAFQKKYpHIKIDFVnPGSSSDFNTKLQNAITAKKGvPEVVQFGYDSYGQFAMTGGLLNFK 131
Cdd:cd13658     1 QLTVWVdedKKMAFIKKIAKQYTKKT-GVKVKLV-EVDQLDQLEKLSLDGPAGKG-PDVMVAPHDRIGSAVLQGLLSPIK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 132 NDSLEKywgDKYLDAAWKGVHLAGGLYAIPQDIAPMVMYVRQDILDQyglkTPTTWDEFYEIGKQLHE----------KN 201
Cdd:cd13658    78 LSKDKK---KGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKN----APKTFDELEALAKDLTKekgkqygflaDA 150


                  ....*..
gi 2648730963 202 PDLYMSY 208
Cdd:cd13658   151 TNFYYSY 157
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 55-297 5.12e-03

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: 39.12  E-value: 5.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963  55 ELTFWA---PSYNAMKASVEAFQKKYpHIKIDFVNPGSSSDfntKLQNAITAKKGvPEVVQFGYDSYGQFAMTGGLLNFK 131
Cdd:cd13656     2 KLVIWIngdKGYNGLAEVGKKFEKDT-GIKVTVEHPDKLEE---KFPQVAATGDG-PDIIFWAHDRFGGYAQSGLLAEIT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 132 NDsleKYWGDKYLDAAWKGVHLAGGLYAIPQDIAPMVMYVRQDILDQyglkTPTTWDEFYEIGKQLHEKNP--------D 203
Cdd:cd13656    77 PD---KAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPN----PPKTWEEIPALDKELKAKGKsalmfnlqE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648730963 204 LYMSYLELGQSKYWSNYYREAGAKIWGVGSDTSlsldfdsdKAKSVDEFLTKCIRDGVLePVNSGTDEFNRDMNNGRYAS 283
Cdd:cd13656   150 PYFTWPLIAADGGYAFKYENGKYDIKDVGVDNA--------GAKAGLTFLVDLIKNKHM-NADTDYSIAEAAFNKGETAM 220

                         250
                  ....*....|....
gi 2648730963 284 WIDEEWRGNLIRSS 297
Cdd:cd13656   221 TINGPWAWSNIDTS 234
 
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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