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Conserved domains on  [gi|696319525|ref|WP_032894932|]
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MULTISPECIES: choline ABC transporter substrate-binding protein [Pseudomonas]

Protein Classification

choline ABC transporter substrate-binding protein( domain architecture ID 10799157)

choline ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of choline

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ABC_choline_bnd TIGR03414
choline ABC transporter, periplasmic binding protein; Partial phylogenetic profiling () vs. ...
21-313 0e+00

choline ABC transporter, periplasmic binding protein; Partial phylogenetic profiling () vs. the genome property of glycine betaine biosynthesis from choline consistently reveals a member of this ABC transporter periplasmic binding protein as the best match, save for the betaine biosynthesis enzymes themselves. Genomes often carry several paralogs, one encoded together with the permease and ATP-binding components and another encoded next to a choline-sulfatase gene, suggesting that different members of this protein family interact with shared components and give some flexibility in substrate. Of two members from Sinorhizobium meliloti 1021, one designated ChoX has been shown experimentally to bind choline (though not various related compounds such as betaine) and to be required for about 60 % of choline uptake. Members of this protein have an invariant Cys residue near the N-terminus and likely are lipoproteins. [Transport and binding proteins, Amino acids, peptides and amines]


:

Pssm-ID: 188316  Cd Length: 290  Bit Score: 501.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525   21 AAEPEQCKTVNFSDVGWTDITVTTATTSEILKGLGYKPRTTMISVPVTYKSLADGkNMDIFLGNWMPTMENDIKQYRDAG 100
Cdd:TIGR03414   1 AAEPASCKTVRFADVGWTDITATTAVASVLLEGLGYQPKVTTLSVPITYAGLKNG-DLDVFLGNWMPAMEPDIKPYLEAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  101 TVETVRANLENAKYTLAVPQALYDKGLKDFADIAKFKDELNGKIYGIEPGNDGNRTIQTLIDKDAFGLKtaGFKVVESSE 180
Cdd:TIGR03414  80 SVEVLGPNLEGAKYTLAVPTYVADAGVKSFADIAKFKDKLDGKIYGIEPGNDGNRLIQKMIDKNAFGLG--GFKLVESSE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  181 AGMLSQVERASKRDQAIVFLGWEPHPMNTRFKMKYLTGGDDSFGPNYGQATIYTNTRKGYTQECSNVGQLLKNLVFTLDM 260
Cdd:TIGR03414 158 AGMLAQVARAVKRKEWIVFLGWEPHPMNTNFKMTYLTGGDDYFGPNYGGATVYTNTRKGYAAECPNVGKLLTNLTFTLDM 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 696319525  261 ESTLMGNVLDDKMKADAAAKAWLQKNPQVLDTWLAGVTTVDGKPGLDAVKAYL 313
Cdd:TIGR03414 238 ENQLMGAILNDGKDPEAAARQWLKANPEVLDPWLAGVTTVDGKDGLAAVKAAL 290
 
Name Accession Description Interval E-value
ABC_choline_bnd TIGR03414
choline ABC transporter, periplasmic binding protein; Partial phylogenetic profiling () vs. ...
21-313 0e+00

choline ABC transporter, periplasmic binding protein; Partial phylogenetic profiling () vs. the genome property of glycine betaine biosynthesis from choline consistently reveals a member of this ABC transporter periplasmic binding protein as the best match, save for the betaine biosynthesis enzymes themselves. Genomes often carry several paralogs, one encoded together with the permease and ATP-binding components and another encoded next to a choline-sulfatase gene, suggesting that different members of this protein family interact with shared components and give some flexibility in substrate. Of two members from Sinorhizobium meliloti 1021, one designated ChoX has been shown experimentally to bind choline (though not various related compounds such as betaine) and to be required for about 60 % of choline uptake. Members of this protein have an invariant Cys residue near the N-terminus and likely are lipoproteins. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 188316  Cd Length: 290  Bit Score: 501.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525   21 AAEPEQCKTVNFSDVGWTDITVTTATTSEILKGLGYKPRTTMISVPVTYKSLADGkNMDIFLGNWMPTMENDIKQYRDAG 100
Cdd:TIGR03414   1 AAEPASCKTVRFADVGWTDITATTAVASVLLEGLGYQPKVTTLSVPITYAGLKNG-DLDVFLGNWMPAMEPDIKPYLEAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  101 TVETVRANLENAKYTLAVPQALYDKGLKDFADIAKFKDELNGKIYGIEPGNDGNRTIQTLIDKDAFGLKtaGFKVVESSE 180
Cdd:TIGR03414  80 SVEVLGPNLEGAKYTLAVPTYVADAGVKSFADIAKFKDKLDGKIYGIEPGNDGNRLIQKMIDKNAFGLG--GFKLVESSE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  181 AGMLSQVERASKRDQAIVFLGWEPHPMNTRFKMKYLTGGDDSFGPNYGQATIYTNTRKGYTQECSNVGQLLKNLVFTLDM 260
Cdd:TIGR03414 158 AGMLAQVARAVKRKEWIVFLGWEPHPMNTNFKMTYLTGGDDYFGPNYGGATVYTNTRKGYAAECPNVGKLLTNLTFTLDM 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 696319525  261 ESTLMGNVLDDKMKADAAAKAWLQKNPQVLDTWLAGVTTVDGKPGLDAVKAYL 313
Cdd:TIGR03414 238 ENQLMGAILNDGKDPEAAARQWLKANPEVLDPWLAGVTTVDGKDGLAAVKAAL 290
PBP2_ChoX cd13640
Substrate binding domain of ABC-type choline transport system; the type 2 periplasmic binding ...
29-297 4.37e-145

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: 408.90  E-value: 4.37e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  29 TVNFSDVGWTDITVTTATTSEILKGLGYKPRTTMISVPVTYKSLADGKnMDIFLGNWMPTMENDIKQYRDAGTVETVRAN 108
Cdd:cd13640    1 TVRFGDVGWTDITVTTAVASQILEALGYETEVKELSVPIIYQGLANGD-IDVFLGNWMPSQEPMIDPYLEKGSIEVVGTN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525 109 LENAKYTLAVPQALYDKGLKDFADIAKFKDELNGKIYGIEPGNDGNRTIQTLIDKDAFGLKtaGFKVVESSEAGMLSQVE 188
Cdd:cd13640   80 LEGAKYTLAVPTYVYEAGVKSFADLAKFADKFDGKIYGIEPGNDGNEIIQKMIDNNTYGLG--DWKLVESSEQGMLAQVE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525 189 RASKRDQAIVFLGWEPHPMNTRFKMKYLTGGDDSFGPNYGQATIYTNTRKGYTQECSNVGQLLKNLVFTLDMESTLMGNV 268
Cdd:cd13640  158 RAIRNKEWIVFLGWEPHPMNVEFDIKYLDGGDDYFGPNYGAATVYTVTRKGYAEDCPNVAKLLSNLKFSVDMENQWMYEI 237
                        250       260
                 ....*....|....*....|....*....
gi 696319525 269 LDDKMKADAAAKAWLQKNPQVLDTWLAGV 297
Cdd:cd13640  238 LNKGRDPEDAAREWIKANPDVVDAWLDGV 266
ProX COG2113
ABC-type proline/glycine betaine transport system, periplasmic component [Amino acid transport ...
18-299 2.91e-109

ABC-type proline/glycine betaine transport system, periplasmic component [Amino acid transport and metabolism];


Pssm-ID: 441716 [Multi-domain]  Cd Length: 297  Bit Score: 319.49  E-value: 2.91e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  18 VAHAAEPEQCKTVNFSDVGWTDITVTTATTSEILKGLGYKPRTTMISVPVTYKSLADGkNMDIFLGNWMPTMENDIKQYR 97
Cdd:COG2113   21 AAAAAAPGSCKTVTIADVGWTSATATTAVAKQILEELGYEVELVELDVPVTYQGLANG-DIDVFLEAWLPTTHADYDEAY 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  98 DAGTVETVRANLENAKYTLAVPQALYDKGLKDFADIAKFKDELNGKIYGIEPGNDGNRTIQTLIDkdAFGLKtaGFKVVE 177
Cdd:COG2113  100 GDGKVEDLGTNYEGAKQGLAVPKYVAEPGIKSIADLKKYADLFDGKIYGIEPGWGCNRVIEEAIK--AYGLD--DFELVE 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525 178 SSEAGMLSQVERASKRDQAIVFLGWEPHPMNTRFKMKYLTGGDDSFGPNYGQATIYTNTRKGYTQECSNVGQLLKNLVFT 257
Cdd:COG2113  176 GSEAAMLAALARAYKRGEPIVFYGWTPHWMFAKYDLKYLEDPKGAFGPNFPAETVHTVARKGFAEDNPEAAKLLENFKFT 255
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 696319525 258 LDMESTLMGNVLDDKMKADAAAKAWLQKNPQVLDTWLAGVTT 299
Cdd:COG2113  256 LEDINALMAAIENDGADPEEAAKEWLKANPDVVDGWLPGVTA 297
OpuAC pfam04069
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity ...
28-268 1.74e-48

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: 162.88  E-value: 1.74e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525   28 KTVNFSDVGWTDITVTTATTSEILKGLGYKPRTTMI-SVPVTYKSLADGkNMDIFLGNWMPTMENDIKQYRDAGTVETVR 106
Cdd:pfam04069   1 KTIVIGSKNWTEQEILANIAAQLLEALGYVVELVGLgSSAVLFAALASG-DIDLYPEEWTGTTYEAYKKAVEEKLGLLVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  107 -ANLENAKYTLAVPQALYDK-GLKDFADIAKFKDELN----GKIYGIEPGNDGNRTIQTLIDkdAFGLKtaGFKVVESSE 180
Cdd:pfam04069  80 gPLGAGNTYGLAVPKYVAEKpGIKSISDLAKPADDLElgfkGEFIGRPDGWGCMRSTEGLLK--AYGLD--KYELVEGSE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  181 AGMLSQVERASKRDQAIVFLGWEPHPMNTRFKMKYLTGGDDSFGPNYgqaTIYTNTRKGYTQECSNVGQLLKNLVFTLDM 260
Cdd:pfam04069 156 AAMDALIYAAYKRGEPDVVYAWTPDWMIKKYDLVVLEDPKGLFPPAY---NVVPVVRKGFAEKHPEVAAFLNKLSLDTED 232

                  ....*...
gi 696319525  261 ESTLMGNV 268
Cdd:pfam04069 233 LNELNAQV 240
 
Name Accession Description Interval E-value
ABC_choline_bnd TIGR03414
choline ABC transporter, periplasmic binding protein; Partial phylogenetic profiling () vs. ...
21-313 0e+00

choline ABC transporter, periplasmic binding protein; Partial phylogenetic profiling () vs. the genome property of glycine betaine biosynthesis from choline consistently reveals a member of this ABC transporter periplasmic binding protein as the best match, save for the betaine biosynthesis enzymes themselves. Genomes often carry several paralogs, one encoded together with the permease and ATP-binding components and another encoded next to a choline-sulfatase gene, suggesting that different members of this protein family interact with shared components and give some flexibility in substrate. Of two members from Sinorhizobium meliloti 1021, one designated ChoX has been shown experimentally to bind choline (though not various related compounds such as betaine) and to be required for about 60 % of choline uptake. Members of this protein have an invariant Cys residue near the N-terminus and likely are lipoproteins. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 188316  Cd Length: 290  Bit Score: 501.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525   21 AAEPEQCKTVNFSDVGWTDITVTTATTSEILKGLGYKPRTTMISVPVTYKSLADGkNMDIFLGNWMPTMENDIKQYRDAG 100
Cdd:TIGR03414   1 AAEPASCKTVRFADVGWTDITATTAVASVLLEGLGYQPKVTTLSVPITYAGLKNG-DLDVFLGNWMPAMEPDIKPYLEAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  101 TVETVRANLENAKYTLAVPQALYDKGLKDFADIAKFKDELNGKIYGIEPGNDGNRTIQTLIDKDAFGLKtaGFKVVESSE 180
Cdd:TIGR03414  80 SVEVLGPNLEGAKYTLAVPTYVADAGVKSFADIAKFKDKLDGKIYGIEPGNDGNRLIQKMIDKNAFGLG--GFKLVESSE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  181 AGMLSQVERASKRDQAIVFLGWEPHPMNTRFKMKYLTGGDDSFGPNYGQATIYTNTRKGYTQECSNVGQLLKNLVFTLDM 260
Cdd:TIGR03414 158 AGMLAQVARAVKRKEWIVFLGWEPHPMNTNFKMTYLTGGDDYFGPNYGGATVYTNTRKGYAAECPNVGKLLTNLTFTLDM 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 696319525  261 ESTLMGNVLDDKMKADAAAKAWLQKNPQVLDTWLAGVTTVDGKPGLDAVKAYL 313
Cdd:TIGR03414 238 ENQLMGAILNDGKDPEAAARQWLKANPEVLDPWLAGVTTVDGKDGLAAVKAAL 290
PBP2_ChoX cd13640
Substrate binding domain of ABC-type choline transport system; the type 2 periplasmic binding ...
29-297 4.37e-145

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: 408.90  E-value: 4.37e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  29 TVNFSDVGWTDITVTTATTSEILKGLGYKPRTTMISVPVTYKSLADGKnMDIFLGNWMPTMENDIKQYRDAGTVETVRAN 108
Cdd:cd13640    1 TVRFGDVGWTDITVTTAVASQILEALGYETEVKELSVPIIYQGLANGD-IDVFLGNWMPSQEPMIDPYLEKGSIEVVGTN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525 109 LENAKYTLAVPQALYDKGLKDFADIAKFKDELNGKIYGIEPGNDGNRTIQTLIDKDAFGLKtaGFKVVESSEAGMLSQVE 188
Cdd:cd13640   80 LEGAKYTLAVPTYVYEAGVKSFADLAKFADKFDGKIYGIEPGNDGNEIIQKMIDNNTYGLG--DWKLVESSEQGMLAQVE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525 189 RASKRDQAIVFLGWEPHPMNTRFKMKYLTGGDDSFGPNYGQATIYTNTRKGYTQECSNVGQLLKNLVFTLDMESTLMGNV 268
Cdd:cd13640  158 RAIRNKEWIVFLGWEPHPMNVEFDIKYLDGGDDYFGPNYGAATVYTVTRKGYAEDCPNVAKLLSNLKFSVDMENQWMYEI 237
                        250       260
                 ....*....|....*....|....*....
gi 696319525 269 LDDKMKADAAAKAWLQKNPQVLDTWLAGV 297
Cdd:cd13640  238 LNKGRDPEDAAREWIKANPDVVDAWLDGV 266
ProX COG2113
ABC-type proline/glycine betaine transport system, periplasmic component [Amino acid transport ...
18-299 2.91e-109

ABC-type proline/glycine betaine transport system, periplasmic component [Amino acid transport and metabolism];


Pssm-ID: 441716 [Multi-domain]  Cd Length: 297  Bit Score: 319.49  E-value: 2.91e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  18 VAHAAEPEQCKTVNFSDVGWTDITVTTATTSEILKGLGYKPRTTMISVPVTYKSLADGkNMDIFLGNWMPTMENDIKQYR 97
Cdd:COG2113   21 AAAAAAPGSCKTVTIADVGWTSATATTAVAKQILEELGYEVELVELDVPVTYQGLANG-DIDVFLEAWLPTTHADYDEAY 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  98 DAGTVETVRANLENAKYTLAVPQALYDKGLKDFADIAKFKDELNGKIYGIEPGNDGNRTIQTLIDkdAFGLKtaGFKVVE 177
Cdd:COG2113  100 GDGKVEDLGTNYEGAKQGLAVPKYVAEPGIKSIADLKKYADLFDGKIYGIEPGWGCNRVIEEAIK--AYGLD--DFELVE 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525 178 SSEAGMLSQVERASKRDQAIVFLGWEPHPMNTRFKMKYLTGGDDSFGPNYGQATIYTNTRKGYTQECSNVGQLLKNLVFT 257
Cdd:COG2113  176 GSEAAMLAALARAYKRGEPIVFYGWTPHWMFAKYDLKYLEDPKGAFGPNFPAETVHTVARKGFAEDNPEAAKLLENFKFT 255
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 696319525 258 LDMESTLMGNVLDDKMKADAAAKAWLQKNPQVLDTWLAGVTT 299
Cdd:COG2113  256 LEDINALMAAIENDGADPEEAAKEWLKANPDVVDGWLPGVTA 297
PBP2_Osm_BCP_like cd13535
Substrate binding domain of osmoregulatory ABC-type glycine betaine/choline/L-proline ...
29-284 6.38e-56

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: 182.75  E-value: 6.38e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  29 TVNFSDVGWTDITVTTATTSEILKGLGYKPRTTMISVPVTYKSLADGKnMDIFLGNWMPTMENDIKQYRDAGTVETVRAN 108
Cdd:cd13535    1 TVKLAVPSWTGETATTHVLGTILEALGYTVDYVSLNNAVTFQSLANGD-IDITVENWLPNHEDFYAKYVEGKKVVVLGQN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525 109 LENAKYTLAVPQALYDKGLKDFADIAKF---------KDELNGKIYGIEPGNDGNRTIqtlIDKDAFGLKTAGFKVVESS 179
Cdd:cd13535   80 LYGAKQGFAVPKKVAELNPITNIADLGRpdaaaladsEGNGKGRLTGCPPGWGCEGAI---EVKLEDYGLLKFVEVVPGS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525 180 EAGMLSQVERASKRDQAIVFLGWEPHPMNTRFKMKYLTGGDDSF---------------GPNYGQATIYTNTRKGYTQEC 244
Cdd:cd13535  157 EGAMTAAIKSAIKQGEPIFFYGWSPHWVWFKFDVVYLSEPTYDEacytmvqpwnekssvGCKFASSTVHIAVNKGLADEN 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 696319525 245 SNVGQLLKNLVFTLDMESTLMGNVLDDKMKADAAAKAWLQ 284
Cdd:cd13535  237 PAAAEILENFSLTVDDVNAFMGEISDNGGDPEEAAAEWLK 276
PBP2_OpuAC_like cd13639
Substrate binding domain of Lactococcus lactis ABC-type transporter OpuA and related proteins; ...
49-295 1.94e-49

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: 165.02  E-value: 1.94e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  49 EILKGLGYKPRTTMISVPVTYKSLADGkNMDIFLGNWMP-TMENDIKQYRDagTVETVRANLENAKYTLAVPQALYDKGL 127
Cdd:cd13639   21 AVLEEKGYDVELTQADAGPMYQGVASG-DIDAFLDAWLPvTHKDYWDKYGD--DLEDLGPWYEGAKLGLAVPSYVDIDSI 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525 128 kdfADIAKFKDELNGKIYGIEPGNDGNRTIQTLIDkdAFGLKtaGFKVVESSEAGMLSQVERASKRDQAIVFLGWEPHPM 207
Cdd:cd13639   98 ---EELLDHADKFGGKIVGIEPGAGLMKLTEEAIE--EYGLL--DYELVTSSTAAMLAELDRAIDNKEPIVVTGWSPHWM 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525 208 NTRFKMKYLTGGDDSFGpnyGQATIYTNTRKGYTQECSNVGQLLKNLVFTLDMESTLMGNVlDDKMKADAAAKAWLQKNP 287
Cdd:cd13639  171 FAKYDLKYLEDPKGVYG---EAESIHTIARKGFEEDHPEAYEFLKNFKLTDEDLESLMLEI-EDGGDPEEAAEEWIDENP 246

                 ....*...
gi 696319525 288 QVLDTWLA 295
Cdd:cd13639  247 DLVDEWLE 254
OpuAC pfam04069
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity ...
28-268 1.74e-48

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: 162.88  E-value: 1.74e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525   28 KTVNFSDVGWTDITVTTATTSEILKGLGYKPRTTMI-SVPVTYKSLADGkNMDIFLGNWMPTMENDIKQYRDAGTVETVR 106
Cdd:pfam04069   1 KTIVIGSKNWTEQEILANIAAQLLEALGYVVELVGLgSSAVLFAALASG-DIDLYPEEWTGTTYEAYKKAVEEKLGLLVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  107 -ANLENAKYTLAVPQALYDK-GLKDFADIAKFKDELN----GKIYGIEPGNDGNRTIQTLIDkdAFGLKtaGFKVVESSE 180
Cdd:pfam04069  80 gPLGAGNTYGLAVPKYVAEKpGIKSISDLAKPADDLElgfkGEFIGRPDGWGCMRSTEGLLK--AYGLD--KYELVEGSE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  181 AGMLSQVERASKRDQAIVFLGWEPHPMNTRFKMKYLTGGDDSFGPNYgqaTIYTNTRKGYTQECSNVGQLLKNLVFTLDM 260
Cdd:pfam04069 156 AAMDALIYAAYKRGEPDVVYAWTPDWMIKKYDLVVLEDPKGLFPPAY---NVVPVVRKGFAEKHPEVAAFLNKLSLDTED 232

                  ....*...
gi 696319525  261 ESTLMGNV 268
Cdd:pfam04069 233 LNELNAQV 240
PBP2_BCP_2 cd13643
Substrate-binding domain of osmoregulatory ABC-type glycine betaine/choline/L-proline ...
49-293 1.09e-10

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: 61.15  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  49 EILKGLGYKPRTTMISVPVTYKSLADGkNMDIFLGNWMPTMENDIKQYRDAGTVETVrANLEN-AKYTLAVPQALYDK-- 125
Cdd:cd13643   21 YLLEKEGYKVEYVTADEQAQWEALAAG-DVDAQLEVWESSMGDKYEKALAAGSVVDL-GDLGLiGREGWWYPKYVEELcp 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525 126 GLKDFADIAKFKDEL-------NGKIYGIEPGNDGNRtiQTLIDkdAFGLKtagFKVVES-SEAGMLSQVERASKRDQAI 197
Cdd:cd13643   99 GLPDWKALNKCAALFatpetgpKGRLLGGPPDWGTND--AARIA--ALGLP---FTVVPAgSEAALWAELRAAYARKKPL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525 198 VFLGWEPHPMNTRFKMKYL-----TGG---DDSFGPN--------YGQATIYTNTRKGYTQECSNVGQLLKNLVFTLDME 261
Cdd:cd13643  172 LIYFWTPHWAFAKYKGVFVelppyEEAcetDPAWGNNppakgdcgYPPGYLKKAAWAGFADKWPAAYELLKNFTLTNEDQ 251
                        250       260       270
                 ....*....|....*....|....*....|..
gi 696319525 262 STLMGNVLDDKMKADAAAKAWLQKNPQVLDTW 293
Cdd:cd13643  252 AAMAALIDVDGMSVEDAAKKWLAANEATWKPW 283
PBP2_BCP_1 cd13642
Substrate-binding domain of osmoregulatory ABC-type glycine betaine/choline/L-proline ...
66-217 9.52e-07

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: 49.31  E-value: 9.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  66 PVTYKSLADGK-NMDIFLGNWMPTMENDIKQYRDAGTVETVRANLENAKYTLAVPQALYDK-GLKDFADIAKFKDELN-- 141
Cdd:cd13642   39 PIIFAAMDKGDgSIDVHPDVWLPNQQALWDKYVTGGGTVALNPNPYEGTQGICVPAATADKyGIKSDLDLTAPEAALFds 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525 142 -----GKIYGIEPGndgnrTIQTLIDK---DAFGLkTAGFKVVESSEAGMLSQVERASKRDQAIVFLGWEPHPMNTRFKM 213
Cdd:cd13642  119 dgdgkGEIWIGAPG-----WASTNIEQikaKSYGY-DETWELEEMSEAVFYAQLDAAYARGEPIVFYCYTPHWVFALYDL 192

                 ....
gi 696319525 214 KYLT 217
Cdd:cd13642  193 VQLE 196
PBP2_EcProx_like cd13638
Substrate binding domain of Escherichia coli betaine transport system-like; the type 2 ...
24-212 2.09e-05

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: 45.36  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525  24 PEQCKTVNFSDVGWTDITVTTATTSEILKGLGYKPR-TTMISVPVTYKSLADGkNMDIFLGNWMPTMEndiKQYRDAG-- 100
Cdd:cd13638    1 PGKGVTVRPAKSTWAEEYFQTEIVSKGLEKLGYKVKePKELDYPLFYVAVANG-DADFWADHWFPLHD---PFFEKAGgd 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696319525 101 TVETVRANL-ENAKYTLAVPQALYDKG----LKDFAD--IAK-FKDELNGK--IYGIEPGNDGNRTIQTLIdkDAFGLKT 170
Cdd:cd13638   77 AKLVRVGVIiGGGLQGYLIDKKTADAYnitsLDQLKDpkIAKlFDSDGDGKadLTGCNPGWGCEKVIEHQL--DAYGLRD 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 696319525 171 AGFKVVESSEAGMLSQVERAsKRDQAIVFLGWEPHPMNTRFK 212
Cdd:cd13638  155 TVNHNQGSYSALMADAIARY-KQGKPVLYYTWTPNWVSNVLV 195
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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