NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|355398085|gb|AER67514|]
View 

Substrate-binding region of ABC-type glycine betaine transport system [Thermovirga lienii DSM 17291]

Protein Classification

osmoprotectant ABC transporter substrate-binding protein( domain architecture ID 10194462)

osmoprotectant ABC transporter substrate-binding protein serves as the initial receptor in the uptake of osmoprotectants such as glycine betaine, carnitine, or choline

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PBP2_OpuCC_like cd13608
Substrate-binding protein OpuCC of ABC-type osmoregulatory transporter and related proteins; ...
38-300 6.14e-139

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: 393.14  E-value: 6.14e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  38 TIRVGGQTVNESVILAWMAKLLLDEYTGLDVKINTEFAASSVLHQAMAQGELDV-YPSWTGTQLMGILRYEgPKLSSEET 116
Cdd:cd13608    1 TIRIGSQSTTESQILAEMVKQLIEHYTDLKVELINNLGSSTVQHQAMLNGDANIsAARYTGTDLTGELGME-PIKDPEKA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 117 FKMVKEGFEKNFDMTWAKPIGFNNTYVMTVRSETAEKYNLHKASDLKGVAEKMKLGCDENFDTRP-DAYPGWSEAYGITF 195
Cdd:cd13608   80 LKVVQKEFQKRFDQTWFDSYGFANTYAFMVTKEFAEKYNLKKVSDLKKVADNLKLGVDTSWLNRKgDGYPGFKETYGFDF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 196 KEVVPMQYAMMYKAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKGFFPDYSAAYVIDMKTLKKYPAILPILEKLSGKIDE 275
Cdd:cd13608  160 GTVYPMQIGLVYDAVASGKMDVVLGYSTDGRIKSYDLVVLEDDKQFFPPYDASPVATNEILKKYPELEEILEKLEGKIST 239
                        250       260
                 ....*....|....*....|....*.
gi 355398085 276 KTMSSLNGRYDN-GEEPEDIAEEFLE 300
Cdd:cd13608  240 ETMQELNYQVDNdLKEPSVVAKEFLE 265
 
Name Accession Description Interval E-value
PBP2_OpuCC_like cd13608
Substrate-binding protein OpuCC of ABC-type osmoregulatory transporter and related proteins; ...
38-300 6.14e-139

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: 393.14  E-value: 6.14e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  38 TIRVGGQTVNESVILAWMAKLLLDEYTGLDVKINTEFAASSVLHQAMAQGELDV-YPSWTGTQLMGILRYEgPKLSSEET 116
Cdd:cd13608    1 TIRIGSQSTTESQILAEMVKQLIEHYTDLKVELINNLGSSTVQHQAMLNGDANIsAARYTGTDLTGELGME-PIKDPEKA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 117 FKMVKEGFEKNFDMTWAKPIGFNNTYVMTVRSETAEKYNLHKASDLKGVAEKMKLGCDENFDTRP-DAYPGWSEAYGITF 195
Cdd:cd13608   80 LKVVQKEFQKRFDQTWFDSYGFANTYAFMVTKEFAEKYNLKKVSDLKKVADNLKLGVDTSWLNRKgDGYPGFKETYGFDF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 196 KEVVPMQYAMMYKAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKGFFPDYSAAYVIDMKTLKKYPAILPILEKLSGKIDE 275
Cdd:cd13608  160 GTVYPMQIGLVYDAVASGKMDVVLGYSTDGRIKSYDLVVLEDDKQFFPPYDASPVATNEILKKYPELEEILEKLEGKIST 239
                        250       260
                 ....*....|....*....|....*.
gi 355398085 276 KTMSSLNGRYDN-GEEPEDIAEEFLE 300
Cdd:cd13608  240 ETMQELNYQVDNdLKEPSVVAKEFLE 265
OsmF COG1732
Periplasmic glycine betaine/choline-binding (lipo)protein of an ABC-type transport system ...
1-301 2.05e-114

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: 332.11  E-value: 2.05e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085   1 MRYFMKVLCLTLLVLSVSVVGGIGVAVAnqdpmeyKGTIRVGGQTVNESVILAWMAKLLLdEYTGLDVKINTEFAASSVL 80
Cdd:COG1732    1 MKRLLLLALALAAALALAGCGLASAAAA-------GDTIVVGSKNFTEQEILAEIYAQAL-EAAGLKVERKLNLGGTEVV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  81 HQAMAQGELDVYPSWTGTQLMGILRYEgPKLSSEETFKMVKEGFEKNFDMTWAKPIGFNNTYVMTVRSETAEKYNLHKAS 160
Cdd:COG1732   73 RQALKSGEIDLYPEYTGTALTTYLKED-PITDPEEVYEAVKEALPEKNGLTWLDPAGFNNTYALAVTKETAEKYGLKTIS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 161 DLKGVAEKMKLGCDENFDTRPDAYPGWSEAYGITFKEVVPMQYAMMYKAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKG 240
Cdd:COG1732  152 DLAKVAGELTLGADPEFAERPDGLPGLKKAYGFEFKEVKPMDTGLTYTALANGQVDVADAYTTDGRIAALDLVVLEDDKN 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 355398085 241 FFPDYSAAYVIDMKTLKKYPAILPILEKLSGKIDEKTMSSLNGRYD-NGEEPEDIAEEFLEE 301
Cdd:COG1732  232 FFPPYNAAPLVRKEVLEKYPELAEVLNKLSGKLTTETMQELNYQVDvDGEDPADVAREFLKE 293
OpuAC pfam04069
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity ...
37-301 1.53e-57

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: 185.61  E-value: 1.53e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085   37 GTIRVGGQTVNESVILAWMAKLLLDEyTGLDVKInTEFAASSVLHQAMAQGELDVYPS-WTGTqlmgilryegpklssee 115
Cdd:pfam04069   1 KTIVIGSKNWTEQEILANIAAQLLEA-LGYVVEL-VGLGSSAVLFAALASGDIDLYPEeWTGT----------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  116 TFKMVKEGFEKNFDMTWAKPIGFNNTYVMTVRSETAEKYNLHKASDLKGVAEKMKLGCDENFDTRPDAYPGWS------E 189
Cdd:pfam04069  62 TYEAYKKAVEEKLGLLVLGPLGAGNTYGLAVPKYVAEKPGIKSISDLAKPADDLELGFKGEFIGRPDGWGCMRstegllK 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  190 AYGITFKEVVPMQYAMM----YKAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKGFFPD-YSAAYVIDMKTLKKYPAILP 264
Cdd:pfam04069 142 AYGLDKYELVEGSEAAMdaliYAAYKRGEPDVVYAWTPDWMIKKYDLVVLEDPKGLFPPaYNVVPVVRKGFAEKHPEVAA 221
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 355398085  265 ILEKLSgkIDEKTMSSLNGRYD-NGEEPEDIAEEFLEE 301
Cdd:pfam04069 222 FLNKLS--LDTEDLNELNAQVDvEGKDPEEVAKDWLAE 257
 
Name Accession Description Interval E-value
PBP2_OpuCC_like cd13608
Substrate-binding protein OpuCC of ABC-type osmoregulatory transporter and related proteins; ...
38-300 6.14e-139

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: 393.14  E-value: 6.14e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  38 TIRVGGQTVNESVILAWMAKLLLDEYTGLDVKINTEFAASSVLHQAMAQGELDV-YPSWTGTQLMGILRYEgPKLSSEET 116
Cdd:cd13608    1 TIRIGSQSTTESQILAEMVKQLIEHYTDLKVELINNLGSSTVQHQAMLNGDANIsAARYTGTDLTGELGME-PIKDPEKA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 117 FKMVKEGFEKNFDMTWAKPIGFNNTYVMTVRSETAEKYNLHKASDLKGVAEKMKLGCDENFDTRP-DAYPGWSEAYGITF 195
Cdd:cd13608   80 LKVVQKEFQKRFDQTWFDSYGFANTYAFMVTKEFAEKYNLKKVSDLKKVADNLKLGVDTSWLNRKgDGYPGFKETYGFDF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 196 KEVVPMQYAMMYKAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKGFFPDYSAAYVIDMKTLKKYPAILPILEKLSGKIDE 275
Cdd:cd13608  160 GTVYPMQIGLVYDAVASGKMDVVLGYSTDGRIKSYDLVVLEDDKQFFPPYDASPVATNEILKKYPELEEILEKLEGKIST 239
                        250       260
                 ....*....|....*....|....*.
gi 355398085 276 KTMSSLNGRYDN-GEEPEDIAEEFLE 300
Cdd:cd13608  240 ETMQELNYQVDNdLKEPSVVAKEFLE 265
OsmF COG1732
Periplasmic glycine betaine/choline-binding (lipo)protein of an ABC-type transport system ...
1-301 2.05e-114

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: 332.11  E-value: 2.05e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085   1 MRYFMKVLCLTLLVLSVSVVGGIGVAVAnqdpmeyKGTIRVGGQTVNESVILAWMAKLLLdEYTGLDVKINTEFAASSVL 80
Cdd:COG1732    1 MKRLLLLALALAAALALAGCGLASAAAA-------GDTIVVGSKNFTEQEILAEIYAQAL-EAAGLKVERKLNLGGTEVV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  81 HQAMAQGELDVYPSWTGTQLMGILRYEgPKLSSEETFKMVKEGFEKNFDMTWAKPIGFNNTYVMTVRSETAEKYNLHKAS 160
Cdd:COG1732   73 RQALKSGEIDLYPEYTGTALTTYLKED-PITDPEEVYEAVKEALPEKNGLTWLDPAGFNNTYALAVTKETAEKYGLKTIS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 161 DLKGVAEKMKLGCDENFDTRPDAYPGWSEAYGITFKEVVPMQYAMMYKAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKG 240
Cdd:COG1732  152 DLAKVAGELTLGADPEFAERPDGLPGLKKAYGFEFKEVKPMDTGLTYTALANGQVDVADAYTTDGRIAALDLVVLEDDKN 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 355398085 241 FFPDYSAAYVIDMKTLKKYPAILPILEKLSGKIDEKTMSSLNGRYD-NGEEPEDIAEEFLEE 301
Cdd:COG1732  232 FFPPYNAAPLVRKEVLEKYPELAEVLNKLSGKLTTETMQELNYQVDvDGEDPADVAREFLKE 293
PBP2_osmoprotectants cd13528
Substrate-binding domain of osmoregulatory ABC-type transporters; the type 2 ...
38-300 5.31e-107

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: 312.22  E-value: 5.31e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  38 TIRVGGQTVNESVILAWMAKLLLDEYTGLDVKINTEFAASSVLHQAMAQGELDVYPSWTGTQLMGILRYEGPKLSSEETF 117
Cdd:cd13528    1 TIVVGSKNFTEQYILGEMLAQLLEANTDLTVERKLNLGGTEVAFNALKNGDIDLYVEYTGTALLTILKEDAPITDPEEVY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 118 KMVKEGFEKNFDMTWAKPIGFNNTYVMTVRSETAEKYNLHKASDLKGVAEKMKLGCDENFDTRPDAYPGWSEAYGITFKE 197
Cdd:cd13528   81 EKVKKEYEEKFGLTWLDPLGFNNTYALAVRKDTAEKYGLKTISDLAPHSDQLVFGADPEFYERSDGLPGLKKTYGFDFKE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 198 VVPMQYAMMYKAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKGFFPDYSAAYVIDMKTLKKYPAILPILEKLSGKIDEKT 277
Cdd:cd13528  161 VKTMDPGLTYEALDNGEVDVIDAFSTDGRIKAFDLVVLEDDKNFFPPYNAAPVVREDVLKKHPELEEVLNKLSGKLTDET 240
                        250       260
                 ....*....|....*....|....
gi 355398085 278 MSSLNGRYD-NGEEPEDIAEEFLE 300
Cdd:cd13528  241 MQQLNYQVDvEGKDPEEVARDFLK 264
PBP2_Opu_like_1 cd13609
Substrate-binding domain of putative ABC-type osmoprotectant uptake system; the type 2 ...
38-300 6.37e-98

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: 289.12  E-value: 6.37e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  38 TIRVGGQTVNESVILAWMAKLLLDEYTGLDVKINTEFAASSVLHQAMAQGELDVYPSWTGTQLMGILRYEgPKLSSEETF 117
Cdd:cd13609    1 TIVIGSKNFTEQLILGNMYADLIEANTDIKVERKLNLGGSSVCFSALKNGDIDMYVDYTGTILVNILKEP-PISDPDEVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 118 KMVKEGFEKNFDMTWAKPIGFNNTYVMTVRSETAEKYNLHKASDLKGVAEKMKLGCDENFDTRPDAYPGWSEAYGITFKE 197
Cdd:cd13609   80 NTVKELMKEKYNLEVLKPLGFNNTYTLAVRKETAEKYNLKTISDLAKVSDELTLGCTLEFLNREDGLPGLEKTYGLNFKD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 198 VVPMQYAMMYKAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKGFFPDYSAAYVIDMKTLKKYPAILPILEKLSGKIDEKT 277
Cdd:cd13609  160 VKGLDGSLRYTALENGEVDVIDAFSTDGLLKKFDLVVLEDDKNFFPPYYAVPLVREETLEKYPELEDVLNKLAGKISEET 239
                        250       260
                 ....*....|....*....|....
gi 355398085 278 MSSLNGRYDN-GEEPEDIAEEFLE 300
Cdd:cd13609  240 MRELNYKVDElGKDPEDVAHEFLV 263
PBP2_ProWX cd13612
Substrate-binding protein ProWX of ABC-type osmoregulated transporter and its related proteins; ...
38-304 4.26e-86

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: 259.09  E-value: 4.26e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  38 TIRVGGQTVNESVILAWMAKLLLDEYTGLDVKINTEFAA-SSVLHQAMAQGELDVYPSWTGTQLMGILRYEGPklSSEET 116
Cdd:cd13612    1 TIHIATKPMTEQYILGEMLKQLIEQDTDLKVELTKGVGGgTSNIHPAMVKGEFDLYPEYTGTGWLFVLKKDGT--YSEEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 117 FKMVKEGFEKNFDMTWAKPIGFNNTYVMTVRSETAEKYNLHKASDLKGVAEKMKLGCDENFDTRPDAYPGWSEAYGITFK 196
Cdd:cd13612   79 FDQLQKEYEEKYNLTWLGLYGFNNTYGLAVRKELAEKYNLKTYSDLAKVSNQLVFGAEYDFFEREDGYDALQKAYGFNFK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 197 EVVPMQYAMMYKAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKGFFPDYSAAYVIDMKTLKKYPAILPILEKLSGKIDEK 276
Cdd:cd13612  159 KTVDMDIGLKYQAIESGKVDVINVFTTDGQLSDADIVVLEDDKGFFPSYYAGTVVREETLEKYPELEDVLEKLTGLISDE 238
                        250       260
                 ....*....|....*....|....*....
gi 355398085 277 TMSSLNGRYD-NGEEPEDIAEEFLEEIGL 304
Cdd:cd13612  239 DMAEMNYQVEiEKKDPKDVAKEFLEEKGL 267
PBP2_QAT_like cd13614
Substrate-binding domain of quaternary amine ABC-type transporter; the type 2 ...
38-300 2.34e-78

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: 239.21  E-value: 2.34e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  38 TIRVGGQTVNESVILAWMAKLLLDEyTGLDVKINTEFAASSVLHQAMAQGELDVYPSWTGTQLMGILRYEgPKLSSEETF 117
Cdd:cd13614    1 AIRVGSKNFTEQFILGEMYALALED-AGIKVERKLNLGGTLIAHQALVNGEIDLYPEYTGTALLTVLKGE-PSSDAKQVY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 118 KMVKEGFEKNFDMTWAKPIGFNNTYVMTVRSETAEKYNLHKASDLKGVAEKMKLGCDENFDTRPDAYPGWSEAYGI-TFK 196
Cdd:cd13614   79 KTVKDAYAEQFQLTWLEPAPFNNTYALVMTRETAEKYGIKTLSDLAKAAGELVFGGGPEFQDREDGLPGLKAKYGAfDFK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 197 EVVPM-QYAMMYKAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKGFFPDYSAAYVIDMKTLKKYPAILPILEKLSGKIDE 275
Cdd:cd13614  159 EFVQVdPLGLRYQALAQGQIDVAVGFGTDGQIAAYGLVVLEDDKNLFPPYQVAPVVRQDVLDANPKIAEVLNKLSALLDN 238
                        250       260
                 ....*....|....*....|....*.
gi 355398085 276 KTMSSLNGRYD-NGEEPEDIAEEFLE 300
Cdd:cd13614  239 ETMQRLNYEVDgNKREPKDVAREFLK 264
PBP2_Opu_like_2 cd13613
Substrate-binding domain of putative ABC-type osmoprotectant uptake system; the type 2 ...
38-299 1.07e-73

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: 227.22  E-value: 1.07e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  38 TIRVGGQTVNESVILAWMAKLLLDEYTGLDVKINTEFAASSVLHQAMAQGELDVYPSWTGTQLMGILRyEGPKLSSEETF 117
Cdd:cd13613    1 RIIIGSKNFTEQVILGELLAQQIEARTDLKVERRFNLGGTFICHQALLSGAIDAYVEYTGTALTAILK-QPPIRDPQRVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 118 KMVKEGFEKNFDMTWAKPIGFNNTYVMTVRSETAEKYNLHKASDLKGVAEKMKLGCDENFDTRPDAYPGWSEAYGI-TFK 196
Cdd:cd13613   80 EQVKQLYADRFGLEVMPPLGFENTFAILVRGEDARKLGLKTLSDAAPYTPGWRAGFGYEFLERADGYPGLAKTYGLkFAK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 197 EVVPMQYAMMYKAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKGFFPDYSAAYVIDMKTLKKYPAILPILEKLSGKIDEK 276
Cdd:cd13613  160 TPRVMDLGLLYRALAQKQVDLIAGNSTDGLIAALDLVILEDDRHYFPPYQAVPVVRQATLAKYPELRTAIAELAGKISAE 239
                        250       260
                 ....*....|....*....|....
gi 355398085 277 TMSSLNGRYDN-GEEPEDIAEEFL 299
Cdd:cd13613  240 TMQQMNYQVDGeHRDVAEVAREFL 263
PBP2_YehZ cd13611
Substrate-binding domain YehZ of an osmoregulated ABC-type transporter; the type 2 ...
38-300 2.18e-73

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: 226.70  E-value: 2.18e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  38 TIRVGGQTVNESVILAWMAKLLLDEyTGLDVKINTEFAASSVLHQAMAQGELDVYPSWTGTQLMGILRYEGPKLSSEETF 117
Cdd:cd13611    1 TITVGSKDFTEQLILGKITVQALQA-AGADVTDKTNLGGSASARQALENGQVDVYWEYTGTAWITYLGHTEPILDPQEQY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 118 KMVKEGFEKNfDMTWAKPIGFNNTYVMTVRSETAEKYNLHKASDLKGVA---EKMKLGCDENFDTRPDAYPGWSEAYGIT 194
Cdd:cd13611   80 EAVKDLDAEK-GLVWLDPAPLNNTYALAMREATAEELGITTLSDLALAKlppGDRTFCVDAEFASRPDGLPPLLEAYGFE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 195 F--KEVVPMQYAMMYKAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKGFFPDYSAAYVIDMKTLKKYPAILPILEKLSGK 272
Cdd:cd13611  159 FprANVRQMDTGLVYTATANGQCDFGEVFTTDGRIKALDLVVLEDDKGFFPAYNAAPVVRTEVLDAHPELAEILNPISAK 238
                        250       260
                 ....*....|....*....|....*....
gi 355398085 273 IDEKTMSSLNGRYD-NGEEPEDIAEEFLE 300
Cdd:cd13611  239 LDNDTMQELNARVDvDGEDPADVARDWLV 267
PBP2_AfProX_like cd13607
Substrate-binding protein ProX of ABC-type osmoregulatory transporter from Archaeoglobus ...
38-300 2.12e-72

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: 224.00  E-value: 2.12e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  38 TIRVGGQTVNESVILAWMAKLLLDEyTGLDVKINTEFAASSVLHQAMAQGELDVYPSWTGT---QLMGILRYEGPKLSSE 114
Cdd:cd13607    1 TVVIGSKTFTEQYILAEMIAQLLEE-AGYPAEHREGLGGTRVLFEALKSGEIDVYVEYTGTlyaEILKRPETWDPAAVLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 115 EtfkmVKEGFEKNfDMTWAKPIGFNNTYVMTVRSETAEKYNLHKASDLKGVAEKMKLGCDENFDTRPDAYPGWSEAYGIT 194
Cdd:cd13607   80 E----LKEALAER-GIVVAGPLGFENTYALAMREDRAEALGIRTISDLLARAPDLRFGFDPEFLDRPDGWPALRRVYGLP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 195 FKEVVPMQYAMMYKAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKGFFPDYSAAYVIDMKTLKKYPAILPILEKLSGKID 274
Cdd:cd13607  155 FKEVRGLDHTLAYRALKSGQVDVIDAYTTDARIDAYDLRVLEDDRGAFPPYDAVLLYRADLAERAPKAVAALRRLEGRID 234
                        250       260
                 ....*....|....*....|....*..
gi 355398085 275 EKTMSSLNGRYDN-GEEPEDIAEEFLE 300
Cdd:cd13607  235 ADTMRALNAQVDLeKRSEAEVAAEFLA 261
PBP2_ChoS cd13610
Substrate-binding domain ChoS of an osmoregulated ABC-type transporter and related proteins; ...
38-300 3.40e-70

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: 218.23  E-value: 3.40e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  38 TIRVGGQTVNESVILAWMAKLLLDEYTG-LDVKINTEFAASSVLHQAMAQGELDVYPSWTGTQLMGILRYEGPKLSSEET 116
Cdd:cd13610    1 SIVIAGKLGSEPDILINMYKLLIEEETPdLQVTLKPNFGKTSFLFNALKSGDIDIYPEFTGTVLETLLKEPPKSNDPMEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 117 FKMVKEGFEKNFDMTWAKPIGFNNTYVMTVRSETAEKYNLHKASDLKGVAEKMKLGCDENFDTRPDAYPGWSEAYGITFK 196
Cdd:cd13610   81 YEQARDGLAKQYQLTYLKPMAYNNTYALAVKKEFAKQHNLKTISDLQKVQDKLKAGFTLEFMDREDGYKGLQKAYGLNFN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 197 eVVPMQYAMMYKAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKGFFPDYSAAYVIDMKTLKKYPAILPILEKLSGKIDEK 276
Cdd:cd13610  161 -VKSMEPALRYQAINNGQVNVIDAYSTDSEIKQYDLVVLKDDKHLFPPYQGAPLMREEFLKKHPELVKALNKLAGKITDE 239
                        250       260
                 ....*....|....*....|....*
gi 355398085 277 TMSSLNGRYD-NGEEPEDIAEEFLE 300
Cdd:cd13610  240 EMQEMNYRVDvKHKSAAKVAKEYLQ 264
PBP2_ProWY cd13615
Substrate-binding domain of ABC-type osmoregulated transporter; the type 2 periplasmic-binding ...
38-300 2.20e-62

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: 198.44  E-value: 2.20e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  38 TIRVGGQTVNESVILAWMAKLLLdEYTGLdvKINTEFA-ASSVLHQAMAQGELDVYPSWTGTQLMGILRyEGPKLSSEET 116
Cdd:cd13615    1 AIRVGSKDFTENLIVAEIYALAL-EDAGY--KVKRKPNiSSSVVHQALTSGQIDLYPEYTGTGLLAVLK-KEAITDPQKV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 117 FKMVKEGFEKNFDMTWAKPIGFNNTYVMTVRSETAEKYNLHKASDLKGVAEKMKLGCDENFDTRPDAYPGWSEAYGIT-F 195
Cdd:cd13615   77 YATVKDGYAKKFNLVWLDYAPANDGQGLVIRTSVAKKYGIKTISDLQKNASQIRFASQGEFDQREDGLPGLEKVYGKFsF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 196 KEVVPMQYAMMYKAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKGFFPDYSAAYVIDMKTLKKYPAILPILEKLSGKIDE 275
Cdd:cd13615  157 KSTKVYDNGLKYQVLANDKADITPAYTTEGQLDTSKFTLLKDDKHVWPPYNLAPVVRKDVLKANPKIASALNKVSAKLTT 236
                        250       260
                 ....*....|....*....|....*.
gi 355398085 276 KTMSSLNGRYD-NGEEPEDIAEEFLE 300
Cdd:cd13615  237 KTLTQLNAKVDvDKQEYADVAKDFYL 262
OpuAC pfam04069
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity ...
37-301 1.53e-57

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: 185.61  E-value: 1.53e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085   37 GTIRVGGQTVNESVILAWMAKLLLDEyTGLDVKInTEFAASSVLHQAMAQGELDVYPS-WTGTqlmgilryegpklssee 115
Cdd:pfam04069   1 KTIVIGSKNWTEQEILANIAAQLLEA-LGYVVEL-VGLGSSAVLFAALASGDIDLYPEeWTGT----------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  116 TFKMVKEGFEKNFDMTWAKPIGFNNTYVMTVRSETAEKYNLHKASDLKGVAEKMKLGCDENFDTRPDAYPGWS------E 189
Cdd:pfam04069  62 TYEAYKKAVEEKLGLLVLGPLGAGNTYGLAVPKYVAEKPGIKSISDLAKPADDLELGFKGEFIGRPDGWGCMRstegllK 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  190 AYGITFKEVVPMQYAMM----YKAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKGFFPD-YSAAYVIDMKTLKKYPAILP 264
Cdd:pfam04069 142 AYGLDKYELVEGSEAAMdaliYAAYKRGEPDVVYAWTPDWMIKKYDLVVLEDPKGLFPPaYNVVPVVRKGFAEKHPEVAA 221
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 355398085  265 ILEKLSgkIDEKTMSSLNGRYD-NGEEPEDIAEEFLEE 301
Cdd:pfam04069 222 FLNKLS--LDTEDLNELNAQVDvEGKDPEEVAKDWLAE 257
PBP2_OsmF cd13616
Substrate-binding domain OsmF of an osmoregulated ABC-type transporter; the type 2 ...
38-299 3.05e-53

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: 175.21  E-value: 3.05e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  38 TIRVGGQTVNESVILAWMAKLLLdEYTGLDVKINTEFAASSVLHQAMAQGELDVYPSWTGTQLMgILRYEGPKLS--SEE 115
Cdd:cd13616    1 PVVVGSKIDTEGALLGNMIVLAL-EAHGFPVEDKTGLGTTPVVRKALLSGEIDLYPEYTGNGAF-FFPEADDPVWkdARK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 116 TFKMVKEGFEKNFDMTWAKPIGFNNTYVMTVRSETAEKYNLHKASDL-KGVAE--KMKLGCDENFDTRPDAYPGWSEAYG 192
Cdd:cd13616   79 GYETVKELDAKNNGLVWLDPAPANNTWAIAVRRDLAEKNNLKTLADLaAYVNEggAFKLAASAEFVERPDALPAFEKAYG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 193 ITFKE----VVPM-QYAMMYKAIANKE--VDAIAAYSTDSRIAKLNLVMLEDDKGFFPDYSAAYVIDMKTLKKYPAILPI 265
Cdd:cd13616  159 FKLSKdqlvILSGgNTAQTEQAAAQGTsgVNAAMAYGTDGAIAALGLVVLEDPKGAQPVYAPAPVVRQEVLEAYPEIAEI 238
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 355398085 266 LEKLSGKIDEKTMSSLNGRYD-NGEEPEDIAEEFL 299
Cdd:cd13616  239 LKPVFATLDLKTLQELNARIAvEGESAEDVARDYL 273
PBP2_ProX_like cd13606
Bacterial substrate-binding protein ProX of ABC-type osmoregulated transporter and its related ...
38-300 4.05e-38

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: 135.39  E-value: 4.05e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  38 TIRVGGQTVNESVILAWM-AKLLldEYTGLDVKINTEFAASSVLHQAMAQGELDVYPSWTGTqlmgILRYEGPKL---SS 113
Cdd:cd13606    1 TVVVGSADFPESEILAEIyAQAL--EAAGVKVTRKLNIGSREVYLPALEDGSIDLVPEYTGN----LLQYLDKDAtatDP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 114 EETFKMVKEGFEKNFDMTWAKPIGFNNTYVmtVRSETAEKYNLHKASDLKGVAEKMKLGCDENFDTRPDAYPGWSEAYGI 193
Cdd:cd13606   75 EEVYAALKAALPEGLEVLDPSPAEDKDALV--VTKETAEKYGLKSIADLAPVAGELTLGGPPEFKTRPYGLPGLKEVYGV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 194 TFKEVVPMQY--AMMYKAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKGFFPDYSAAYVIDMKTLKkyPAILPILEKLSG 271
Cdd:cd13606  153 TFKEFKPLDAggPLTVKALKDGTVQVANIFTTDPAIADNGLVVLEDPKNLFPAQNVVPLVRKAKLD--DKAADALNAVSA 230
                        250       260       270
                 ....*....|....*....|....*....|
gi 355398085 272 KIDEKTMSSLNGRYDNG-EEPEDIAEEFLE 300
Cdd:cd13606  231 KLTTEDLTELNKQVVGDkADPADVAKEWLK 260
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
12-263 6.73e-11

ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 61.94  E-value: 6.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  12 LLVLSVSVVGGIGVAVANQDPMeykgTIRVGGQTVNESVILAWMAKL-LLDEYtGLDVKInTEFAASSVLHQAMAQGELD 90
Cdd:COG0715    1 LAALAALALAACSAAAAAAEKV----TLRLGWLPNTDHAPLYVAKEKgYFKKE-GLDVEL-VEFAGGAAALEALAAGQAD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  91 VYPSWTGTQLMGIlryegpklsseetfkmvkegfEKNFDMTWAKPIGFNNTYVMTVRsetaEKYNLHKASDLKGvaekMK 170
Cdd:COG0715   75 FGVAGAPPALAAR---------------------AKGAPVKAVAALSQSGGNALVVR----KDSGIKSLADLKG----KK 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 171 LGCDENFDTRPdAYPGWSEAYGITFKEV--VPMQYAMMYKAIANKEVDAIAAYSTD-SRIAKLNLV-MLEDDKGFFPD-Y 245
Cdd:COG0715  126 VAVPGGSTSHY-LLRALLAKAGLDPKDVeiVNLPPPDAVAALLAGQVDAAVVWEPFeSQAEKKGGGrVLADSADLVPGyP 204
                        250
                 ....*....|....*...
gi 355398085 246 SAAYVIDMKTLKKYPAIL 263
Cdd:COG0715  205 GDVLVASEDFLEENPEAV 222
PBP2_OpuAC_like cd13639
Substrate binding domain of Lactococcus lactis ABC-type transporter OpuA and related proteins; ...
204-301 2.73e-06

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: 47.53  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 204 AMMY---KAIANKEVDAIAAYSTDSRIAKLNLVMLEDDKGFFPDYSAAYVIDMKTLKK-YPAILPILEKLsgKIDEKTMS 279
Cdd:cd13639  145 AMLAeldRAIDNKEPIVVTGWSPHWMFAKYDLKYLEDPKGVYGEAESIHTIARKGFEEdHPEAYEFLKNF--KLTDEDLE 222
                         90       100
                 ....*....|....*....|..
gi 355398085 280 SLNGRYDNGEEPEDIAEEFLEE 301
Cdd:cd13639  223 SLMLEIEDGGDPEEAAEEWIDE 244
PBP2_NrtA_SsuA_CpmA_like cd01008
Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of ...
38-263 1.12e-03

Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily; This family represents the periplasmic binding proteins involved in nitrate, alkanesulfonate, and bicarbonate transport. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates. Other closest homologs involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB) are also included in this family. After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. These binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270229 [Multi-domain]  Cd Length: 212  Bit Score: 39.58  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  38 TIRVGGQTVNESVILAWM-AKLLLDEYT-GLDVKInTEFAASSVLHQAMAQGELDVypsWTGTQLMGILryegpKLSSEE 115
Cdd:cd01008    1 TVRIGYQAGPLAGPLIVAkEKGLFEKEKeGIDVEW-VEFTSGPPALEALAAGSLDF---GTGGDTPALL-----AAAGGV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 116 TFKMVkegfekNFDMTWAKPIGFnntyvmTVRSEtaekYNLHKASDLKG--VAekMKLGCDENFDTRpdaypGWSEAYGI 193
Cdd:cd01008   72 PVVLI------AALSRSPNGNGI------VVRKD----SGITSLADLKGkkIA--VTKGTTGHFLLL-----KALAKAGL 128
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 355398085 194 TFK--EVVPMQYAMMYKAIANKEVDAIAAYS--TDSRIAKLNLVMLEDDKGFFPDYSAAYVIDMKTLKKYPAIL 263
Cdd:cd01008  129 SVDdvELVNLGPADAAAALASGDVDAWVTWEpfLSLAEKGGDARIIVDGGGLPYTDPSVLVARRDFVEENPEAV 202
Periplasmic_Binding_Protein_Type_2 cd00648
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
38-248 7.38e-03

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They 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. The origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


Pssm-ID: 270214 [Multi-domain]  Cd Length: 196  Bit Score: 36.78  E-value: 7.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085  38 TIRVGGQTVNESVILAWMAKLLLDEYTGLDVKInTEFAASSVLHQAMAQGELDVYPSwtgtqlmgilryeGPKLSSEETF 117
Cdd:cd00648    1 TLTVASIGPPPYAGFAEDAAKQLAKETGIKVEL-VPGSSIGTLIEALAAGDADVAVG-------------PIAPALEAAA 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355398085 118 KMVKEGfeknfDMTWAKPIgFNNTYVMTVRsETAEKYNLHKASDLKGVaekmKLGcdenfdTRPDAYPGWSEAYGI---- 193
Cdd:cd00648   67 DKLAPG-----GLYIVPEL-YVGGYVLVVR-KGSSIKGLLAVADLDGK----RVG------VGDPGSTAVRQARLAlgay 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 355398085 194 ----TFKEVVPMQ-YAMMYKAIANKEVDAIAAYSTDS---RIAKLNLVMLEDDKG-FFPDYSAA 248
Cdd:cd00648  130 glkkKDPEVVPVPgTSGALAAVANGAVDAAIVWVPAAeraQLGNVQLEVLPDDLGpLVTTFGVA 193
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH