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Conserved domains on  [gi|782700300|ref|WP_045611137|]
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MULTISPECIES: ABC transporter substrate-binding protein [Streptococcus]

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 ...
 25-439 6.52e-50

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 173.31  E-value: 6.52e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  25 SGGSKDAAKSGGDGAKTEITWWAfpvftqekTGDGVGTYEKSIIEAFEKANPDVKVKLETIDFKSGPEKITTAIEAGTAP 104
Cdd:COG1653   17 AACGGGGSGAAAAAGKVTLTVWH--------TGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 105 DVLFDAPGRIIQYGKNGKLAELNDLFT-DEFVKDVNNENIVQASKAGDKAYMYPISSAPFYMAMNKKMLEEAGvanlVKE 183
Cdd:COG1653   89 DVVQVDSGWLAEFAAAGALVPLDDLLDdDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAG----LDP 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 184 GWTTDDFEKVLKALKDK-GYTPgslFSSGQGGDQGTRAFISNlYGGSVTDKDvTKYTTDDPKFVKGLEKAAGWIKDGLLN 262
Cdd:COG1653  165 PKTWDELLAAAKKLKAKdGVYG---FALGGKDGAAWLDLLLS-AGGDLYDED-GKPAFDSPEAVEALEFLKDLVKDGYVP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 263 NGS-QFDGGADIQNFANGQTSYTILWAPAQNGIQAkllEASKVEVVEVPFPSDSGKPALEYLVNGFAVFNNKDDKKVAAS 341
Cdd:COG1653  240 PGAlGTDWDDARAAFASGKAAMMINGSWALGALKD---AAPDFDVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 342 KKFVQFIADDKEWgpkdvvrtgafpvrtsfgklyedkrmetisgwtkyyspyyntingfaemrtLWFPMLQSVSNGDEKP 421
Cdd:COG1653  317 WKFLKFLTSPEAQ---------------------------------------------------AKWDALQAVLLGQKTP 345

                        410
                 ....*....|....*...
gi 782700300 422 ADALKAFTEKANETIKKA 439
Cdd:COG1653  346 EEALDAAQAAANAALARA 363
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 25-439 6.52e-50

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 173.31  E-value: 6.52e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  25 SGGSKDAAKSGGDGAKTEITWWAfpvftqekTGDGVGTYEKSIIEAFEKANPDVKVKLETIDFKSGPEKITTAIEAGTAP 104
Cdd:COG1653   17 AACGGGGSGAAAAAGKVTLTVWH--------TGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 105 DVLFDAPGRIIQYGKNGKLAELNDLFT-DEFVKDVNNENIVQASKAGDKAYMYPISSAPFYMAMNKKMLEEAGvanlVKE 183
Cdd:COG1653   89 DVVQVDSGWLAEFAAAGALVPLDDLLDdDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAG----LDP 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 184 GWTTDDFEKVLKALKDK-GYTPgslFSSGQGGDQGTRAFISNlYGGSVTDKDvTKYTTDDPKFVKGLEKAAGWIKDGLLN 262
Cdd:COG1653  165 PKTWDELLAAAKKLKAKdGVYG---FALGGKDGAAWLDLLLS-AGGDLYDED-GKPAFDSPEAVEALEFLKDLVKDGYVP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 263 NGS-QFDGGADIQNFANGQTSYTILWAPAQNGIQAkllEASKVEVVEVPFPSDSGKPALEYLVNGFAVFNNKDDKKVAAS 341
Cdd:COG1653  240 PGAlGTDWDDARAAFASGKAAMMINGSWALGALKD---AAPDFDVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 342 KKFVQFIADDKEWgpkdvvrtgafpvrtsfgklyedkrmetisgwtkyyspyyntingfaemrtLWFPMLQSVSNGDEKP 421
Cdd:COG1653  317 WKFLKFLTSPEAQ---------------------------------------------------AKWDALQAVLLGQKTP 345

                        410
                 ....*....|....*...
gi 782700300 422 ADALKAFTEKANETIKKA 439
Cdd:COG1653  346 EEALDAAQAAANAALARA 363
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 42-432 8.71e-49

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: 171.05  E-value: 8.71e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  42 EITWWAFPVFTQEKtgdgvgtYEKSIIEAFEKANPDVKVKLETIDFKSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKNG 121
Cdd:cd13585    1 TLTFWDWGQPAETA-------ALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 122 KLAELNDLFTDEFVKDVNNENIVQASKAGDKAYMYPISSAPFYMAMNKKMLEEAGVAnlVKEGWTTDDFEKVLKALKDKG 201
Cdd:cd13585   74 ALLDLDDYIEKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPG--PKPPWTWDELLEAAKKLTDKK 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 202 YTPGSLFSSGQGGDQGTRAFISNLYGGSVTDKDVTKYTTDDPKFVKGLEKAAGWIKDGLLNNGSQFDGGADIQNFANGQT 281
Cdd:cd13585  152 GGQYGFALRGGSGGQTQWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFASGKV 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 282 SYTILWAPAQNGIQAkllEASKVEVVEVPFPS-DSGKPALEYLVNGFAVFNNKDDKKVAAskKFVQFIADD---KEWGPK 357
Cdd:cd13585  232 AMMIDGPWALGTLKD---SKVKFKWGVAPLPAgPGGKRASVLGGWGLAISKNSKHPEAAW--KFIKFLTSKenqLKLGGA 306

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 782700300 358 DVVRTGAFPVRTSFGKLYEDKRMETISGWTKYYSPYYNTINGFAEMRTLWFPMLQSVSNGDEK--PADALKAFTEKA 432
Cdd:cd13585  307 AGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGALGksPEEALKEAAKEI 383
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 65-352 6.76e-22

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: 95.18  E-value: 6.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300   65 KSIIEAFEKANPDVKVKLETIDFKSGPEKITTAIEAGTAP-DVLFDAPGRIIQYGKNGKLAELNDLFTDEFVKDVNneni 143
Cdd:pfam01547  11 QALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVANYLVLGVP---- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  144 vqaskagdKAYMYPISSAPFYMAMNKKMLEEAGvanlVKEGWTTDDFEKVLKALKDKGYTPGSLFSSGQGGDQGTRA-FI 222
Cdd:pfam01547  87 --------KLYGVPLAAETLGLIYNKDLFKKAG----LDPPKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGYFTlAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  223 SNLYGGSVTDKDVTKYTT----DDPKFVKGLEKAAGWIKDGLLNNGSQFDGGADIQNFANGQTSYTILW-----APAQNG 293
Cdd:pfam01547 155 LASLGGPLFDKDGGGLDNpeavDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGpwaalAANKVK 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 782700300  294 IQAKLLEASKVEVVEVPFPSDSGKPALEYLVNGFAVFNNKDDKKVAasKKFVQFIADDK 352
Cdd:pfam01547 235 LKVAFAAPAPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGSKNKEAA--KKFLDFLTSPE 291
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 25-439 6.52e-50

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 173.31  E-value: 6.52e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  25 SGGSKDAAKSGGDGAKTEITWWAfpvftqekTGDGVGTYEKSIIEAFEKANPDVKVKLETIDFKSGPEKITTAIEAGTAP 104
Cdd:COG1653   17 AACGGGGSGAAAAAGKVTLTVWH--------TGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 105 DVLFDAPGRIIQYGKNGKLAELNDLFT-DEFVKDVNNENIVQASKAGDKAYMYPISSAPFYMAMNKKMLEEAGvanlVKE 183
Cdd:COG1653   89 DVVQVDSGWLAEFAAAGALVPLDDLLDdDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAG----LDP 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 184 GWTTDDFEKVLKALKDK-GYTPgslFSSGQGGDQGTRAFISNlYGGSVTDKDvTKYTTDDPKFVKGLEKAAGWIKDGLLN 262
Cdd:COG1653  165 PKTWDELLAAAKKLKAKdGVYG---FALGGKDGAAWLDLLLS-AGGDLYDED-GKPAFDSPEAVEALEFLKDLVKDGYVP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 263 NGS-QFDGGADIQNFANGQTSYTILWAPAQNGIQAkllEASKVEVVEVPFPSDSGKPALEYLVNGFAVFNNKDDKKVAAS 341
Cdd:COG1653  240 PGAlGTDWDDARAAFASGKAAMMINGSWALGALKD---AAPDFDVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPEAA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 342 KKFVQFIADDKEWgpkdvvrtgafpvrtsfgklyedkrmetisgwtkyyspyyntingfaemrtLWFPMLQSVSNGDEKP 421
Cdd:COG1653  317 WKFLKFLTSPEAQ---------------------------------------------------AKWDALQAVLLGQKTP 345

                        410
                 ....*....|....*...
gi 782700300 422 ADALKAFTEKANETIKKA 439
Cdd:COG1653  346 EEALDAAQAAANAALARA 363
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 42-432 8.71e-49

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: 171.05  E-value: 8.71e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  42 EITWWAFPVFTQEKtgdgvgtYEKSIIEAFEKANPDVKVKLETIDFKSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKNG 121
Cdd:cd13585    1 TLTFWDWGQPAETA-------ALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 122 KLAELNDLFTDEFVKDVNNENIVQASKAGDKAYMYPISSAPFYMAMNKKMLEEAGVAnlVKEGWTTDDFEKVLKALKDKG 201
Cdd:cd13585   74 ALLDLDDYIEKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPG--PKPPWTWDELLEAAKKLTDKK 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 202 YTPGSLFSSGQGGDQGTRAFISNLYGGSVTDKDVTKYTTDDPKFVKGLEKAAGWIKDGLLNNGSQFDGGADIQNFANGQT 281
Cdd:cd13585  152 GGQYGFALRGGSGGQTQWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFASGKV 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 282 SYTILWAPAQNGIQAkllEASKVEVVEVPFPS-DSGKPALEYLVNGFAVFNNKDDKKVAAskKFVQFIADD---KEWGPK 357
Cdd:cd13585  232 AMMIDGPWALGTLKD---SKVKFKWGVAPLPAgPGGKRASVLGGWGLAISKNSKHPEAAW--KFIKFLTSKenqLKLGGA 306

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 782700300 358 DVVRTGAFPVRTSFGKLYEDKRMETISGWTKYYSPYYNTINGFAEMRTLWFPMLQSVSNGDEK--PADALKAFTEKA 432
Cdd:cd13585  307 AGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGALGksPEEALKEAAKEI 383
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
25-438 4.26e-39

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 145.48  E-value: 4.26e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  25 SGGSKDAAKSGGDGAKTEITWWAfpvftqektGDGVGTYEKSIIEAFEKAnPDVKVKLETIDFKSGPEKITTAIEAGTAP 104
Cdd:COG2182   23 GSGSSSSGSSSAAGAGGTLTVWV---------DDDEAEALEEAAAAFEEE-PGIKVKVVEVPWDDLREKLTTAAPAGKGP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 105 DVLFDAPGRIIQYGKNGKLAELNDLFTDefvKDVNNENIVQASKAGDKAYMYPISSAPFYMAMNKKMLEEAGVAnlvkeg 184
Cdd:COG2182   93 DVFVGAHDWLGELAEAGLLAPLDDDLAD---KDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKAEPPK------ 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 185 wTTDDFEKVLKALKDKGYTPgslFSSGQGGDQGTRAFISNlYGGSVTDK---DVTKYTTDDPKFVKGLEKAAGWIKDGLL 261
Cdd:COG2182  164 -TWDELIAAAKKLTAAGKYG---LAYDAGDAYYFYPFLAA-FGGYLFGKdgdDPKDVGLNSPGAVAALEYLKDLIKDGVL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 262 NNGSqfDGGADIQNFANGQTSYTILWAPAQNGIQAKLleASKVEVVEVPFPSDsGKPALEYL-VNGFAVFNNKDDKKVAa 340
Cdd:COG2182  239 PADA--DYDAADALFAEGKAAMIINGPWAAADLKKAL--GIDYGVAPLPTLAG-GKPAKPFVgVKGFGVSAYSKNKEAA- 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 341 sKKFVQFIADDkewgpkDVVR-----TGAFPVRTSFGKLYEDKRMETISGWTKYYSpyyNTIN--GFAEMRTLWFPM--- 410
Cdd:COG2182  313 -QEFAEYLTSP------EAQKalfeaTGRIPANKAAAEDAEVKADPLIAAFAEQAE---YAVPmpNIPEMGAVWTPLgta 382

                        410       420
                 ....*....|....*....|....*...
gi 782700300 411 LQSVSNGDEKPADALKAFTEKANETIKK 438
Cdd:COG2182  383 LQAIASGKADPAEALDAAQKQIEAAIAQ 410
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 42-432 2.10e-36

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: 137.42  E-value: 2.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  42 EITWWAFpvftqekTGDGVGTYEKSIIEAFEKANPDVKVKLETI-DFKSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKN 120
Cdd:cd14748    1 EITFWHG-------MSGPDGKALEELVDEFNKSHPDIKVKAVYQgSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 121 GKLAELNDLFTDEFVKDVN-NENIVQASKAGDKAYMYPISSAPFYMAMNKKMLEEAGVaNLVKEGWTTDDFEKVLKALKD 199
Cdd:cd14748   74 GALEPLDDYIDKDGVDDDDfYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGL-DPEKPPKTWDELEEAAKKLKD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 200 KGYTPGSL-FSSGQGGDQGTRAFISNLYGGSVTDKDVTKYTTDDPKFVKGLEKAAGWI-KDGLLNNGSQFDGGadiQNFA 277
Cdd:cd14748  153 KGGKTGRYgFALPPGDGGWTFQALLWQNGGDLLDEDGGKVTFNSPEGVEALEFLVDLVgKDGVSPLNDWGDAQ---DAFI 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 278 NGQTSYTILWAPAQNGIQAKlleASKVEVVEVPFPSDSGKPaleYLV----NGFAVFNNKDDKKvAASKKFVQFIAdDKE 353
Cdd:cd14748  230 SGKVAMTINGTWSLAGIRDK---GAGFEYGVAPLPAGKGKK---GATpaggASLVIPKGSSKKK-EAAWEFIKFLT-SPE 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 354 WGPKDVVRTGAFPVRTS-----FGKLYEDKRMETISGWTKYYSPYYNTINGFAEMRTLWFPMLQSVSNGDEKPADALKAF 428
Cdd:cd14748  302 NQAKWAKATGYLPVRKSaaedpEEFLAENPNYKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEA 381


                 ....
gi 782700300 429 TEKA 432
Cdd:cd14748  382 QEKI 385
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 42-390 3.61e-33

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: 128.65  E-value: 3.61e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  42 EITWWAFPvftqekTGDGVGTYEKSIIEAFEKANPDVKVKLETIDFKSGPEKITTAIEAGTAPDVLFDAPGRIIQ-YGKN 120
Cdd:cd14749    1 TITYWQYF------TGDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPGGWLAeFVKA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 121 GKLAELNDLFTDEFVKDVNNENIVQASKAGDKAYMYPISSAPFYMAMNKKMLEEAGVANLVKegwTTDDFEKVLKALKDK 200
Cdd:cd14749   75 GLLLPLTDYLDPNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGVKPPK---TWDELIEAAKKDKFK 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 201 GY--TPGSLfssgQGGDQGTRAFISNL---YGGSVTDKDVTKYTT-DDPKFVKGLEKAAGWIKDGLLN-NGSQFDGGADI 273
Cdd:cd14749  152 AKgqTGFGL----LLGAQGGHWYFQYLvrqAGGGPLSDDGSGKATfNDPAFVQALQKLQDLVKAGAFQeGFEGIDYDDAG 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 274 QNFANGQTSYTILwAPAQNGIQAKLLEASKVEVVEVPFPSDSGKPALEYlVNGFAVFNNKDDKKVAASKKFVQFIADD-- 351
Cdd:cd14749  228 QAFAQGKAAMNIG-GSWDLGAIKAGEPGGKIGVFPFPTVGKGAQTSTIG-GSDWAIAISANGKKKEAAVKFLKYLTSPev 305

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 782700300 352 -KEWgpkdVVRTGAFPVRTSFGKLYEDKRMETISGWTKYY 390
Cdd:cd14749  306 mKQY----LEDVGLLPAKEVVAKDEDPDPVAILGPFADVL 341
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 42-437 3.20e-24

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: 103.55  E-value: 3.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  42 EITWWAFPVFTQEKtgdgvgtYEKSIIEAFEKANPDVKVKLETIDFKSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKNG 121
Cdd:cd14747    1 TLTVWAMGNSAEAE-------LLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 122 KLAELNDLFTDEFVKDVNNENIVQASKAGDKAYMYPI---SSAPFYmamNKKMLEEAGVANLVKegwTTDDFEKVLKALK 198
Cdd:cd14747   74 ALEDLTPYLEDLGGDKDLFPGLVDTGTVDGKYYGVPWyadTRALFY---RTDLLKKAGGDEAPK---TWDELEAAAKKIK 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 199 DKGYT-PGSLFSSGQGGDQGTRAFISNlYGGSVTDKDVTKYTTDDPKFVKGLEKAAGWIKDGLLNNGSQFDGGADIQNFA 277
Cdd:cd14747  148 ADGPDvSGFAIPGKNDVWHNALPFVWG-AGGDLATKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSADVEQAFA 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 278 NGQTSyTILWAPA-QNGIQ-AKLLEASKVEVveVPFPSDSGKPALEYL-VNGFAVFNNKDDKKvaASKKFVQFIAdDKEW 354
Cdd:cd14747  227 NGKVA-MIISGPWeIGAIReAGPDLAGKWGV--APLPGGPGGGSPSFAgGSNLAVFKGSKNKD--LAWKFIEFLS-SPEN 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 355 GPKDVVRTGAFPVRTSF---GKLYEDKRMETISGwTKYYSPYYNTINGFAEMRTLWFPMLQSVSNGD-EKPADALKAFTE 430
Cdd:cd14747  301 QAAYAKATGMLPANTSAwddPSLANDPLLAVFAE-QLKTGKATPATPEWGEIEAELVLVLEEVWIGVgADVEDALDKAAA 379


                 ....*..
gi 782700300 431 KANETIK 437
Cdd:cd14747  380 EINEILN 386
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 65-436 2.81e-22

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: 97.75  E-value: 2.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  65 KSIIEAFEKANpDVKVKLETIDFKSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKNGKLAELNDLFTDefvKDVNNENIV 144
Cdd:cd13586   16 KELAEEFEKKY-GIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLAV---KIKNLPVAL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 145 QASKAGDKAYMYPISSAPFYMAMNKKMLEEAgvanlVKegwTTDDFEKVLKALKDKGYTpGSLFSSGQGGDQGTRAFISn 224
Cdd:cd13586   92 AAVTYNGKLYGVPVSVETIALFYNKDLVPEP-----PK---TWEELIALAKKFNDKAGG-KYGFAYDQTNPYFSYPFLA- 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 225 LYGGSV---TDKDVTKYTTDDPKFVKGLEKAAGWIKDGLLNNGSQFDGGADiQNFANGQTSYTI--LWApaqngiqAKLL 299
Cdd:cd13586  162 AFGGYVfgeNGGDPTDIGLNNEGAVKGLKFIKDLKKKYKVLPPDLDYDIAD-ALFKEGKAAMIIngPWD-------LADY 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 300 EASKVEVVEVPFPSDSGKPALEYLVNGFAVFNNKDDKKVAASKKFVQFIADDKEwGPKDVVRTGAFPVRTSFGKLYEDKR 379
Cdd:cd13586  234 KDAGINFGVAPLPTLPGGKQAAPFVGVQGAFVSAYSKNKEAAVEFAEYLTSDEA-QLLLFEKTGRIPALKDALNDAAVKN 312

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 782700300 380 METISGWTKYYSpyyntiNGFA-----EMRTLWFPM---LQSVSNGDEKPADALKafteKANETI 436
Cdd:cd13586  313 DPLVKAFAEQAQ------YGVPmpnipEMAAVWDAMgnaLNLVASGKATPEEAAK----DAVAAI 367
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 65-352 6.76e-22

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: 95.18  E-value: 6.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300   65 KSIIEAFEKANPDVKVKLETIDFKSGPEKITTAIEAGTAP-DVLFDAPGRIIQYGKNGKLAELNDLFTDEFVKDVNneni 143
Cdd:pfam01547  11 QALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVANYLVLGVP---- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  144 vqaskagdKAYMYPISSAPFYMAMNKKMLEEAGvanlVKEGWTTDDFEKVLKALKDKGYTPGSLFSSGQGGDQGTRA-FI 222
Cdd:pfam01547  87 --------KLYGVPLAAETLGLIYNKDLFKKAG----LDPPKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGYFTlAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  223 SNLYGGSVTDKDVTKYTT----DDPKFVKGLEKAAGWIKDGLLNNGSQFDGGADIQNFANGQTSYTILW-----APAQNG 293
Cdd:pfam01547 155 LASLGGPLFDKDGGGLDNpeavDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGpwaalAANKVK 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 782700300  294 IQAKLLEASKVEVVEVPFPSDSGKPALEYLVNGFAVFNNKDDKKVAasKKFVQFIADDK 352
Cdd:pfam01547 235 LKVAFAAPAPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGSKNKEAA--KKFLDFLTSPE 291
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 67-351 9.04e-20

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 89.00  E-value: 9.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300   67 IIEAFEKANpDVKVKLETIDFKSGPEKITTAIEAGTAPD--VLFDAPGRIIQYGKNGKLAELNDLFTDEFVKDVNNEniv 144
Cdd:pfam13416   2 LAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDldVVWIAADQLATLAEAGLLADLSDVDNLDDLPDALDA--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  145 qASKAGDKAYMYPISSAPFYMAMNKKMLEEAGvanlvKEGWTTDDFEKVLKALKDKGYTPGSLFSSGQGGDQgtrafisn 224
Cdd:pfam13416  78 -AGYDGKLYGVPYAASTPTVLYYNKDLLKKAG-----EDPKTWDELLAAAAKLKGKTGLTDPATGWLLWALL-------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  225 lYGGsvtdkdvtKYTTDDPKFVKGLEKAAGWIKDgLLNNGSQFDGGAD-IQNFANGQTSYTILWAPAQNGIQAkllEASK 303
Cdd:pfam13416 144 -ADG--------VDLTDDGKGVEALDEALAYLKK-LKDNGKVYNTGADaVQLFANGEVAMTVNGTWAAAAAKK---AGKK 210

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 782700300  304 VEVVevpFPsdsgKPALEYLVNGFAVFNNKDDKKVAAsKKFVQFIADD 351
Cdd:pfam13416 211 LGAV---VP----KDGSFLGGKGLVVPAGAKDPRLAA-LDFIKFLTSP 250
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 43-427 2.84e-18

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: 85.89  E-value: 2.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  43 ITWWAfpVFTQEKTGdgvgTYEKsIIEAFEKANPDVKVKLETIDFKSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKNGK 122
Cdd:cd14751    2 ITFWH--TSSDEEKV----LYEK-LIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 123 LAELNDLFTDEFVKDVnNENIVQASKAGDKAYMYPISS---APFYmamNKKMLEEAGVAnlVKEGWttDDFEKVLKALKD 199
Cdd:cd14751   75 LQPLDGTPAFDDIVDY-LPGPMETNRYNGHYYGVPQVTntlALFY---NKRLLEEAGTE--VPKTM--DELVAAAKAIKK 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 200 KGYTPGsLFSSGQGGDQGTRAFISnlYGGSVTDKDVTKYTTDDPKFVKGLEKAAGWIKDGLLnnGSQFDGGADiqNFANG 279
Cdd:cd14751  147 KKGRYG-LYISGDGPYWLLPFLWS--FGGDLTDEKKATGYLNSPESVRALETIVDLYDEGAI--TPCASGGYP--NMQDG 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 280 QTSYTIL------WAPAQngIQAKLLEASKVEVVEVPFPSDSGKPAleyLVNG---FAVFNNKDDKKvaASKKFVQFIAD 350
Cdd:cd14751  220 FKSGRYAmivngpWAYAD--ILGGKEFKDPDNLGIAPVPAGPGGSG---SPVGgedLVIFKGSKNKD--AAWKFVKFMSS 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 351 DKEwGPKDVVRTGAFPVRTSfgkLYEDkrmETISGwTKYYSPYYN---------TINGFAEMRTLWFPMLQSVSNGDEKP 421
Cdd:cd14751  293 AEA-QALTAAKLGLLPTRTS---AYES---PEVAN-NPMVAAFKPaletavprpPIPEWGELFEPLTLAFAKVLRGEKSP 364


                 ....*.
gi 782700300 422 ADALKA 427
Cdd:cd14751  365 REALDE 370
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 43-432 2.32e-17

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: 83.23  E-value: 2.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  43 ITWWafpvfTQEKTGDGVGTyeKSIIEAFEKANPDVKVKLETIDFKSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKNGK 122
Cdd:cd13522    2 ITVW-----HQYDTGENQAV--NELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 123 LAELNDLFTDefvKDVNNENIVQASKAGDKAYMYPISSAPFYMAMNKKMLEEAGVAnlvkegwTTDDFEKVLKALKDKGy 202
Cdd:cd13522   75 LAPLDEYVSK---SGKYAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVPKNPPK-------TWQELIALAQGLKAKN- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 203 tpGSLFSSGQGGDQGTRAFISNlYGGSVTDKDVTKY--TTDDPKFVKGLEKAAGWIKDGLLNNGSQFDGGADiQNFANGQ 280
Cdd:cd13522  144 --VWGLVYNQNEPYFFAAWIGG-FGGQVFKANNGKNnpTLDTPGAVEALQFLVDLKSKYKIMPPETDYSIAD-ALFKAGK 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 281 TSYTILWAPAQNGIQakllEASKVEVVEVPFPSDSG-KPALEYlVNGFAVFNNKDDKKVAASKKFVQFI---------AD 350
Cdd:cd13522  220 AAMIINGPWDLGDYR----QALKINLGVAPLPTFSGtKHAAPF-VGGKGFGINKESQNKAAAVEFVKYLtsyqaqlvlFD 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 351 DKEWGPKDVVRTGAFPVRTSFGKLYEDKRMEtisgwtkYYSPYYNTingfAEMRTLWFPM---LQSVSNGDEKPADALKA 427
Cdd:cd13522  295 DAGDIPANLQAYESPAVQNKPAQKASAEQAA-------YGVPMPNI----PEMRAVWDAFriaVNSVLAGKVTPEAAAKD 363


                 ....*
gi 782700300 428 FTEKA 432
Cdd:cd13522  364 AQQEA 368
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 63-436 1.62e-16

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: 80.61  E-value: 1.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  63 YEKSIIEAFEKANpDVKVKLETIDFKSGPEKITTAIEAGTAPDVLFDAPGRIIQYGKNGKLAELNdlfTDEFVKDVNNEN 142
Cdd:cd13658   14 FIKKIAKQYTKKT-GVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIK---LSKDKKKGFTDQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 143 IVQASKAGDKAYMYPISSAPFYMAMNKKMLEEAGVanlvkegwTTDDFEKVLKAL-KDKGYTPGSLFSSGQGgdQGTRAF 221
Cdd:cd13658   90 ALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPK--------TFDELEALAKDLtKEKGKQYGFLADATNF--YYSYGL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 222 ISNlYGGSV-----TDKDVTKYTTDDPKFVKGLEKAAGWIKDGLLNNGSQFDggADIQNFANGQTSYTI--LWApaqngi 294
Cdd:cd13658  160 LAG-NGGYIfkkngSDLDINDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGD--VIQGLFKEGKAAAVIdgPWA------ 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 295 qAKLLEASKVEVVEVPFPS-DSGKPALEYL-VNGFAVfnNKDDKKVAASKKFVQFIAdDKEWGPKDVVRTGAFPVRTSFG 372
Cdd:cd13658  231 -IQEYQEAGVNYGVAPLPTlPNGKPMAPFLgVKGWYL--SAYSKHKEWAQKFMEFLT-SKENLKKRYDETNEIPPRKDVR 306

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 782700300 373 KLYEDKRMETISGWTKYYSPYYNTINgFAEMRTLWFPM---LQSVSNGDEKPADALKAFTEKANETI 436
Cdd:cd13658  307 SDPEIKNNPLTSAFAKQASRAVPMPN-IPEMGAVWEPAnnaLFFILSGKKTPKQALNDAVNDIKENI 372
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 65-427 5.81e-16

The periplasmic binding component of ABC transport system specific for maltodextrin; This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270375 [Multi-domain]  Cd Length: 368  Bit Score: 78.96  E-value: 5.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  65 KSIIEAFEKANPDVKVKletIDFKSGPE---KITTAIEAGTAPDVLFDAPGRIIQYGKNGKLAELNDLFTDEFVKDVnNE 141
Cdd:cd13657   17 QQIIDEFEAKYPVPNVK---VPFEKKPDlqnKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISDYLSEDDFENY-LP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 142 NIVQASKAGDKAYMYPISS---APFYmamNKKMLEEAGVanlvkegwTTDDFEKVLKALKDKgyTPGslfSSGQGGDQGT 218
Cdd:cd13657   93 TAVEAVTYKGKVYGLPEAYetvALIY---NKALVDQPPE--------TTDELLAIMKDHTDP--AAG---SYGLAYQVSD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 219 RAFIS---NLYGGSVTDKDVTKYTTDDPKFVKGLEKAAGWIKDGLLNNGSqfdgGADIQN-FANGQTSYTIL--WAPAqn 292
Cdd:cd13657  157 AYFVSawiFGFGGYYFDDETDKPGLDTPETIKGIQFLKDFSWPYMPSDPS----YNTQTSlFNEGKAAMIINgpWFIG-- 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 293 GIQAKLleaSKVEVVEVPfPSDSGKPALEYL-VNGFAVFNNKDDKKVAASKKFVQFIADDkewgpkDVVRT-----GAFP 366
Cdd:cd13657  231 GIKAAG---IDLGVAPLP-TVDGTNPPRPYSgVEGIYVTKYAERKNKEAALDFAKFFTTA------EASKIladenGYVP 300

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 367 VRTsfgKLYEDKRM---ETISGWTK---YYSPYYNTingfAEMRTLWFPM---LQSVSNGDEKPADALKA 427
Cdd:cd13657  301 AAT---NAYDDAEVaadPVIAAFKAqaeHGVPMPNS----PEMASVWGPVtlaLAAVYQGGQDPQEALAA 363
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 42-431 7.00e-15

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: 75.79  E-value: 7.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  42 EITWWAFPVFTQEKtgdgvgtYEKSIIEAFEKANPDVKVKLETI-----DFKSgpeKITTAIEAG-TAPDVL-FDAPgRI 114
Cdd:cd14750    1 TITFAAGSDGQEGE-------LLKKAIAAFEKKHPDIKVEIEELpassdDQRQ---QLVTALAAGsSAPDVLgLDVI-WI 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 115 IQYGKNGKLAELNDLFTDEFVKDVNnENIVQASKAGDKAYmypisSAPFY-----MAMNKKMLEEAGVAnlVKEGWttDD 189
Cdd:cd14750   70 PEFAEAGWLLPLTEYLKEEEDDDFL-PATVEANTYDGKLY-----ALPWFtdaglLYYRKDLLEKYGPE--PPKTW--DE 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 190 FEKVLKALKDKGYTP-GSLFSSGQGGdqgtrAFISNL------YGGSVTDKDVTKYTTDDPKFVKGLEKAAGWIKDGLLN 262
Cdd:cd14750  140 LLEAAKKRKAGEPGIwGYVFQGKQYE-----GLVCNFlellwsNGGDIFDDDSGKVTVDSPEALEALQFLRDLIGEGISP 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 263 NGSQFDGGADIQN-FANGQTSYTILWaPAQNGiqakLLEASKVEVVEV----PFPS-DSGKPALeyLVNGFAVFNNKDDK 336
Cdd:cd14750  215 KGVLTYGEEEARAaFQAGKAAFMRNW-PYAYA----LLQGPESAVAGKvgvaPLPAgPGGGSAS--TLGGWNLAISANSK 287

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 337 KVAASKKFVQFIAdDKEWGPKDVVRTGAFPVRTSfgkLYEDKRMET-ISGWTKYY-----------SPYYNtingfaEMR 404
Cdd:cd14750  288 HKEAAWEFVKFLT-SPEVQKRRAINGGLPPTRRA---LYDDPEVLEaYPFLPALLealenavprpvTPKYP------EVS 357

                        410       420
                 ....*....|....*....|....*..
gi 782700300 405 TLWFPMLQSVSNGDEKPADALKAFTEK 431
Cdd:cd14750  358 TAIQIALSAALSGQATPEEALKQAQEK 384
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 40-442 1.49e-11

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: 66.20  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  40 KTEITWWAFPVFTQEKTGDGVGTYEKsiIEafEKANpdVKVKLETIDFKSGPEKITTAIEAGTAPDVLF-DAPGRIIQYG 118
Cdd:cd13580    2 PVTITIVANLGGNPKPDPDDNPYTKY--LE--EKTN--IDVKVKWVPDSSYDEKLNLALASGDLPDIVVvNDPQLSITLV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 119 KNGKLAELNDLFTDEF--VKDVNNENIVQASKAGDKAYMYPISSAP---FYMAMNKKMLEEAGVanlvKEGWTTDDFEKV 193
Cdd:cd13580   76 KQGALWDLTDYLDKYYpnLKKIIEQEGWDSASVDGKIYGIPRKRPLigrNGLWIRKDWLDKLGL----EVPKTLDELYEV 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 194 LKALKDK---GY----TPGSLFSSGQGGdqGTRAFISNLYGGSV----TDKDVT-KYTTDDPKFVKGLEKAAGWIKDGLL 261
Cdd:cd13580  152 AKAFTEKdpdGNgkkdTYGLTDTKDLIG--SGFTGLFGAFGAPPnnwwKDEDGKlVPGSIQPEMKEALKFLKKLYKEGLI 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 262 NNGSQFDGGADIQN-FANGQT--SYTILWAPAQNGIQAKlLEASKVEVVEVPFPSDSGKP---ALEYLVNGFAVFnNKDD 335
Cdd:cd13580  230 DPEFAVNDGTKANEkFISGKAgiFVGNWWDPAWPQASLK-KNDPDAEWVAVPIPSGPDGKygvWAESGVNGFFVI-PKKS 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 336 KKVAASKKFVQFIADD-----KEWGPKDVVRTGA-------FPVRTSFGKLYEDKRMETISGWTKYYSPYYNTINGFAEM 403
Cdd:cd13580  308 KKPEAILKLLDFLSDPevqklLDYGIEGVHYTVKdggpvniIPPDKQEVGDATLDYFQGSLALEKYKLTNNGERKSDAKK 387

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 782700300 404 RTLWFPMLQSVSNGDEK-----PADALKAFTEKANETIKKATKQ 442
Cdd:cd13580  388 EALDERVVNANDEENENiavgpPTETLVSPTEKYGATLDKLEDD 431
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 73-348 3.95e-11

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: 64.69  E-value: 3.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  73 KANPDVKVKLETIDFKSGPEKITTAIEAGTAPD---VLFdaPGRIIQYGKNGKLAELNDlFTDE------FVKDVNNENI 143
Cdd:cd13583   27 EEKTNVKFKRTPIPSSDYETKRSLLIASGDAPDiipVLY--PGEENEFVASGALLPISD-YLDYmpnykkYVEKWGLGKE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 144 VQASKAGD-KAYMYP---ISSAPFY-MAMNKKMLEEAGVanlvKEGWTTDDFEKVLKALKDKgyTPGSLFSSGQGGDQGT 218
Cdd:cd13583  104 LATGRQSDgKYYSLPglhEDPGVQYsFLYRKDIFEKAGI----KIPTTWDEFYAALKKLKEK--YPDSYPYSDRWNSNAL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 219 RAFISNLYGGS-VTDKDVTKYTTDDPKFVKG---------LEKAAGWIKDGLLNNGSQFDGGADI-QNFANGQTSYTILW 287
Cdd:cd13583  178 LLIAAPAFGTTaGWGFSNYTYDPDTDKFVYGattdeykdmLQYFNKLYAEGLLDPESFTQTDDQAkAKFLNGKSFVITTN 257

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 782700300 288 APAQNGIQAKLLEASKVEVVEVPFPSDSGKPALEY----LVNGFAVF-NNKDDKKVAASKKFVQFI 348
Cdd:cd13583  258 PQTVDELQRNLRAADGGNYEVVSITPPAGPAGKAIngsrLENGFMISsKAKDSKNFEALLQFLDWL 323
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 72-291 2.11e-09

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


Pssm-ID: 270299 [Multi-domain]  Cd Length: 490  Bit Score: 59.26  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  72 EKANpdVKVKLETIDFKSGPEKITTAIEAGTAPDVLFDA---PGRIIQYGKNGKLAELNDLFtDEF---VKDVNNEN--I 143
Cdd:cd13581   28 EKTG--IKIEWETVPEDAWAEKKNLMLASGDLPDAFLGAgasDADLMTYGKQGLFLPLEDLI-DKYapnLKALFDENpdI 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 144 VQASKAGD-KAYMYP------ISSAPFYMAMNKKMLEEAGVAnlVKEgwTTDDFEKVLKALKDK--------GYTPGSlF 208
Cdd:cd13581  105 KAAITAPDgHIYALPsvnecyHCSYGQRMWINKKWLDKLGLE--MPT--TTDELYEVLKAFKEQdpngngkaDEIPLS-F 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 209 SSGQGGDQGTR----AFISNLYGGS----VTDKDVTKYTTDDPKFVKGLEKAAGWIKDGLLNNGSqF--DGGADIQNFAN 278
Cdd:cd13581  180 SGLNGGTDDPAfllnSFGINDGGYGgygfVVKDGKVIYTATDPEYKEALAYLNKLYKEGLIDPEA-FtqDYDQLAAKGKA 258

                        250
                 ....*....|....*
gi 782700300 279 G--QTSYTILWAPAQ 291
Cdd:cd13581  259 StaKVGVFFGWDPGL 273
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 63-352 2.48e-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: 51.84  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  63 YEKSIIEAFEKANPdVKVKLETIdfkSGPEKITTAIEAGTAP--DVLFDAPGRIIQYGKNGKLAELNDlftdefvKDVNN 140
Cdd:cd13589   15 QRKAVIEPFEKETG-IKVVYDTG---TSADRLAKLQAQAGNPqwDVVDLDDGDAARAIAEGLLEPLDY-------SKIPN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 141 ENIVQASKAGDKAYMYPISSAPFYMAMNKKMLEEAGVAnlvkegWTTDDFekvlkalKDKGYTPGSLFSSGQGgdQGTRA 220
Cdd:cd13589   84 AAKDKAPAALKTGYGVGYTLYSTGIAYNTDKFKEPPTS------WWLADF-------WDVGKFPGPRILNTSG--LALLE 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 221 FISNLYGGSVTDKDVtkyttdDPKFvKGLEKaagwIKDGLLnngSQFDGGADIQN-FANGQTSYTILW-APAQNGIQAKL 298
Cdd:cd13589  149 AALLADGVDPYPLDV------DRAF-AKLKE----LKPNVV---TWWTSGAQLAQlLQSGEVDMAPAWnGRAQALIDAGA 214

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 782700300 299 leasKVEVVevpFPsDSGKPAleyLVNGFAVfnNKDDKKVAASKKFVQFIADDK 352
Cdd:cd13589  215 ----PVAFV---WP-KEGAIL---GPDTLAI--VKGAPNKELAMKFINFALSPE 255
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 65-211 2.63e-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: 49.27  E-value: 2.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  65 KSIIEAFEKANPDVKvkletIDFKSGPEKITTAIE-----AGTAPDVLFDAPGRIIQYGKNGKLAELNDlFTDEFVKDVN 139
Cdd:cd13655   15 KEMVDAFKEKHPEWK-----ITITIGVVGEADAKDevlkdPSAAADVFAFANDQLGELVDAGAIYPLTG-SAVDKIKNTN 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 782700300 140 NENIVQASKAGDKAYMYPISSAPFYMAMNKKMLEEAGVANLvkegwttddfEKVLKALKDKGYTPGSLFSSG 211
Cdd:cd13655   89 SEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLTEDDVKSL----------DTMLAKAPDAKGKVSFDLSNS 150
PBP2_AlgQ1_2 cd13584
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 ...
 69-343 2.39e-05

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: 46.66  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  69 EAFEKANpdvkVKLETIDFKSG---PEKITTAIEAGTAPDVL----FDAPGRIIQYGKNGKLAELNDL----------FT 131
Cdd:cd13584   25 EMERKTN----VKLNFVANPVAqnsQEQFNLMMASGQLPDIIggdwLKDKGGFEKYGEDGAFLPLNDLidqyapnlkkFL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 132 DEfvkdvnNENIVQASKAGD-KAYMYPissapfYMAMNKKMLEEAGVAnlVKEGW----------TTDDFEKVLKALKDK 200
Cdd:cd13584  101 DE------HPDVKKAITTDDgNIYGFP------YLPDGDVAKEARGYF--IRKDWldklglktpsTIDEWYTVLKAFKER 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300 201 -----GYTPGSLFSSGQGGDQGTRAFIsNLYG---GSVTDKDVTKYTTDDPKFVKGLEKAAGWIKDGLLN-NGSQFDGGA 271
Cdd:cd13584  167 dpngnGKADEVPLILTKPGYDETGRLI-NAWGaymDFYQENGKVKYGPLEPGFKDFLKTMNQWYKEGLIDpDFFTRKAKA 245

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 782700300 272 DIQNFANGQT-SYTILWAPAQNGIQAKLLEA-SKVEVVEVPFP--SDSGKPALEYLVNGFavfnNKDDKKVAASKK 343
Cdd:cd13584  246 REQNIMNGNIgGFTHDWFASTGTFNLALLKNvPDFKLVAVPPPvlNKGQTPYEEDSRQIA----KGDGAAITASNK 317
PBP2_Fbp_like_2 cd13547
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 65-170 9.54e-04

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


Pssm-ID: 270265 [Multi-domain]  Cd Length: 259  Bit Score: 40.67  E-value: 9.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 782700300  65 KSIIEAFEKANPDVKVKLetidFKSGPEKITTAIEA-----GTAPDVLFDA-PGRIIQYGKNGKLAElndlftdefVKDV 138
Cdd:cd13547   14 NALVEAFEKKYPGVKVEV----FRAGTGKLMAKLAAeaeagNPQADVLWVAdPPTAEALKKEGLLLP---------YKSP 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 782700300 139 NNENIVQASKAGDKAYmYPISSAPFYMAMNKK 170
Cdd:cd13547   81 EADAIPAPFYDKDGYY-YGTRLSAMGIAYNTD 111
 
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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