|
Name |
Accession |
Description |
Interval |
E-value |
| proX |
PRK11119 |
proline/glycine betaine ABC transporter substrate-binding protein ProX; |
1-331 |
0e+00 |
|
proline/glycine betaine ABC transporter substrate-binding protein ProX;
Pssm-ID: 236852 [Multi-domain] Cd Length: 331 Bit Score: 676.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 1 MRHNVLFATAFATLVSTSTFAADLPGKGITVQPVQSTISEESFQTLIVSRALEKLGYTVNTPSEVDYNVGYTSIASGDAT 80
Cdd:PRK11119 1 MRKTVLLALALATLASTQAFAADLPGKGITVQPAQSTIAEETFQTLLVSRALEKLGYDVNKPKEVDYNVFYTSIANGDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 81 FTAVNWQPLHDDMYAAAGGDKKFYREGTFVTGAAQGYLIDKKTADKYHITNIEQLKDPKIAKLFDTNGDGKADMMGCSPG 160
Cdd:PRK11119 81 FTAVNWFPLHDDMYEAAGGDKKFYREGVYVGGAAQGYLIDKKTADKYNITNIAQLKDPKIAKLFDTNGDGKADLTGCNPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 161 WGCEAVINHQNKAYDLAKTVDVSHGNYSAMMADTIARFKEGKPVIYYTWTPYWVSDVLKPGKDVVWLQVPFSSLPGEQKD 240
Cdd:PRK11119 161 WGCEAVINHQLKAYGLEDTVTHNQGNYAALMADTIARYKEGKPVLYYTWTPYWVSDVLKPGKDVVWLQVPFSSLPGDQKN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 241 IDTKLPNGMNYGFPVNTMHIVANKAWSEKNPAAAKLFSVMKLPLADINAQNAMMHAGKSSEADVKGHVDGWIKAHEQQFD 320
Cdd:PRK11119 241 ADTKLPNGKNYGFPVNTMHIVANKAFAEKNPAAAKLFEIMKLPLADINAQNLRMHEGESSEADIERHVDGWIKAHQAQFD 320
|
330
....*....|.
gi 556489957 321 GWVKEALAAQK 331
Cdd:PRK11119 321 GWVKEARAAAK 331
|
|
| PBP2_EcProx_like |
cd13638 |
Substrate binding domain of Escherichia coli betaine transport system-like; the type 2 ... |
25-323 |
0e+00 |
|
Substrate binding domain of Escherichia coli betaine transport system-like; the type 2 periplasmic binding protein fold; This group includes the periplasmic substrate-binding protein ProX. ProX from the Escherichia coli ATP-binding cassette transport system ProU binds the compatible solutes glycine betaine and proline betaine with high affinity and specificity. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. The ProX belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270356 [Multi-domain] Cd Length: 299 Bit Score: 519.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 25 PGKGITVQPVQSTISEESFQTLIVSRALEKLGYTVNTPSEVDYNVGYTSIASGDATFTAVNWQPLHDDMYAAAGGDKKFY 104
Cdd:cd13638 1 PGKGVTVRPAKSTWAEEYFQTEIVSKGLEKLGYKVKEPKELDYPLFYVAVANGDADFWADHWFPLHDPFFEKAGGDAKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 105 REGTFVTGAAQGYLIDKKTADKYHITNIEQLKDPKIAKLFDTNGDGKADMMGCSPGWGCEAVINHQNKAYDLAKTVDVSH 184
Cdd:cd13638 81 RVGVIIGGGLQGYLIDKKTADAYNITSLDQLKDPKIAKLFDSDGDGKADLTGCNPGWGCEKVIEHQLDAYGLRDTVNHNQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 185 GNYSAMMADTIARFKEGKPVIYYTWTPYWVSDVLKPGKDVVWLQVPFSSLPGEQKDIDTKLPNGMNYGFPVNTMHIVANK 264
Cdd:cd13638 161 GSYSALMADAIARYKQGKPVLYYTWTPNWVSNVLVPGKDVVWLEVPFTALPGDQAGATTGVANGKNLGFPVNDIRIVANK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 556489957 265 AWSEKNPAAAKLFSVMKLPLADINAQNAMMHAGKSSEADVKGHVDGWIKAHEQQFDGWV 323
Cdd:cd13638 241 AFLEANPAAKKLFELVQIPLADISAQNLLMNQGEGSPEDIRRHADEWIAANQDTFDGWI 299
|
|
| ProX |
COG2113 |
ABC-type proline/glycine betaine transport system, periplasmic component [Amino acid transport ... |
5-328 |
1.61e-97 |
|
ABC-type proline/glycine betaine transport system, periplasmic component [Amino acid transport and metabolism];
Pssm-ID: 441716 [Multi-domain] Cd Length: 297 Bit Score: 290.21 E-value: 1.61e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 5 VLFATAFATLVSTSTFAADLPGKGITVQPVQSTISEESFQTLIVSRALEKLGYTVNTpSEVDYNVGYTSIASGDATFTAV 84
Cdd:COG2113 7 LLLAAALALALAGCAAAAAAPGSCKTVTIADVGWTSATATTAVAKQILEELGYEVEL-VELDVPVTYQGLANGDIDVFLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 85 NWQPLHDDMYAAAGGDKKFYREGTFVTGAAQGYLIDKKTADkYHITNIEQLKdpKIAKLFDTngdgkaDMMGCSPGWGCE 164
Cdd:COG2113 86 AWLPTTHADYDEAYGDGKVEDLGTNYEGAKQGLAVPKYVAE-PGIKSIADLK--KYADLFDG------KIYGIEPGWGCN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 165 AVINHQNKAYDLAKtVDVSHGNYSAMMADTIARFKEGKPVIYYTWTPYWVSDVLkpgkDVVWLQVPfsslpgeqkdidtk 244
Cdd:COG2113 157 RVIEEAIKAYGLDD-FELVEGSEAAMLAALARAYKRGEPIVFYGWTPHWMFAKY----DLKYLEDP-------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 245 lPNGMNYGFPVNTMHIVANKAWSEKNPAAAKLFSVMKLPLADINAQNAMMHAGKSSEADvkgHVDGWIKAHEQQFDGWVK 324
Cdd:COG2113 218 -KGAFGPNFPAETVHTVARKGFAEDNPEAAKLLENFKFTLEDINALMAAIENDGADPEE---AAKEWLKANPDVVDGWLP 293
|
....
gi 556489957 325 EALA 328
Cdd:COG2113 294 GVTA 297
|
|
| OpuAC |
pfam04069 |
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity ... |
30-314 |
1.96e-51 |
|
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity multicomponent binding-protein-dependent transport system involved in bacterial osmoregulation. This domain is often fused to the permease component of the transporter complex. Family members are often integral membrane proteins or predicted to be attached to the membrane by a lipid anchor. Glycine betaine is involved in protection from high osmolarity environments for example in Bacillus subtilis. The family member OpuBC is closely related, and involved in choline transport. Choline is necessary for the biosynthesis of glycine betaine. L-carnitine is important for osmoregulation in Listeria monocytogenes. Family also contains proteins binding l-proline (ProX), histidine (HisX) and taurine (TauA).
Pssm-ID: 397954 [Multi-domain] Cd Length: 257 Bit Score: 170.97 E-value: 1.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 30 TVQPVQSTISEESFQTLIVSRALEKLGYTVNTPSEVDYNVGYTSIASGDATFTAVNWQP-LHDDMYAAAGGDKKFYREGT 108
Cdd:pfam04069 2 TIVIGSKNWTEQEILANIAAQLLEALGYVVELVGLGSSAVLFAALASGDIDLYPEEWTGtTYEAYKKAVEEKLGLLVLGP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 109 FVTGAAQGYLIDKKTADKYHITNIEQLKDPKIaklfDTNGDGKADMMGCSPGWGCEAVINHQNKAYDLAKTVDVShGNYS 188
Cdd:pfam04069 82 LGAGNTYGLAVPKYVAEKPGIKSISDLAKPAD----DLELGFKGEFIGRPDGWGCMRSTEGLLKAYGLDKYELVE-GSEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 189 AMMADTIARFKEGKPVIYYTWTPYWVSDVLkpgkDVVWLQvpfsslpgeqkdiDTKlpngmNYGFPVNTMHIVANKAWSE 268
Cdd:pfam04069 157 AMDALIYAAYKRGEPDVVYAWTPDWMIKKY----DLVVLE-------------DPK-----GLFPPAYNVVPVVRKGFAE 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 556489957 269 KNPAAAKLFSVMKLPLADINAQNAMMHAGKSSEADVkghVDGWIKA 314
Cdd:pfam04069 215 KHPEVAAFLNKLSLDTEDLNELNAQVDVEGKDPEEV---AKDWLAE 257
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| proX |
PRK11119 |
proline/glycine betaine ABC transporter substrate-binding protein ProX; |
1-331 |
0e+00 |
|
proline/glycine betaine ABC transporter substrate-binding protein ProX;
Pssm-ID: 236852 [Multi-domain] Cd Length: 331 Bit Score: 676.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 1 MRHNVLFATAFATLVSTSTFAADLPGKGITVQPVQSTISEESFQTLIVSRALEKLGYTVNTPSEVDYNVGYTSIASGDAT 80
Cdd:PRK11119 1 MRKTVLLALALATLASTQAFAADLPGKGITVQPAQSTIAEETFQTLLVSRALEKLGYDVNKPKEVDYNVFYTSIANGDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 81 FTAVNWQPLHDDMYAAAGGDKKFYREGTFVTGAAQGYLIDKKTADKYHITNIEQLKDPKIAKLFDTNGDGKADMMGCSPG 160
Cdd:PRK11119 81 FTAVNWFPLHDDMYEAAGGDKKFYREGVYVGGAAQGYLIDKKTADKYNITNIAQLKDPKIAKLFDTNGDGKADLTGCNPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 161 WGCEAVINHQNKAYDLAKTVDVSHGNYSAMMADTIARFKEGKPVIYYTWTPYWVSDVLKPGKDVVWLQVPFSSLPGEQKD 240
Cdd:PRK11119 161 WGCEAVINHQLKAYGLEDTVTHNQGNYAALMADTIARYKEGKPVLYYTWTPYWVSDVLKPGKDVVWLQVPFSSLPGDQKN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 241 IDTKLPNGMNYGFPVNTMHIVANKAWSEKNPAAAKLFSVMKLPLADINAQNAMMHAGKSSEADVKGHVDGWIKAHEQQFD 320
Cdd:PRK11119 241 ADTKLPNGKNYGFPVNTMHIVANKAFAEKNPAAAKLFEIMKLPLADINAQNLRMHEGESSEADIERHVDGWIKAHQAQFD 320
|
330
....*....|.
gi 556489957 321 GWVKEALAAQK 331
Cdd:PRK11119 321 GWVKEARAAAK 331
|
|
| PBP2_EcProx_like |
cd13638 |
Substrate binding domain of Escherichia coli betaine transport system-like; the type 2 ... |
25-323 |
0e+00 |
|
Substrate binding domain of Escherichia coli betaine transport system-like; the type 2 periplasmic binding protein fold; This group includes the periplasmic substrate-binding protein ProX. ProX from the Escherichia coli ATP-binding cassette transport system ProU binds the compatible solutes glycine betaine and proline betaine with high affinity and specificity. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. The ProX belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270356 [Multi-domain] Cd Length: 299 Bit Score: 519.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 25 PGKGITVQPVQSTISEESFQTLIVSRALEKLGYTVNTPSEVDYNVGYTSIASGDATFTAVNWQPLHDDMYAAAGGDKKFY 104
Cdd:cd13638 1 PGKGVTVRPAKSTWAEEYFQTEIVSKGLEKLGYKVKEPKELDYPLFYVAVANGDADFWADHWFPLHDPFFEKAGGDAKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 105 REGTFVTGAAQGYLIDKKTADKYHITNIEQLKDPKIAKLFDTNGDGKADMMGCSPGWGCEAVINHQNKAYDLAKTVDVSH 184
Cdd:cd13638 81 RVGVIIGGGLQGYLIDKKTADAYNITSLDQLKDPKIAKLFDSDGDGKADLTGCNPGWGCEKVIEHQLDAYGLRDTVNHNQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 185 GNYSAMMADTIARFKEGKPVIYYTWTPYWVSDVLKPGKDVVWLQVPFSSLPGEQKDIDTKLPNGMNYGFPVNTMHIVANK 264
Cdd:cd13638 161 GSYSALMADAIARYKQGKPVLYYTWTPNWVSNVLVPGKDVVWLEVPFTALPGDQAGATTGVANGKNLGFPVNDIRIVANK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 556489957 265 AWSEKNPAAAKLFSVMKLPLADINAQNAMMHAGKSSEADVKGHVDGWIKAHEQQFDGWV 323
Cdd:cd13638 241 AFLEANPAAKKLFELVQIPLADISAQNLLMNQGEGSPEDIRRHADEWIAANQDTFDGWI 299
|
|
| PBP2_Osm_BCP_like |
cd13535 |
Substrate binding domain of osmoregulatory ABC-type glycine betaine/choline/L-proline ... |
30-314 |
2.61e-105 |
|
Substrate binding domain of osmoregulatory ABC-type glycine betaine/choline/L-proline transport system and related proteins; the type 2 periplasmic binding protein fold; This family is part of a high affinity multicomponent binding-protein-dependent ATP-binding cassette transport system specific to certain quaternary ammonium compounds for osmoregulation. The periplasmic substrate-binding domain, which is often fused to the permease component of the ATP-binding cassette transporter complex, is involved in uptake of osmoprotectants (also termed compatible solutes) such as betaines, choline, and L-proline. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. This domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270253 [Multi-domain] Cd Length: 277 Bit Score: 309.48 E-value: 2.61e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 30 TVQPVQSTISEESFQTLIVSRALEKLGYTVNTPSEvDYNVGYTSIASGDATFTAVNWQPLHDDMYAAAGGDKKFYREGTF 109
Cdd:cd13535 1 TVKLAVPSWTGETATTHVLGTILEALGYTVDYVSL-NNAVTFQSLANGDIDITVENWLPNHEDFYAKYVEGKKVVVLGQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 110 VTGAAQGYLIDKKTADKYHITNIEQLKDPKIAKLFDTNGDGKADMMGCSPGWGCEAVINHQNKAYDLAKTVDVSHGNYSA 189
Cdd:cd13535 80 LYGAKQGFAVPKKVAELNPITNIADLGRPDAAALADSEGNGKGRLTGCPPGWGCEGAIEVKLEDYGLLKFVEVVPGSEGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 190 MMADTIARFKEGKPVIYYTWTPYWVsdvlKPGKDVVWLQVPFSSLPGEQKDIDTKLPNGMNYGFPVNTMHIVANKAWSEK 269
Cdd:cd13535 160 MTAAIKSAIKQGEPIFFYGWSPHWV----WFKFDVVYLSEPTYDEACYTMVQPWNEKSSVGCKFASSTVHIAVNKGLADE 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 556489957 270 NPAAAKLFSVMKLPLADINAQNAMMHAGKsseADVKGHVDGWIKA 314
Cdd:cd13535 236 NPAAAEILENFSLTVDDVNAFMGEISDNG---GDPEEAAAEWLKA 277
|
|
| ProX |
COG2113 |
ABC-type proline/glycine betaine transport system, periplasmic component [Amino acid transport ... |
5-328 |
1.61e-97 |
|
ABC-type proline/glycine betaine transport system, periplasmic component [Amino acid transport and metabolism];
Pssm-ID: 441716 [Multi-domain] Cd Length: 297 Bit Score: 290.21 E-value: 1.61e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 5 VLFATAFATLVSTSTFAADLPGKGITVQPVQSTISEESFQTLIVSRALEKLGYTVNTpSEVDYNVGYTSIASGDATFTAV 84
Cdd:COG2113 7 LLLAAALALALAGCAAAAAAPGSCKTVTIADVGWTSATATTAVAKQILEELGYEVEL-VELDVPVTYQGLANGDIDVFLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 85 NWQPLHDDMYAAAGGDKKFYREGTFVTGAAQGYLIDKKTADkYHITNIEQLKdpKIAKLFDTngdgkaDMMGCSPGWGCE 164
Cdd:COG2113 86 AWLPTTHADYDEAYGDGKVEDLGTNYEGAKQGLAVPKYVAE-PGIKSIADLK--KYADLFDG------KIYGIEPGWGCN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 165 AVINHQNKAYDLAKtVDVSHGNYSAMMADTIARFKEGKPVIYYTWTPYWVSDVLkpgkDVVWLQVPfsslpgeqkdidtk 244
Cdd:COG2113 157 RVIEEAIKAYGLDD-FELVEGSEAAMLAALARAYKRGEPIVFYGWTPHWMFAKY----DLKYLEDP-------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 245 lPNGMNYGFPVNTMHIVANKAWSEKNPAAAKLFSVMKLPLADINAQNAMMHAGKSSEADvkgHVDGWIKAHEQQFDGWVK 324
Cdd:COG2113 218 -KGAFGPNFPAETVHTVARKGFAEDNPEAAKLLENFKFTLEDINALMAAIENDGADPEE---AAKEWLKANPDVVDGWLP 293
|
....
gi 556489957 325 EALA 328
Cdd:COG2113 294 GVTA 297
|
|
| OpuAC |
pfam04069 |
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity ... |
30-314 |
1.96e-51 |
|
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity multicomponent binding-protein-dependent transport system involved in bacterial osmoregulation. This domain is often fused to the permease component of the transporter complex. Family members are often integral membrane proteins or predicted to be attached to the membrane by a lipid anchor. Glycine betaine is involved in protection from high osmolarity environments for example in Bacillus subtilis. The family member OpuBC is closely related, and involved in choline transport. Choline is necessary for the biosynthesis of glycine betaine. L-carnitine is important for osmoregulation in Listeria monocytogenes. Family also contains proteins binding l-proline (ProX), histidine (HisX) and taurine (TauA).
Pssm-ID: 397954 [Multi-domain] Cd Length: 257 Bit Score: 170.97 E-value: 1.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 30 TVQPVQSTISEESFQTLIVSRALEKLGYTVNTPSEVDYNVGYTSIASGDATFTAVNWQP-LHDDMYAAAGGDKKFYREGT 108
Cdd:pfam04069 2 TIVIGSKNWTEQEILANIAAQLLEALGYVVELVGLGSSAVLFAALASGDIDLYPEEWTGtTYEAYKKAVEEKLGLLVLGP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 109 FVTGAAQGYLIDKKTADKYHITNIEQLKDPKIaklfDTNGDGKADMMGCSPGWGCEAVINHQNKAYDLAKTVDVShGNYS 188
Cdd:pfam04069 82 LGAGNTYGLAVPKYVAEKPGIKSISDLAKPAD----DLELGFKGEFIGRPDGWGCMRSTEGLLKAYGLDKYELVE-GSEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 189 AMMADTIARFKEGKPVIYYTWTPYWVSDVLkpgkDVVWLQvpfsslpgeqkdiDTKlpngmNYGFPVNTMHIVANKAWSE 268
Cdd:pfam04069 157 AMDALIYAAYKRGEPDVVYAWTPDWMIKKY----DLVVLE-------------DPK-----GLFPPAYNVVPVVRKGFAE 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 556489957 269 KNPAAAKLFSVMKLPLADINAQNAMMHAGKSSEADVkghVDGWIKA 314
Cdd:pfam04069 215 KHPEVAAFLNKLSLDTEDLNELNAQVDVEGKDPEEV---AKDWLAE 257
|
|
| PBP2_BCP_1 |
cd13642 |
Substrate-binding domain of osmoregulatory ABC-type glycine betaine/choline/L-proline ... |
85-322 |
2.63e-22 |
|
Substrate-binding domain of osmoregulatory ABC-type glycine betaine/choline/L-proline transport system-like; the type 2 periplasmic-binding protein fold; This subfamily is part of a high affinity multicomponent binding-protein-dependent transport system specific to certain quaternary ammonium compounds for osmoregulation. The periplasmic substrate-binding domain, which is often fused to the permease component of the ATP-binding cassette transporter complex, is involved in uptake of osmoprotectants (also termed compatible solutes) such as glycine betaine, proline betaine, choline, and carnitine. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. This domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270360 [Multi-domain] Cd Length: 292 Bit Score: 94.76 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 85 NWQPLHDDmYAAAGGDKKFYREGTfvtGAAQGYLIDKKTADKYHITNIEQLKDPKiAKLFDTNGDGKADMMGCSPGWGCE 164
Cdd:cd13642 62 NQQALWDK-YVTGGGTVALNPNPY---EGTQGICVPAATADKYGIKSDLDLTAPE-AALFDSDGDGKGEIWIGAPGWAST 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 165 AVINHQNKAYDLAKTVDVSHGNYSAMMADTIARFKEGKPVIYYTWTPYWVSDVLkpgkDVVWLQVPFSSLPGEQKDIDTK 244
Cdd:cd13642 137 NIEQIKAKSYGYDETWELEEMSEAVFYAQLDAAYARGEPIVFYCYTPHWVFALY----DLVQLEEPAYDAAKWTTVLPTE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 245 LPNGMNYG-----FPVNTMHIVANKAWSEKNPAAAKLFSVMKLPLADInaqNAMMHAGKSSEADVKGHVDGWIKAHEQQF 319
Cdd:cd13642 213 DPDWLEKSnaacaWADASVHIAYSASLEERAPEVAAFLSRIRLTPEEV---NAMSYAVDVDGKDPAAVAREWVAANADRV 289
|
...
gi 556489957 320 DGW 322
Cdd:cd13642 290 DEW 292
|
|
| PBP2_BCP_2 |
cd13643 |
Substrate-binding domain of osmoregulatory ABC-type glycine betaine/choline/L-proline ... |
47-322 |
8.10e-21 |
|
Substrate-binding domain of osmoregulatory ABC-type glycine betaine/choline/L-proline transport system-like; the type 2 periplasmic-binding protein fold; This subfamily is part of a high affinity multicomponent binding-protein-dependent transport system specific to certain quaternary ammonium compounds for osmoregulation. The periplasmic substrate-binding domain, which is often fused to the permease component of the ATP-binding cassette transporter complex, is involved in uptake of osmoprotectants (also termed compatible solutes) such as glycine betaine, proline betaine, choline, and carnitine. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. This domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270361 [Multi-domain] Cd Length: 283 Bit Score: 90.43 E-value: 8.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 47 IVSRALEKLGYTVNTPsEVDYNVGYTSIASGDATFTAVNWQPLHDDMYAAAGGDKKFYREGTFVTGAAQGYLIDKKTADK 126
Cdd:cd13643 18 VAGYLLEKEGYKVEYV-TADEQAQWEALAAGDVDAQLEVWESSMGDKYEKALAAGSVVDLGDLGLIGREGWWYPKYVEEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 127 Y-HITNIEQLKdpKIAKLFDT-NGDGKADMMGCSPGWGCEAVInhQNKAYDLAKTVdVSHGNYSAMMADTIARFKEGKPV 204
Cdd:cd13643 97 CpGLPDWKALN--KCAALFATpETGPKGRLLGGPPDWGTNDAA--RIAALGLPFTV-VPAGSEAALWAELRAAYARKKPL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 205 IYYTWTPYWVSDVLkpgkDVVWLQVPfssLPGEQKDIDTKLPNGMNY----GFPVNTMHIVANKAWSEKNPAAAKLFSVM 280
Cdd:cd13643 172 LIYFWTPHWAFAKY----KGVFVELP---PYEEACETDPAWGNNPPAkgdcGYPPGYLKKAAWAGFADKWPAAYELLKNF 244
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 556489957 281 KLPLADINAQNAMMHAGKSSEADVkghVDGWIKAHEQQFDGW 322
Cdd:cd13643 245 TLTNEDQAAMAALIDVDGMSVEDA---AKKWLAANEATWKPW 283
|
|
| PBP2_HisX_like |
cd13641 |
Substrate-binding domain of ABC-type histidine transporter involves in betaine and proline ... |
69-323 |
3.42e-17 |
|
Substrate-binding domain of ABC-type histidine transporter involves in betaine and proline uptake; the type 2 periplasmic-binding protein fold; This subfamily is part of a high affinity multicomponent binding-protein-dependent transport system specific to certain quaternary ammonium compounds for osmoregulation. The periplasmic substrate-binding domain, which is often fused to the permease component of the ATP-binding cassette transporter complex, is involved in uptake of osmoprotectants (also termed compatible solutes) such as glycine betaine, proline betaine, choline, and carnitine. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. This domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270359 [Multi-domain] Cd Length: 261 Bit Score: 79.99 E-value: 3.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 69 VGYTSIASGDATFTAVNWQPLHDDMYAAAGGDKKFYREGTFVTGAAQG-----YLIDKKtadkyhitnieqlkdpkiakl 143
Cdd:cd13641 40 PTLTALARGDIDVAMELWTDNISEAYNKAVEEGKVLDLGTNFDDARQGwyvptYVIEGR--------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 144 fdtngdgkadMMGCSPGWGCEaVINHQN-KAYDLAKT-VDVSHGNYSAMMADTIARFKEGKPVIYYTWTPYWVSdvlkpG 221
Cdd:cd13641 99 ----------FYNCPTGWGCE-IINTNKlKAYGLDEGyTNFRPGSGAALDAAIASAYERGEPWVGYYWEPTWLM-----G 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 222 K-DVVWLQVPfsslPGEQKDIDTKLPNGMNYG---FPVNTMHIVANKAWSEKNPAAAKLFSVMKLPLADINAQNAMMHAG 297
Cdd:cd13641 163 KyDMTLLEEP----PYDEECWNCLCADCANPGacaFPSSTVTIAVNTDFAEKAPEIVEFLEKYETSLELTNEALAYMAEN 238
|
250 260
....*....|....*....|....*.
gi 556489957 298 KSSEADVKGHvdgWIKAHEQQFDGWV 323
Cdd:cd13641 239 KASAEEAAKW---FLKNHPDVWTQWV 261
|
|
| PBP2_OpuAC_like |
cd13639 |
Substrate binding domain of Lactococcus lactis ABC-type transporter OpuA and related proteins; ... |
39-324 |
2.15e-16 |
|
Substrate binding domain of Lactococcus lactis ABC-type transporter OpuA and related proteins; the type 2 periplasmic binding protein fold; This subfamily is part of a high affinity multicomponent binding-protein-dependent transport system specific to betaine compounds for osmoregulation. The periplasmic substrate-binding domain, which is often fused to the permease component of the ATP-binding cassette transporter complex, is involved in uptake of osmoprotectants (also termed compatible solutes) such as glycine betaine and proline betaine. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. This domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270357 [Multi-domain] Cd Length: 254 Bit Score: 77.58 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 39 SEESFQTLIVSRALEKLGYTVNTpSEVDYNVGYTSIASGDATFTAVNWQPLHDDMYAAAGGDkKFYREGTFVTGAAQGyL 118
Cdd:cd13639 10 DEAIAVTNLAKAVLEEKGYDVEL-TQADAGPMYQGVASGDIDAFLDAWLPVTHKDYWDKYGD-DLEDLGPWYEGAKLG-L 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 119 IDKKTADkyhITNIEQLKDpkIAKLFdtngDGKadMMGCSPGWGC-----EAVINHQNKAYDLAKtvdvshGNYSAMMAD 193
Cdd:cd13639 87 AVPSYVD---IDSIEELLD--HADKF----GGK--IVGIEPGAGLmklteEAIEEYGLLDYELVT------SSTAAMLAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 194 TIARFKEGKPVIYYTWTPYWVSDVLkpgkDVVWLQVPfsslpgeqKDIdtklpngmnYGfPVNTMHIVANKAWSEKNPAA 273
Cdd:cd13639 150 LDRAIDNKEPIVVTGWSPHWMFAKY----DLKYLEDP--------KGV---------YG-EAESIHTIARKGFEEDHPEA 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 556489957 274 AKLFSVMKLPLADINAQNAMMHAGKSSEADVKghvdGWIKAHEQQFDGWVK 324
Cdd:cd13639 208 YEFLKNFKLTDEDLESLMLEIEDGGDPEEAAE----EWIDENPDLVDEWLE 254
|
|
| PBP2_ChoX |
cd13640 |
Substrate binding domain of ABC-type choline transport system; the type 2 periplasmic binding ... |
44-324 |
2.54e-16 |
|
Substrate binding domain of ABC-type choline transport system; the type 2 periplasmic binding protein fold; This subfamily is part of a high affinity multicomponent binding-protein-dependent transport system specific to choline and acetylcholine for osmoregulation. The periplasmic substrate-binding domain, which is often fused to the permease component of the ATP-binding cassette transporter complex, is involved in uptake of osmoprotectants (also termed compatible solutes) such as choline and betaines. Choline is necessary for the biosynthesis of glycine betaine. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. In the case of the Sinorhizobium meliloti choline uptake system ChoVWX, ChoV is the nucleotide-binding domain that provides energy for the transport process via ATP hydrolysis, ChoW is the integral transmembrane protein that forms the substrate translaocation pathway, and ChoX is the substrate-binding domain. ChoX belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270358 [Multi-domain] Cd Length: 266 Bit Score: 77.63 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 44 QTLIVSRALEKLGYTVNTpSEVDYNVGYTSIASGDA-TFTAvNWQPLHDDMYAAAGGDKKFYREGTFVTGAAQGYLIDKK 122
Cdd:cd13640 15 TTAVASQILEALGYETEV-KELSVPIIYQGLANGDIdVFLG-NWMPSQEPMIDPYLEKGSIEVVGTNLEGAKYTLAVPTY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 123 TADKyHITNIEQLKdpKIAKLFDtngdGKadMMGCSPGWGCEAVINH--QNKAYDLA--KTVDVSHgnySAMMADTIARF 198
Cdd:cd13640 93 VYEA-GVKSFADLA--KFADKFD----GK--IYGIEPGNDGNEIIQKmiDNNTYGLGdwKLVESSE---QGMLAQVERAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489957 199 KEGKPVIYYTWTPYWVSDVLkpgkDVVWLQVPfsslpgeqKDIdtklpNGMNYGfpVNTMHIVANKAWSEKNPAAAKLFS 278
Cdd:cd13640 161 RNKEWIVFLGWEPHPMNVEF----DIKYLDGG--------DDY-----FGPNYG--AATVYTVTRKGYAEDCPNVAKLLS 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 556489957 279 VMKLPLADinaQNAMMHAGKSSEADVKGHVDGWIKAHEQQFDGWVK 324
Cdd:cd13640 222 NLKFSVDM---ENQWMYEILNKGRDPEDAAREWIKANPDVVDAWLD 264
|
|
|