|
Name |
Accession |
Description |
Interval |
E-value |
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
37-411 |
0e+00 |
|
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: 542.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 37 VLTVSVEETYKES-IESIKAKFEKENDVTIKIVEKQMFEQLEALPLDGPAGNAPDVMLAAYDRIGGLGQQGHLLEIKPSN 115
Cdd:cd13658 1 QLTVWVDEDKKMAfIKKIAKQYTKKTGVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 116 --TNSFGDKEMQQVTVDGKVYGMPLVIETLVLYYNKDLLQTAPKTFKDLEKLTEDsrfaFASEKGKSTGFLAKWTDFYMS 193
Cdd:cd13658 81 dkKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKD----LTKEKGKQYGFLADATNFYYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 194 YGLLAGYGGYVFGKNGTDS--GDIGLNNKGAVEAVKYAEKWF-KTYWPKGMQDnssadDFIQQMFLDGKAGAIIGGPWSA 270
Cdd:cd13658 157 YGLLAGNGGYIFKKNGSDLdiNDIGLNSPGAVKAVKFLKKWYtEGYLPKGMTG-----DVIQGLFKEGKAAAVIDGPWAI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 271 ANYKEAKLNYGAAPIPTLPNGEEYAPFAGGKGWVASKYTKEPELAEKWLEYATNDANAYAFYENTNEVPANTAARKKAGE 350
Cdd:cd13658 232 QEYQEAGVNYGVAPLPTLPNGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFLTSKENLKKRYDETNEIPPRKDVRSDPEI 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2080717491 351 QKNDLTSAVIKQYETATPTPNIPEMAEVWTGAESLIFDAVSGKKAAQTSANDAVNVIRDNI 411
Cdd:cd13658 312 KNNPLTSAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKTPKQALNDAVNDIKENI 372
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
38-407 |
9.45e-136 |
|
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: 393.58 E-value: 9.45e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 38 LTV-SVEETYKESIESIKAKFEKENDVTIKIVEKQMFEQLEALPLDGPAGNAPDVMLAAYDRIGGLGQQGHLLEIKPSNT 116
Cdd:cd13586 2 ITVwTDEDGELEYLKELAEEFEKKYGIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 117 NSFG--DKEMQQVTVDGKVYGMPLVIETLVLYYNKDLLQTAPKTFKDLEKLTEDsrfaFASEKGKSTGFLAKWTDFYMSY 194
Cdd:cd13586 82 VKIKnlPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPEPPKTWEELIALAKK----FNDKAGGKYGFAYDQTNPYFSY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 195 GLLAGYGGYVFGKNGTDSGDIGLNNKGAVEAVKYAEKWFKTY--WPKGMQDnssadDFIQQMFLDGKAGAIIGGPWSAAN 272
Cdd:cd13586 158 PFLAAFGGYVFGENGGDPTDIGLNNEGAVKGLKFIKDLKKKYkvLPPDLDY-----DIADALFKEGKAAMIINGPWDLAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 273 YKEAKLNYGAAPIPTLPNGEEYAPFAGGKGWVASKYTKEPELAEKWLEYATNDANAYAFYENTNEVPANTAARKKAGEQK 352
Cdd:cd13586 233 YKDAGINFGVAPLPTLPGGKQAAPFVGVQGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALKDALNDAAVKN 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2080717491 353 NDLTSAVIKQYETATPTPNIPEMAEVWTGAESLIFDAVSGKKAAQTSANDAVNVI 407
Cdd:cd13586 313 DPLVKAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEEAAKDAVAAI 367
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
5-413 |
2.09e-131 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 383.92 E-value: 2.09e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 5 KKGFALLAASVLTFGLAACSNSKDP----ASSDGKKVLTVSVEETYKESIESIKAKFEKENDVTIKIVEKQMFEQLEALP 80
Cdd:COG2182 4 RLLAALALALALALALAACGSGSSSsgssSAAGAGGTLTVWVDDDEAEALEEAAAAFEEEPGIKVKVVEVPWDDLREKLT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 81 LDGPAGNAPDVMLAAYDRIGGLGQQGHLLEIKPS--NTNSFGDKEMQQVTVDGKVYGMPLVIETLVLYYNKDLL-QTAPK 157
Cdd:COG2182 84 TAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDlaDKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVkAEPPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 158 TFKDLEKLTEDsrfafASEKGKStGFLAKWTDFYMSYGLLAGYGGYVFGKNGTDSGDIGLNNKGAVEAVKYAEKWFKtyw 237
Cdd:COG2182 164 TWDELIAAAKK-----LTAAGKY-GLAYDAGDAYYFYPFLAAFGGYLFGKDGDDPKDVGLNSPGAVAALEYLKDLIK--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 238 pKGMQDNSSADDFIQQMFLDGKAGAIIGGPWSAANYKEA-KLNYGAAPIPTLPNGEEYAPFAGGKGWVASKYTKEPELAE 316
Cdd:COG2182 235 -DGVLPADADYDAADALFAEGKAAMIINGPWAAADLKKAlGIDYGVAPLPTLAGGKPAKPFVGVKGFGVSAYSKNKEAAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 317 KWLEYATNDANAYAFYENTNEVPANTAARKKAGEQKNDLTSAVIKQYETATPTPNIPEMAEVWTGAESLIFDAVSGKKAA 396
Cdd:COG2182 314 EFAEYLTSPEAQKALFEATGRIPANKAAAEDAEVKADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADP 393
|
410
....*....|....*..
gi 2080717491 397 QTSANDAVNVIRDNIKE 413
Cdd:COG2182 394 AEALDAAQKQIEAAIAQ 410
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
43-404 |
1.65e-59 |
|
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: 197.98 E-value: 1.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 43 EETYKESIESIKAKFEKENDVT-IKIVEKQMFEQLEALPLDGPAGNAPDVMLAAYDRIGGLGQQGHLLEI----KPSNTN 117
Cdd:cd13657 9 TGAEEDALQQIIDEFEAKYPVPnVKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPIsdylSEDDFE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 118 SFGDKEMQQVTVDGKVYGMPLVIETLVLYYNKDLLQTAPKTFKDLEKLTEDSRFAFASekgkSTGFLAKWTDFYMSYGLL 197
Cdd:cd13657 89 NYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQPPETTDELLAIMKDHTDPAAG----SYGLAYQVSDAYFVSAWI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 198 AGYGGYVFGKNGTdsgDIGLNNKGAVEAVKYAEKWFKTYWPkgmQDNSsaDDFIQQMFLDGKAGAIIGGPWSAANYKEAK 277
Cdd:cd13657 165 FGFGGYYFDDETD---KPGLDTPETIKGIQFLKDFSWPYMP---SDPS--YNTQTSLFNEGKAAMIINGPWFIGGIKAAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 278 LNYGAAPIPTLPNGEEYAPFAGGKGWVASKYT--KEPELAEKWLEY-ATNDANAYAFYENtNEVPANTAARKKAGEQKND 354
Cdd:cd13657 237 IDLGVAPLPTVDGTNPPRPYSGVEGIYVTKYAerKNKEAALDFAKFfTTAEASKILADEN-GYVPAATNAYDDAEVAADP 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2080717491 355 LTSAVIKQYETATPTPNIPEMAEVWTGAESLIFDAVSGKKAAQTSANDAV 404
Cdd:cd13657 316 VIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQEALAAAQ 365
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
6-331 |
4.77e-56 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 188.71 E-value: 4.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 6 KGFALLAASVLTFGLAACSNSKDPASSDGKKV-LTV-SVEETYKESIESIKAKFEKEN-DVTIKIVEKQMFEQLEALPLD 82
Cdd:COG1653 2 RRLALALAAALALALAACGGGGSGAAAAAGKVtLTVwHTGGGEAAALEALIKEFEAEHpGIKVEVESVPYDDYRTKLLTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 83 GPAGNAPDVMLAAYDRIGGLGQQGHLLEIKP------SNTNSFGDKEMQQVTVDGKVYGMPLVIETLVLYYNKDLLQ--- 153
Cdd:COG1653 82 LAAGNAPDVVQVDSGWLAEFAAAGALVPLDDlldddgLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEkag 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 154 -TAPKTFKDLEKLTEdsrfAFASEKGKsTGFLAKWTDFYMSYGLLAGYGGYVFGKNGTdsgdIGLNNKGAVEAVKYAEKW 232
Cdd:COG1653 162 lDPPKTWDELLAAAK----KLKAKDGV-YGFALGGKDGAAWLDLLLSAGGDLYDEDGK----PAFDSPEAVEALEFLKDL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 233 FKT-YWPKGMQDNSSADdfIQQMFLDGKAGAIIGGPWSAANYKEA--KLNYGAAPIPTLPNGEEYAPFAGGKGWVASKYT 309
Cdd:COG1653 233 VKDgYVPPGALGTDWDD--ARAAFASGKAAMMINGSWALGALKDAapDFDVGVAPLPGGPGGKKPASVLGGSGLAIPKGS 310
|
330 340
....*....|....*....|..
gi 2080717491 310 KEPELAEKWLEYATNDANAYAF 331
Cdd:COG1653 311 KNPEAAWKFLKFLTSPEAQAKW 332
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
55-404 |
5.00e-54 |
|
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: 183.77 E-value: 5.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 55 AKFEKEN-DVTIkIVEKQMFEQL-EALPLDGPAGNAPDVMLAAYDRIGGLGQQGHLLEIKP--SNTNSFGDKEMQQVTVD 130
Cdd:cd13522 21 AKFEKAYpGITV-EVTYQDTEARrQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDEyvSKSGKYAPNTIAAMKLN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 131 GKVYGMPLVIETLVLYYNKDLL-QTAPKTFKDLEKLTEDSrfafaSEKGKStGFLAKWTDFYMSYGLLAGYGGYVFGKNG 209
Cdd:cd13522 100 GKLYGVPVSVGAHLMYYNKKLVpKNPPKTWQELIALAQGL-----KAKNVW-GLVYNQNEPYFFAAWIGGFGGQVFKANN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 210 tDSGDIGLNNKGAVEAVKYAEKWFKTYW--PKGMqDNSSADdfiqQMFLDGKAGAIIGGPWSAANYKEA-KLNYGAAPIP 286
Cdd:cd13522 174 -GKNNPTLDTPGAVEALQFLVDLKSKYKimPPET-DYSIAD----ALFKAGKAAMIINGPWDLGDYRQAlKINLGVAPLP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 287 TLPNGEEYAPFAGGKGWVASKYTKEPELAEKWLEYATNDANAYAFYENTNEVPANTAARKKAGEQKNDLTSAVIKQYETA 366
Cdd:cd13522 248 TFSGTKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDIPANLQAYESPAVQNKPAQKASAEQAAYG 327
|
330 340 350
....*....|....*....|....*....|....*...
gi 2080717491 367 TPTPNIPEMAEVWTGAESLIFDAVSGKKAAQTSANDAV 404
Cdd:cd13522 328 VPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQ 365
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
5-408 |
6.46e-50 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 173.66 E-value: 6.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 5 KKGFALLAASVLTfgLAACSNSKDPASSDGKKVLTVSVEETYKeSIESIKAKFEKENDVTIKIVEKQMFEqlEALPLDGP 84
Cdd:PRK09474 4 KKGLRTLALSALA--TLMFSASALAKIEEGKLVIWINGDKGYN-GLAEVGKKFEKDTGIKVTVEHPDKLE--EKFPQVAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 85 AGNAPDVMLAAYDRIGGLGQQGHLLEIKPSNT--NSFGDKEMQQVTVDGKVYGMPLVIETLVLYYNKDLLQTAPKTFKDL 162
Cdd:PRK09474 79 TGDGPDIIFWAHDRFGGYAQSGLLAEVTPSKAfkDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 163 EKLTEDSRfafasEKGKStGFLAKWTDFYMSYGLLAGYGGYVFGKN--GTDSGDIGLNNKGAVEAVKYAEKWFKT-YWPK 239
Cdd:PRK09474 159 PALDKELK-----AKGKS-AIMWNLQEPYFTWPLIAADGGYAFKFEngGYDVKDVGVNNAGAKAGLQFLVDLVKNkHMNA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 240 GMqDNSSADdfiqQMFLDGKAGAIIGGPWSAANYKEAKLNYGAAPIPTLpNGEEYAPFAG--GKGWVASKYTKepELAEK 317
Cdd:PRK09474 233 DT-DYSIAE----AAFNKGETAMTINGPWAWSNIDKSGINYGVTVLPTF-NGKPSKPFVGvlSAGINAASPNK--ELAKE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 318 WLE-YA-TNDANAYAFYENTNEVPANTAARKKAgeQKNDLTSAVIKQYETATPTPNIPEMAEVWTGAESLIFDAVSGKKA 395
Cdd:PRK09474 305 FLEnYLlTDEGLETVNKDKPLGAVALKSFQEEL--AKDPRIAATMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQT 382
|
410
....*....|...
gi 2080717491 396 AQTSANDAVNVIR 408
Cdd:PRK09474 383 VDAALDDAAKRIT 395
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
48-407 |
2.99e-46 |
|
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: 163.64 E-value: 2.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 48 ESIESIKAKFEKEN-DVTIKIVEKQMFEQLEALPLDGPAGNAPDVMLAAYDRIGGLGQQGHLLEIKPSNTNSFGDKE--- 123
Cdd:cd14747 14 ELLKELADEFEKENpGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMGALEDLTPYLEDLGGDKDlfp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 124 --MQQVTVDGKVYGMPLVIETLVLYYNKDLLQ-----TAPKTF----KDLEKLTE--DSRFAFAsekgkstgFLAKWTDF 190
Cdd:cd14747 94 glVDTGTVDGKYYGVPWYADTRALFYRTDLLKkaggdEAPKTWdeleAAAKKIKAdgPDVSGFA--------IPGKNDVW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 191 YMSYGLLAGYGGYVFGKngtDSGDIGLNNKGAVEAVKYAEKWFKTYWPKGMQDNSSADdfIQQMFLDGKAGAIIGGPWSA 270
Cdd:cd14747 166 HNALPFVWGAGGDLATK---DKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSAD--VEQAFANGKVAMIISGPWEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 271 ANYKEA----KLNYGAAPIPTlPNGEEYAPFAGGKGWVASKYTKEPELAEKWLEYATNDANAYAFYENTNEVPANTAARK 346
Cdd:cd14747 241 GAIREAgpdlAGKWGVAPLPG-GPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGMLPANTSAWD 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2080717491 347 KAGEQKNDLTSAVIKQYETATPTPNIPEMAEVWTGAESLIFDAVSGKKA----AQTSANDAVNVI 407
Cdd:cd14747 320 DPSLANDPLLAVFAEQLKTGKATPATPEWGEIEAELVLVLEEVWIGVGAdvedALDKAAAEINEI 384
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
45-411 |
9.23e-45 |
|
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: 159.49 E-value: 9.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 45 TYKESIESIKAKFEKEN-DVTIKIV---EKQMFEQLEAlplDGPAGNAPDVMLAAYDRIGGLGQQGHLLEIKPSNTNSFG 120
Cdd:cd13585 11 AETAALKKLIDAFEKENpGVKVEVVpvpYDDYWTKLTT---AAAAGTAPDVFYVDGPWVPEFASNGALLDLDDYIEKDGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 121 DKE-----MQQVTVDGKVYGMPLVIETLVLYYNKDLLQTA------PKTFKDLEKLTEdsrfAFASEKGKSTGFLA--KW 187
Cdd:cd13585 88 DDDfppglLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAgpgpkpPWTWDELLEAAK----KLTDKKGGQYGFALrgGS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 188 TDFYMSYGLLAGYGGYVFGKngtDSGDIGLNNKGAVEAVKYAEKWFKTYWPKGMQDNSSADdfIQQMFLDGKAGAIIGGP 267
Cdd:cd13585 164 GGQTQWYPFLWSNGGDLLDE---DDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDE--AVDLFASGKVAMMIDGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 268 WSAANYK--EAKLNYGAAPIPTLPNGEEYApFAGGKGWVASKYTKEPELAEKWLEYATNDANAYAFYENTNEVPANTAAR 345
Cdd:cd13585 239 WALGTLKdsKVKFKWGVAPLPAGPGGKRAS-VLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2080717491 346 KKAGEQKND--LTSAVIKQYETATPTPNIPEMAEVWTGAESLIFDAVSGKkaAQTSANDAVNVIRDNI 411
Cdd:cd13585 318 SAAAPDAKPalALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGA--LGKSPEEALKEAAKEI 383
|
|
| PBP2_MBP |
cd13656 |
The periplasmic binding component of ABC tansport system specific for maltose; possess the ... |
34-403 |
1.02e-43 |
|
The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold; This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270374 [Multi-domain] Cd Length: 364 Bit Score: 156.22 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 34 GKKVLTVSVEETYKeSIESIKAKFEKENDVTIKIVEKQMFEqlEALPLDGPAGNAPDVMLAAYDRIGGLGQQGHLLEIKP 113
Cdd:cd13656 1 GKLVIWINGDKGYN-GLAEVGKKFEKDTGIKVTVEHPDKLE--EKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 114 SNT--NSFGDKEMQQVTVDGKVYGMPLVIETLVLYYNKDLLQTAPKTFKDLEKLTEDsrfafASEKGKStGFLAKWTDFY 191
Cdd:cd13656 78 DKAfqDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKE-----LKAKGKS-ALMFNLQEPY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 192 MSYGLLAGYGGYVFGK--NGTDSGDIGLNNKGAVEAVKYAEKWFKtywpKGMQDNSSADDFIQQMFLDGKAGAIIGGPWS 269
Cdd:cd13656 152 FTWPLIAADGGYAFKYenGKYDIKDVGVDNAGAKAGLTFLVDLIK----NKHMNADTDYSIAEAAFNKGETAMTINGPWA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 270 AANYKEAKLNYGAAPIPTLpNGEEYAPFAGGKGWVASKYTKEPELAEKWLE-YATNDANayafYENTN-EVPANTAARKK 347
Cdd:cd13656 228 WSNIDTSKVNYGVTVLPTF-KGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEG----LEAVNkDKPLGAVALKS 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2080717491 348 AGEQ--KNDLTSAVIKQYETATPTPNIPEMAEVWTGAESLIFDAVSGKKAAQTSANDA 403
Cdd:cd13656 303 YEEElaKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDA 360
|
|
| PBP2_oligosaccharide_1 |
cd13655 |
The periplasmic binding component of ABC tansport system specific for an unknown ... |
38-402 |
7.16e-43 |
|
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: 154.04 E-value: 7.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 38 LTVSVEETYKESIESIKAKFEKEN-DVTIKIVEKQMFEQLEALPLDGPAGNAPDVMLAAYDRIGGLGQQGHLLEI----- 111
Cdd:cd13655 2 LTVWGPQEDQEWLKEMVDAFKEKHpEWKITITIGVVGEADAKDEVLKDPSAAADVFAFANDQLGELVDAGAIYPLtgsav 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 112 -KPSNTNSfgDKEMQQVTVDGKVYGMPLVIETLVLYYNKDLLQTapKTFKDLEKLTedsrfAFASEKGKSTGFlaKWTDF 190
Cdd:cd13655 82 dKIKNTNS--EATVDAVTYNGKLYGYPFTANTWFMYYDKSKLTE--DDVKSLDTML-----AKAPDAKGKVSF--DLSNS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 191 YMSYGLLAGYGGYVFGKNGTDSGDIGLNNKGAVEAVKYAEKWFKTywPKGMQDNSsaDDFIQQMfLDGKAGAIIGGPWSA 270
Cdd:cd13655 151 WYLYAFFFGAGCKLFGNNGGDTAGCDFNNEKGVAVTNYLVDLVAN--PKFVNDAD--GDAISGL-KDGTLGAGVSGPWDA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 271 ANYKEA-KLNYGAAPIPTL-PNGEEY--APFAGGKGWVASKYTKEPELAEKWLEYATNDANAYAFYENTNEVPANTAARK 346
Cdd:cd13655 226 ANLKKAlGDNYAVAKLPTYtLGGKDVqmKSFAGYKAIGVNSNTKNPEAAMALADYLTNEESQLTRFEKRGIGPTNKEAAE 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2080717491 347 KAGEQKNDLTSAVIKQY-ETATPTPNIPEMAEVWTGAESLIFDAVSGKKAAQTSAND 402
Cdd:cd13655 306 SDAVKADPAAKALIAQSnEASVVQPKLPKMSNFWTPAEAFGKGIVDGTVTAENAQQK 362
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
47-407 |
9.91e-43 |
|
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: 153.99 E-value: 9.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 47 KESIESIKAKFEKEN-DVTIKIV-EKQMFEQLEALPLDGPAGNAPDVMLAAYDRIGGLGQQGHLLEIKP------SNTNS 118
Cdd:cd14748 13 GKALEELVDEFNKSHpDIKVKAVyQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDDyidkdgVDDDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 119 FGDKEMQQVTVDGKVYGMPLVIETLVLYYNKDLLQTA-------PKTFKDLEKLTEdsRFAFASEKGKSTGF-LAKWTDF 190
Cdd:cd14748 93 FYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAgldpekpPKTWDELEEAAK--KLKDKGGKTGRYGFaLPPGDGG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 191 YMSYGLLAGYGGYVFGKngtDSGDIGLNNKGAVEAVKYAEKWFKtywPKGMQDNSSADDfIQQMFLDGKAGAIIGGPWSA 270
Cdd:cd14748 171 WTFQALLWQNGGDLLDE---DGGKVTFNSPEGVEALEFLVDLVG---KDGVSPLNDWGD-AQDAFISGKVAMTINGTWSL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 271 ANYK--EAKLNYGAAPIPTlPNGEEYAPFAGGKGWVASK-YTKEPELAEKWLEYATNDANAYAFYENTNEVPANTAARKK 347
Cdd:cd14748 244 AGIRdkGAGFEYGVAPLPA-GKGKKGATPAGGASLVIPKgSSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRKSAAED 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2080717491 348 AGE--QKNDLTSAVIKQYETATPT-PNIPEMAEVWTGAESLIFDAVSGKKAAQTSANDAVNVI 407
Cdd:cd14748 323 PEEflAENPNYKVAVDQLDYAKPWgPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
43-403 |
1.37e-35 |
|
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: 134.81 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 43 EETYKESIESIKAKFEKEN-DVTIKIVEKQMFEQLEALPLDGPAGNAPDVM-LAAYDRIGGLGQQGHLLEIKP------- 113
Cdd:cd14749 10 GDTKKKYMDELIADFEKENpNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPLTDyldpngv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 114 SNTNSFGDKEMqqVTVDGKVYGMPLVIETLVLYYNKDLLQ-----TAPKTFKDLEKLTEDSRFAFASEKGKSTGFLAKWT 188
Cdd:cd14749 90 DKRFLPGLADA--VTFNGKVYGIPFAARALALFYNKDLFEeaggvKPPKTWDELIEAAKKDKFKAKGQTGFGLLLGAQGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 189 DFYMSYgLLAGYGGYVFGKNGTDSGDIglNNKGAVEAVKYAEKWFKT-YWPKGMQDNSSADDfiQQMFLDGKAGAIIGGP 267
Cdd:cd14749 168 HWYFQY-LVRQAGGGPLSDDGSGKATF--NDPAFVQALQKLQDLVKAgAFQEGFEGIDYDDA--GQAFAQGKAAMNIGGS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 268 WSAANYK--EAKLNYGAAPIPTLPNGEEYAP-FAGGKGWVASKYTKEPELAEKWLEYATNDANAYAFYENTNEVPANTAA 344
Cdd:cd14749 243 WDLGAIKagEPGGKIGVFPFPTVGKGAQTSTiGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQYLEDVGLLPAKEVV 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2080717491 345 RKKAGEQKNDLTSAVIKQYETATPTP----NIPEMAEVWTGAeslIFDAVSGKKAAQTSANDA 403
Cdd:cd14749 323 AKDEDPDPVAILGPFADVLNAAGSTPfldeYWPAAAQVHKDA---VQKLLTGKIDPEQVVKQA 382
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
37-403 |
2.11e-35 |
|
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: 134.34 E-value: 2.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 37 VLTVSVEETYKESIESIKAKFEKEN-DVTIKIVE---------KQMFEQLEAlpldgpAGNAPDVMLAAYDRIGGLGQQG 106
Cdd:cd14750 3 TFAAGSDGQEGELLKKAIAAFEKKHpDIKVEIEElpassddqrQQLVTALAA------GSSAPDVLGLDVIWIPEFAEAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 107 HLLEIkPSNTNSFGDKEMQQV-----TVDGKVYGMPLVIETLVLYYNKDLLQ----TAPKTFKDLEkltEDSRFAFASEK 177
Cdd:cd14750 77 WLLPL-TEYLKEEEDDDFLPAtveanTYDGKLYALPWFTDAGLLYYRKDLLEkygpEPPKTWDELL---EAAKKRKAGEP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 178 GKStGFLAKW-------TDFYMsygLLAGYGGYVFGKngtDSGDIGLNNKGAVEAVKYAEKWFKTYWPKGMQDNSSADDf 250
Cdd:cd14750 153 GIW-GYVFQGkqyeglvCNFLE---LLWSNGGDIFDD---DSGKVTVDSPEALEALQFLRDLIGEGISPKGVLTYGEEE- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 251 IQQMFLDGKAGAIIGGPWSAANYKEAKLNY----GAAPIPTLPnGEEYAPFAGGKGWVASKYTKEPELAEKWLEYATNDA 326
Cdd:cd14750 225 ARAAFQAGKAAFMRNWPYAYALLQGPESAVagkvGVAPLPAGP-GGGSASTLGGWNLAISANSKHKEAAWEFVKFLTSPE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 327 NAYAFYENTNEVPANTAARKKAGEQKN-----DLTSAVikqyETATPTPNIPEMAEVWTGAESLIFDAVSGKKAAQTSAN 401
Cdd:cd14750 304 VQKRRAINGGLPPTRRALYDDPEVLEAypflpALLEAL----ENAVPRPVTPKYPEVSTAIQIALSAALSGQATPEEALK 379
|
..
gi 2080717491 402 DA 403
Cdd:cd14750 380 QA 381
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
55-344 |
2.87e-34 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 128.68 E-value: 2.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 55 AKFEKENDVTIKIVEKQMFEQLEALPLDGPAGNAPDVML--AAYDRIGGLGQQGHLLEIKPSNTNSFGDKEMQQVTVDGK 132
Cdd:pfam13416 4 KAFEKKTGVTVEVEPQASNDLQAKLLAAAAAGNAPDLDVvwIAADQLATLAEAGLLADLSDVDNLDDLPDALDAAGYDGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 133 VYGMPLVIET-LVLYYNKDLLQTA---PKTFKDLEKLTEDSrfafaseKGKSTgfLAKWTDFYMSYGLLAGyggyvfGKN 208
Cdd:pfam13416 84 LYGVPYAASTpTVLYYNKDLLKKAgedPKTWDELLAAAAKL-------KGKTG--LTDPATGWLLWALLAD------GVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 209 GTDSGDiglnnkgAVEAVKYAEKWFKTYWPKGMQDNSSADdfIQQMFLDGKAGAIIGGPWSAANYKEAKLNYGAAPIPTl 288
Cdd:pfam13416 149 LTDDGK-------GVEALDEALAYLKKLKDNGKVYNTGAD--AVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVPKD- 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2080717491 289 pngeeyAPFAGGKGWVASKYTKEPEL-AEKWLEYATNDANAYAFYENTNEVPANTAA 344
Cdd:pfam13416 219 ------GSFLGGKGLVVPAGAKDPRLaALDFIKFLTSPENQAALAEDTGYIPANKSA 269
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
39-403 |
6.64e-32 |
|
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: 124.41 E-value: 6.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 39 TVSVEEtyKESIESIKAKFEKENDvTIKIVEKQM-FEQLEALPLDGPAGN-APDVMLAAYDRIGGLGQQGHLLEIKP--- 113
Cdd:cd14751 7 TSSDEE--KVLYEKLIPAFEKEYP-KIKVKAVRVpFDGLHNQIKTAAAGGqAPDVMRADIAWVPEFAKLGYLQPLDGtpa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 114 -SNTNSFGDKEMQQVTVDGKVYGMPLVIETLVLYYNKDLLQTA----PKTFKDLEKLTEDsrfafASEKGKSTGFLAKWT 188
Cdd:cd14751 84 fDDIVDYLPGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAgtevPKTMDELVAAAKA-----IKKKKGRYGLYISGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 189 DFYMSYGLLAGYGG-YVFGKNGTdsgdIGLNNKGAVEAVKYAEKWFKTYwpKGMQDNSSADDFIQQMFLDGKAGAIIGGP 267
Cdd:cd14751 159 GPYWLLPFLWSFGGdLTDEKKAT----GYLNSPESVRALETIVDLYDEG--AITPCASGGYPNMQDGFKSGRYAMIVNGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 268 WSAANYKEAKL-----NYGAAPIPTLPNGEeyAPFAGGKGWVASKYTKEPELAEKWLEYATNDANAYAFYENTNEVPANT 342
Cdd:cd14751 233 WAYADILGGKEfkdpdNLGIAPVPAGPGGS--GSPVGGEDLVIFKGSKNKDAAWKFVKFMSSAEAQALTAAKLGLLPTRT 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2080717491 343 AARKKAGEQKNDLTSAVIKQYETATPTPNIPEMAEVWTGAESLIFDAVSGKKAAQTSANDA 403
Cdd:cd14751 311 SAYESPEVANNPMVAAFKPALETAVPRPPIPEWGELFEPLTLAFAKVLRGEKSPREALDEA 371
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
43-328 |
3.19e-27 |
|
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: 109.81 E-value: 3.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 43 EETYKESIESIKAKFEKEN-DVTIKIVEKQMFEQLEALPLDGPAGNAP-DVMLAAYDRIGGLGQQGHLLEIKPSNTNSFG 120
Cdd:pfam01547 3 SLTEAAALQALVKEFEKEHpGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVANYLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 121 DKemqqvtvDGKVYGMPLVIETLVLYYNKDLLQTA----PKTFKDLEKLTEDSRFAFASeKGKSTGFLAKWTDFYMSYGL 196
Cdd:pfam01547 83 LG-------VPKLYGVPLAAETLGLIYNKDLFKKAgldpPKTWDELLEAAKKLKEKGKS-PGGAGGGDASGTLGYFTLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 197 LAGYGGYVFGKNG-TDSGDIGLNNKGAVEAVKYAEKWFKTYWPKGMQDNSSadDFIQQMFLDGKAGAIIGGPWSAANYKE 275
Cdd:pfam01547 155 LASLGGPLFDKDGgGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADG--REALALFEQGKAAMGIVGPWAALAANK 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2080717491 276 AKLNYGAAPIPTLPNGE-EYAPFAGGK-------GWVASKYTKEPELAEKWLEYATNDANA 328
Cdd:pfam01547 233 VKLKVAFAAPAPDPKGDvGYAPLPAGKggkgggyGLAIPKGSKNKEAAKKFLDFLTSPEAQ 293
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
5-380 |
1.15e-19 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 89.58 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 5 KKGFALLAASVLTFGLAACSnskdpASSDGKKVLTVSveeTYKESI-ESIKAKFEKENDVTIKIVEKQMFEQLEALPLDG 83
Cdd:COG0687 3 RRSLLGLAAAALAAALAGGA-----PAAAAEGTLNVY---NWGGYIdPDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 84 PAGnaPDVMLAAYDRIGGLGQQGHLLEIKPSNTNSFG--DKEMQQVTVD-GKVYGMPLVIETLVLYYNKDLLQTAPKTFK 160
Cdd:COG0687 75 GSG--YDVVVPSDYFVARLIKAGLLQPLDKSKLPNLAnlDPRFKDPPFDpGNVYGVPYTWGTTGIAYNTDKVKEPPTSWA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 161 DLekltedsrfaFASE-KGKsTGFLAKWTDFYmsyGLLAGYGGYVFgkNGTDSGDIglnnKGAVEAVKYAEKWFKTYWpk 239
Cdd:COG0687 153 DL----------WDPEyKGK-VALLDDPREVL---GAALLYLGYDP--NSTDPADL----DAAFELLIELKPNVRAFW-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 240 gmqdnSSADDFIQqMFLDGKAGAIIGGPWSAANYKEAKLNYGAApIPtlpngEEYAPFAGGkGWVASKYTKEPELAEKWL 319
Cdd:COG0687 211 -----SDGAEYIQ-LLASGEVDLAVGWSGDALALRAEGPPIAYV-IP-----KEGALLWFD-NMAIPKGAPNPDLAYAFI 277
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2080717491 320 EYATNDANAYAFYENTNEVPANTAARKKAG-EQKNDL----TSAVIKQYETATPTP--NIPEMAEVWT 380
Cdd:COG0687 278 NFMLSPEVAAALAEYVGYAPPNKAARELLPpELAANPaiypPEEVLDKLEFWNPLPpeNRELYTRRWT 345
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
85-321 |
1.11e-13 |
|
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: 72.36 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 85 AGNAPDVMLA-AYDRIGGLGQQGHLLEI-------KPSNTNSFGDKEMQQVTVDGKVYGMP---LVIETLVLYYNKDLLQ 153
Cdd:cd13580 56 SGDLPDIVVVnDPQLSITLVKQGALWDLtdyldkyYPNLKKIIEQEGWDSASVDGKIYGIPrkrPLIGRNGLWIRKDWLD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 154 ----TAPKTFKDLEKLTEdsrfAFAsEKG------KSTGFLA--KWTDFYMSYGLLAGYGGYVFGKNGTDSGDI--GLNN 219
Cdd:cd13580 136 klglEVPKTLDELYEVAK----AFT-EKDpdgngkKDTYGLTdtKDLIGSGFTGLFGAFGAPPNNWWKDEDGKLvpGSIQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 220 KGAVEAVKYAEKWFKtywpKGMQDNSSA---DDFIQQMFLDGKAGAIIGGPWSAANYKEAKLN------YGAAPIPTLPN 290
Cdd:cd13580 211 PEMKEALKFLKKLYK----EGLIDPEFAvndGTKANEKFISGKAGIFVGNWWDPAWPQASLKKndpdaeWVAVPIPSGPD 286
|
250 260 270
....*....|....*....|....*....|...
gi 2080717491 291 GEEY--APFAGGKGWVASKYTKEPELAEKWLEY 321
Cdd:cd13580 287 GKYGvwAESGVNGFFVIPKKSKKPEAILKLLDF 319
|
|
| PBP2_AlgQ_like |
cd13521 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
58-332 |
1.33e-12 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This family represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria and related proteins. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. In Sphingomonas sp. A1, the transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins AlgQ1 and AlgQ2. Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270239 [Multi-domain] Cd Length: 483 Bit Score: 69.02 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 58 EKENDVTIKIVEKQMFEQLEALPLDGPAGNAPDVMLAAY--DRIGGLGQQGHLLEIKP-----SNTNSF----GDKEMQQ 126
Cdd:cd13521 27 EKLTNVKLEIVAVTAATSQQKLNLMLASGDLPDIVGADYlkDKFIAYGMEGAFLPLSKyidqyPNLKAFfkqhPDVLRAS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 127 VTVDGKVYGMPLVIETLVLYY----NKDLLQT----APKTFKDLEKLTEDSRFAFASEKGKST--GFLAKWtDFYMSYGL 196
Cdd:cd13521 107 TASDGKIYLIPYEPPKDVPNQgyfiRKDWLDKlnlkTPKTLDELYNVLKAFKEKDPNGNGKADeiPFIDRD-PLYGAFRL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 197 LAGYGGYVFGKNgTDSGDIGLNNK----GAVEAVKYAEKWFKTYWPKGMQDNSSA---DDFIQQMFLDGKAGAIIGGPWS 269
Cdd:cd13521 186 INSWGARSAGGS-TDSDWYEDNGKfkhpFASEEYKDGMKYMNKLYTEGLIDKESFtqkDDQAEQKFSNGKLGGFTHNWFA 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2080717491 270 AANYKEA-----KLNYGAAPIPTLPNG-----EEYAPFAGGKGWVASKYTKEPELAEKWLE-YATNDANAYAFY 332
Cdd:cd13521 265 SDNLFTAqlgkeKPMYILLPIAPAGNVkgrreEDSPGYTGPDGVAISKKAKNPVAALKFFDwLASEEGRELANF 338
|
|
| PBP2_polyamine_1 |
cd13588 |
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
54-346 |
1.37e-10 |
|
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that functions as the primary high-affinity receptor of an uncharactertized ABC-type polyamine transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270306 [Multi-domain] Cd Length: 279 Bit Score: 61.54 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 54 KAKFEKENDVTIKIV----EKQMFEQLEAlpldGPAGnaPDVMLAAYDRIGGLGQQGHLLEIKPSNTNSFGD--KEMQQ- 126
Cdd:cd13588 16 VTAFEEATGCKVVVKffgsEDEMVAKLRS----GGGD--YDVVTPSGDALLRLIAAGLVQPIDTSKIPNYANidPRLRNl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 127 --VTVDGKVYGMPLVIETLVLYYNKDLLQTAPKTfkdLEKLTEDSRFafaseKGKstgfLAKWTDFYMSYGLLAGYggyv 204
Cdd:cd13588 90 pwLTVDGKVYGVPYDWGANGLAYNTKKVKTPPTS---WLALLWDPKY-----KGR----VAARDDPIDAIADAALY---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 205 fgkngTDSGDIGLNNKGAVEAVKYA----EKWFKTYWpkgmqdnSSADDfIQQMFLDGkaGAIIGGPWSAANYKEAKLNy 280
Cdd:cd13588 154 -----LGQDPPFNLTDEQLDAVKAKlreqRPLVRKYW-------SDGAE-LVQLFANG--EVVAATAWSGQVNALQKAG- 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 281 gaapiptlPNGEEYAPFAGGKGWVAS----KYTKEPELAEKWLEYATNDANAYAFYENTNEVPANTAARK 346
Cdd:cd13588 218 --------KPVAYVIPKEGATGWVDTwmilKDAKNPDCAYKWLNYMLSPKVQAAVAEWTGYAPSNPEACA 279
|
|
| PRK10974 |
PRK10974 |
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB; |
131-404 |
1.88e-10 |
|
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
Pssm-ID: 182876 [Multi-domain] Cd Length: 438 Bit Score: 62.12 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 131 GKVYGMPLVIETLVLYYNKDLLQTA-------PKTFKDLEKLTEDSRFAfasekGKSTGFLAKWTDFYMSYGLLAGYGGY 203
Cdd:PRK10974 135 GHLLSQPFNSSTPVLYYNKDAFKKAgldpeqpPKTWQDLAAYAAKLRAA-----GMKCGYASGWQGWIQLENFSAWHGLP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 204 VFGK-NGTDSGDIGL--NNKGAVEAVKYAEKWFK----TYWpkGMQDNSSADdfiqqmFLDGKAGAIIGGPWSAANYKE- 275
Cdd:PRK10974 210 FASKnNGFDGTDAVLefNKPEQVKHIALLEEMNKkgdfTYV--GRKDESTEK------FYNGDCAITTASSGSLANIRKy 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 276 AKLNYGAAPIP---TLPNGEEYAPFAGGKGWVASKytKEPEL---AEKWLEYATNDANAYAFYENTNEVPANTAA----R 345
Cdd:PRK10974 282 AKFNYGVGMMPydaDVKGAPQNAIIGGASLWVMQG--KDKETykgVAKFLDFLAKPENAAEWHQKTGYLPITTAAydltR 359
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2080717491 346 KKAGEQKNDLTSAVIKQYETATPTP--------NIP--------EMAEVWTgaeslifdavsGKKAAQTSANDAV 404
Cdd:PRK10974 360 EQGFYEKNPGADTATRQMLNKPPLPftkglrlgNMPqirtivdeELESVWT-----------GKKTPQQALDSAV 423
|
|
| PBP2_PotD_PotF_like |
cd13590 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
51-379 |
1.58e-06 |
|
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. 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: 270308 [Multi-domain] Cd Length: 315 Bit Score: 49.54 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 51 ESIKAKFEKENDVTIKIVE----KQMFEQLEAlpldgpAGNAP-DVMLAAYDRIGGLGQQGHLLEIKPSN-TN-SFGDKE 123
Cdd:cd13590 13 PEVLKAFEKETGVKVNYDTydsnEEMLAKLRA------GGGSGyDLVVPSDYMVERLIKQGLLEPLDHSKlPNlKNLDPQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 124 MQQVTVD-GKVYGMPLVIETLVLYYNKDLLQTAPKTFKDlekltedsrFAFASEKGKSTGFLAKWTDfYMSYGLLA-GYG 201
Cdd:cd13590 87 FLNPPYDpGNRYSVPYQWGTTGIAYNKDKVKEPPTSWDL---------DLWDPALKGRIAMLDDARE-VLGAALLAlGYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 202 gyvfgKNGTDSGDIglnnKGAVEAVKYAEKWFKTYwpkgmqdnssADDFIQQMFLDGKAGAIIG--GPWSAANYKEAKLN 279
Cdd:cd13590 157 -----PNTTDPAEL----AAAAELLIKQKPNVRAF----------DSDSYVQDLASGEIWLAQAwsGDALQANRENPNLK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 280 YgaapipTLPngEEyapfaGGKGWVAS----KYTKEPELAEKWLEYATNDANAYAFYENTNEVPANTAARKK-----AGE 350
Cdd:cd13590 218 F------VIP--KE-----GGLLWVDNmaipKGAPNPELAHAFINFLLDPEVAAKNAEYIGYATPNKAALELlppelLDN 284
|
330 340 350
....*....|....*....|....*....|.
gi 2080717491 351 QKNDLTSAVIKQYETATPTP--NIPEMAEVW 379
Cdd:cd13590 285 PALYPPIEPLAKLLTFKDVDgeALELYDRIW 315
|
|
| PBP2_polyamines |
cd13523 |
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
51-321 |
5.93e-06 |
|
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding proteins that function as the primary high-affinity receptors of ABC-type polyamine transport systems. 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, as well as 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: 270241 [Multi-domain] Cd Length: 268 Bit Score: 47.43 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 51 ESIKAKFEKENDVTIKIVEKQMFEQLEALPLDGPAGnAPDVMLAAYDRIGGLGQQGHL--LEIKPSNTNSFGDKEMQ--- 125
Cdd:cd13523 13 QDIIDPFEKETGIKVVVDTAANSERMIKKLSAGGSG-GFDLVTPSDSYTSRQLGVGLMqpIDKSLLPSWATLDPHLTlaa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 126 QVTVDGKVYGMPLVIETLVLYYNKDLLQTAPKTFKDlekltedsrFAFASEKGKSTGFLAKWTDFYMSYGLLAGYGGyvf 205
Cdd:cd13523 92 VLTVPGKKYGVPYQWGATGLVYNTDKVKAPPKSYAA---------DLDDPKYKGRVSFSDIPRETFAMALANLGADG--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 206 gkNGTDSGDIglnNKGAVEAVKYAEKWFKTYWpkgmqdnsSADDFIQQMFLDGKAGAIIGGPWSAanykeAKLNYGAAPI 285
Cdd:cd13523 160 --NEELYPDF---TDAAAALLKELKPNVKKYW--------SNASQPANLLLNGEVVLAMAWLGSG-----FKLKQAGAPI 221
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2080717491 286 ptlpngEEYAPFAGGKGWVAS----KYTKEPELAEKWLEY 321
Cdd:cd13523 222 ------EFVVPKEGAVGWLDTfavpANAPNKDGAYKLLNA 255
|
|
| PBP2_AlgQ1_2 |
cd13584 |
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 ... |
121-322 |
1.82e-03 |
|
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: 40.50 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 121 DKEMQqvTVDGKVYGMPLV------IETLVLYYNKDLLQ----TAPKTFKDLEKLTedsrFAFASEKGKSTG-------F 183
Cdd:cd13584 107 KKAIT--TDDGNIYGFPYLpdgdvaKEARGYFIRKDWLDklglKTPSTIDEWYTVL----KAFKERDPNGNGkadevplI 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 184 LAKWTDFYMsyGLLAGYGG-----YVfgkngtDSGDI--GLNNKGAVEAVKYAEKWFKTYW--PKGMQDNSSADdfiQQM 254
Cdd:cd13584 181 LTKPGYDET--GRLINAWGaymdfYQ------ENGKVkyGPLEPGFKDFLKTMNQWYKEGLidPDFFTRKAKAR---EQN 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080717491 255 FLDGKAGA---IIGGPWSAANY----KEAKLNYGAAPIPTLPNG----EEYAPFAG-GKGWVASKYTKEPELAEKWLEYA 322
Cdd:cd13584 250 IMNGNIGGfthDWFASTGTFNLallkNVPDFKLVAVPPPVLNKGqtpyEEDSRQIAkGDGAAITASNKNPVLAIKWLDYA 329
|
|
| |
