NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|737225886|ref|WP_035210296|]
View 

extracellular solute-binding protein [Agrobacterium pusense]

Protein Classification

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Periplasmic_Binding_Protein_Type_2 super family cl21456
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 29-440 4.64e-110

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


The actual alignment was detected with superfamily member PRK10974:

Pssm-ID: 473866 [Multi-domain]  Cd Length: 438  Bit Score: 331.76  E-value: 4.64e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886  29 TKFEFWYGLSGDLGERVQDTCKKFNESQAEFEIVCTSQNDYDATLQNTIAAYRAKKQPAITQIYDAGTLDMMLSKAFVPA 108
Cdd:PRK10974  26 TEIPFWHSMEGELGKEVDSLAQRFNASQPDYKIVPVYKGNYEQSLAAGIAAFRSGNAPAILQVYEVGTATMMASKAIKPV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 109 KKLMADNGYKIDWDNYFPGIANYYATA-AGELNSFPYNSSTAVFYYNVDAFEKAGITFK--PDTWEQVEEAAKKLKAAGF 185
Cdd:PRK10974 106 YDVFKDAGIPFDESQFVPTVAGYYSDAkTGHLLSQPFNSSTPVLYYNKDAFKKAGLDPEqpPKTWQDLAAYAAKLRAAGM 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 186 ECPLAFNFDTWMLMEQFSAIHNQPIATKGNGYQGLDAELTINKTKFVDHVKFFKKMQDEKLFVVKTKQlgMDILPAFTSQ 265
Cdd:PRK10974 186 KCGYASGWQGWIQLENFSAWHGLPFASKNNGFDGTDAVLEFNKPEQVKHIALLEEMNKKGDFTYVGRK--DESTEKFYNG 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 266 TCQMFMSSIAGHGTVGKgmpeGVKWD--VAMLPV---WKGTQrQNSLVGGASLWVMAGRPEAEYKGAAAFLNFIAQPEMV 340
Cdd:PRK10974 264 DCAITTASSGSLANIRK----YAKFNygVGMMPYdadVKGAP-QNAIIGGASLWVMQGKDKETYKGVAKFLDFLAKPENA 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 341 QWWSTVTGYIPVTKTGFDAMKANGFYDKAPykGREKAIESLTFTPPSEYTRGIRLGNFTQIRKEVSTALEAIFMQNADVQ 420
Cdd:PRK10974 339 AEWHQKTGYLPITTAAYDLTREQGFYEKNP--GADTATRQMLNKPPLPFTKGLRLGNMPQIRTIVDEELESVWTGKKTPQ 416

                        410       420
                 ....*....|....*....|
gi 737225886 421 GELDKAVERSNAGLRRFEKT 440
Cdd:PRK10974 417 QALDSAVERGNQLLRRFEKS 436
 
Name Accession Description Interval E-value
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
29-440 4.64e-110

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 331.76  E-value: 4.64e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886  29 TKFEFWYGLSGDLGERVQDTCKKFNESQAEFEIVCTSQNDYDATLQNTIAAYRAKKQPAITQIYDAGTLDMMLSKAFVPA 108
Cdd:PRK10974  26 TEIPFWHSMEGELGKEVDSLAQRFNASQPDYKIVPVYKGNYEQSLAAGIAAFRSGNAPAILQVYEVGTATMMASKAIKPV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 109 KKLMADNGYKIDWDNYFPGIANYYATA-AGELNSFPYNSSTAVFYYNVDAFEKAGITFK--PDTWEQVEEAAKKLKAAGF 185
Cdd:PRK10974 106 YDVFKDAGIPFDESQFVPTVAGYYSDAkTGHLLSQPFNSSTPVLYYNKDAFKKAGLDPEqpPKTWQDLAAYAAKLRAAGM 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 186 ECPLAFNFDTWMLMEQFSAIHNQPIATKGNGYQGLDAELTINKTKFVDHVKFFKKMQDEKLFVVKTKQlgMDILPAFTSQ 265
Cdd:PRK10974 186 KCGYASGWQGWIQLENFSAWHGLPFASKNNGFDGTDAVLEFNKPEQVKHIALLEEMNKKGDFTYVGRK--DESTEKFYNG 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 266 TCQMFMSSIAGHGTVGKgmpeGVKWD--VAMLPV---WKGTQrQNSLVGGASLWVMAGRPEAEYKGAAAFLNFIAQPEMV 340
Cdd:PRK10974 264 DCAITTASSGSLANIRK----YAKFNygVGMMPYdadVKGAP-QNAIIGGASLWVMQGKDKETYKGVAKFLDFLAKPENA 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 341 QWWSTVTGYIPVTKTGFDAMKANGFYDKAPykGREKAIESLTFTPPSEYTRGIRLGNFTQIRKEVSTALEAIFMQNADVQ 420
Cdd:PRK10974 339 AEWHQKTGYLPITTAAYDLTREQGFYEKNP--GADTATRQMLNKPPLPFTKGLRLGNMPQIRTIVDEELESVWTGKKTPQ 416

                        410       420
                 ....*....|....*....|
gi 737225886 421 GELDKAVERSNAGLRRFEKT 440
Cdd:PRK10974 417 QALDSAVERGNQLLRRFEKS 436
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 30-429 7.09e-61

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: 202.91  E-value: 7.09e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886  30 KFEFWYGLSGDLGERVQDTCKKFNESQAEFEIVCTSQNDYDATLQNTIAAYRAKKQPAITQIYDAGTLDMMLSKAFVPAK 109
Cdd:cd14748    1 EITFWHGMSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 110 KLMADNGYkiDWDNYFPGIANYYaTAAGELNSFPYNSSTAVFYYNVDAFEKAGITFK--PDTWEQVEEAAKKLKA----- 182
Cdd:cd14748   81 DYIDKDGV--DDDDFYPAALDAG-TYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEkpPKTWDELEEAAKKLKDkggkt 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 183 --AGFEcplAFNFDTWMLMEQFSAIHNQPIATKGNGyqgldaELTINKTKFVDHVKFFKKM-QDEKlfvVKTKQLGMDIL 259
Cdd:cd14748  158 grYGFA---LPPGDGGWTFQALLWQNGGDLLDEDGG------KVTFNSPEGVEALEFLVDLvGKDG---VSPLNDWGDAQ 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 260 PAFTSQTCQMFMSSIAGHGTVgKGMPEGVKWDVAMLPVWKGTQRqNSLVGGASLWVMAGRPEaEYKGAAAFLNFIAQPEM 339
Cdd:cd14748  226 DAFISGKVAMTINGTWSLAGI-RDKGAGFEYGVAPLPAGKGKKG-ATPAGGASLVIPKGSSK-KKEAAWEFIKFLTSPEN 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 340 VQWWSTVTGYIPVTKTGFDAmkANGFYDKAPYkgREKAIESLTFTPPseytRGIRLGNFTQIRKEVSTALEAIFMQNADV 419
Cdd:cd14748  303 QAKWAKATGYLPVRKSAAED--PEEFLAENPN--YKVAVDQLDYAKP----WGPPVPNGAEIRDELNEALEAALLGKKTP 374

                        410
                 ....*....|
gi 737225886 420 QGELDKAVER 429
Cdd:cd14748  375 EEALKEAQEK 384
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 27-350 1.36e-46

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 164.45  E-value: 1.36e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886  27 EKTKFEFWYGlSGDLGERVQDTCKKFNESQAEFEIVCTSQnDYDATLQNTIAAYRAKKQPAITQIYDAGTLDMMLSKAFV 106
Cdd:COG1653   31 GKVTLTVWHT-GGGEAAALEALIKEFEAEHPGIKVEVESV-PYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALV 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 107 PAKKLMADNGykIDWDNYFPGIANYYaTAAGELNSFPYNSSTAVFYYNVDAFEKAGITFkPDTWEQVEEAAKKLKAAGFE 186
Cdd:COG1653  109 PLDDLLDDDG--LDKDDFLPGALDAG-TYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDP-PKTWDELLAAAKKLKAKDGV 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 187 CPLAFNFDTWMLMEQFsaihnqpIATKGNGYQGLDAELTINKTKFVDHVKFFKKMQDEKLFVVKTKQLGM-DILPAFTSQ 265
Cdd:COG1653  185 YGFALGGKDGAAWLDL-------LLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKDGYVPPGALGTDWdDARAAFASG 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 266 TCQMFMSSIAGHGTVGKGMPeGVKWDVAMLPVWKGTQRQNSLVGGASLWVMAGRPEAEykGAAAFLNFIAQPEMVQWWST 345
Cdd:COG1653  258 KAAMMINGSWALGALKDAAP-DFDVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPE--AAWKFLKFLTSPEAQAKWDA 334


                 ....*
gi 737225886 346 VTGYI 350
Cdd:COG1653  335 LQAVL 339
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 49-355 7.27e-18

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 83.22  E-value: 7.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886   49 CKKFNEsQAEFEIVCTSQnDYDATLQNTIAAYRAKKQPAITQIYDAGtldmmlskafvPAKKLMADNGYKIDWDnYFPGI 128
Cdd:pfam13416   3 AKAFEK-KTGVTVEVEPQ-ASNDLQAKLLAAAAAGNAPDLDVVWIAA-----------DQLATLAEAGLLADLS-DVDNL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886  129 ANYYATAA-----GELNSFPYNSSTA-VFYYNVDAFEKAGITfkPDTWEQVEEAAKKLKAAGfecplAFNFDTWMLMEQF 202
Cdd:pfam13416  69 DDLPDALDaagydGKLYGVPYAASTPtVLYYNKDLLKKAGED--PKTWDELLAAAAKLKGKT-----GLTDPATGWLLWA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886  203 SAIHNQPIATKGNGYQGLDAELTInKTKFVDHVKFFKKmqdeklfvvktkqlGMDILPAFTSQTCQMFMSSIaghGTVGK 282
Cdd:pfam13416 142 LLADGVDLTDDGKGVEALDEALAY-LKKLKDNGKVYNT--------------GADAVQLFANGEVAMTVNGT---WAAAA 203

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737225886  283 GMPEGVKWDVAMLPvwkgtqrQNSLVGGASLWVMAGRPEAEYkGAAAFLNFIAQPEMVQWWSTVTGYIPVTKT 355
Cdd:pfam13416 204 AKKAGKKLGAVVPK-------DGSFLGGKGLVVPAGAKDPRL-AALDFIKFLTSPENQAALAEDTGYIPANKS 268
 
Name Accession Description Interval E-value
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
29-440 4.64e-110

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 331.76  E-value: 4.64e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886  29 TKFEFWYGLSGDLGERVQDTCKKFNESQAEFEIVCTSQNDYDATLQNTIAAYRAKKQPAITQIYDAGTLDMMLSKAFVPA 108
Cdd:PRK10974  26 TEIPFWHSMEGELGKEVDSLAQRFNASQPDYKIVPVYKGNYEQSLAAGIAAFRSGNAPAILQVYEVGTATMMASKAIKPV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 109 KKLMADNGYKIDWDNYFPGIANYYATA-AGELNSFPYNSSTAVFYYNVDAFEKAGITFK--PDTWEQVEEAAKKLKAAGF 185
Cdd:PRK10974 106 YDVFKDAGIPFDESQFVPTVAGYYSDAkTGHLLSQPFNSSTPVLYYNKDAFKKAGLDPEqpPKTWQDLAAYAAKLRAAGM 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 186 ECPLAFNFDTWMLMEQFSAIHNQPIATKGNGYQGLDAELTINKTKFVDHVKFFKKMQDEKLFVVKTKQlgMDILPAFTSQ 265
Cdd:PRK10974 186 KCGYASGWQGWIQLENFSAWHGLPFASKNNGFDGTDAVLEFNKPEQVKHIALLEEMNKKGDFTYVGRK--DESTEKFYNG 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 266 TCQMFMSSIAGHGTVGKgmpeGVKWD--VAMLPV---WKGTQrQNSLVGGASLWVMAGRPEAEYKGAAAFLNFIAQPEMV 340
Cdd:PRK10974 264 DCAITTASSGSLANIRK----YAKFNygVGMMPYdadVKGAP-QNAIIGGASLWVMQGKDKETYKGVAKFLDFLAKPENA 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 341 QWWSTVTGYIPVTKTGFDAMKANGFYDKAPykGREKAIESLTFTPPSEYTRGIRLGNFTQIRKEVSTALEAIFMQNADVQ 420
Cdd:PRK10974 339 AEWHQKTGYLPITTAAYDLTREQGFYEKNP--GADTATRQMLNKPPLPFTKGLRLGNMPQIRTIVDEELESVWTGKKTPQ 416

                        410       420
                 ....*....|....*....|
gi 737225886 421 GELDKAVERSNAGLRRFEKT 440
Cdd:PRK10974 417 QALDSAVERGNQLLRRFEKS 436
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 30-429 7.09e-61

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: 202.91  E-value: 7.09e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886  30 KFEFWYGLSGDLGERVQDTCKKFNESQAEFEIVCTSQNDYDATLQNTIAAYRAKKQPAITQIYDAGTLDMMLSKAFVPAK 109
Cdd:cd14748    1 EITFWHGMSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 110 KLMADNGYkiDWDNYFPGIANYYaTAAGELNSFPYNSSTAVFYYNVDAFEKAGITFK--PDTWEQVEEAAKKLKA----- 182
Cdd:cd14748   81 DYIDKDGV--DDDDFYPAALDAG-TYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEkpPKTWDELEEAAKKLKDkggkt 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 183 --AGFEcplAFNFDTWMLMEQFSAIHNQPIATKGNGyqgldaELTINKTKFVDHVKFFKKM-QDEKlfvVKTKQLGMDIL 259
Cdd:cd14748  158 grYGFA---LPPGDGGWTFQALLWQNGGDLLDEDGG------KVTFNSPEGVEALEFLVDLvGKDG---VSPLNDWGDAQ 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 260 PAFTSQTCQMFMSSIAGHGTVgKGMPEGVKWDVAMLPVWKGTQRqNSLVGGASLWVMAGRPEaEYKGAAAFLNFIAQPEM 339
Cdd:cd14748  226 DAFISGKVAMTINGTWSLAGI-RDKGAGFEYGVAPLPAGKGKKG-ATPAGGASLVIPKGSSK-KKEAAWEFIKFLTSPEN 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 340 VQWWSTVTGYIPVTKTGFDAmkANGFYDKAPYkgREKAIESLTFTPPseytRGIRLGNFTQIRKEVSTALEAIFMQNADV 419
Cdd:cd14748  303 QAKWAKATGYLPVRKSAAED--PEEFLAENPN--YKVAVDQLDYAKP----WGPPVPNGAEIRDELNEALEAALLGKKTP 374

                        410
                 ....*....|
gi 737225886 420 QGELDKAVER 429
Cdd:cd14748  375 EEALKEAQEK 384
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 27-350 1.36e-46

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 164.45  E-value: 1.36e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886  27 EKTKFEFWYGlSGDLGERVQDTCKKFNESQAEFEIVCTSQnDYDATLQNTIAAYRAKKQPAITQIYDAGTLDMMLSKAFV 106
Cdd:COG1653   31 GKVTLTVWHT-GGGEAAALEALIKEFEAEHPGIKVEVESV-PYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALV 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 107 PAKKLMADNGykIDWDNYFPGIANYYaTAAGELNSFPYNSSTAVFYYNVDAFEKAGITFkPDTWEQVEEAAKKLKAAGFE 186
Cdd:COG1653  109 PLDDLLDDDG--LDKDDFLPGALDAG-TYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDP-PKTWDELLAAAKKLKAKDGV 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 187 CPLAFNFDTWMLMEQFsaihnqpIATKGNGYQGLDAELTINKTKFVDHVKFFKKMQDEKLFVVKTKQLGM-DILPAFTSQ 265
Cdd:COG1653  185 YGFALGGKDGAAWLDL-------LLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKDGYVPPGALGTDWdDARAAFASG 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 266 TCQMFMSSIAGHGTVGKGMPeGVKWDVAMLPVWKGTQRQNSLVGGASLWVMAGRPEAEykGAAAFLNFIAQPEMVQWWST 345
Cdd:COG1653  258 KAAMMINGSWALGALKDAAP-DFDVGVAPLPGGPGGKKPASVLGGSGLAIPKGSKNPE--AAWKFLKFLTSPEAQAKWDA 334


                 ....*
gi 737225886 346 VTGYI 350
Cdd:COG1653  335 LQAVL 339
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 30-429 1.64e-34

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: 132.53  E-value: 1.64e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886  30 KFEFWYGLSGDLGERVQDTCKKFNES--QAEFEIVCTSQNDYDATLQNTIAAyraKKQPAITQIYDAGTLDMMLSKAFVP 107
Cdd:cd13585    1 TLTFWDWGQPAETAALKKLIDAFEKEnpGVKVEVVPVPYDDYWTKLTTAAAA---GTAPDVFYVDGPWVPEFASNGALLD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 108 AKKLMADNGYKidwDNYFPGIANYYaTAAGELNSFPYNSSTAVFYYNVDAFEKAGITFKPD-TWEQVEEAAKKLKAA--- 183
Cdd:cd13585   78 LDDYIEKDGLD---DDFPPGLLDAG-TYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPwTWDELLEAAKKLTDKkgg 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 184 --GFecPLAFNFDTWMLMEQFSAIHNQPIATKGNGyqgldaELTINKTKFVDHVKFFKKMQDEKLFVVKTKQLGMDILPA 261
Cdd:cd13585  154 qyGF--ALRGGSGGQTQWYPFLWSNGGDLLDEDDG------KATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDL 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 262 FTSQTCQMFMSSIAGHGTVGKGMPEGvKWDVAMLPVWKGTQRQnSLVGGASLWVMAG--RPEAeykgAAAFLNFIAQPEM 339
Cdd:cd13585  226 FASGKVAMMIDGPWALGTLKDSKVKF-KWGVAPLPAGPGGKRA-SVLGGWGLAISKNskHPEA----AWKFIKFLTSKEN 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 340 VQWWstvtGYIPVTKTGFDAMKANGFYDKAPYKGREKAIESLTFTPPSEYTRgirlgNFTQIRKEVSTALEAIF--MQNA 417
Cdd:cd13585  300 QLKL----GGAAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPP-----PWPEVYPILSEALQEALlgALGK 370

                        410
                 ....*....|..
gi 737225886 418 DVQGELDKAVER 429
Cdd:cd13585  371 SPEEALKEAAKE 382
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 32-371 2.85e-20

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: 92.06  E-value: 2.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886  32 EFWYGLSGDlgervqDTCKKFNESQAEFE--------IVCTSQNDYDATLQNTIAAyrAKKQPAITQIYDAGTL-DMMLS 102
Cdd:cd14749    3 TYWQYFTGD------TKKKYMDELIADFEkenpnikvKVVVFPYDNYKTKLKTAVA--AGEGPDVFNLWPGGWLaEFVKA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 103 KAFVPAKKLMADNGYkidWDNYFPGIANYYaTAAGELNSFPYNSSTAVFYYNVDAFEKAGITFKPDTWEQVEEAAKKLK- 181
Cdd:cd14749   75 GLLLPLTDYLDPNGV---DKRFLPGLADAV-TFNGKVYGIPFAARALALFYNKDLFEEAGGVKPPKTWDELIEAAKKDKf 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 182 ----AAGFECPLAFNFDTWmlmeQFSAIhnqpiaTKGNGYqGLDAELTINKTKFVD--HVKFFKKMQDeklfVVKTKQLG 255
Cdd:cd14749  151 kakgQTGFGLLLGAQGGHW----YFQYL------VRQAGG-GPLSDDGSGKATFNDpaFVQALQKLQD----LVKAGAFQ 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 256 MDILPAFTSQTCQMFMS-----SIAGHGTVG---KGMPeGVKWDVAMLPVwKGTQRQNSLVGGASLWVMAGRPEAEYKGA 327
Cdd:cd14749  216 EGFEGIDYDDAGQAFAQgkaamNIGGSWDLGaikAGEP-GGKIGVFPFPT-VGKGAQTSTIGGSDWAIAISANGKKKEAA 293

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 737225886 328 AAFLNFIAQPEMVQWWSTVTGYIPVTKTGFDAMKANGFYDKAPY 371
Cdd:cd14749  294 VKFLKYLTSPEVMKQYLEDVGLLPAKEVVAKDEDPDPVAILGPF 337
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 49-355 7.27e-18

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 83.22  E-value: 7.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886   49 CKKFNEsQAEFEIVCTSQnDYDATLQNTIAAYRAKKQPAITQIYDAGtldmmlskafvPAKKLMADNGYKIDWDnYFPGI 128
Cdd:pfam13416   3 AKAFEK-KTGVTVEVEPQ-ASNDLQAKLLAAAAAGNAPDLDVVWIAA-----------DQLATLAEAGLLADLS-DVDNL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886  129 ANYYATAA-----GELNSFPYNSSTA-VFYYNVDAFEKAGITfkPDTWEQVEEAAKKLKAAGfecplAFNFDTWMLMEQF 202
Cdd:pfam13416  69 DDLPDALDaagydGKLYGVPYAASTPtVLYYNKDLLKKAGED--PKTWDELLAAAAKLKGKT-----GLTDPATGWLLWA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886  203 SAIHNQPIATKGNGYQGLDAELTInKTKFVDHVKFFKKmqdeklfvvktkqlGMDILPAFTSQTCQMFMSSIaghGTVGK 282
Cdd:pfam13416 142 LLADGVDLTDDGKGVEALDEALAY-LKKLKDNGKVYNT--------------GADAVQLFANGEVAMTVNGT---WAAAA 203

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737225886  283 GMPEGVKWDVAMLPvwkgtqrQNSLVGGASLWVMAGRPEAEYkGAAAFLNFIAQPEMVQWWSTVTGYIPVTKT 355
Cdd:pfam13416 204 AKKAGKKLGAVVPK-------DGSFLGGKGLVVPAGAKDPRL-AALDFIKFLTSPENQAALAEDTGYIPANKS 268
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 115-431 2.42e-17

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: 83.52  E-value: 2.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 115 NGYKIDWD---NYFPGIANYyATAAGELNSFPYNSSTAVFYYNVDAFEKAGITFKPDTWEQVEEAAKKLKAAGFE-CPLA 190
Cdd:cd14747   79 TPYLEDLGgdkDLFPGLVDT-GTVDGKYYGVPWYADTRALFYRTDLLKKAGGDEAPKTWDELEAAAKKIKADGPDvSGFA 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 191 F--NFDTWMLMEQFSAIHNQPIATKGNGYQGLDAEltinktKFVDHVKFFKKMQDEKLFVVKTKQLGMDILPAFTSQTCQ 268
Cdd:cd14747  158 IpgKNDVWHNALPFVWGAGGDLATKDKWKATLDSP------EAVAGLEFYTSLYQKGLSPKSTLENSADVEQAFANGKVA 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 269 MFMSSIAGHGTVGKGMPEGV-KWDVAMLPVWKGTQRQnSLVGGASLWVMAGrpeAEYK-GAAAFLNFIAQPEMVQWWSTV 346
Cdd:cd14747  232 MIISGPWEIGAIREAGPDLAgKWGVAPLPGGPGGGSP-SFAGGSNLAVFKG---SKNKdLAWKFIEFLSSPENQAAYAKA 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 347 TGYIPVTKTGFDAMKangFYDKAPYKGREKAIESLTFTPPseytrgirLGNFTQIRKEVSTALEAIFM-QNADVQGELDK 425
Cdd:cd14747  308 TGMLPANTSAWDDPS---LANDPLLAVFAEQLKTGKATPA--------TPEWGEIEAELVLVLEEVWIgVGADVEDALDK 376


                 ....*.
gi 737225886 426 AVERSN 431
Cdd:cd14747  377 AAAEIN 382
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
115-434 1.24e-16

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 81.53  E-value: 1.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 115 NGYKIDWDNYFPGIANYyATAAGELNSFPYNSSTAVFYYNVDAFEKAgitfKPDTWEQVEEAAKKLKAAGFEcPLAFNFD 194
Cdd:COG2182  115 DDDLADKDDFLPAALDA-VTYDGKLYGVPYAVETLALYYNKDLVKAE----PPKTWDELIAAAKKLTAAGKY-GLAYDAG 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 195 ----TWMLMEQFSAihnQPIATKGNGyqglDAELTINKTKFVDHVKFFKKMQDEKLFvvkTKQLGMDI-LPAFTSQTCQM 269
Cdd:COG2182  189 dayyFYPFLAAFGG---YLFGKDGDD----PKDVGLNSPGAVAALEYLKDLIKDGVL---PADADYDAaDALFAEGKAAM 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 270 FMSSIAGHGTVGKGMpeGVKWDVAMLPVWKGTQRQNSLVGGASLWVMAGRPEAEykGAAAFLNFIAQPEMVQWWSTVTGY 349
Cdd:COG2182  259 IINGPWAAADLKKAL--GIDYGVAPLPTLAGGKPAKPFVGVKGFGVSAYSKNKE--AAQEFAEYLTSPEAQKALFEATGR 334

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 350 IPVTKTgfdamkangFYDKAPYKGREKA---IESLTFTPP----SEYtrgirlgnfTQIRKEVSTALEAIFMQNADVQGE 422
Cdd:COG2182  335 IPANKA---------AAEDAEVKADPLIaafAEQAEYAVPmpniPEM---------GAVWTPLGTALQAIASGKADPAEA 396

                        330
                 ....*....|..
gi 737225886 423 LDKAVERSNAGL 434
Cdd:COG2182  397 LDAAQKQIEAAI 408
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 79-338 1.02e-13

Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.


Pssm-ID: 460248 [Multi-domain]  Cd Length: 294  Bit Score: 71.29  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886   79 AYRAKKQPAITQiyDAGTLDMMLSKAFVPAKklMADNGYKIDWDNYFpgiANYYATAAGELNSFPYNSSTAVFYYNVDAF 158
Cdd:pfam01547  35 SLAQKLTTAIAA--GDGPADVFASDNDWIAE--LAKAGLLLPLDDYV---ANYLVLGVPKLYGVPLAAETLGLIYNKDLF 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886  159 EKAGITfKPDTWEQVEEAAKKLKAAGFECPLAFNFDTWmlmeQFSAIHNQPIATKGNGYQGLDAELTINKTKFVDHVKFF 238
Cdd:pfam01547 108 KKAGLD-PPKTWDELLEAAKKLKEKGKSPGGAGGGDAS----GTLGYFTLALLASLGGPLFDKDGGGLDNPEAVDAITYY 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886  239 KKMQDEKLFVVKTKQL------GMDILPAFTSQTCQMFMSSIAGH----------GTVGKGMPEGVKWDVAMLPVWKgtq 302
Cdd:pfam01547 183 VDLYAKVLLLKKLKNPgvagadGREALALFEQGKAAMGIVGPWAAlaankvklkvAFAAPAPDPKGDVGYAPLPAGK--- 259

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 737225886  303 rqNSLVGGASLWVMAGRPEAEykGAAAFLNFIAQPE 338
Cdd:pfam01547 260 --GGKGGGYGLAIPKGSKNKE--AAKKFLDFLTSPE 291
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 114-429 3.89e-11

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: 64.24  E-value: 3.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 114 DNGYKIDWDNYFPGIANYyATAAGELNSFPYNSSTAVFYYNVDAFEKAGITfKPDTWEQVEEAAKKLKAA--GFEcPLAF 191
Cdd:cd14750   83 EYLKEEEDDDFLPATVEA-NTYDGKLYALPWFTDAGLLYYRKDLLEKYGPE-PPKTWDELLEAAKKRKAGepGIW-GYVF 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 192 NFDTW-----MLMEQFsaihnqpiatKGNGYQGLDA---ELTINKTKFVDHVKFFKKMQDEKlfVVKTKQLGM---DILP 260
Cdd:cd14750  160 QGKQYeglvcNFLELL----------WSNGGDIFDDdsgKVTVDSPEALEALQFLRDLIGEG--ISPKGVLTYgeeEARA 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 261 AFTSQTCQMFMSSIAGHGTVGKGMPEGV-KWDVAMLPVWKGTQRQNSLvGGaslWVMAGRPEAEYKGAA-AFLNFIAQPE 338
Cdd:cd14750  228 AFQAGKAAFMRNWPYAYALLQGPESAVAgKVGVAPLPAGPGGGSASTL-GG---WNLAISANSKHKEAAwEFVKFLTSPE 303

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 339 MVQWWSTVTGYIPVTKTGFDAMKangFYDKAPYKGR-EKAIESLTFTPPSEYtrgirlgnFTQIRKEVSTALEAIFMQNA 417
Cdd:cd14750  304 VQKRRAINGGLPPTRRALYDDPE---VLEAYPFLPAlLEALENAVPRPVTPK--------YPEVSTAIQIALSAALSGQA 372

                        330
                 ....*....|..
gi 737225886 418 DVQGELDKAVER 429
Cdd:cd14750  373 TPEEALKQAQEK 384
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 134-429 3.39e-05

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: 45.75  E-value: 3.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 134 TAAGELNSFPYNSSTAVFYYNVDAFEKAgitfkPDTWEQVEEAAKKL-KAAGFECPLAFNFDtwmlmeqfSAIHNQPIAT 212
Cdd:cd13586   95 TYNGKLYGVPVSVETIALFYNKDLVPEP-----PKTWEELIALAKKFnDKAGGKYGFAYDQT--------NPYFSYPFLA 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 213 kGNGYQGLDAE------LTINKTKFVDHVKFFKKMQDEklfvvktkqlgMDILPA-FTSQTC-QMFMSS-----IAGHGT 279
Cdd:cd13586  162 -AFGGYVFGENggdptdIGLNNEGAVKGLKFIKDLKKK-----------YKVLPPdLDYDIAdALFKEGkaamiINGPWD 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 280 VGKGMPEGVKWDVAMLPVWKGTQRQNSLVGGaSLWVMAgRPEAEYKGAAAFLNFIAQPEMVQWWSTVTGYIPVTKtgfDA 359
Cdd:cd13586  230 LADYKDAGINFGVAPLPTLPGGKQAAPFVGV-QGAFVS-AYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALK---DA 304

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737225886 360 MKANGFYDKAPYKGrekaiesltFTPPSEYtrGIRLGNFTQIRK---EVSTALEAIFMQNADVQGELDKAVER 429
Cdd:cd13586  305 LNDAAVKNDPLVKA---------FAEQAQY--GVPMPNIPEMAAvwdAMGNALNLVASGKATPEEAAKDAVAA 366
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 151-183 1.17e-03

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


Pssm-ID: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 41.19  E-value: 1.17e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 737225886 151 FYYNVDAFEKAGITFkPDTWEQVEEAAKKLKAA 183
Cdd:cd13583  130 FLYRKDIFEKAGIKI-PTTWDEFYAALKKLKEK 161
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
112-402 5.20e-03

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 38.74  E-value: 5.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 112 MADNGY--KID------WDNYFPGIANYyATAAGELNSFPYNSSTAVFYYNVDAFEKAgitfkPDTWEQV--EEAAKKLk 181
Cdd:COG0687   91 LIKAGLlqPLDksklpnLANLDPRFKDP-PFDPGNVYGVPYTWGTTGIAYNTDKVKEP-----PTSWADLwdPEYKGKV- 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 182 aagfecpLAFNFDTWMLmeqfsaihnqPIATKGNGYqgldaelTINKTKFVDHVKFFKKMQDEKLFVVKTKQLGMDILPA 261
Cdd:COG0687  164 -------ALLDDPREVL----------GAALLYLGY-------DPNSTDPADLDAAFELLIELKPNVRAFWSDGAEYIQL 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737225886 262 FTSQTCQMfmsSIAGHGTVGKGMPEGVKWDVAmLPvwkgtqrqnslVGGASLW-----VMAGRPEAEykGAAAFLNFIAQ 336
Cdd:COG0687  220 LASGEVDL---AVGWSGDALALRAEGPPIAYV-IP-----------KEGALLWfdnmaIPKGAPNPD--LAYAFINFMLS 282

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 737225886 337 PEMVQWWSTVTGYIPVTKTGFDAMKANGFYDKAPYKGREKAIESLTFTPPSEYTRGIRLGNFTQIR 402
Cdd:COG0687  283 PEVAAALAEYVGYAPPNKAARELLPPELAANPAIYPPEEVLDKLEFWNPLPPENRELYTRRWTEIK 348
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH