|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10974 |
PRK10974 |
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB; |
1-437 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
Pssm-ID: 182876 [Multi-domain] Cd Length: 438 Bit Score: 915.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 1 MKPLRYTASALALGLALMANAQAVTTIPFWHSMEGELGKEVDSLAQRFNAENPDYKIVPTYKGNYEQNLSAGIAAFRTGN 80
Cdd:PRK10974 2 MKSLRSTALGLALGLALSGNAQAVTEIPFWHSMEGELGKEVDSLAQRFNASQPDYKIVPVYKGNYEQSLAAGIAAFRSGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 81 APAILQVYEVGTATMMASKAIKPVYDVFKEAGIQFDESQFVPTVSGYYSDSKTGHLLSQPFNSSTPVLYYNKDAFKKAGL 160
Cdd:PRK10974 82 APAILQVYEVGTATMMASKAIKPVYDVFKDAGIPFDESQFVPTVAGYYSDAKTGHLLSQPFNSSTPVLYYNKDAFKKAGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 161 DPEQPPKTWQDLADYAAKLKASGMKCGYASGWQGWIQLENFSAWNGLPFASKNNGFDGTDAVLEFNKPEQVKHIAMLEEM 240
Cdd:PRK10974 162 DPEQPPKTWQDLAAYAAKLRAAGMKCGYASGWQGWIQLENFSAWHGLPFASKNNGFDGTDAVLEFNKPEQVKHIALLEEM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 241 NKKGDFSYVGRKDESTEKFYNGDCAMTTASSGSLANIREYAKFNYGVGMMPYDADAKDAPQNAIIGGASLWVMQGKDKET 320
Cdd:PRK10974 242 NKKGDFTYVGRKDESTEKFYNGDCAITTASSGSLANIRKYAKFNYGVGMMPYDADVKGAPQNAIIGGASLWVMQGKDKET 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 321 YTGVAKFLDFLAKPENAAEWHQKTGYLPITKAAYDLTREQGFYEKNPGADIATRQMLNKPPLPFTKGLRLGNMPQIRVIV 400
Cdd:PRK10974 322 YKGVAKFLDFLAKPENAAEWHQKTGYLPITTAAYDLTREQGFYEKNPGADTATRQMLNKPPLPFTKGLRLGNMPQIRTIV 401
|
410 420 430
....*....|....*....|....*....|....*..
gi 446726267 401 DEELESVWTGKKTPQQALDTAVERGNQLLRRFEKSTK 437
Cdd:PRK10974 402 DEELESVWTGKKTPQQALDSAVERGNQLLRRFEKSTK 438
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
26-424 |
4.25e-107 |
|
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: 321.93 E-value: 4.25e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 26 TIPFWHSMEGELGKEVDSLAQRFNAENPDYKIVPTYKGNYEQNLSAGIAAFRTGNAPAILQVYEVGTATMMASKAIKPVY 105
Cdd:cd14748 1 EITFWHGMSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 106 DVFKEAGiqFDESQFVPTVSGYYsdSKTGHLLSQPFNSSTPVLYYNKDAFKKAGLDPEQPPKTWQDLADYAAKLKASGMK 185
Cdd:cd14748 81 DYIDKDG--VDDDDFYPAALDAG--TYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKDKGGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 186 -----CGYASGWQGWIqLENFSAWNGLPFASKnngfDGTDAVleFNKPEQVKHIAMLEEMNKKGDFSYVGRKDESTEKFY 260
Cdd:cd14748 157 tgrygFALPPGDGGWT-FQALLWQNGGDLLDE----DGGKVT--FNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 261 NGDCAMTTASSGSLANIREY-AKFNYGVGMMPYDADAKDApqnAIIGGASLWVMQGKDKETYtGVAKFLDFLAKPENAAE 339
Cdd:cd14748 230 SGKVAMTINGTWSLAGIRDKgAGFEYGVAPLPAGKGKKGA---TPAGGASLVIPKGSSKKKE-AAWEFIKFLTSPENQAK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 340 WHQKTGYLPITKAAYDLTREqgFYEKNPGADIATRQMLNKPPLPFtkglRLGNMPQIRVIVDEELESVWTGKKTPQQALD 419
Cdd:cd14748 306 WAKATGYLPVRKSAAEDPEE--FLAENPNYKVAVDQLDYAKPWGP----PVPNGAEIRDELNEALEAALLGKKTPEEALK 379
|
....*
gi 446726267 420 TAVER 424
Cdd:cd14748 380 EAQEK 384
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
22-432 |
4.26e-62 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 205.28 E-value: 4.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 22 QAVTTIPFWHSMEGElGKEVDSLAQRFNAENPDYKIVPTYKG--NYEQNLsagIAAFRTGNAPAILQVYEVGTATMMASK 99
Cdd:COG1653 30 AGKVTLTVWHTGGGE-AAALEALIKEFEAEHPGIKVEVESVPydDYRTKL---LTALAAGNAPDVVQVDSGWLAEFAAAG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 100 AIKPVYDVFKEAGiqFDESQFVPTVSGYYSDSktGHLLSQPFNSSTPVLYYNKDAFKKAGLDpeqPPKTWQDLADYAAKL 179
Cdd:COG1653 106 ALVPLDDLLDDDG--LDKDDFLPGALDAGTYD--GKLYGVPFNTDTLGLYYNKDLFEKAGLD---PPKTWDELLAAAKKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 180 KASGMKCGYASGWQGWIQLENFSAWNGLPFASKnngfdgtDAVLEFNKPEQVKHIAMLEEMNKKGDF---SYVGRKDEST 256
Cdd:COG1653 179 KAKDGVYGFALGGKDGAAWLDLLLSAGGDLYDE-------DGKPAFDSPEAVEALEFLKDLVKDGYVppgALGTDWDDAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 257 EKFYNGDCAMTTASSGSLANIREYA-KFNYGVGMMPYDADAKdaPQNAIIGGASLWVMQG-KDKEtytGVAKFLDFLAKP 334
Cdd:COG1653 252 AAFASGKAAMMINGSWALGALKDAApDFDVGVAPLPGGPGGK--KPASVLGGSGLAIPKGsKNPE---AAWKFLKFLTSP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 335 ENAAEWhqktgylpitkaaydltreqgfyeknpgadiatrqmlnkpplpftkglrlgnmpqirvivdEELESVWTGKKTP 414
Cdd:COG1653 327 EAQAKW-------------------------------------------------------------DALQAVLLGQKTP 345
|
410
....*....|....*...
gi 446726267 415 QQALDTAVERGNQLLRRF 432
Cdd:COG1653 346 EEALDAAQAAANAALARA 363
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
26-424 |
1.89e-52 |
|
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: 180.29 E-value: 1.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 26 TIPFWHSMEGELGKEVDSLAQRFNAENPDYKI--VPTYKGNYEQNLSAGIAAfrtGNAPAILQVYEVGTATMMASKAIKP 103
Cdd:cd13585 1 TLTFWDWGQPAETAALKKLIDAFEKENPGVKVevVPVPYDDYWTKLTTAAAA---GTAPDVFYVDGPWVPEFASNGALLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 104 VYDVFKEAGIQFDesqFVPTVSGYYSdsKTGHLLSQPFNSSTPVLYYNKDAFKKAGLDPEqPPKTWQDLADYAAKLKA-S 182
Cdd:cd13585 78 LDDYIEKDGLDDD---FPPGLLDAGT--YDGKLYGLPFDADTLVLFYNKDLFDKAGPGPK-PPWTWDELLEAAKKLTDkK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 183 GMKCGYASGWQ--GWIQLENFSAWNGLPFasknngFDGTDAVLEFNKPEQVKHIAMLEEMNKKGDF--SYVGRKDESTEK 258
Cdd:cd13585 152 GGQYGFALRGGsgGQTQWYPFLWSNGGDL------LDEDDGKATLNSPEAVEALQFYVDLYKDGVApsSATTGGDEAVDL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 259 FYNGDCAMTTASSGSLANIRE-YAKFNYGVGMMPYdadAKDAPQNAIIGGASLWVM-QGKDKETytgVAKFLDFLAKPEN 336
Cdd:cd13585 226 FASGKVAMMIDGPWALGTLKDsKVKFKWGVAPLPA---GPGGKRASVLGGWGLAISkNSKHPEA---AWKFIKFLTSKEN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 337 AAEWHQKTGYLPITKAAYDLTREQGFYEKNPGADIATRQMLNKPPLPFtkglrlgNMPQIRVIVDEELESVWTGK--KTP 414
Cdd:cd13585 300 QLKLGGAAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPP-------PWPEVYPILSEALQEALLGAlgKSP 372
|
410
....*....|
gi 446726267 415 QQALDTAVER 424
Cdd:cd13585 373 EEALKEAAKE 382
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
26-429 |
3.35e-34 |
|
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: 131.67 E-value: 3.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 26 TIPFWHSMEGELGKEVDSLAQRFNAENPDYKIVPTYK--GNYEQNLSAGIAAfrtGNAPAILQVYEVGTATMMASKAIKP 103
Cdd:cd14747 1 TLTVWAMGNSAEAELLKELADEFEKENPGIEVKVQVLpwGDAHTKITTAAAS---GDGPDVVQLGNTWVAEFAAMGALED 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 104 VYDVFKEAGIqfDESQFVPTVSGYYSDSKTghlLSQPFNSSTPVLYYNKDAFKKAGldPEQPPKTWQDLADYAAKLKASG 183
Cdd:cd14747 78 LTPYLEDLGG--DKDLFPGLVDTGTVDGKY---YGVPWYADTRALFYRTDLLKKAG--GDEAPKTWDELEAAAKKIKADG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 184 M-KCGYASGWQGWIQlENFSAW---NGLPFASKNNGfdgtdaVLEFNKPEQVKHIAMLEEMNKKGDFSYVGRKDEST--E 257
Cdd:cd14747 151 PdVSGFAIPGKNDVW-HNALPFvwgAGGDLATKDKW------KATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSADveQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 258 KFYNGDCAMTTASSGSLANIREY---AKFNYGVGMMPydadAKDAPQNA-IIGGASLWVMQG-KDKEtytGVAKFLDFLA 332
Cdd:cd14747 224 AFANGKVAMIISGPWEIGAIREAgpdLAGKWGVAPLP----GGPGGGSPsFAGGSNLAVFKGsKNKD---LAWKFIEFLS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 333 KPENAAEWHQKTGYLPITKAAYDLtreqGFYEKNPGADIATRQMLNKPPLPFTKGLrlgnmPQIRVIVDEELESVWTG-K 411
Cdd:cd14747 297 SPENQAAYAKATGMLPANTSAWDD----PSLANDPLLAVFAEQLKTGKATPATPEW-----GEIEAELVLVLEEVWIGvG 367
|
410
....*....|....*...
gi 446726267 412 KTPQQALDTAVERGNQLL 429
Cdd:cd14747 368 ADVEDALDKAAAEINEIL 385
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
26-421 |
1.45e-32 |
|
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: 127.11 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 26 TIPFWHSMEGELGKE-VDSLAQRFNAENPDYKIVPTYKG--NYEQNLSAGIAAfrtGNAPAILQVYEVG-TATMMASKAI 101
Cdd:cd14749 1 TITYWQYFTGDTKKKyMDELIADFEKENPNIKVKVVVFPydNYKTKLKTAVAA---GEGPDVFNLWPGGwLAEFVKAGLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 102 KPVYDVFKEAGiqFDESQFVPTVSGYYSDsktGHLLSQPFNSSTPVLYYNKDAFKKAGldPEQPPKTWQDLADYAAKLKA 181
Cdd:cd14749 78 LPLTDYLDPNG--VDKRFLPGLADAVTFN---GKVYGIPFAARALALFYNKDLFEEAG--GVKPPKTWDELIEAAKKDKF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 182 -SGMKCGYASG----WQGWIqLENFSAWNGLPFASKNNGFDGTdavleFNKPEQVKHIAMLEEMNKKGDFSYVG---RKD 253
Cdd:cd14749 151 kAKGQTGFGLLlgaqGGHWY-FQYLVRQAGGGPLSDDGSGKAT-----FNDPAFVQALQKLQDLVKAGAFQEGFegiDYD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 254 ESTEKFYNGDCAMTTASSGSLANIREY-AKFNYGVGMMPydaDAKDAPQNAIIGGASLWVMQGKDKETYTGVAKFLDFLA 332
Cdd:cd14749 225 DAGQAFAQGKAAMNIGGSWDLGAIKAGePGGKIGVFPFP---TVGKGAQTSTIGGSDWAIAISANGKKKEAAVKFLKYLT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 333 KPENAAEWHQKTGYLPITKAAyDLTREQGFYEKNPGADIATRQMLNKPPLPFTKGlrlgnmPQIRVIVDeELESVWTGKK 412
Cdd:cd14749 302 SPEVMKQYLEDVGLLPAKEVV-AKDEDPDPVAILGPFADVLNAAGSTPFLDEYWP------AAAQVHKD-AVQKLLTGKI 373
|
....*....
gi 446726267 413 TPQQALDTA 421
Cdd:cd14749 374 DPEQVVKQA 382
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
26-424 |
1.21e-31 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 125.06 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 26 TIPFWHSmEGElGKEVDSLAQRFNAEnPDYKIVPTYKG--NYEQNLSAGIAAfrtGNAPAILQVYEVGTATMMASKAIKP 103
Cdd:COG2182 40 TLTVWVD-DDE-AEALEEAAAAFEEE-PGIKVKVVEVPwdDLREKLTTAAPA---GKGPDVFVGAHDWLGELAEAGLLAP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 104 VYDVFKeagiqfDESQFVPT-VSGYYSDsktGHLLSQPFNSSTPVLYYNKDAFkkagldPEQPPKTWQDLADYAAKLKAS 182
Cdd:COG2182 114 LDDDLA------DKDDFLPAaLDAVTYD---GKLYGVPYAVETLALYYNKDLV------KAEPPKTWDELIAAAKKLTAA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 183 GMKCGYASGWQGWiqleNFSAW----NGLPFasKNNGFDGTDavLEFNKPEQVKHIAMLEEMNKKG----DFSYvgrkDE 254
Cdd:COG2182 179 GKYGLAYDAGDAY----YFYPFlaafGGYLF--GKDGDDPKD--VGLNSPGAVAALEYLKDLIKDGvlpaDADY----DA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 255 STEKFYNGDCAMTTASSGSLANIREYAKFNYGVGMMPYDADAKDAPqnAIIGGASLWVM-QGKDKETytgVAKFLDFLAK 333
Cdd:COG2182 247 ADALFAEGKAAMIINGPWAAADLKKALGIDYGVAPLPTLAGGKPAK--PFVGVKGFGVSaYSKNKEA---AQEFAEYLTS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 334 PENAAEWHQKTGYLPITKAAYDltreQGFYEKNPGADiATRQMLNK-PPLPFTKglrlgNMPQIRVIVDEELESVWTGKK 412
Cdd:COG2182 322 PEAQKALFEATGRIPANKAAAE----DAEVKADPLIA-AFAEQAEYaVPMPNIP-----EMGAVWTPLGTALQAIASGKA 391
|
410
....*....|..
gi 446726267 413 TPQQALDTAVER 424
Cdd:COG2182 392 DPAEALDAAQKQ 403
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
44-369 |
6.21e-30 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 117.51 E-value: 6.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 44 LAQRFNAENpDYKIVPTYKG--NYEQNLSAGIAAfrtGNAPAILQVYEVG--TATMMASKAIKPVYDVfkeagiqfDESQ 119
Cdd:pfam13416 2 LAKAFEKKT-GVTVEVEPQAsnDLQAKLLAAAAA---GNAPDLDVVWIAAdqLATLAEAGLLADLSDV--------DNLD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 120 FVPTVSGYYSDSktGHLLSQPFNSSTP-VLYYNKDAFKKAGLDPeqppKTWQDLADYAAKLKAsgmKCGYASGWQGWIQl 198
Cdd:pfam13416 70 DLPDALDAAGYD--GKLYGVPYAASTPtVLYYNKDLLKKAGEDP----KTWDELLAAAAKLKG---KTGLTDPATGWLL- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 199 enFSAW-NGLPFASKNNGFDGTDAVLEFnkpeqvkhiamLEEMNKKGDFsyVGRKDESTEKFYNGDCAMTTASSGSLANI 277
Cdd:pfam13416 140 --WALLaDGVDLTDDGKGVEALDEALAY-----------LKKLKDNGKV--YNTGADAVQLFANGEVAMTVNGTWAAAAA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 278 REyAKFNYGVGMmpydadakdAPQNAIIGGASLWVMQGKDKETYTGvAKFLDFLAKPENAAEWHQKTGYLPITKAAYDLt 357
Cdd:pfam13416 205 KK-AGKKLGAVV---------PKDGSFLGGKGLVVPAGAKDPRLAA-LDFIKFLTSPENQAALAEDTGYIPANKSAALS- 272
|
330
....*....|..
gi 446726267 358 reqGFYEKNPGA 369
Cdd:pfam13416 273 ---DEVKADPAL 281
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
44-338 |
5.03e-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: 5.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 44 LAQRFNAENPDYKIVPTYKGnYEQNLSAGIAAFRTGNAPA-ILQVYEVGTATMMASKAIKPVYDVFKEAGIQFDesqfvp 122
Cdd:pfam01547 13 LVKEFEKEHPGIKVEVESVG-SGSLAQKLTTAIAAGDGPAdVFASDNDWIAELAKAGLLLPLDDYVANYLVLGV------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 123 tvsgyysdsktGHLLSQPFNSSTPVLYYNKDAFKKAGLDPeqpPKTWQDLADYAAKLKASG----MKCGYASGWQGWIQL 198
Cdd:pfam01547 86 -----------PKLYGVPLAAETLGLIYNKDLFKKAGLDP---PKTWDELLEAAKKLKEKGkspgGAGGGDASGTLGYFT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 199 ENFSAWNGLPFASKNNGFDGTDAVLEFNKPEQVKHIAMLEEMNKKGDFSYVGRKDESTEKFYNGDCAMTTASSGS----- 273
Cdd:pfam01547 152 LALLASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAalaan 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446726267 274 -------LANIREYAKFNYGVGMMPYDADAKDAPQNAIIGGASlwvmqgKDKEtytGVAKFLDFLAKPENAA 338
Cdd:pfam01547 232 kvklkvaFAAPAPDPKGDVGYAPLPAGKGGKGGGYGLAIPKGS------KNKE---AAKKFLDFLTSPEAQA 294
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
26-421 |
2.68e-23 |
|
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: 100.53 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 26 TIPFWHSMEGELGKEVDSLAQRFNAENPDYKI----VPtykgnYEQNLSAGIAAFRTGNAPAILQVYEVGTATMMASKAI 101
Cdd:cd14751 1 TITFWHTSSDEEKVLYEKLIPAFEKEYPKIKVkavrVP-----FDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 102 KPVYDV--FKEAGIQFDEsqfvPTVSGYYSdsktGHLLSQPFNSSTPVLYYNKDAFKKAGLDpeqPPKTWQDLADYAAKL 179
Cdd:cd14751 76 QPLDGTpaFDDIVDYLPG----PMETNRYN----GHYYGVPQVTNTLALFYNKRLLEEAGTE---VPKTMDELVAAAKAI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 180 KASGMKCGYAsgwqgwiqLENFSAWNGLPFASKNNG--FDGTDAVLEFNKPEQVKHIAMLEEMNKKG------DFSYVGR 251
Cdd:cd14751 145 KKKKGRYGLY--------ISGDGPYWLLPFLWSFGGdlTDEKKATGYLNSPESVRALETIVDLYDEGaitpcaSGGYPNM 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 252 KDEstekFYNGDCAMTT----ASSGSLANIREYAKFNYGVGMMPydadAKDAPQNAIIGGASLWVMQGKD--KETYtgva 325
Cdd:cd14751 217 QDG----FKSGRYAMIVngpwAYADILGGKEFKDPDNLGIAPVP----AGPGGSGSPVGGEDLVIFKGSKnkDAAW---- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 326 KFLDFLAKPENAAEWHQKTGYLPITKAAYDLTREQgfyeKNPGADIATRQM---LNKPPLPftkglrlgNMPQIRVIVDE 402
Cdd:cd14751 285 KFVKFMSSAEAQALTAAKLGLLPTRTSAYESPEVA----NNPMVAAFKPALetaVPRPPIP--------EWGELFEPLTL 352
|
410
....*....|....*....
gi 446726267 403 ELESVWTGKKTPQQALDTA 421
Cdd:cd14751 353 AFAKVLRGEKSPREALDEA 371
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
26-424 |
3.54e-20 |
|
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: 91.32 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 26 TIPFWHSMEGELGKEVDSLAQRFNAENPDYKIVPTYKG--NYEQNLSagiAAFRTGNAPAILqvyevgtatMMASKAIKP 103
Cdd:cd13522 1 TITVWHQYDTGENQAVNELIAKFEKAYPGITVEVTYQDteARRQFFS---TAAAGGKGPDVV---------FGPSDSLGP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 104 vydvFKEAGIQFDESQFVP-----TVSGYYSDSKTGHLLSQPFNSSTPVLYYNKDAFkkagldPEQPPKTWQDLADYAAK 178
Cdd:cd13522 69 ----FAAAGLLAPLDEYVSksgkyAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLV------PKNPPKTWQELIALAQG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 179 LKASGMKC-----GYASGWQGWIQlenfsAWNGLPFASKNNGFDGTdavleFNKPEQVKHIAMLEEMNKKGDFSYvGRKD 253
Cdd:cd13522 139 LKAKNVWGlvynqNEPYFFAAWIG-----GFGGQVFKANNGKNNPT-----LDTPGAVEALQFLVDLKSKYKIMP-PETD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 254 ESTEK--FYNGDCAMTTASSGSLANIREYAKFNYGVGMMPydADAKDAPQNAIIGGASlwVMQGKDKETYTGVAKFLDFL 331
Cdd:cd13522 208 YSIADalFKAGKAAMIINGPWDLGDYRQALKINLGVAPLP--TFSGTKHAAPFVGGKG--FGINKESQNKAAAVEFVKYL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 332 AKPENAAEWHQKTGYLPITKAAYDLTREQgfyeKNPGADIATRQMLNKPPLPftkglrlgNMPQIRVIVD---EELESVW 408
Cdd:cd13522 284 TSYQAQLVLFDDAGDIPANLQAYESPAVQ----NKPAQKASAEQAAYGVPMP--------NIPEMRAVWDafrIAVNSVL 351
|
410
....*....|....*.
gi 446726267 409 TGKKTPQQALDTAVER 424
Cdd:cd13522 352 AGKVTPEAAAKDAQQE 367
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
26-424 |
1.05e-19 |
|
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: 90.43 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 26 TIPFWHSMEGELGKEVDSLAQRFNAENPD--YKIVPTyKGNYEQNLSAGIAAFRTGN-APAILQVYEVGTATMMASKAIK 102
Cdd:cd14750 1 TITFAAGSDGQEGELLKKAIAAFEKKHPDikVEIEEL-PASSDDQRQQLVTALAAGSsAPDVLGLDVIWIPEFAEAGWLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 103 PVYDVFKEAGiqfDESQFVPTVSGYYSDsktGHLLSQPFNSSTPVLYYNKDAFKKAGLdpeQPPKTWQDLADyAAKLKAS 182
Cdd:cd14750 80 PLTEYLKEEE---DDDFLPATVEANTYD---GKLYALPWFTDAGLLYYRKDLLEKYGP---EPPKTWDELLE-AAKKRKA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 183 GMKCGYASGWQGwIQLENFSAwNGLPFASKNNG--FDGTDAVLEFNKPEQVKHIAMLEEMNKKG---DFSYVGRKDESTE 257
Cdd:cd14750 150 GEPGIWGYVFQG-KQYEGLVC-NFLELLWSNGGdiFDDDSGKVTVDSPEALEALQFLRDLIGEGispKGVLTYGEEEARA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 258 KFYNGDCAM----TTASSGSLANIREYA-KFnyGVGMMPydadAKDAPQNA-IIGGASLWVMQG-KDKETytgVAKFLDF 330
Cdd:cd14750 228 AFQAGKAAFmrnwPYAYALLQGPESAVAgKV--GVAPLP----AGPGGGSAsTLGGWNLAISANsKHKEA---AWEFVKF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 331 LAKPENAAEWHQKTGYLPITKAAYDltrEQGFYEKNPGADIATRQMLN---KPPLPFtkglrlgnMPQIRVIVDEELESV 407
Cdd:cd14750 299 LTSPEVQKRRAINGGLPPTRRALYD---DPEVLEAYPFLPALLEALENavpRPVTPK--------YPEVSTAIQIALSAA 367
|
410
....*....|....*..
gi 446726267 408 WTGKKTPQQALDTAVER 424
Cdd:cd14750 368 LSGQATPEEALKQAQEK 384
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
134-424 |
4.00e-19 |
|
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: 88.31 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 134 GHLLSQPFNSSTPVLYYNKDAFKKAgldpeqpPKTWQDLADYAAKL-KASGMKCGYASGWQGWIQLENFSAWNGlPFASK 212
Cdd:cd13658 98 GKLYGLPAAVETLALYYNKDLVKNA-------PKTFDELEALAKDLtKEKGKQYGFLADATNFYYSYGLLAGNG-GYIFK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 213 NNGFDGTDAVLEFNKPEQVKHIAMLEEMNKKGDFSYVGRKDESTEKFYNGDCAMTTASSGSLANIREyAKFNYGVGMMPY 292
Cdd:cd13658 170 KNGSDLDINDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAVIDGPWAIQEYQE-AGVNYGVAPLPT 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 293 DADAKDApqnAIIGGASLWVMQGKDKETYTGvAKFLDFLAKPENAAEWHQKTGYLPITKAAydltREQGFYEKNPGADIA 372
Cdd:cd13658 249 LPNGKPM---APFLGVKGWYLSAYSKHKEWA-QKFMEFLTSKENLKKRYDETNEIPPRKDV----RSDPEIKNNPLTSAF 320
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446726267 373 TRQMLNKPPLPftkglrlgNMPQIRVI---VDEELESVWTGKKTPQQALDTAVER 424
Cdd:cd13658 321 AKQASRAVPMP--------NIPEMGAVwepANNALFFILSGKKTPKQALNDAVND 367
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
26-424 |
4.22e-18 |
|
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: 85.42 E-value: 4.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 26 TIPFWHSMEGELgKEVDSLAQRFNAENpDYKIVPTYKGNYEQNlSAGIAAFRTGNAPAILQVYEVGTATMMASKAIKPVY 105
Cdd:cd13586 1 TITVWTDEDGEL-EYLKELAEEFEKKY-GIKVEVVYVDSGDTR-EKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 106 DVFKEAgiQFDESQFVPTVSgyYSdsktGHLLSQPFNSSTPVLYYNKDAFKkagldpeQPPKTWQDLADYAAKL-KASGM 184
Cdd:cd13586 78 EYLAVK--IKNLPVALAAVT--YN----GKLYGVPVSVETIALFYNKDLVP-------EPPKTWEELIALAKKFnDKAGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 185 KCGYASGWQ------GWIQlenfsAWNGLPFASKNNGFDGtdavLEFNKPEQVKHIAMLEEMNKKGDFSYVGRKDESTEK 258
Cdd:cd13586 143 KYGFAYDQTnpyfsyPFLA-----AFGGYVFGENGGDPTD----IGLNNEGAVKGLKFIKDLKKKYKVLPPDLDYDIADA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 259 -FYNGDCAMTTASSGSLANIREyAKFNYGVGMMP-YDADAKDAPqnaiIGGASLWVMQGKDKEtYTGVAKFLDFLAKPEN 336
Cdd:cd13586 214 lFKEGKAAMIINGPWDLADYKD-AGINFGVAPLPtLPGGKQAAP----FVGVQGAFVSAYSKN-KEAAVEFAEYLTSDEA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 337 AAEWHQKTGYLPITKAAYDLTREQgfyeKNPGADIATRQMLNKPPLPftkglrlgNMPQIRVI---VDEELESVWTGKKT 413
Cdd:cd13586 288 QLLLFEKTGRIPALKDALNDAAVK----NDPLVKAFAEQAQYGVPMP--------NIPEMAAVwdaMGNALNLVASGKAT 355
|
410
....*....|.
gi 446726267 414 PQQALDTAVER 424
Cdd:cd13586 356 PEEAAKDAVAA 366
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
26-424 |
2.19e-15 |
|
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: 77.03 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 26 TIPFWHSMEGELGKEVDSLAQRFNAENPDYKIVPTYKGNYEQNLsAGIAAFRTGNAPAILQVYEVGTATMMASKAIKPVY 105
Cdd:cd13657 1 TITIWHALTGAEEDALQQIIDEFEAKYPVPNVKVPFEKKPDLQN-KLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 106 DVFKEagiqFDESQFVP-TVSGYYSDsktGHLLSQPFNSSTPVLYYNKDAFKkagldpeQPPKTWQDLADYAAKLKASGm 184
Cdd:cd13657 80 DYLSE----DDFENYLPtAVEAVTYK---GKVYGLPEAYETVALIYNKALVD-------QPPETTDELLAIMKDHTDPA- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 185 KCGYASGWQgwIQLENFSAWngLPFASKNNGFDGTDAVLEFNKPEQVKHIAMLEEMNKK---GDFSYvgrkDESTEKFYN 261
Cdd:cd13657 145 AGSYGLAYQ--VSDAYFVSA--WIFGFGGYYFDDETDKPGLDTPETIKGIQFLKDFSWPympSDPSY----NTQTSLFNE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 262 GDCAMTTASSGSLANIREyAKFNYGVGMMPYDADAKdaPQNAIIGGASLWVMQGKDKETYTGVAKFLDFLAKPENAAEWH 341
Cdd:cd13657 217 GKAAMIINGPWFIGGIKA-AGIDLGVAPLPTVDGTN--PPRPYSGVEGIYVTKYAERKNKEAALDFAKFFTTAEASKILA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 342 QKTGYLPITKAAYDLTRE------QGFYEKnpgADIATrqmlnkpPLPftkglrlgNMPQIRVI---VDEELESVWTGKK 412
Cdd:cd13657 294 DENGYVPAATNAYDDAEVaadpviAAFKAQ---AEHGV-------PMP--------NSPEMASVwgpVTLALAAVYQGGQ 355
|
410
....*....|..
gi 446726267 413 TPQQALDTAVER 424
Cdd:cd13657 356 DPQEALAAAQQE 367
|
|
| PBP2_AlgQ_like_4 |
cd13583 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
54-335 |
3.92e-08 |
|
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: 55.44 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 54 DYKIVPTYkgNYEQNLSAGIAAfrtGNAPAILQV-YEVGTATMMASKAIKPVydvfkeagiqFDESQFVPTVSGYYSDSK 132
Cdd:cd13583 35 KRTPIPSS--DYETKRSLLIAS---GDAPDIIPVlYPGEENEFVASGALLPI----------SDYLDYMPNYKKYVEKWG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 133 TGHLLS---QP--FNSSTPVL----------YYNKDAFKKAGLdpeQPPKTWQDLADYAAKLK-ASGMKCGYASGWQGWI 196
Cdd:cd13583 100 LGKELAtgrQSdgKYYSLPGLhedpgvqysfLYRKDIFEKAGI---KIPTTWDEFYAALKKLKeKYPDSYPYSDRWNSNA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 197 QLENFSAWNGLP-FASKNNG-FDGTDAVLEFnKPEQVKHIAMLEEMNK---KG--DFSYVGRKDES-TEKFYNGDCAMTT 268
Cdd:cd13583 177 LLLIAAPAFGTTaGWGFSNYtYDPDTDKFVY-GATTDEYKDMLQYFNKlyaEGllDPESFTQTDDQaKAKFLNGKSFVIT 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446726267 269 ASSGSLANI--REYAKF--NYGVGMMPYDAdakdAPQNAIIGGASL---WVMQGK--DKETYTGVAKFLDFLAKPE 335
Cdd:cd13583 256 TNPQTVDELqrNLRAADggNYEVVSITPPA----GPAGKAINGSRLengFMISSKakDSKNFEALLQFLDWLYSDE 327
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
54-336 |
9.20e-08 |
|
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: 54.26 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 54 DYKIVPTykGNYEQNLSAGIAAfrtGNAPAILQVYEVGTATMMA-SKAIKPVYDVFKEAGiqfDESQFVPTVSGYYSDSK 132
Cdd:cd13580 37 KVKWVPD--SSYDEKLNLALAS---GDLPDIVVVNDPQLSITLVkQGALWDLTDYLDKYY---PNLKKIIEQEGWDSASV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 133 TGHLLSQPF---NSSTPVLYYNKDAFKKAGLdpeQPPKTWQDLADYAAKLKASGMK-------CGYASGWQGWIQ-LENF 201
Cdd:cd13580 109 DGKIYGIPRkrpLIGRNGLWIRKDWLDKLGL---EVPKTLDELYEVAKAFTEKDPDgngkkdtYGLTDTKDLIGSgFTGL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 202 SAWNGLPFASKNNGFDGTDaVLEFNKPEQVKHIAMLEEMNKKG----DFSyVGRKDESTEKFYNGDCAMTTASSGSLANI 277
Cdd:cd13580 186 FGAFGAPPNNWWKDEDGKL-VPGSIQPEMKEALKFLKKLYKEGlidpEFA-VNDGTKANEKFISGKAGIFVGNWWDPAWP 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 278 REYAKFNygvgmmpyDADAKDAPQNAIIG-----------GASLWVMQGKDKETYTGVAKFLDFLAKPEN 336
Cdd:cd13580 264 QASLKKN--------DPDAEWVAVPIPSGpdgkygvwaesGVNGFFVIPKKSKKPEAILKLLDFLSDPEV 325
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
148-291 |
1.49e-06 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 50.01 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 148 LYYNKDAFKkagldpeQPPKTWQDLADYAAKLKASGMKcgyASGWqgwiQLEN-------FSAWNGLPFASKNNGFDGTD 220
Cdd:PRK09474 141 LIYNKDLVP-------TPPKTWEEIPALDKELKAKGKS---AIMW----NLQEpyftwplIAADGGYAFKFENGGYDVKD 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446726267 221 AvlEFNKPEQVKHIAMLEEMNKKG----DFSYvgrkdESTE-KFYNGDCAMTTASSGSLANIREyAKFNYGVGMMP 291
Cdd:PRK09474 207 V--GVNNAGAKAGLQFLVDLVKNKhmnaDTDY-----SIAEaAFNKGETAMTINGPWAWSNIDK-SGINYGVTVLP 274
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
134-356 |
2.14e-05 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 46.44 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 134 GHLLSQPFNSSTPVLYYNKDAFKKagldpeqPPKTWQDLADyaaklkasgmkcgyaSGWQGWIQLENfSAWNGLPFASKN 213
Cdd:COG0687 123 GNVYGVPYTWGTTGIAYNTDKVKE-------PPTSWADLWD---------------PEYKGKVALLD-DPREVLGAALLY 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 214 NGFDGTDAvlefnKPEQVKHI-AMLEEMnKKGDFSYVGRKDESTEKFYNGDCAMTTASSGS-LANIREYAKFNYGVgmmp 291
Cdd:COG0687 180 LGYDPNST-----DPADLDAAfELLIEL-KPNVRAFWSDGAEYIQLLASGEVDLAVGWSGDaLALRAEGPPIAYVI---- 249
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446726267 292 ydadakdaPQNaiigGASLWV---MQGKDKETYTGVAKFLDFLAKPENAAEWHQKTGYLPITKAAYDL 356
Cdd:COG0687 250 --------PKE----GALLWFdnmAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAAREL 305
|
|
| PBP2_MBP |
cd13656 |
The periplasmic binding component of ABC tansport system specific for maltose; possess the ... |
134-291 |
9.89e-04 |
|
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: 41.04 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 134 GHLLSQPFNSSTPVLYYNKDAFKkagldpeQPPKTWQDLADYAAKLKASGMKC---GYASGWQGWIQLenfSAWNGLPFA 210
Cdd:cd13656 97 GKLIAYPIAVEALSLIYNKDLLP-------NPPKTWEEIPALDKELKAKGKSAlmfNLQEPYFTWPLI---AADGGYAFK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 211 SKNNGFDGTDavLEFNKPEQVKHIAMLEEMNKKGDFSYVGRKDESTEKFYNGDCAMTTASSGSLANIREyAKFNYGVGMM 290
Cdd:cd13656 167 YENGKYDIKD--VGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDT-SKVNYGVTVL 243
|
.
gi 446726267 291 P 291
Cdd:cd13656 244 P 244
|
|
| PBP2_BitB |
cd13546 |
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ... |
61-224 |
3.37e-03 |
|
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270264 [Multi-domain] Cd Length: 258 Bit Score: 39.16 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 61 YKGNYEQNLSAGIAAFRtgNAPAI-LQVYEVGTATMMA---SKAIKPVYDVFKEAGIQFDES---QFVPTVS-------- 125
Cdd:cd13546 5 YSPNSEEIIEPIIKEFE--EKPGIkVEVVTGGTGELLArikAEADNPQADVMWGGGIETLEAykdLFEPYESpeaaaipd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446726267 126 GYYSDSKTGHllsqPFNSSTPVLYYNKDAFKKAGldpeqPPKTWQDLADYAAKLK---ASGMKCGYAsgwqgWIQLENF- 201
Cdd:cd13546 83 AYKSPEGLWT----GFSVLPVVLMVNTDLVKNIG-----APKGWKDLLDPKWKGKiafADPNKSGSA-----YTILYTIl 148
|
170 180
....*....|....*....|....*....
gi 446726267 202 ----SAWNGLPFASKNNGF--DGTDAVLE 224
Cdd:cd13546 149 klygGAWEYIEKLLDNLGVilSSSSAVYK 177
|
|
| |
