|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10974 |
PRK10974 |
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB; |
2-439 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
Pssm-ID: 182876 [Multi-domain] Cd Length: 438 Bit Score: 935.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 2 LTYAIRKTTLCVALTLAVSAQALAATEIPFWHSMEGELGKEVDSLADRFNQSHSDVKIVPVYKGNYEQSLAAGIAAYRSG 81
Cdd:PRK10974 1 FMKSLRSTALGLALGLALSGNAQAVTEIPFWHSMEGELGKEVDSLAQRFNASQPDYKIVPVYKGNYEQSLAAGIAAFRSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 82 KAPAILQVYEVGTATMMASKAIKPVYEVFKEAGINFDESVFVPTVAGYYTDNKSGHLLSQPFNSSTPVLYYNKDAFKKAG 161
Cdd:PRK10974 81 NAPAILQVYEVGTATMMASKAIKPVYDVFKDAGIPFDESQFVPTVAGYYSDAKTGHLLSQPFNSSTPVLYYNKDAFKKAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 162 LNPDQPPKTWQELAADTAKLREAGMKCGYASGWQGWIQLENFSAWHGVPFASENNGFGGTSAKLEFNQPLQVKHIALLEA 241
Cdd:PRK10974 161 LDPEQPPKTWQDLAAYAAKLRAAGMKCGYASGWQGWIQLENFSAWHGLPFASKNNGFDGTDAVLEFNKPEQVKHIALLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 242 MNKKGDFTYFGRKDESTEKFYNGDCAITTASSGSLADIKHYAKFNYGVGMMPYDADAKNAPQNAIIGGASLWVMNGKDAA 321
Cdd:PRK10974 241 MNKKGDFTYVGRKDESTEKFYNGDCAITTASSGSLANIRKYAKFNYGVGMMPYDADVKGAPQNAIIGGASLWVMQGKDKE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 322 TYKGVAEFLQYLAQPEIAAEWHQKTGYLPITTAAYDLTKQQGFYDKNPGADVATRQMLNKPPLPFTKGLRLGNMPQIRSV 401
Cdd:PRK10974 321 TYKGVAKFLDFLAKPENAAEWHQKTGYLPITTAAYDLTREQGFYEKNPGADTATRQMLNKPPLPFTKGLRLGNMPQIRTI 400
|
410 420 430
....*....|....*....|....*....|....*...
gi 491072773 402 VDEELEGVWTGKKTPQQALDAAVQRGDVLLRRFEASTK 439
Cdd:PRK10974 401 VDEELESVWTGKKTPQQALDSAVERGNQLLRRFEKSTK 438
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
28-426 |
1.82e-99 |
|
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: 302.29 E-value: 1.82e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 28 EIPFWHSMEGELGKEVDSLADRFNQSHSDVKIVPVYKGNYEQSLAAGIAAYRSGKAPAILQVYEVGTATMMASKAIKPVY 107
Cdd:cd14748 1 EITFWHGMSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 108 EVFKEAGinFDESVFVPTVAGYYTDNksGHLLSQPFNSSTPVLYYNKDAFKKAGLNPDQPPKTWQELAADTAKLREAGMK 187
Cdd:cd14748 81 DYIDKDG--VDDDDFYPAALDAGTYD--GKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKDKGGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 188 -----CGYASGWQGWIqLENFSAWHGVPFASENNGfggtsaKLEFNQPLQVKHIALLEAMNKKGDFTYFGRKDESTEKFY 262
Cdd:cd14748 157 tgrygFALPPGDGGWT-FQALLWQNGGDLLDEDGG------KVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 263 NGDCAITTASSGSLADIKHY-AKFNYGVGMMPYDADAKNApqnAIIGGASLWVMNGkDAATYKGVAEFLQYLAQPEIAAE 341
Cdd:cd14748 230 SGKVAMTINGTWSLAGIRDKgAGFEYGVAPLPAGKGKKGA---TPAGGASLVIPKG-SSKKKEAAWEFIKFLTSPENQAK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 342 WHQKTGYLPITTAAYDLTKQqgFYDKNPGADVATRQMLNKPPLPFtkglRLGNMPQIRSVVDEELEGVWTGKKTPQQALD 421
Cdd:cd14748 306 WAKATGYLPVRKSAAEDPEE--FLAENPNYKVAVDQLDYAKPWGP----PVPNGAEIRDELNEALEAALLGKKTPEEALK 379
|
....*
gi 491072773 422 AAVQR 426
Cdd:cd14748 380 EAQEK 384
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
7-434 |
9.87e-57 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 191.03 E-value: 9.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 7 RKTTLCVALTLAV-----------SAQALAATEIPFWHSMEGElGKEVDSLADRFNQSHSDVKIVPVYKG--NYEQSLAA 73
Cdd:COG1653 2 RRLALALAAALALalaacggggsgAAAAAGKVTLTVWHTGGGE-AAALEALIKEFEAEHPGIKVEVESVPydDYRTKLLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 74 GIAAyrsGKAPAILQVYEVGTATMMASKAIKPVYEVFKEAGinFDESVFVPTVAGYYTDNksGHLLSQPFNSSTPVLYYN 153
Cdd:COG1653 81 ALAA---GNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDG--LDKDDFLPGALDAGTYD--GKLYGVPFNTDTLGLYYN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 154 KDAFKKAGLnpdQPPKTWQELAADTAKLREAGMKCGYASGWQGWIQLENFSAWHGVPFASENNgfggtsaKLEFNQPLQV 233
Cdd:COG1653 154 KDLFEKAGL---DPPKTWDELLAAAKKLKAKDGVYGFALGGKDGAAWLDLLLSAGGDLYDEDG-------KPAFDSPEAV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 234 KHIALLEAMNKKGDF---TYFGRKDESTEKFYNGDCAITTASSGSLADIKHYA-KFNYGVGMMPYDADAKnaPQNAIIGG 309
Cdd:COG1653 224 EALEFLKDLVKDGYVppgALGTDWDDARAAFASGKAAMMINGSWALGALKDAApDFDVGVAPLPGGPGGK--KPASVLGG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 310 ASLWVMngKDAATYKGVAEFLQYLAQPEIAAEWhqktgylpittaaydltkqqgfydknpgadvatrqmlnkpplpftkg 389
Cdd:COG1653 302 SGLAIP--KGSKNPEAAWKFLKFLTSPEAQAKW----------------------------------------------- 332
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 491072773 390 lrlgnmpqirsvvdEELEGVWTGKKTPQQALDAAVQRGDVLLRRF 434
Cdd:COG1653 333 --------------DALQAVLLGQKTPEEALDAAQAAANAALARA 363
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
46-357 |
9.75e-25 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 102.87 E-value: 9.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 46 LADRFNQSHsDVKIVPVYkGNYEQSLAAGIAAYRSGKAPAILQVYEVG--TATMMASKAIKPVYEVfkeaginfDESVFV 123
Cdd:pfam13416 2 LAKAFEKKT-GVTVEVEP-QASNDLQAKLLAAAAAGNAPDLDVVWIAAdqLATLAEAGLLADLSDV--------DNLDDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 124 PTVAGYYTDNksGHLLSQPFNSSTP-VLYYNKDAFKKAGlnpdQPPKTWQELAADTAKLREAGMKCGYASGWQGWIQLEn 202
Cdd:pfam13416 72 PDALDAAGYD--GKLYGVPYAASTPtVLYYNKDLLKKAG----EDPKTWDELLAAAAKLKGKTGLTDPATGWLLWALLA- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 203 fsawHGVPFASENNGFGGTsaklefnqplqVKHIALLEAMNKKGDFtyFGRKDESTEKFYNGDCAITTASSGSLADIKHy 282
Cdd:pfam13416 145 ----DGVDLTDDGKGVEAL-----------DEALAYLKKLKDNGKV--YNTGADAVQLFANGEVAMTVNGTWAAAAAKK- 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491072773 283 AKFNYGVGMmpydadaknAPQNAIIGGASLWVMNGKDAATYkGVAEFLQYLAQPEIAAEWHQKTGYLPITTAAYD 357
Cdd:pfam13416 207 AGKKLGAVV---------PKDGSFLGGKGLVVPAGAKDPRL-AALDFIKFLTSPENQAALAEDTGYIPANKSAAL 271
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10974 |
PRK10974 |
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB; |
2-439 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
Pssm-ID: 182876 [Multi-domain] Cd Length: 438 Bit Score: 935.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 2 LTYAIRKTTLCVALTLAVSAQALAATEIPFWHSMEGELGKEVDSLADRFNQSHSDVKIVPVYKGNYEQSLAAGIAAYRSG 81
Cdd:PRK10974 1 FMKSLRSTALGLALGLALSGNAQAVTEIPFWHSMEGELGKEVDSLAQRFNASQPDYKIVPVYKGNYEQSLAAGIAAFRSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 82 KAPAILQVYEVGTATMMASKAIKPVYEVFKEAGINFDESVFVPTVAGYYTDNKSGHLLSQPFNSSTPVLYYNKDAFKKAG 161
Cdd:PRK10974 81 NAPAILQVYEVGTATMMASKAIKPVYDVFKDAGIPFDESQFVPTVAGYYSDAKTGHLLSQPFNSSTPVLYYNKDAFKKAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 162 LNPDQPPKTWQELAADTAKLREAGMKCGYASGWQGWIQLENFSAWHGVPFASENNGFGGTSAKLEFNQPLQVKHIALLEA 241
Cdd:PRK10974 161 LDPEQPPKTWQDLAAYAAKLRAAGMKCGYASGWQGWIQLENFSAWHGLPFASKNNGFDGTDAVLEFNKPEQVKHIALLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 242 MNKKGDFTYFGRKDESTEKFYNGDCAITTASSGSLADIKHYAKFNYGVGMMPYDADAKNAPQNAIIGGASLWVMNGKDAA 321
Cdd:PRK10974 241 MNKKGDFTYVGRKDESTEKFYNGDCAITTASSGSLANIRKYAKFNYGVGMMPYDADVKGAPQNAIIGGASLWVMQGKDKE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 322 TYKGVAEFLQYLAQPEIAAEWHQKTGYLPITTAAYDLTKQQGFYDKNPGADVATRQMLNKPPLPFTKGLRLGNMPQIRSV 401
Cdd:PRK10974 321 TYKGVAKFLDFLAKPENAAEWHQKTGYLPITTAAYDLTREQGFYEKNPGADTATRQMLNKPPLPFTKGLRLGNMPQIRTI 400
|
410 420 430
....*....|....*....|....*....|....*...
gi 491072773 402 VDEELEGVWTGKKTPQQALDAAVQRGDVLLRRFEASTK 439
Cdd:PRK10974 401 VDEELESVWTGKKTPQQALDSAVERGNQLLRRFEKSTK 438
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
28-426 |
1.82e-99 |
|
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: 302.29 E-value: 1.82e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 28 EIPFWHSMEGELGKEVDSLADRFNQSHSDVKIVPVYKGNYEQSLAAGIAAYRSGKAPAILQVYEVGTATMMASKAIKPVY 107
Cdd:cd14748 1 EITFWHGMSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 108 EVFKEAGinFDESVFVPTVAGYYTDNksGHLLSQPFNSSTPVLYYNKDAFKKAGLNPDQPPKTWQELAADTAKLREAGMK 187
Cdd:cd14748 81 DYIDKDG--VDDDDFYPAALDAGTYD--GKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKDKGGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 188 -----CGYASGWQGWIqLENFSAWHGVPFASENNGfggtsaKLEFNQPLQVKHIALLEAMNKKGDFTYFGRKDESTEKFY 262
Cdd:cd14748 157 tgrygFALPPGDGGWT-FQALLWQNGGDLLDEDGG------KVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 263 NGDCAITTASSGSLADIKHY-AKFNYGVGMMPYDADAKNApqnAIIGGASLWVMNGkDAATYKGVAEFLQYLAQPEIAAE 341
Cdd:cd14748 230 SGKVAMTINGTWSLAGIRDKgAGFEYGVAPLPAGKGKKGA---TPAGGASLVIPKG-SSKKKEAAWEFIKFLTSPENQAK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 342 WHQKTGYLPITTAAYDLTKQqgFYDKNPGADVATRQMLNKPPLPFtkglRLGNMPQIRSVVDEELEGVWTGKKTPQQALD 421
Cdd:cd14748 306 WAKATGYLPVRKSAAEDPEE--FLAENPNYKVAVDQLDYAKPWGP----PVPNGAEIRDELNEALEAALLGKKTPEEALK 379
|
....*
gi 491072773 422 AAVQR 426
Cdd:cd14748 380 EAQEK 384
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
7-434 |
9.87e-57 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 191.03 E-value: 9.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 7 RKTTLCVALTLAV-----------SAQALAATEIPFWHSMEGElGKEVDSLADRFNQSHSDVKIVPVYKG--NYEQSLAA 73
Cdd:COG1653 2 RRLALALAAALALalaacggggsgAAAAAGKVTLTVWHTGGGE-AAALEALIKEFEAEHPGIKVEVESVPydDYRTKLLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 74 GIAAyrsGKAPAILQVYEVGTATMMASKAIKPVYEVFKEAGinFDESVFVPTVAGYYTDNksGHLLSQPFNSSTPVLYYN 153
Cdd:COG1653 81 ALAA---GNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDG--LDKDDFLPGALDAGTYD--GKLYGVPFNTDTLGLYYN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 154 KDAFKKAGLnpdQPPKTWQELAADTAKLREAGMKCGYASGWQGWIQLENFSAWHGVPFASENNgfggtsaKLEFNQPLQV 233
Cdd:COG1653 154 KDLFEKAGL---DPPKTWDELLAAAKKLKAKDGVYGFALGGKDGAAWLDLLLSAGGDLYDEDG-------KPAFDSPEAV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 234 KHIALLEAMNKKGDF---TYFGRKDESTEKFYNGDCAITTASSGSLADIKHYA-KFNYGVGMMPYDADAKnaPQNAIIGG 309
Cdd:COG1653 224 EALEFLKDLVKDGYVppgALGTDWDDARAAFASGKAAMMINGSWALGALKDAApDFDVGVAPLPGGPGGK--KPASVLGG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 310 ASLWVMngKDAATYKGVAEFLQYLAQPEIAAEWhqktgylpittaaydltkqqgfydknpgadvatrqmlnkpplpftkg 389
Cdd:COG1653 302 SGLAIP--KGSKNPEAAWKFLKFLTSPEAQAKW----------------------------------------------- 332
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 491072773 390 lrlgnmpqirsvvdEELEGVWTGKKTPQQALDAAVQRGDVLLRRF 434
Cdd:COG1653 333 --------------DALQAVLLGQKTPEEALDAAQAAANAALARA 363
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
28-426 |
2.04e-47 |
|
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: 167.20 E-value: 2.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 28 EIPFWHSMEGELGKEVDSLADRFNQSHSDVKI--VPVYKGNYEQSLAAGIAAyrsGKAPAILQVYEVGTATMMASKAIKP 105
Cdd:cd13585 1 TLTFWDWGQPAETAALKKLIDAFEKENPGVKVevVPVPYDDYWTKLTTAAAA---GTAPDVFYVDGPWVPEFASNGALLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 106 VYEVFKEAGINFDesvFVPTVAGYYTDNksGHLLSQPFNSSTPVLYYNKDAFKKAGLNPDqPPKTWQELAADTAKLRE-A 184
Cdd:cd13585 78 LDDYIEKDGLDDD---FPPGLLDAGTYD--GKLYGLPFDADTLVLFYNKDLFDKAGPGPK-PPWTWDELLEAAKKLTDkK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 185 GMKCGYASGWQ--GWIQLENFSAWHGVPFASENNGfggtsaKLEFNQPLQVKHIALLEAMNKKG---DFTYFGRkDESTE 259
Cdd:cd13585 152 GGQYGFALRGGsgGQTQWYPFLWSNGGDLLDEDDG------KATLNSPEAVEALQFYVDLYKDGvapSSATTGG-DEAVD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 260 KFYNGDCAITTASSGSLADIKH-YAKFNYGVGMMPYDADAKNApqnAIIGGASLWVMNG---KDAAtykgvAEFLQYLAQ 335
Cdd:cd13585 225 LFASGKVAMMIDGPWALGTLKDsKVKFKWGVAPLPAGPGGKRA---SVLGGWGLAISKNskhPEAA-----WKFIKFLTS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 336 PEIAAEWHQKTGYLPITTAAYDLTKQQGFYDKNPGADVATRQMLNKPPLPFtkglrlgNMPQIRSVVDEELEGVWTGK-- 413
Cdd:cd13585 297 KENQLKLGGAAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPP-------PWPEVYPILSEALQEALLGAlg 369
|
410
....*....|...
gi 491072773 414 KTPQQALDAAVQR 426
Cdd:cd13585 370 KSPEEALKEAAKE 382
|
|
| PBP2_XBP1_like |
cd14749 |
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
28-423 |
9.46e-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: 124.80 E-value: 9.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 28 EIPFWHSMEGELGKE-VDSLADRFNQSHSDVKIVPVYKG--NYEQSLAAGIAAyrsGKAPAILQVYEVG-TATMMASKAI 103
Cdd:cd14749 1 TITYWQYFTGDTKKKyMDELIADFEKENPNIKVKVVVFPydNYKTKLKTAVAA---GEGPDVFNLWPGGwLAEFVKAGLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 104 KPVYEVFKEAGinfDESVFVPTVAGYYTDNksGHLLSQPFNSSTPVLYYNKDAFKKAGlnPDQPPKTWQELAADTAKLRE 183
Cdd:cd14749 78 LPLTDYLDPNG---VDKRFLPGLADAVTFN--GKVYGIPFAARALALFYNKDLFEEAG--GVKPPKTWDELIEAAKKDKF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 184 AGMK-CGYASGWqgwiqlenFSAWHGVPFASENNGFGGT------SAKLEFNQPLQVKHIALLEAMNKKGDFTY-FGRKD 255
Cdd:cd14749 151 KAKGqTGFGLLL--------GAQGGHWYFQYLVRQAGGGplsddgSGKATFNDPAFVQALQKLQDLVKAGAFQEgFEGID 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 256 --ESTEKFYNGDCAITTASSGSLADIK-HYAKFNYGVGMMPydaDAKNAPQNAIIGGASLWVMNGKDAATYKGVAEFLQY 332
Cdd:cd14749 223 ydDAGQAFAQGKAAMNIGGSWDLGAIKaGEPGGKIGVFPFP---TVGKGAQTSTIGGSDWAIAISANGKKKEAAVKFLKY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 333 LAQPEIAAEWHQKTGYLPI-----TTAAYDLTKQQGFYDKNPGADVATrqmlnkPPLPFTKglrlgnmPQIRSVVDEELE 407
Cdd:cd14749 300 LTSPEVMKQYLEDVGLLPAkevvaKDEDPDPVAILGPFADVLNAAGST------PFLDEYW-------PAAAQVHKDAVQ 366
|
410
....*....|....*.
gi 491072773 408 GVWTGKKTPQQALDAA 423
Cdd:cd14749 367 KLLTGKIDPEQVVKQA 382
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
10-426 |
1.78e-30 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 121.60 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 10 TLCVALTLA----------VSAQALAATEIPFWHSmEGElGKEVDSLADRFNQSHS-DVKIVPVYKGNYEQSLAAGIAAy 78
Cdd:COG2182 12 ALALALALAacgsgssssgSSSAAGAGGTLTVWVD-DDE-AEALEEAAAAFEEEPGiKVKVVEVPWDDLREKLTTAAPA- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 79 rsGKAPAILQVYEVGTATMMASKAIKPVYEVFKeaginfDESVFVPTVAGYYTDNksGHLLSQPFNSSTPVLYYNKDAFk 158
Cdd:COG2182 89 --GKGPDVFVGAHDWLGELAEAGLLAPLDDDLA------DKDDFLPAALDAVTYD--GKLYGVPYAVETLALYYNKDLV- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 159 kaglnPDQPPKTWQELAADTAKLREAGMKCgyasgwqgwIQLENFSAWHGVPFAsenNGFGGT--------SAKLEFNQP 230
Cdd:COG2182 158 -----KAEPPKTWDELIAAAKKLTAAGKYG---------LAYDAGDAYYFYPFL---AAFGGYlfgkdgddPKDVGLNSP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 231 LQVKHIALLEAMNKKG----DFTYfgrkDESTEKFYNGDCAITTASSGSLADIKHYAKFNYGVGMMPYDADAKNAPqnAI 306
Cdd:COG2182 221 GAVAALEYLKDLIKDGvlpaDADY----DAADALFAEGKAAMIINGPWAAADLKKALGIDYGVAPLPTLAGGKPAK--PF 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 307 IGGASLWVMNG---KDAATykgvaEFLQYLAQPEIAAEWHQKTGYLPITTAAYDLTKQQgfydKNPGADVATRQMLNKPP 383
Cdd:COG2182 295 VGVKGFGVSAYsknKEAAQ-----EFAEYLTSPEAQKALFEATGRIPANKAAAEDAEVK----ADPLIAAFAEQAEYAVP 365
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 491072773 384 LPFTKglrlgNMPQIRSVVDEELEGVWTGKKTPQQALDAAVQR 426
Cdd:COG2182 366 MPNIP-----EMGAVWTPLGTALQAIASGKADPAEALDAAQKQ 403
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
31-431 |
1.18e-29 |
|
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: 118.95 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 31 FWHSMEGELGKEVDSLADRFNQSHSDVKIVPVYK--GNYEQSLAAGIAayrSGKAPAILQVYEVGTATMMASKAIKPVYE 108
Cdd:cd14747 4 VWAMGNSAEAELLKELADEFEKENPGIEVKVQVLpwGDAHTKITTAAA---SGDGPDVVQLGNTWVAEFAAMGALEDLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 109 VFKEAGINFDesVFVPTVAGYYTDNKsghLLSQPFNSSTPVLYYNKDAFKKAGlnPDQPPKTWQELAADTAKLREAGMKc 188
Cdd:cd14747 81 YLEDLGGDKD--LFPGLVDTGTVDGK---YYGVPWYADTRALFYRTDLLKKAG--GDEAPKTWDELEAAAKKIKADGPD- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 189 GYASGWQGwiqleNFSAWHGV-PFASENngfGGTSA-----KLEFNQPLQVKHIALLEAMNKKGDFTYFGRKDES--TEK 260
Cdd:cd14747 153 VSGFAIPG-----KNDVWHNAlPFVWGA---GGDLAtkdkwKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSAdvEQA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 261 FYNGDCAITTASSGSLADIKHY---AKFNYGVGMMPyDADAKNAPqnAIIGGASLWVMNG---KDAAtykgvAEFLQYLA 334
Cdd:cd14747 225 FANGKVAMIISGPWEIGAIREAgpdLAGKWGVAPLP-GGPGGGSP--SFAGGSNLAVFKGsknKDLA-----WKFIEFLS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 335 QPEIAAEWHQKTGYLPITTAAYDLTKQQgfydKNPGADVATRQMLNKPPLPFTKGLrlgnmPQIRSVVDEELEGVWTG-K 413
Cdd:cd14747 297 SPENQAAYAKATGMLPANTSAWDDPSLA----NDPLLAVFAEQLKTGKATPATPEW-----GEIEAELVLVLEEVWIGvG 367
|
410
....*....|....*...
gi 491072773 414 KTPQQALDAAVQRGDVLL 431
Cdd:cd14747 368 ADVEDALDKAAAEINEIL 385
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
46-357 |
9.75e-25 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 102.87 E-value: 9.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 46 LADRFNQSHsDVKIVPVYkGNYEQSLAAGIAAYRSGKAPAILQVYEVG--TATMMASKAIKPVYEVfkeaginfDESVFV 123
Cdd:pfam13416 2 LAKAFEKKT-GVTVEVEP-QASNDLQAKLLAAAAAGNAPDLDVVWIAAdqLATLAEAGLLADLSDV--------DNLDDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 124 PTVAGYYTDNksGHLLSQPFNSSTP-VLYYNKDAFKKAGlnpdQPPKTWQELAADTAKLREAGMKCGYASGWQGWIQLEn 202
Cdd:pfam13416 72 PDALDAAGYD--GKLYGVPYAASTPtVLYYNKDLLKKAG----EDPKTWDELLAAAAKLKGKTGLTDPATGWLLWALLA- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 203 fsawHGVPFASENNGFGGTsaklefnqplqVKHIALLEAMNKKGDFtyFGRKDESTEKFYNGDCAITTASSGSLADIKHy 282
Cdd:pfam13416 145 ----DGVDLTDDGKGVEAL-----------DEALAYLKKLKDNGKV--YNTGADAVQLFANGEVAMTVNGTWAAAAAKK- 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491072773 283 AKFNYGVGMmpydadaknAPQNAIIGGASLWVMNGKDAATYkGVAEFLQYLAQPEIAAEWHQKTGYLPITTAAYD 357
Cdd:pfam13416 207 AGKKLGAVV---------PKDGSFLGGKGLVVPAGAKDPRL-AALDFIKFLTSPENQAALAEDTGYIPANKSAAL 271
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
46-340 |
7.55e-22 |
|
Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.
Pssm-ID: 460248 [Multi-domain] Cd Length: 294 Bit Score: 95.18 E-value: 7.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 46 LADRFNQSHSDVKIVPVYK--GNYEQSLAAGIAAyrSGKAPAILQVYEVGTATMMASKAIKPVYEVFKEaginfdesvfv 123
Cdd:pfam01547 13 LVKEFEKEHPGIKVEVESVgsGSLAQKLTTAIAA--GDGPADVFASDNDWIAELAKAGLLLPLDDYVAN----------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 124 ptvagyYTDNKSGHLLSQPFNSSTPVLYYNKDAFKKAGLNpdqPPKTWQELAADTAKLREAG----MKCGYASGWQGWIQ 199
Cdd:pfam01547 80 ------YLVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLD---PPKTWDELLEAAKKLKEKGkspgGAGGGDASGTLGYF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 200 LENFSAWHGVPFASENNGFGGTSAKLEFNQPLQVKHIALLEAMNKKGDFTYFGRKDESTEKFYNGDCAITTASSGS---- 275
Cdd:pfam01547 151 TLALLASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGPWAalaa 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491072773 276 --------LADIKHYAKFNYGVGMMPYDADAKNAPQNAIIggaslwvmnGKDAATYKGVAEFLQYLAQPEIAA 340
Cdd:pfam01547 231 nkvklkvaFAAPAPDPKGDVGYAPLPAGKGGKGGGYGLAI---------PKGSKNKEAAKKFLDFLTSPEAQA 294
|
|
| PBP2_Maltose_binding_like |
cd13586 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
28-426 |
1.41e-19 |
|
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: 89.66 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 28 EIPFWHSMEGELgKEVDSLADRFNQSHsDVKIVPVYKGNyEQSLAAGIAAYRSGKAPAILQVYEVGTATMMASKAIKPVY 107
Cdd:cd13586 1 TITVWTDEDGEL-EYLKELAEEFEKKY-GIKVEVVYVDS-GDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 108 EVFKEAgiNFDESVFVPTVagyyTDNksGHLLSQPFNSSTPVLYYNKDAFKkaglnpdQPPKTWQELAADTAKL-REAGM 186
Cdd:cd13586 78 EYLAVK--IKNLPVALAAV----TYN--GKLYGVPVSVETIALFYNKDLVP-------EPPKTWEELIALAKKFnDKAGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 187 KCGYASGWQgwiqlenfSAWHGVPFASENNG--FG---GTSAKLEFNQPLQVKHIALLEAMNKKGDFTYFGRKDESTEK- 260
Cdd:cd13586 143 KYGFAYDQT--------NPYFSYPFLAAFGGyvFGengGDPTDIGLNNEGAVKGLKFIKDLKKKYKVLPPDLDYDIADAl 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 261 FYNGDCAITTASSGSLADIKHyAKFNYGVGMMPydaDAKNAPQNAIIGGASLWVMNGKdAATYKGVAEFLQYLAQPEIAA 340
Cdd:cd13586 215 FKEGKAAMIINGPWDLADYKD-AGINFGVAPLP---TLPGGKQAAPFVGVQGAFVSAY-SKNKEAAVEFAEYLTSDEAQL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 341 EWHQKTGYLPITTAAYDLTKQQgfydKNPGADVATRQMLNKPPLPftkglrlgNMPQIRSV---VDEELEGVWTGKKTPQ 417
Cdd:cd13586 290 LLFEKTGRIPALKDALNDAAVK----NDPLVKAFAEQAQYGVPMP--------NIPEMAAVwdaMGNALNLVASGKATPE 357
|
....*....
gi 491072773 418 QALDAAVQR 426
Cdd:cd13586 358 EAAKDAVAA 366
|
|
| PBP2_ABC_oligosaccharides |
cd13522 |
The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
29-426 |
1.18e-18 |
|
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: 87.08 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 29 IPFWHSMEGELGKEVDSLADRFNQSHSDVKIVPVYKGNYEQSLAAgIAAYRSGKAPAILqvyevgtatMMASKAIKPvye 108
Cdd:cd13522 2 ITVWHQYDTGENQAVNELIAKFEKAYPGITVEVTYQDTEARRQFF-STAAAGGKGPDVV---------FGPSDSLGP--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 109 vFKEAGINFDESVFVP---TVAGYYTDNKS--GHLLSQPFNSSTPVLYYNKDAFkkaglnPDQPPKTWQELAADTAKLRE 183
Cdd:cd13522 69 -FAAAGLLAPLDEYVSksgKYAPNTIAAMKlnGKLYGVPVSVGAHLMYYNKKLV------PKNPPKTWQELIALAQGLKA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 184 AGMKC-----GYASGWQGWIQlenfsAWHGVPFASENNGFggtsaKLEFNQPLQVKHIALLEAMNKKGDFTyFGRKDEST 258
Cdd:cd13522 142 KNVWGlvynqNEPYFFAAWIG-----GFGGQVFKANNGKN-----NPTLDTPGAVEALQFLVDLKSKYKIM-PPETDYSI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 259 EK--FYNGDCAITTASSGSLADIKHYAKFNYGVGMMPydADAKNAPQNAIIGGASlWVMNgKDAATYKGVAEFLQYLAQP 336
Cdd:cd13522 211 ADalFKAGKAAMIINGPWDLGDYRQALKINLGVAPLP--TFSGTKHAAPFVGGKG-FGIN-KESQNKAAAVEFVKYLTSY 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 337 EIAAEWHQKTGYLPITTAAYDLTKQQgfydKNPGADVATRQMLNKPPLPftkglrlgNMPQIRSVVD---EELEGVWTGK 413
Cdd:cd13522 287 QAQLVLFDDAGDIPANLQAYESPAVQ----NKPAQKASAEQAAYGVPMP--------NIPEMRAVWDafrIAVNSVLAGK 354
|
410
....*....|...
gi 491072773 414 KTPQQALDAAVQR 426
Cdd:cd13522 355 VTPEAAAKDAQQE 367
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
29-423 |
3.50e-18 |
|
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold; This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270454 [Multi-domain] Cd Length: 376 Bit Score: 85.51 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 29 IPFWHSMEGELGKEVDSLADRFNQSHSDVKiVPVYKGNYEQSLAAGIAAYRSGKAPAILQVYEVGTATMMASKAIKPV-- 106
Cdd:cd14751 2 ITFWHTSSDEEKVLYEKLIPAFEKEYPKIK-VKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 107 YEVFKEAGINFDEsvfvPTVAGYYtdnkSGHLLSQPFNSSTPVLYYNKDAFKKAGLnpdQPPKTWQELAADTAKLREAGM 186
Cdd:cd14751 81 TPAFDDIVDYLPG----PMETNRY----NGHYYGVPQVTNTLALFYNKRLLEEAGT---EVPKTMDELVAAAKAIKKKKG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 187 KCGYAsgwqgwiqLENFSAWHGVPFAsenNGFGGT-----SAKLEFNQPLQVKHI-ALLEAMNKKGDFTY-FGRKDESTE 259
Cdd:cd14751 150 RYGLY--------ISGDGPYWLLPFL---WSFGGDltdekKATGYLNSPESVRALeTIVDLYDEGAITPCaSGGYPNMQD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 260 KFYNGDCAITTASSGSLADIKH----YAKFNYGVGMMPydadAKNAPQNAIIGGASLWVMNG---KDAATykgvaEFLQY 332
Cdd:cd14751 219 GFKSGRYAMIVNGPWAYADILGgkefKDPDNLGIAPVP----AGPGGSGSPVGGEDLVIFKGsknKDAAW-----KFVKF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 333 LAQPEIAAEWHQKTGYLPITTAAYD---LTKQQGFYDKNPGADVATrqmlNKPPLPftkglrlgNMPQIRSVVDEELEGV 409
Cdd:cd14751 290 MSSAEAQALTAAKLGLLPTRTSAYEspeVANNPMVAAFKPALETAV----PRPPIP--------EWGELFEPLTLAFAKV 357
|
410
....*....|....
gi 491072773 410 WTGKKTPQQALDAA 423
Cdd:cd14751 358 LRGEKSPREALDEA 371
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
43-426 |
2.33e-17 |
|
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: 83.50 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 43 VDSLADRFNQSHSDVKIVPVYKGNYEQSLAAGIAAYRSGKAPA--ILQVYEVGTATMMASKAIKPVYEVFKEAGinfDES 120
Cdd:cd14750 16 LKKAIAAFEKKHPDIKVEIEELPASSDDQRQQLVTALAAGSSApdVLGLDVIWIPEFAEAGWLLPLTEYLKEEE---DDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 121 VFVPTVAGYYTDNKsghLLSQPFNSSTPVLYYNKDAFKKAGLnpdQPPKTWQELAAdTAKLREAGMKCGYASGWQGwiql 200
Cdd:cd14750 93 FLPATVEANTYDGK---LYALPWFTDAGLLYYRKDLLEKYGP---EPPKTWDELLE-AAKKRKAGEPGIWGYVFQG---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 201 enfSAWHGVP--FASENNGFGG-----TSAKLEFNQPLQVKHIALLEAMNKKG---DFTYFGRKDESTEKFYNGDCAI-- 268
Cdd:cd14750 162 ---KQYEGLVcnFLELLWSNGGdifddDSGKVTVDSPEALEALQFLRDLIGEGispKGVLTYGEEEARAAFQAGKAAFmr 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 269 --TTASSGSLADIKHYA-KFnyGVGMMPYDADAKNApqnAIIGGaslWVM------NGKDAAtykgvAEFLQYLAQPEIA 339
Cdd:cd14750 239 nwPYAYALLQGPESAVAgKV--GVAPLPAGPGGGSA---STLGG---WNLaisansKHKEAA-----WEFVKFLTSPEVQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 340 AEWHQKTGYLPITTAAYDltkQQGFYDKNPGADVATRQMLN---KPPLPFtkglrlgnMPQIRSVVDEELEGVWTGKKTP 416
Cdd:cd14750 306 KRRAINGGLPPTRRALYD---DPEVLEAYPFLPALLEALENavpRPVTPK--------YPEVSTAIQIALSAALSGQATP 374
|
410
....*....|
gi 491072773 417 QQALDAAVQR 426
Cdd:cd14750 375 EEALKQAQEK 384
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
136-426 |
3.94e-17 |
|
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: 82.53 E-value: 3.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 136 GHLLSQPFNSSTPVLYYNKDAFKKAglnpdqpPKTWQELAADTAKL-REAGMKCGYASGWqgwiqlENFsaWHGVPFASE 214
Cdd:cd13658 98 GKLYGLPAAVETLALYYNKDLVKNA-------PKTFDELEALAKDLtKEKGKQYGFLADA------TNF--YYSYGLLAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 215 NNG--FGGTSAKLEFNQ-PLQVKHIalLEAMNKKGDFTYFGRKDESTEkfynGDCAITTASSGSLA-------DIKHY-- 282
Cdd:cd13658 163 NGGyiFKKNGSDLDINDiGLNSPGA--VKAVKFLKKWYTEGYLPKGMT----GDVIQGLFKEGKAAavidgpwAIQEYqe 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 283 AKFNYGVGMMPYDADAKnaPQNAIIGGASlWVMNgkDAATYKGVA-EFLQYLAQPEIAAEWHQKTGYLPITTAAYDLTKQ 361
Cdd:cd13658 237 AGVNYGVAPLPTLPNGK--PMAPFLGVKG-WYLS--AYSKHKEWAqKFMEFLTSKENLKKRYDETNEIPPRKDVRSDPEI 311
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491072773 362 QgfydKNPGADVATRQMLNKPPLPftkglrlgNMPQIRSV---VDEELEGVWTGKKTPQQALDAAVQR 426
Cdd:cd13658 312 K----NNPLTSAFAKQASRAVPMP--------NIPEMGAVwepANNALFFILSGKKTPKQALNDAVND 367
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
28-426 |
3.93e-14 |
|
The periplasmic binding component of ABC transport system specific for maltodextrin; This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270375 [Multi-domain] Cd Length: 368 Bit Score: 73.57 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 28 EIPFWHSMEGELGKEVDSLADRFNQSHS--DVKIVPVYKGNYEQSLAAGIAayrSGKAPAILQVYEVGTATMMASKAIKP 105
Cdd:cd13657 1 TITIWHALTGAEEDALQQIIDEFEAKYPvpNVKVPFEKKPDLQNKLLTAIP---AGEGPDLFIWAHDWIGQFAEAGLLVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 106 VYEVFKEaginFDESVFVPTV--AGYYtdnkSGHLLSQPFNSSTPVLYYNKDAFkkaglnpDQPPKTWQELAAdTAKLRE 183
Cdd:cd13657 78 ISDYLSE----DDFENYLPTAveAVTY----KGKVYGLPEAYETVALIYNKALV-------DQPPETTDELLA-IMKDHT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 184 AGMKCGYASGWQGwIQLENFSAWHgvpfasenNGFGG-----TSAKLEFNQPLQVKHIALLEAMNKK---GDFTYfgrkD 255
Cdd:cd13657 142 DPAAGSYGLAYQV-SDAYFVSAWI--------FGFGGyyfddETDKPGLDTPETIKGIQFLKDFSWPympSDPSY----N 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 256 ESTEKFYNGDCAITTASSGSLADIKHyAKFNYGVGMMPyDADAKNAPQnAIIGGASLWVMNGKDAATYKGVAEFLQYLAQ 335
Cdd:cd13657 209 TQTSLFNEGKAAMIINGPWFIGGIKA-AGIDLGVAPLP-TVDGTNPPR-PYSGVEGIYVTKYAERKNKEAALDFAKFFTT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 336 PEIAAEWHQKTGYLPITTAAYDLTKQQGfydkNPGADVATRQMLNKPPLPftkglrlgNMPQIRSV---VDEELEGVWTG 412
Cdd:cd13657 286 AEASKILADENGYVPAATNAYDDAEVAA----DPVIAAFKAQAEHGVPMP--------NSPEMASVwgpVTLALAAVYQG 353
|
410
....*....|....
gi 491072773 413 KKTPQQALDAAVQR 426
Cdd:cd13657 354 GQDPQEALAAAQQE 367
|
|
| PBP2_AlgQ_like_4 |
cd13583 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
56-339 |
5.73e-09 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270301 [Multi-domain] Cd Length: 478 Bit Score: 57.75 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 56 DVKIVPVYKGNYEQSLAAGIAayrSGKAPAILQV-YEVGTATMMASKAIKPVyevfkeaginFDESVFVPTVAGYYTDNK 134
Cdd:cd13583 33 KFKRTPIPSSDYETKRSLLIA---SGDAPDIIPVlYPGEENEFVASGALLPI----------SDYLDYMPNYKKYVEKWG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 135 SGHLLS---QP--FNSSTPVL----------YYNKDAFKKAGLnpdQPPKTWQELAADTAKLREA-GMKCGYASGWQ--- 195
Cdd:cd13583 100 LGKELAtgrQSdgKYYSLPGLhedpgvqysfLYRKDIFEKAGI---KIPTTWDEFYAALKKLKEKyPDSYPYSDRWNsna 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 196 -GWIQLENFSAWHGVPFASENngFGGTSAKLEFNqPLQVKHIALLEAMNK---KG--DFTYFGRKDES-TEKFYNGDCAI 268
Cdd:cd13583 177 lLLIAAPAFGTTAGWGFSNYT--YDPDTDKFVYG-ATTDEYKDMLQYFNKlyaEGllDPESFTQTDDQaKAKFLNGKSFV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 269 TTASSGSLADI--KHYAKF--NYGVGMMPYDAdaknAPQNAIIGGASL---WVMNGK--DAATYKGVAEFLQYLAQPEIA 339
Cdd:cd13583 254 ITTNPQTVDELqrNLRAADggNYEVVSITPPA----GPAGKAINGSRLengFMISSKakDSKNFEALLQFLDWLYSDEGQ 329
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
46-176 |
6.00e-04 |
|
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: 41.93 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 46 LADRFNQshsDVKIVPVYKGNYEQSLAAGIAayrSGKAPAILQVYEVGTATMMA-SKAIKPVYEVFKEAGINFDEsvfVP 124
Cdd:cd13580 28 LEEKTNI---DVKVKWVPDSSYDEKLNLALA---SGDLPDIVVVNDPQLSITLVkQGALWDLTDYLDKYYPNLKK---II 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 491072773 125 TVAGYYTDNKSGHLLSQPF---NSSTPVLYYNKDAFKKAGLnpdQPPKTWQELAA 176
Cdd:cd13580 99 EQEGWDSASVDGKIYGIPRkrpLIGRNGLWIRKDWLDKLGL---EVPKTLDELYE 150
|
|
| PBP2_polyamine_1 |
cd13588 |
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
255-357 |
7.40e-03 |
|
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: 38.05 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491072773 255 DESTEKFYNGDCAITTASSGSLADIKhyakfnygvgmmpydadAKNAPQNAII--GGASLWV---MNGKDAATYKGVAEF 329
Cdd:cd13588 189 AELVQLFANGEVVAATAWSGQVNALQ-----------------KAGKPVAYVIpkEGATGWVdtwMILKDAKNPDCAYKW 251
|
90 100
....*....|....*....|....*...
gi 491072773 330 LQYLAQPEIAAEWHQKTGYLPITTAAYD 357
Cdd:cd13588 252 LNYMLSPKVQAAVAEWTGYAPSNPEACA 279
|
|
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