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Conserved domains on  [gi|519083150|ref|WP_020239025|]
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glycine betaine ABC transporter substrate-binding protein OsmF [Escherichia coli]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 10194472)

ABC transporter substrate-binding protein similar to OsmF (YehZ), which is part of the YehZYXW complex, a non-osmoregulatory betaine-specific ABC transporter

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP2_OsmF cd13616
Substrate-binding domain OsmF of an osmoregulated ABC-type transporter; the type 2 ...
26-299 2.32e-176

Substrate-binding domain OsmF of an osmoregulated ABC-type transporter; the type 2 periplasmic-binding protein fold; Osmoprotectant binding lipoprotein OsmF of an ABC transporter (YehZYXW) from Escherichia coli is predicted to be involved in uptake of compatible solutes such as choline, L-proline and glycine betaine, but the relative substrate preference is not known. To counteract the efflux of water, microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. OsmF 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: 270334  Cd Length: 274  Bit Score: 487.99  E-value: 2.32e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  26 PVKVGSKIDTEGALLGNIILQVLESHGVPTVNKVQLGTTPVVRGAITSGELDIYPEYTGNGAFFFKDENDTVWKNAQQGY 105
Cdd:cd13616    1 PVVVGSKIDTEGALLGNMIVLALEAHGFPVEDKTGLGTTPVVRKALLSGEIDLYPEYTGNGAFFFPEADDPVWKDARKGY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 106 EKVKKLDAEQNKLIWLTPAPANNTWTIAVRQDVAEKNKLTSLAELSRYLKEGGNFKLAASAEFIERADALPAFEKAYGFK 185
Cdd:cd13616   81 ETVKELDAKNNGLVWLDPAPANNTWAIAVRRDLAEKNNLKTLADLAAYVNEGGAFKLAASAEFVERPDALPAFEKAYGFK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 186 LGQDQLLSLAGGDTAVTIKAAAQQTSGVNAAMAYGTDGPVAALGLQTLSDPQGVQPIYAPAPVGRESVLKEYPQMAQWLR 265
Cdd:cd13616  161 LSKDQLVILSGGNTAQTEQAAAQGTSGVNAAMAYGTDGAIAALGLVVLEDPKGAQPVYAPAPVVRQEVLEAYPEIAEILK 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 519083150 266 PVFASLDEKTLQQLNASIAVEGLDAKKVAADYLK 299
Cdd:cd13616  241 PVFATLDLKTLQELNARIAVEGESAEDVARDYLK 274
 
Name Accession Description Interval E-value
PBP2_OsmF cd13616
Substrate-binding domain OsmF of an osmoregulated ABC-type transporter; the type 2 ...
26-299 2.32e-176

Substrate-binding domain OsmF of an osmoregulated ABC-type transporter; the type 2 periplasmic-binding protein fold; Osmoprotectant binding lipoprotein OsmF of an ABC transporter (YehZYXW) from Escherichia coli is predicted to be involved in uptake of compatible solutes such as choline, L-proline and glycine betaine, but the relative substrate preference is not known. To counteract the efflux of water, microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. OsmF 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: 270334  Cd Length: 274  Bit Score: 487.99  E-value: 2.32e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  26 PVKVGSKIDTEGALLGNIILQVLESHGVPTVNKVQLGTTPVVRGAITSGELDIYPEYTGNGAFFFKDENDTVWKNAQQGY 105
Cdd:cd13616    1 PVVVGSKIDTEGALLGNMIVLALEAHGFPVEDKTGLGTTPVVRKALLSGEIDLYPEYTGNGAFFFPEADDPVWKDARKGY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 106 EKVKKLDAEQNKLIWLTPAPANNTWTIAVRQDVAEKNKLTSLAELSRYLKEGGNFKLAASAEFIERADALPAFEKAYGFK 185
Cdd:cd13616   81 ETVKELDAKNNGLVWLDPAPANNTWAIAVRRDLAEKNNLKTLADLAAYVNEGGAFKLAASAEFVERPDALPAFEKAYGFK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 186 LGQDQLLSLAGGDTAVTIKAAAQQTSGVNAAMAYGTDGPVAALGLQTLSDPQGVQPIYAPAPVGRESVLKEYPQMAQWLR 265
Cdd:cd13616  161 LSKDQLVILSGGNTAQTEQAAAQGTSGVNAAMAYGTDGAIAALGLVVLEDPKGAQPVYAPAPVVRQEVLEAYPEIAEILK 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 519083150 266 PVFASLDEKTLQQLNASIAVEGLDAKKVAADYLK 299
Cdd:cd13616  241 PVFATLDLKTLQELNARIAVEGESAEDVARDYLK 274
OsmF COG1732
Periplasmic glycine betaine/choline-binding (lipo)protein of an ABC-type transport system ...
6-301 1.98e-111

Periplasmic glycine betaine/choline-binding (lipo)protein of an ABC-type transport system (osmoprotectant binding protein) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441338 [Multi-domain]  Cd Length: 294  Bit Score: 324.41  E-value: 1.98e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150   6 LWAGSLVLLAAVSLPLQAAS--PVKVGSKIDTEGALLGNIILQVLESHGVPTVNKVQLGTTPVVRGAITSGELDIYPEYT 83
Cdd:COG1732    9 LALAAALALAGCGLASAAAAgdTIVVGSKNFTEQEILAEIYAQALEAAGLKVERKLNLGGTEVVRQALKSGEIDLYPEYT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  84 GNGAFFFKDENDTvwKNAQQGYEKVKKLDAEQNKLIWLTPAPANNTWTIAVRQDVAEKNKLTSLAELSRYLkegGNFKLA 163
Cdd:COG1732   89 GTALTTYLKEDPI--TDPEEVYEAVKEALPEKNGLTWLDPAGFNNTYALAVTKETAEKYGLKTISDLAKVA---GELTLG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 164 ASAEFIERADALPAFEKAYGFKLGQdqLLSLAGGdtavtIKAAAQQTSGVNAAMAYGTDGPVAALGLQTLSDPQGVQPIY 243
Cdd:COG1732  164 ADPEFAERPDGLPGLKKAYGFEFKE--VKPMDTG-----LTYTALANGQVDVADAYTTDGRIAALDLVVLEDDKNFFPPY 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 519083150 244 APAPVGRESVLKEYPQMAQWLRPVFASLDEKTLQQLNASIAVEGLDAKKVAADYLKQK 301
Cdd:COG1732  237 NAAPLVRKEVLEKYPELAEVLNKLSGKLTTETMQELNYQVDVDGEDPADVAREFLKEK 294
OpuAC pfam04069
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity ...
26-300 4.19e-56

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: 182.14  E-value: 4.19e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150   26 PVKVGSKIDTEGALLGNIILQVLESHGVpTVNKVQLGTTPVVRGAITSGELDIYP-EYTGNGafffkdendtvwknaqqg 104
Cdd:pfam04069   2 TIVIGSKNWTEQEILANIAAQLLEALGY-VVELVGLGSSAVLFAALASGDIDLYPeEWTGTT------------------ 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  105 YEKVKKLDAEQNKLIWLTPAPANNTWTIAVRQDVAEKNKLTSLAELSRYlkeGGNFKLAASAEFIERADALP------AF 178
Cdd:pfam04069  63 YEAYKKAVEEKLGLLVLGPLGAGNTYGLAVPKYVAEKPGIKSISDLAKP---ADDLELGFKGEFIGRPDGWGcmrsteGL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  179 EKAYGFKLGQDQLLSLAGGDTAvtIKAAAQQTSgVNAAMAYGTDGPVAALGLQTLSDPQGVQ-PIYAPAPVGRESVLKEY 257
Cdd:pfam04069 140 LKAYGLDKYELVEGSEAAMDAL--IYAAYKRGE-PDVVYAWTPDWMIKKYDLVVLEDPKGLFpPAYNVVPVVRKGFAEKH 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 519083150  258 PQMAQWLRPVfaSLDEKTLQQLNASIAVEGLDAKKVAADYLKQ 300
Cdd:pfam04069 217 PEVAAFLNKL--SLDTEDLNELNAQVDVEGKDPEEVAKDWLAE 257
 
Name Accession Description Interval E-value
PBP2_OsmF cd13616
Substrate-binding domain OsmF of an osmoregulated ABC-type transporter; the type 2 ...
26-299 2.32e-176

Substrate-binding domain OsmF of an osmoregulated ABC-type transporter; the type 2 periplasmic-binding protein fold; Osmoprotectant binding lipoprotein OsmF of an ABC transporter (YehZYXW) from Escherichia coli is predicted to be involved in uptake of compatible solutes such as choline, L-proline and glycine betaine, but the relative substrate preference is not known. To counteract the efflux of water, microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. OsmF 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: 270334  Cd Length: 274  Bit Score: 487.99  E-value: 2.32e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  26 PVKVGSKIDTEGALLGNIILQVLESHGVPTVNKVQLGTTPVVRGAITSGELDIYPEYTGNGAFFFKDENDTVWKNAQQGY 105
Cdd:cd13616    1 PVVVGSKIDTEGALLGNMIVLALEAHGFPVEDKTGLGTTPVVRKALLSGEIDLYPEYTGNGAFFFPEADDPVWKDARKGY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 106 EKVKKLDAEQNKLIWLTPAPANNTWTIAVRQDVAEKNKLTSLAELSRYLKEGGNFKLAASAEFIERADALPAFEKAYGFK 185
Cdd:cd13616   81 ETVKELDAKNNGLVWLDPAPANNTWAIAVRRDLAEKNNLKTLADLAAYVNEGGAFKLAASAEFVERPDALPAFEKAYGFK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 186 LGQDQLLSLAGGDTAVTIKAAAQQTSGVNAAMAYGTDGPVAALGLQTLSDPQGVQPIYAPAPVGRESVLKEYPQMAQWLR 265
Cdd:cd13616  161 LSKDQLVILSGGNTAQTEQAAAQGTSGVNAAMAYGTDGAIAALGLVVLEDPKGAQPVYAPAPVVRQEVLEAYPEIAEILK 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 519083150 266 PVFASLDEKTLQQLNASIAVEGLDAKKVAADYLK 299
Cdd:cd13616  241 PVFATLDLKTLQELNARIAVEGESAEDVARDYLK 274
OsmF COG1732
Periplasmic glycine betaine/choline-binding (lipo)protein of an ABC-type transport system ...
6-301 1.98e-111

Periplasmic glycine betaine/choline-binding (lipo)protein of an ABC-type transport system (osmoprotectant binding protein) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441338 [Multi-domain]  Cd Length: 294  Bit Score: 324.41  E-value: 1.98e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150   6 LWAGSLVLLAAVSLPLQAAS--PVKVGSKIDTEGALLGNIILQVLESHGVPTVNKVQLGTTPVVRGAITSGELDIYPEYT 83
Cdd:COG1732    9 LALAAALALAGCGLASAAAAgdTIVVGSKNFTEQEILAEIYAQALEAAGLKVERKLNLGGTEVVRQALKSGEIDLYPEYT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  84 GNGAFFFKDENDTvwKNAQQGYEKVKKLDAEQNKLIWLTPAPANNTWTIAVRQDVAEKNKLTSLAELSRYLkegGNFKLA 163
Cdd:COG1732   89 GTALTTYLKEDPI--TDPEEVYEAVKEALPEKNGLTWLDPAGFNNTYALAVTKETAEKYGLKTISDLAKVA---GELTLG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 164 ASAEFIERADALPAFEKAYGFKLGQdqLLSLAGGdtavtIKAAAQQTSGVNAAMAYGTDGPVAALGLQTLSDPQGVQPIY 243
Cdd:COG1732  164 ADPEFAERPDGLPGLKKAYGFEFKE--VKPMDTG-----LTYTALANGQVDVADAYTTDGRIAALDLVVLEDDKNFFPPY 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 519083150 244 APAPVGRESVLKEYPQMAQWLRPVFASLDEKTLQQLNASIAVEGLDAKKVAADYLKQK 301
Cdd:COG1732  237 NAAPLVRKEVLEKYPELAEVLNKLSGKLTTETMQELNYQVDVDGEDPADVAREFLKEK 294
PBP2_osmoprotectants cd13528
Substrate-binding domain of osmoregulatory ABC-type transporters; the type 2 ...
26-299 5.18e-98

Substrate-binding domain of osmoregulatory ABC-type transporters; the type 2 periplasmic-binding protein fold; This family represents the periplasmic substrate-binding component of ABC transport systems that are involved in uptake of osmoprotectants (also termed compatible solutes) such as betaine, choline, proline betaine, carnitine, and L-proline. To counteract the efflux of water, bacteria and archaea accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding 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: 270246 [Multi-domain]  Cd Length: 264  Bit Score: 289.11  E-value: 5.18e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  26 PVKVGSKIDTEGALLGNIILQVLESHGVPTVN-KVQLGTTPVVRGAITSGELDIYPEYTGNGAFFFKDEnDTVWKNAQQG 104
Cdd:cd13528    1 TIVVGSKNFTEQYILGEMLAQLLEANTDLTVErKLNLGGTEVAFNALKNGDIDLYVEYTGTALLTILKE-DAPITDPEEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 105 YEKVKKLDAEQNKLIWLTPAPANNTWTIAVRQDVAEKNKLTSLAELsryLKEGGNFKLAASAEFIERADALPAFEKAYGF 184
Cdd:cd13528   80 YEKVKKEYEEKFGLTWLDPLGFNNTYALAVRKDTAEKYGLKTISDL---APHSDQLVFGADPEFYERSDGLPGLKKTYGF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 185 KLGQDQLLslaggDTAVTIKAAAQQTsgVNAAMAYGTDGPVAALGLQTLSDPQGVQPIYAPAPVGRESVLKEYPQMAQWL 264
Cdd:cd13528  157 DFKEVKTM-----DPGLTYEALDNGE--VDVIDAFSTDGRIKAFDLVVLEDDKNFFPPYNAAPVVREDVLKKHPELEEVL 229
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 519083150 265 RPVFASLDEKTLQQLNASIAVEGLDAKKVAADYLK 299
Cdd:cd13528  230 NKLSGKLTDETMQQLNYQVDVEGKDPEEVARDFLK 264
PBP2_YehZ cd13611
Substrate-binding domain YehZ of an osmoregulated ABC-type transporter; the type 2 ...
26-299 3.67e-78

Substrate-binding domain YehZ of an osmoregulated ABC-type transporter; the type 2 periplasmic-binding protein fold; Osmoprotectant binding lipoprotein YehZ of Clostridium sticklandii is predicted to be involved in uptake of compatible solutes such as choline, L-proline and glycine betaine, but the relative substrate preference is not known. To counteract the efflux of water, microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. YehZ 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: 270329  Cd Length: 267  Bit Score: 238.64  E-value: 3.67e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  26 PVKVGSKIDTEGALLGNIILQVLESHGVPTVNKVQLGTTPVVRGAITSGELDIYPEYTGNGAFFFKDENDTVwKNAQQGY 105
Cdd:cd13611    1 TITVGSKDFTEQLILGKITVQALQAAGADVTDKTNLGGSASARQALENGQVDVYWEYTGTAWITYLGHTEPI-LDPQEQY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 106 EKVKKLDAEQNkLIWLTPAPANNTWTIAVRQDVAEKNKLTSLAELSRYLKEGGNFKLAASAEFIERADALPAFEKAYGFK 185
Cdd:cd13611   80 EAVKDLDAEKG-LVWLDPAPLNNTYALAMREATAEELGITTLSDLALAKLPPGDRTFCVDAEFASRPDGLPPLLEAYGFE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 186 LGQDQLLSLaggDTAVTIKAAAQQTsgVNAAMAYGTDGPVAALGLQTLSDPQGVQPIYAPAPVGRESVLKEYPQMAQWLR 265
Cdd:cd13611  159 FPRANVRQM---DTGLVYTATANGQ--CDFGEVFTTDGRIKALDLVVLEDDKGFFPAYNAAPVVRTEVLDAHPELAEILN 233
                        250       260       270
                 ....*....|....*....|....*....|....
gi 519083150 266 PVFASLDEKTLQQLNASIAVEGLDAKKVAADYLK 299
Cdd:cd13611  234 PISAKLDNDTMQELNARVDVDGEDPADVARDWLV 267
PBP2_QAT_like cd13614
Substrate-binding domain of quaternary amine ABC-type transporter; the type 2 ...
26-299 3.17e-65

Substrate-binding domain of quaternary amine ABC-type transporter; the type 2 periplasmic-binding protein fold; This group includes the periplasmic substrate-binding component of a putative quaternary amine ABC transport system that is predicted to be involved in uptake of osmoprotectants (also termed compatible solutes) such as betaine, choline, proline betaine, carnitine, and L-proline. The relative substrate preference of this group is not known. To counteract the efflux of water, many microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding 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: 270332  Cd Length: 264  Bit Score: 205.70  E-value: 3.17e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  26 PVKVGSKIDTEGALLGNIILQVLESHGVPTVNKVQLGTTPVVRGAITSGELDIYPEYTGNG-AFFFKDENDTvwkNAQQG 104
Cdd:cd13614    1 AIRVGSKNFTEQFILGEMYALALEDAGIKVERKLNLGGTLIAHQALVNGEIDLYPEYTGTAlLTVLKGEPSS---DAKQV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 105 YEKVKKLDAEQNKLIWLTPAPANNTWTIAVRQDVAEKNKLTSLAELSrylKEGGNFKLAASAEFIERADALPAFEKAYG- 183
Cdd:cd13614   78 YKTVKDAYAEQFQLTWLEPAPFNNTYALVMTRETAEKYGIKTLSDLA---KAAGELVFGGGPEFQDREDGLPGLKAKYGa 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 184 FKLGQDQLLSLAGgdtaVTIKAAAQQTSGVnaAMAYGTDGPVAALGLQTLSDPQGVQPIYAPAPVGRESVLKEYPQMAQW 263
Cdd:cd13614  155 FDFKEFVQVDPLG----LRYQALAQGQIDV--AVGFGTDGQIAAYGLVVLEDDKNLFPPYQVAPVVRQDVLDANPKIAEV 228
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 519083150 264 LRPVFASLDEKTLQQLNASIAVEGLDAKKVAADYLK 299
Cdd:cd13614  229 LNKLSALLDNETMQRLNYEVDGNKREPKDVAREFLK 264
OpuAC pfam04069
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity ...
26-300 4.19e-56

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: 182.14  E-value: 4.19e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150   26 PVKVGSKIDTEGALLGNIILQVLESHGVpTVNKVQLGTTPVVRGAITSGELDIYP-EYTGNGafffkdendtvwknaqqg 104
Cdd:pfam04069   2 TIVIGSKNWTEQEILANIAAQLLEALGY-VVELVGLGSSAVLFAALASGDIDLYPeEWTGTT------------------ 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  105 YEKVKKLDAEQNKLIWLTPAPANNTWTIAVRQDVAEKNKLTSLAELSRYlkeGGNFKLAASAEFIERADALP------AF 178
Cdd:pfam04069  63 YEAYKKAVEEKLGLLVLGPLGAGNTYGLAVPKYVAEKPGIKSISDLAKP---ADDLELGFKGEFIGRPDGWGcmrsteGL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  179 EKAYGFKLGQDQLLSLAGGDTAvtIKAAAQQTSgVNAAMAYGTDGPVAALGLQTLSDPQGVQ-PIYAPAPVGRESVLKEY 257
Cdd:pfam04069 140 LKAYGLDKYELVEGSEAAMDAL--IYAAYKRGE-PDVVYAWTPDWMIKKYDLVVLEDPKGLFpPAYNVVPVVRKGFAEKH 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 519083150  258 PQMAQWLRPVfaSLDEKTLQQLNASIAVEGLDAKKVAADYLKQ 300
Cdd:pfam04069 217 PEVAAFLNKL--SLDTEDLNELNAQVDVEGKDPEEVAKDWLAE 257
PBP2_Opu_like_1 cd13609
Substrate-binding domain of putative ABC-type osmoprotectant uptake system; the type 2 ...
27-299 6.29e-53

Substrate-binding domain of putative ABC-type osmoprotectant uptake system; the type 2 periplasmic-binding protein fold; This group includes the periplasmic substrate-binding component of a putative ABC transport system that is predicted to be involved in uptake of osmoprotectants (also termed compatible solutes) such as betaine, choline, proline betaine, carnitine, and L-proline. The relative substrate preference of this group is not known. To counteract the efflux of water, many microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding 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: 270327  Cd Length: 263  Bit Score: 173.94  E-value: 6.29e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  27 VKVGSKIDTEGALLGNIILQVLESHGVPTVN-KVQLGTTPVVRGAITSGELDIYPEYTGNG-AFFFKDENDTvwkNAQQG 104
Cdd:cd13609    2 IVIGSKNFTEQLILGNMYADLIEANTDIKVErKLNLGGSSVCFSALKNGDIDMYVDYTGTIlVNILKEPPIS---DPDEV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 105 YEKVKKLDAEQNKLIWLTPAPANNTWTIAVRQDVAEKNKLTSLAELSRYlkeGGNFKLAASAEFIERADALPAFEKAYGF 184
Cdd:cd13609   79 YNTVKELMKEKYNLEVLKPLGFNNTYTLAVRKETAEKYNLKTISDLAKV---SDELTLGCTLEFLNREDGLPGLEKTYGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 185 KLGqdQLLSLAGGdtavtIKAAAQQTSGVNAAMAYGTDGPVAALGLQTLSDPQGVQPIYAPAPVGRESVLKEYPQmaqwL 264
Cdd:cd13609  156 NFK--DVKGLDGS-----LRYTALENGEVDVIDAFSTDGLLKKFDLVVLEDDKNFFPPYYAVPLVREETLEKYPE----L 224
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 519083150 265 RPVFASL----DEKTLQQLNASIAVEGLDAKKVAADYLK 299
Cdd:cd13609  225 EDVLNKLagkiSEETMRELNYKVDELGKDPEDVAHEFLV 263
PBP2_ProWY cd13615
Substrate-binding domain of ABC-type osmoregulated transporter; the type 2 periplasmic-binding ...
26-299 3.33e-52

Substrate-binding domain of ABC-type osmoregulated transporter; the type 2 periplasmic-binding protein fold; Osmoprotectant binding lipoprotein ProWY of Streptococcus thermophilus is predicted to be involved in uptake of compatible solutes such as choline, L-proline and glycine betaine, but the relative substrate preference is not known. To counteract the efflux of water, microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. ProWY 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: 270333  Cd Length: 262  Bit Score: 172.24  E-value: 3.33e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  26 PVKVGSKIDTEGALLGNIILQVLESHGVPTVNKVQLGTTpVVRGAITSGELDIYPEYTGNGAFFFKDENDTvwKNAQQGY 105
Cdd:cd13615    1 AIRVGSKDFTENLIVAEIYALALEDAGYKVKRKPNISSS-VVHQALTSGQIDLYPEYTGTGLLAVLKKEAI--TDPQKVY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 106 EKVKKLDAEQNKLIWLTPAPANNTWTIAVRQDVAEKNKLTSLAELSrylKEGGNFKLAASAEFIERADALPAFEKAYG-- 183
Cdd:cd13615   78 ATVKDGYAKKFNLVWLDYAPANDGQGLVIRTSVAKKYGIKTISDLQ---KNASQIRFASQGEFDQREDGLPGLEKVYGkf 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 184 -FKLGQDQllslaggDTAVTIKAAAQQTSgvNAAMAYGTDGPVAALGLQTLSDPQGVQPIYAPAPVGRESVLKEYPQMAQ 262
Cdd:cd13615  155 sFKSTKVY-------DNGLKYQVLANDKA--DITPAYTTEGQLDTSKFTLLKDDKHVWPPYNLAPVVRKDVLKANPKIAS 225
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 519083150 263 WLRPVFASLDEKTLQQLNASIAVEGLDAKKVAADYLK 299
Cdd:cd13615  226 ALNKVSAKLTTKTLTQLNAKVDVDKQEYADVAKDFYL 262
PBP2_Opu_like_2 cd13613
Substrate-binding domain of putative ABC-type osmoprotectant uptake system; the type 2 ...
26-299 3.85e-49

Substrate-binding domain of putative ABC-type osmoprotectant uptake system; the type 2 periplasmic-binding protein fold; This group includes the periplasmic substrate-binding component of a putative ABC transport system that is predicted to be involved in uptake of osmoprotectants (also termed compatible solutes) such as betaine, choline, proline betaine, carnitine, and L-proline. The relative substrate preference of this group is not known. To counteract the efflux of water, many microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding 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: 270331  Cd Length: 264  Bit Score: 164.43  E-value: 3.85e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  26 PVKVGSKIDTEGALLGNIILQVLESHGVPTVN-KVQLGTTPVVRGAITSGELDIYPEYTGNG--AFFFKDendtVWKNAQ 102
Cdd:cd13613    1 RIIIGSKNFTEQVILGELLAQQIEARTDLKVErRFNLGGTFICHQALLSGAIDAYVEYTGTAltAILKQP----PIRDPQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 103 QGYEKVKKLDAEQNKLIWLTPAPANNTWTIAVRQDVAEKNKLTSLAELSRYLKeggNFKLAASAEFIERADALPAFEKAY 182
Cdd:cd13613   77 RVYEQVKQLYADRFGLEVMPPLGFENTFAILVRGEDARKLGLKTLSDAAPYTP---GWRAGFGYEFLERADGYPGLAKTY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 183 GFKLGQD-QLLslaggDTAVTIKAAAQQTsgVNAAMAYGTDGPVAALGLQTLSDPQGVQPIYAPAPVGRESVLKEYPQma 261
Cdd:cd13613  154 GLKFAKTpRVM-----DLGLLYRALAQKQ--VDLIAGNSTDGLIAALDLVILEDDRHYFPPYQAVPVVRQATLAKYPE-- 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 519083150 262 qwLRPVFASLDEK----TLQQLNASIAVEGLDAKKVAADYLK 299
Cdd:cd13613  225 --LRTAIAELAGKisaeTMQQMNYQVDGEHRDVAEVAREFLK 264
PBP2_ProWX cd13612
Substrate-binding protein ProWX of ABC-type osmoregulated transporter and its related proteins; ...
26-302 2.43e-44

Substrate-binding protein ProWX of ABC-type osmoregulated transporter and its related proteins; the type 2 periplasmic-binding protein fold; Osmoprotectant binding lipoprotein ProWX of Helicobacter pylori is predicted to be involved in uptake of compatible solutes such as choline, L-proline and glycine betaine, but the relative substrate preference is not known. To counteract the efflux of water, microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. ProWX 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: 270330  Cd Length: 267  Bit Score: 152.01  E-value: 2.43e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  26 PVKVGSKIDTEGALLGNIILQVLESHGVPTVNKVQL--GTTPVVRGAITSGELDIYPEYTGNG-AFFFKDEN---DTVWK 99
Cdd:cd13612    1 TIHIATKPMTEQYILGEMLKQLIEQDTDLKVELTKGvgGGTSNIHPAMVKGEFDLYPEYTGTGwLFVLKKDGtysEELFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 100 NAQQGYEkvkkldaEQNKLIWLTPAPANNTWTIAVRQDVAEKNKLTSLAELSRYlkeGGNFKLAASAEFIERADALPAFE 179
Cdd:cd13612   81 QLQKEYE-------EKYNLTWLGLYGFNNTYGLAVRKELAEKYNLKTYSDLAKV---SNQLVFGAEYDFFEREDGYDALQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 180 KAYGFKLGQDQllslaggDTAVTIKAAAQQTSGVNAAMAYGTDGPVAALGLQTLSDPQGVQPIYAPAPVGRESVLKEYPQ 259
Cdd:cd13612  151 KAYGFNFKKTV-------DMDIGLKYQAIESGKVDVINVFTTDGQLSDADIVVLEDDKGFFPSYYAGTVVREETLEKYPE 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 519083150 260 MAQWLRPVFASLDEKTLQQLNASIAVEGLDAKKVAADYLKQKG 302
Cdd:cd13612  224 LEDVLEKLTGLISDEDMAEMNYQVEIEKKDPKDVAKEFLEEKG 266
PBP2_AfProX_like cd13607
Substrate-binding protein ProX of ABC-type osmoregulatory transporter from Archaeoglobus ...
26-299 3.06e-44

Substrate-binding protein ProX of ABC-type osmoregulatory transporter from Archaeoglobus fulgidus and its related proteins; the type 2 periplasmic-binding protein fold; This subfamily includes the periplasmic substrate-binding protein ProX from the hyperthermophilic archaeon Archaeoglobus fulgidus and its related proteins. AfProX is involved in uptake of compatible solutes such as the trimethylammonium compound glycine betaine and the dimethylammonium compound proline betaine, but the relative substrate preference is not known. To counteract the efflux of water, many microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. AfProX 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: 270325  Cd Length: 261  Bit Score: 151.58  E-value: 3.06e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  26 PVKVGSKIDTEGALLGNIILQVLESHGVPTVNKVQLGTTPVVRGAITSGELDIYPEYTGngafffkdendTVWKNA---- 101
Cdd:cd13607    1 TVVIGSKTFTEQYILAEMIAQLLEEAGYPAEHREGLGGTRVLFEALKSGEIDVYVEYTG-----------TLYAEIlkrp 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 102 -----QQGYEKVKKLDAEQNKLIwLTPAPANNTWTIAVRQDVAEKNKLTSLAELSRYLKEggnFKLAASAEFIERADALP 176
Cdd:cd13607   70 etwdpAAVLAELKEALAERGIVV-AGPLGFENTYALAMREDRAEALGIRTISDLLARAPD---LRFGFDPEFLDRPDGWP 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 177 AFEKAYGfkLGQDQLLSLaggDTAVTIKAAAqqtSG-VNAAMAYGTDGPVAALGLQTLSDPQGVQPIYAPAPVGRESVLK 255
Cdd:cd13607  146 ALRRVYG--LPFKEVRGL---DHTLAYRALK---SGqVDVIDAYTTDARIDAYDLRVLEDDRGAFPPYDAVLLYRADLAE 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 519083150 256 EYPQMAQWLRPVFASLDEKTLQQLNASIAVEGLDAKKVAADYLK 299
Cdd:cd13607  218 RAPKAVAALRRLEGRIDADTMRALNAQVDLEKRSEAEVAAEFLA 261
PBP2_ChoS cd13610
Substrate-binding domain ChoS of an osmoregulated ABC-type transporter and related proteins; ...
29-299 9.16e-41

Substrate-binding domain ChoS of an osmoregulated ABC-type transporter and related proteins; type 2 periplasmic-binding protein fold; Osmoprotectant binding lipoprotein ChoS of Lactococcus lactis is predicted to be involved in uptake of compatible solutes such as choline and glycine betaine, but the relative substrate preference is not known. To counteract the efflux of water, microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. ChoS 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: 270328  Cd Length: 264  Bit Score: 142.34  E-value: 9.16e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  29 VGSKIDTEGALLGNIILQVLESHGVP-TVN-KVQLGTTPVVRGAITSGELDIYPEYTGnGAFFFKDENDTVWKNAQQGYE 106
Cdd:cd13610    4 IAGKLGSEPDILINMYKLLIEEETPDlQVTlKPNFGKTSFLFNALKSGDIDIYPEFTG-TVLETLLKEPPKSNDPMEVYE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 107 KVKKLDAEQNKLIWLTPAPANNTWTIAVRQDVAEKNKLTSLAELSRYLkegGNFKLAASAEFIERADALPAFEKAYGFKL 186
Cdd:cd13610   83 QARDGLAKQYQLTYLKPMAYNNTYALAVKKEFAKQHNLKTISDLQKVQ---DKLKAGFTLEFMDREDGYKGLQKAYGLNF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 187 gqdQLLSLaggDTAVTIKAAAQQTsgVNAAMAYGTDGPVAALGLQTLSDPQGVQPIYAPAPVGRESVLKEYPQMAQWLRP 266
Cdd:cd13610  160 ---NVKSM---EPALRYQAINNGQ--VNVIDAYSTDSEIKQYDLVVLKDDKHLFPPYQGAPLMREEFLKKHPELVKALNK 231
                        250       260       270
                 ....*....|....*....|....*....|...
gi 519083150 267 VFASLDEKTLQQLNASIAVEGLDAKKVAADYLK 299
Cdd:cd13610  232 LAGKITDEEMQEMNYRVDVKHKSAAKVAKEYLQ 264
PBP2_OpuCC_like cd13608
Substrate-binding protein OpuCC of ABC-type osmoregulatory transporter and related proteins; ...
26-299 7.82e-36

Substrate-binding protein OpuCC of ABC-type osmoregulatory transporter and related proteins; the type 2 periplasmic-binding protein fold; This subfamily includes the periplasmic substrate-binding protein OpuCC of the ABC transporter OpuC (where Opu is osmoprotectant uptake), which can recognize a broad spectrum of compatible solutes, and its paralog OpuBC that can solely bind choline. To counteract the efflux of water, many microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding 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: 270326  Cd Length: 265  Bit Score: 129.67  E-value: 7.82e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  26 PVKVGSKIDTEGALLGNIILQVLESHGVPTVNKV-QLGTTPVVRGAITSGELDI-YPEYTG---NGAFFFKDENDTvwkn 100
Cdd:cd13608    1 TIRIGSQSTTESQILAEMVKQLIEHYTDLKVELInNLGSSTVQHQAMLNGDANIsAARYTGtdlTGELGMEPIKDP---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 101 aQQGYEKVKKLDAEQNKLIWLTPAPANNTWTIAVRQDVAEKNKLTSLAELSRYLKeggNFKLAASAEFIER-ADALPAFE 179
Cdd:cd13608   77 -EKALKVVQKEFQKRFDQTWFDSYGFANTYAFMVTKEFAEKYNLKKVSDLKKVAD---NLKLGVDTSWLNRkGDGYPGFK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 180 KAYGFKLGQdqllsLAGGDTAVTIKAAAQQTsgVNAAMAYGTDGPVAALGLQTLSDPQGVQPIYAPAPVGRESVLKEYPQ 259
Cdd:cd13608  153 ETYGFDFGT-----VYPMQIGLVYDAVASGK--MDVVLGYSTDGRIKSYDLVVLEDDKQFFPPYDASPVATNEILKKYPE 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 519083150 260 MAQWLRPVFASLDEKTLQQLNASIAVEGLDAKKVAADYLK 299
Cdd:cd13608  226 LEEILEKLEGKISTETMQELNYQVDNDLKEPSVVAKEFLE 265
PBP2_ProX_like cd13606
Bacterial substrate-binding protein ProX of ABC-type osmoregulated transporter and its related ...
26-299 6.95e-33

Bacterial substrate-binding protein ProX of ABC-type osmoregulated transporter and its related proteins; the type 2 periplasmic-binding protein fold; This group includes periplasmic substrate-binding component of ABC transport systems from gram-negative and -positive bacteria that are involved in uptake of osmoprotectants (also termed compatible solutes) such as betaine, choline, proline betaine, carnitine, and L-proline. To counteract the efflux of water, many microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding 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: 270324  Cd Length: 260  Bit Score: 121.90  E-value: 6.95e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150  26 PVKVGSKIDTEGALLGNIILQVLESHGVPTVNKVQLGTTPVVRGAITSGELDIYPEYTGNGAFFFKDENDTvwKNAQQGY 105
Cdd:cd13606    1 TVVVGSADFPESEILAEIYAQALEAAGVKVTRKLNIGSREVYLPALEDGSIDLVPEYTGNLLQYLDKDATA--TDPEEVY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 106 EKVKKLDAEqnKLIWLTPAPANNTWTIAVRQDVAEKNKLTSLAELSrylKEGGNFKLAASAEFIERADALPAFEKAYGFK 185
Cdd:cd13606   79 AALKAALPE--GLEVLDPSPAEDKDALVVTKETAEKYGLKSIADLA---PVAGELTLGGPPEFKTRPYGLPGLKEVYGVT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519083150 186 LGQDQLLSLAGgdtAVTIKAAAQQTsgVNAAMAYGTDGPVAALGLQTLSDPQGVQPIYAPAPVGRESVLKeyPQMAQWLR 265
Cdd:cd13606  154 FKEFKPLDAGG---PLTVKALKDGT--VQVANIFTTDPAIADNGLVVLEDPKNLFPAQNVVPLVRKAKLD--DKAADALN 226
                        250       260       270
                 ....*....|....*....|....*....|....
gi 519083150 266 PVFASLDEKTLQQLNASIAVEGLDAKKVAADYLK 299
Cdd:cd13606  227 AVSAKLTTEDLTELNKQVVGDKADPADVAKEWLK 260
 
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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