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Conserved domains on  [gi|1772215112|gb|QFY37211|]
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osmoprotectant ABC transporter substrate-binding protein [Bacillus paralicheniformis]

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

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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; ...
35-299 0e+00

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: 501.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  35 TIKIGAQNLTESEILANMISLLIEHDTDLNTVLVKNLGSNYVQHQAMLGGDIDISATRYSGTDLTSTLGREAEKDPEKAL 114
Cdd:cd13608     1 TIRIGSQSTTESQILAEMVKQLIEHYTDLKVELINNLGSSTVQHQAMLNGDANISAARYTGTDLTGELGMEPIKDPEKAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 115 HIVQQDFKKKFNYKWFDSYGFDNTYAFTVTKELAEKGNYETISDLKKDADKLKLGVDNAWLKRKGDGYPGFKQEYGFSFG 194
Cdd:cd13608    81 KVVQKEFQKRFDQTWFDSYGFANTYAFMVTKEFAEKYNLKKVSDLKKVADNLKLGVDTSWLNRKGDGYPGFKETYGFDFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 195 STFPMQIGLVYDAVKNGKMDIVLAYSTDGRIKAYDLKLLKDDKRFFPPYDCSPVVPEKVLKEHPELKETINKLIGKIDTE 274
Cdd:cd13608   161 TVYPMQIGLVYDAVASGKMDVVLGYSTDGRIKSYDLVVLEDDKQFFPPYDASPVATNEILKKYPELEEILEKLEGKISTE 240
                         250       260
                  ....*....|....*....|....*
gi 1772215112 275 TMQELNYEVDGKLKEPSVVAAEFLK 299
Cdd:cd13608   241 TMQELNYQVDNDLKEPSVVAKEFLE 265
 
Name Accession Description Interval E-value
PBP2_OpuCC_like cd13608
Substrate-binding protein OpuCC of ABC-type osmoregulatory transporter and related proteins; ...
35-299 0e+00

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: 501.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  35 TIKIGAQNLTESEILANMISLLIEHDTDLNTVLVKNLGSNYVQHQAMLGGDIDISATRYSGTDLTSTLGREAEKDPEKAL 114
Cdd:cd13608     1 TIRIGSQSTTESQILAEMVKQLIEHYTDLKVELINNLGSSTVQHQAMLNGDANISAARYTGTDLTGELGMEPIKDPEKAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 115 HIVQQDFKKKFNYKWFDSYGFDNTYAFTVTKELAEKGNYETISDLKKDADKLKLGVDNAWLKRKGDGYPGFKQEYGFSFG 194
Cdd:cd13608    81 KVVQKEFQKRFDQTWFDSYGFANTYAFMVTKEFAEKYNLKKVSDLKKVADNLKLGVDTSWLNRKGDGYPGFKETYGFDFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 195 STFPMQIGLVYDAVKNGKMDIVLAYSTDGRIKAYDLKLLKDDKRFFPPYDCSPVVPEKVLKEHPELKETINKLIGKIDTE 274
Cdd:cd13608   161 TVYPMQIGLVYDAVASGKMDVVLGYSTDGRIKSYDLVVLEDDKQFFPPYDASPVATNEILKKYPELEEILEKLEGKISTE 240
                         250       260
                  ....*....|....*....|....*
gi 1772215112 275 TMQELNYEVDGKLKEPSVVAAEFLK 299
Cdd:cd13608   241 TMQELNYQVDNDLKEPSVVAKEFLE 265
OsmF COG1732
Periplasmic glycine betaine/choline-binding (lipo)protein of an ABC-type transport system ...
5-301 3.06e-132

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: 377.18  E-value: 3.06e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112   5 KLRRLGAVMLVFSLLISGCALPGlGGASDKTIKIGAQNLTESEILANMISLLIEHDtDLNTVLVKNLGSNYVQHQAMLGG 84
Cdd:COG1732     2 KRLLLLALALAAALALAGCGLAS-AAAAGDTIVVGSKNFTEQEILAEIYAQALEAA-GLKVERKLNLGGTEVVRQALKSG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  85 DIDIsATRYSGTDLTSTLGREAEKDPEKALHIVQQDFKKKFNYKWFDSYGFDNTYAFTVTKELAEKGNYETISDLKKDAD 164
Cdd:COG1732    80 EIDL-YPEYTGTALTTYLKEDPITDPEEVYEAVKEALPEKNGLTWLDPAGFNNTYALAVTKETAEKYGLKTISDLAKVAG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 165 KLKLGVDNAWLKRKgDGYPGFKQEYGFSFGSTFPMQIGLVYDAVKNGKMDIVLAYSTDGRIKAYDLKLLKDDKRFFPPYD 244
Cdd:COG1732   159 ELTLGADPEFAERP-DGLPGLKKAYGFEFKEVKPMDTGLTYTALANGQVDVADAYTTDGRIAALDLVVLEDDKNFFPPYN 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1772215112 245 CSPVVPEKVLKEHPELKETINKLIGKIDTETMQELNYEVDGKLKEPSVVAAEFLKKH 301
Cdd:COG1732   238 AAPLVRKEVLEKYPELAEVLNKLSGKLTTETMQELNYQVDVDGEDPADVAREFLKEK 294
OpuAC pfam04069
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity ...
34-300 4.56e-66

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: 207.56  E-value: 4.56e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  34 KTIKIGAQNLTESEILANMISLLIEHDtDLNTVLVkNLGSNYVQHQAMLGGDIDISATRYSGTdltstlgreaekdpekA 113
Cdd:pfam04069   1 KTIVIGSKNWTEQEILANIAAQLLEAL-GYVVELV-GLGSSAVLFAALASGDIDLYPEEWTGT----------------T 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 114 LHIVQQDFKKKFNYKWFDSYGFDNTYAFTVTKELAEKGNYETISDLKKDADKLKLGVDNAWLKRkGDGYP------GFKQ 187
Cdd:pfam04069  63 YEAYKKAVEEKLGLLVLGPLGAGNTYGLAVPKYVAEKPGIKSISDLAKPADDLELGFKGEFIGR-PDGWGcmrsteGLLK 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 188 EYGFS----FGSTFPMQIGLVYDAVKNGKMDIVLAYSTDGRIKAYDLKLLKDDKRFFPP-YDCSPVVPEKVLKEHPELKE 262
Cdd:pfam04069 142 AYGLDkyelVEGSEAAMDALIYAAYKRGEPDVVYAWTPDWMIKKYDLVVLEDPKGLFPPaYNVVPVVRKGFAEKHPEVAA 221
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1772215112 263 TINKLigKIDTETMQELNYEVDGKLKEPSVVAAEFLKK 300
Cdd:pfam04069 222 FLNKL--SLDTEDLNELNAQVDVEGKDPEEVAKDWLAE 257
 
Name Accession Description Interval E-value
PBP2_OpuCC_like cd13608
Substrate-binding protein OpuCC of ABC-type osmoregulatory transporter and related proteins; ...
35-299 0e+00

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: 501.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  35 TIKIGAQNLTESEILANMISLLIEHDTDLNTVLVKNLGSNYVQHQAMLGGDIDISATRYSGTDLTSTLGREAEKDPEKAL 114
Cdd:cd13608     1 TIRIGSQSTTESQILAEMVKQLIEHYTDLKVELINNLGSSTVQHQAMLNGDANISAARYTGTDLTGELGMEPIKDPEKAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 115 HIVQQDFKKKFNYKWFDSYGFDNTYAFTVTKELAEKGNYETISDLKKDADKLKLGVDNAWLKRKGDGYPGFKQEYGFSFG 194
Cdd:cd13608    81 KVVQKEFQKRFDQTWFDSYGFANTYAFMVTKEFAEKYNLKKVSDLKKVADNLKLGVDTSWLNRKGDGYPGFKETYGFDFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 195 STFPMQIGLVYDAVKNGKMDIVLAYSTDGRIKAYDLKLLKDDKRFFPPYDCSPVVPEKVLKEHPELKETINKLIGKIDTE 274
Cdd:cd13608   161 TVYPMQIGLVYDAVASGKMDVVLGYSTDGRIKSYDLVVLEDDKQFFPPYDASPVATNEILKKYPELEEILEKLEGKISTE 240
                         250       260
                  ....*....|....*....|....*
gi 1772215112 275 TMQELNYEVDGKLKEPSVVAAEFLK 299
Cdd:cd13608   241 TMQELNYQVDNDLKEPSVVAKEFLE 265
OsmF COG1732
Periplasmic glycine betaine/choline-binding (lipo)protein of an ABC-type transport system ...
5-301 3.06e-132

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: 377.18  E-value: 3.06e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112   5 KLRRLGAVMLVFSLLISGCALPGlGGASDKTIKIGAQNLTESEILANMISLLIEHDtDLNTVLVKNLGSNYVQHQAMLGG 84
Cdd:COG1732     2 KRLLLLALALAAALALAGCGLAS-AAAAGDTIVVGSKNFTEQEILAEIYAQALEAA-GLKVERKLNLGGTEVVRQALKSG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  85 DIDIsATRYSGTDLTSTLGREAEKDPEKALHIVQQDFKKKFNYKWFDSYGFDNTYAFTVTKELAEKGNYETISDLKKDAD 164
Cdd:COG1732    80 EIDL-YPEYTGTALTTYLKEDPITDPEEVYEAVKEALPEKNGLTWLDPAGFNNTYALAVTKETAEKYGLKTISDLAKVAG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 165 KLKLGVDNAWLKRKgDGYPGFKQEYGFSFGSTFPMQIGLVYDAVKNGKMDIVLAYSTDGRIKAYDLKLLKDDKRFFPPYD 244
Cdd:COG1732   159 ELTLGADPEFAERP-DGLPGLKKAYGFEFKEVKPMDTGLTYTALANGQVDVADAYTTDGRIAALDLVVLEDDKNFFPPYN 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1772215112 245 CSPVVPEKVLKEHPELKETINKLIGKIDTETMQELNYEVDGKLKEPSVVAAEFLKKH 301
Cdd:COG1732   238 AAPLVRKEVLEKYPELAEVLNKLSGKLTTETMQELNYQVDVDGEDPADVAREFLKEK 294
PBP2_osmoprotectants cd13528
Substrate-binding domain of osmoregulatory ABC-type transporters; the type 2 ...
35-299 3.17e-115

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: 333.03  E-value: 3.17e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  35 TIKIGAQNLTESEILANMISLLIEHDTDLNTVLVKNLGSNYVQHQAMLGGDIDISAtRYSGTDLTSTLGREA-EKDPEKA 113
Cdd:cd13528     1 TIVVGSKNFTEQYILGEMLAQLLEANTDLTVERKLNLGGTEVAFNALKNGDIDLYV-EYTGTALLTILKEDApITDPEEV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 114 LHIVQQDFKKKFNYKWFDSYGFDNTYAFTVTKELAEKGNYETISDLKKDADKLKLGVDNAWLKRkGDGYPGFKQEYGFSF 193
Cdd:cd13528    80 YEKVKKEYEEKFGLTWLDPLGFNNTYALAVRKDTAEKYGLKTISDLAPHSDQLVFGADPEFYER-SDGLPGLKKTYGFDF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 194 GSTFPMQIGLVYDAVKNGKMDIVLAYSTDGRIKAYDLKLLKDDKRFFPPYDCSPVVPEKVLKEHPELKETINKLIGKIDT 273
Cdd:cd13528   159 KEVKTMDPGLTYEALDNGEVDVIDAFSTDGRIKAFDLVVLEDDKNFFPPYNAAPVVREDVLKKHPELEEVLNKLSGKLTD 238
                         250       260
                  ....*....|....*....|....*.
gi 1772215112 274 ETMQELNYEVDGKLKEPSVVAAEFLK 299
Cdd:cd13528   239 ETMQQLNYQVDVEGKDPEEVARDFLK 264
PBP2_Opu_like_1 cd13609
Substrate-binding domain of putative ABC-type osmoprotectant uptake system; the type 2 ...
35-299 1.39e-97

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: 287.96  E-value: 1.39e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  35 TIKIGAQNLTESEILANMISLLIEHDTDLNTVLVKNLGSNYVQHQAMLGGDIDISAtRYSGTDLTSTLGREAEKDPEKAL 114
Cdd:cd13609     1 TIVIGSKNFTEQLILGNMYADLIEANTDIKVERKLNLGGSSVCFSALKNGDIDMYV-DYTGTILVNILKEPPISDPDEVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 115 HIVQQDFKKKFNYKWFDSYGFDNTYAFTVTKELAEKGNYETISDLKKDADKLKLGVDNAWLKRKgDGYPGFKQEYGFSFG 194
Cdd:cd13609    80 NTVKELMKEKYNLEVLKPLGFNNTYTLAVRKETAEKYNLKTISDLAKVSDELTLGCTLEFLNRE-DGLPGLEKTYGLNFK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 195 STFPMQIGLVYDAVKNGKMDIVLAYSTDGRIKAYDLKLLKDDKRFFPPYDCSPVVPEKVLKEHPELKETINKLIGKIDTE 274
Cdd:cd13609   159 DVKGLDGSLRYTALENGEVDVIDAFSTDGLLKKFDLVVLEDDKNFFPPYYAVPLVREETLEKYPELEDVLNKLAGKISEE 238
                         250       260
                  ....*....|....*....|....*
gi 1772215112 275 TMQELNYEVDGKLKEPSVVAAEFLK 299
Cdd:cd13609   239 TMRELNYKVDELGKDPEDVAHEFLV 263
PBP2_Opu_like_2 cd13613
Substrate-binding domain of putative ABC-type osmoprotectant uptake system; the type 2 ...
35-299 8.25e-89

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: 265.74  E-value: 8.25e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  35 TIKIGAQNLTESEILANMISLLIEHDTDLnTVLVK-NLGSNYVQHQAMLGGDIDISaTRYSGTDLTSTLGREAEKDPEKA 113
Cdd:cd13613     1 RIIIGSKNFTEQVILGELLAQQIEARTDL-KVERRfNLGGTFICHQALLSGAIDAY-VEYTGTALTAILKQPPIRDPQRV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 114 LHIVQQDFKKKFNYKWFDSYGFDNTYAFTVTKELAEKGNYETISDLKKDADKLKLGVDNAWLKRKgDGYPGFKQEYGFSF 193
Cdd:cd13613    79 YEQVKQLYADRFGLEVMPPLGFENTFAILVRGEDARKLGLKTLSDAAPYTPGWRAGFGYEFLERA-DGYPGLAKTYGLKF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 194 GSTfP--MQIGLVYDAVKNGKMDIVLAYSTDGRIKAYDLKLLKDDKRFFPPYDCSPVVPEKVLKEHPELKETINKLIGKI 271
Cdd:cd13613   158 AKT-PrvMDLGLLYRALAQKQVDLIAGNSTDGLIAALDLVILEDDRHYFPPYQAVPVVRQATLAKYPELRTAIAELAGKI 236
                         250       260
                  ....*....|....*....|....*...
gi 1772215112 272 DTETMQELNYEVDGKLKEPSVVAAEFLK 299
Cdd:cd13613   237 SAETMQQMNYQVDGEHRDVAEVAREFLK 264
PBP2_ProWX cd13612
Substrate-binding protein ProWX of ABC-type osmoregulated transporter and its related proteins; ...
35-300 9.31e-83

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: 250.62  E-value: 9.31e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  35 TIKIGAQNLTESEILANMISLLIEHDTDLNTVLVKNLG---SNYvqHQAMLGGDIDISAtRYSGTDLTSTLGREaEKDPE 111
Cdd:cd13612     1 TIHIATKPMTEQYILGEMLKQLIEQDTDLKVELTKGVGggtSNI--HPAMVKGEFDLYP-EYTGTGWLFVLKKD-GTYSE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 112 KALHIVQQDFKKKFNYKWFDSYGFDNTYAFTVTKELAEKGNYETISDLKKDADKLKLGVDNAWLKRKgDGYPGFKQEYGF 191
Cdd:cd13612    77 ELFDQLQKEYEEKYNLTWLGLYGFNNTYGLAVRKELAEKYNLKTYSDLAKVSNQLVFGAEYDFFERE-DGYDALQKAYGF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 192 SFGSTFPMQIGLVYDAVKNGKMDIVLAYSTDGRIKAYDLKLLKDDKRFFPPYDCSPVVPEKVLKEHPELKETINKLIGKI 271
Cdd:cd13612   156 NFKKTVDMDIGLKYQAIESGKVDVINVFTTDGQLSDADIVVLEDDKGFFPSYYAGTVVREETLEKYPELEDVLEKLTGLI 235
                         250       260
                  ....*....|....*....|....*....
gi 1772215112 272 DTETMQELNYEVDGKLKEPSVVAAEFLKK 300
Cdd:cd13612   236 SDEDMAEMNYQVEIEKKDPKDVAKEFLEE 264
PBP2_QAT_like cd13614
Substrate-binding domain of quaternary amine ABC-type transporter; the type 2 ...
35-299 6.52e-81

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: 245.76  E-value: 6.52e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  35 TIKIGAQNLTESEILANMISLLIEhDTDLNTVLVKNLGSNYVQHQAMLGGDIDISAtRYSGTDLTSTLGREAEKDPEKAL 114
Cdd:cd13614     1 AIRVGSKNFTEQFILGEMYALALE-DAGIKVERKLNLGGTLIAHQALVNGEIDLYP-EYTGTALLTVLKGEPSSDAKQVY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 115 HIVQQDFKKKFNYKWFDSYGFDNTYAFTVTKELAEKGNYETISDLKKDADKLKLGVDNAWLKRKgDGYPGFKQEYG-FSF 193
Cdd:cd13614    79 KTVKDAYAEQFQLTWLEPAPFNNTYALVMTRETAEKYGIKTLSDLAKAAGELVFGGGPEFQDRE-DGLPGLKAKYGaFDF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 194 GSTFPM-QIGLVYDAVKNGKMDIVLAYSTDGRIKAYDLKLLKDDKRFFPPYDCSPVVPEKVLKEHPELKETINKLIGKID 272
Cdd:cd13614   158 KEFVQVdPLGLRYQALAQGQIDVAVGFGTDGQIAAYGLVVLEDDKNLFPPYQVAPVVRQDVLDANPKIAEVLNKLSALLD 237
                         250       260
                  ....*....|....*....|....*..
gi 1772215112 273 TETMQELNYEVDGKLKEPSVVAAEFLK 299
Cdd:cd13614   238 NETMQRLNYEVDGNKREPKDVAREFLK 264
PBP2_AfProX_like cd13607
Substrate-binding protein ProX of ABC-type osmoregulatory transporter from Archaeoglobus ...
35-299 1.29e-76

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: 234.79  E-value: 1.29e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  35 TIKIGAQNLTESEILANMISLLIEhDTDLNTVLVKNLGSNYVQHQAMLGGDIDISAtRYSGTDLTSTLGREAEKDPEKAL 114
Cdd:cd13607     1 TVVIGSKTFTEQYILAEMIAQLLE-EAGYPAEHREGLGGTRVLFEALKSGEIDVYV-EYTGTLYAEILKRPETWDPAAVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 115 HIVQQDFKKKfNYKWFDSYGFDNTYAFTVTKELAEKGNYETISDLKKDADKLKLGVDNAWLKRkGDGYPGFKQEYGFSFG 194
Cdd:cd13607    79 AELKEALAER-GIVVAGPLGFENTYALAMREDRAEALGIRTISDLLARAPDLRFGFDPEFLDR-PDGWPALRRVYGLPFK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 195 STFPMQIGLVYDAVKNGKMDIVLAYSTDGRIKAYDLKLLKDDKRFFPPYDCSPVVPEKVLKEHPELKETINKLIGKIDTE 274
Cdd:cd13607   157 EVRGLDHTLAYRALKSGQVDVIDAYTTDARIDAYDLRVLEDDRGAFPPYDAVLLYRADLAERAPKAVAALRRLEGRIDAD 236
                         250       260
                  ....*....|....*....|....*
gi 1772215112 275 TMQELNYEVDGKLKEPSVVAAEFLK 299
Cdd:cd13607   237 TMRALNAQVDLEKRSEAEVAAEFLA 261
PBP2_ChoS cd13610
Substrate-binding domain ChoS of an osmoregulated ABC-type transporter and related proteins; ...
37-299 9.12e-74

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: 227.47  E-value: 9.12e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  37 KIGAqnltESEILANMISLLIEHDTDLNTVLVK-NLGSNYVQHQAMLGGDIDISAtRYSGTDLTSTLGREAE-KDPEKAL 114
Cdd:cd13610     7 KLGS----EPDILINMYKLLIEEETPDLQVTLKpNFGKTSFLFNALKSGDIDIYP-EFTGTVLETLLKEPPKsNDPMEVY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 115 HIVQQDFKKKFNYKWFDSYGFDNTYAFTVTKELAEKGNYETISDLKKDADKLKLGVDNAWLKRKgDGYPGFKQEYGFSFg 194
Cdd:cd13610    82 EQARDGLAKQYQLTYLKPMAYNNTYALAVKKEFAKQHNLKTISDLQKVQDKLKAGFTLEFMDRE-DGYKGLQKAYGLNF- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 195 STFPMQIGLVYDAVKNGKMDIVLAYSTDGRIKAYDLKLLKDDKRFFPPYDCSPVVPEKVLKEHPELKETINKLIGKIDTE 274
Cdd:cd13610   160 NVKSMEPALRYQAINNGQVNVIDAYSTDSEIKQYDLVVLKDDKHLFPPYQGAPLMREEFLKKHPELVKALNKLAGKITDE 239
                         250       260
                  ....*....|....*....|....*
gi 1772215112 275 TMQELNYEVDGKLKEPSVVAAEFLK 299
Cdd:cd13610   240 EMQEMNYRVDVKHKSAAKVAKEYLQ 264
PBP2_YehZ cd13611
Substrate-binding domain YehZ of an osmoregulated ABC-type transporter; the type 2 ...
35-299 1.08e-69

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: 217.07  E-value: 1.08e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  35 TIKIGAQNLTESEILANMISLLIE---HDTDLNTvlvkNLGSNYVQHQAMLGGDIDISaTRYSGTDLTSTLGREAEK-DP 110
Cdd:cd13611     1 TITVGSKDFTEQLILGKITVQALQaagADVTDKT----NLGGSASARQALENGQVDVY-WEYTGTAWITYLGHTEPIlDP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 111 EKALHIV-QQDFKKkfNYKWFDSYGFDNTYAFTVTKELAEKGNYETISDL---KKDADKLKLGVDNAWLKRkGDGYPGFK 186
Cdd:cd13611    76 QEQYEAVkDLDAEK--GLVWLDPAPLNNTYALAMREATAEELGITTLSDLalaKLPPGDRTFCVDAEFASR-PDGLPPLL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 187 QEYGFSFG--STFPMQIGLVYDAVKNGKMDIVLAYSTDGRIKAYDLKLLKDDKRFFPPYDCSPVVPEKVLKEHPELKETI 264
Cdd:cd13611   153 EAYGFEFPraNVRQMDTGLVYTATANGQCDFGEVFTTDGRIKALDLVVLEDDKGFFPAYNAAPVVRTEVLDAHPELAEIL 232
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1772215112 265 NKLIGKIDTETMQELNYEVDGKLKEPSVVAAEFLK 299
Cdd:cd13611   233 NPISAKLDNDTMQELNARVDVDGEDPADVARDWLV 267
OpuAC pfam04069
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity ...
34-300 4.56e-66

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: 207.56  E-value: 4.56e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  34 KTIKIGAQNLTESEILANMISLLIEHDtDLNTVLVkNLGSNYVQHQAMLGGDIDISATRYSGTdltstlgreaekdpekA 113
Cdd:pfam04069   1 KTIVIGSKNWTEQEILANIAAQLLEAL-GYVVELV-GLGSSAVLFAALASGDIDLYPEEWTGT----------------T 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 114 LHIVQQDFKKKFNYKWFDSYGFDNTYAFTVTKELAEKGNYETISDLKKDADKLKLGVDNAWLKRkGDGYP------GFKQ 187
Cdd:pfam04069  63 YEAYKKAVEEKLGLLVLGPLGAGNTYGLAVPKYVAEKPGIKSISDLAKPADDLELGFKGEFIGR-PDGWGcmrsteGLLK 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 188 EYGFS----FGSTFPMQIGLVYDAVKNGKMDIVLAYSTDGRIKAYDLKLLKDDKRFFPP-YDCSPVVPEKVLKEHPELKE 262
Cdd:pfam04069 142 AYGLDkyelVEGSEAAMDALIYAAYKRGEPDVVYAWTPDWMIKKYDLVVLEDPKGLFPPaYNVVPVVRKGFAEKHPEVAA 221
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1772215112 263 TINKLigKIDTETMQELNYEVDGKLKEPSVVAAEFLKK 300
Cdd:pfam04069 222 FLNKL--SLDTEDLNELNAQVDVEGKDPEEVAKDWLAE 257
PBP2_ProWY cd13615
Substrate-binding domain of ABC-type osmoregulated transporter; the type 2 periplasmic-binding ...
35-299 6.69e-63

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: 199.59  E-value: 6.69e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  35 TIKIGAQNLTESEILANMISLLIEhDTDLNTVLVKNLGSNYVqHQAMLGGDIDISAtRYSGTDLTSTLGREAEKDPEKAL 114
Cdd:cd13615     1 AIRVGSKDFTENLIVAEIYALALE-DAGYKVKRKPNISSSVV-HQALTSGQIDLYP-EYTGTGLLAVLKKEAITDPQKVY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 115 HIVQQDFKKKFNYKWFDSYGFDNTYAFTVTKELAEKGNYETISDLKKDADKLKLGVDNAWLKRKgDGYPGFKQEYG-FSF 193
Cdd:cd13615    78 ATVKDGYAKKFNLVWLDYAPANDGQGLVIRTSVAKKYGIKTISDLQKNASQIRFASQGEFDQRE-DGLPGLEKVYGkFSF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 194 GSTFPMQIGLVYDAVKNGKMDIVLAYSTDGRIKAYDLKLLKDDKRFFPPYDCSPVVPEKVLKEHPELKETINKLIGKIDT 273
Cdd:cd13615   157 KSTKVYDNGLKYQVLANDKADITPAYTTEGQLDTSKFTLLKDDKHVWPPYNLAPVVRKDVLKANPKIASALNKVSAKLTT 236
                         250       260
                  ....*....|....*....|....*.
gi 1772215112 274 ETMQELNYEVDGKLKEPSVVAAEFLK 299
Cdd:cd13615   237 KTLTQLNAKVDVDKQEYADVAKDFYL 262
PBP2_OsmF cd13616
Substrate-binding domain OsmF of an osmoregulated ABC-type transporter; the type 2 ...
35-299 5.55e-44

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: 151.33  E-value: 5.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  35 TIKIGAQNLTESEILANMISLLIEHdtdlNTVLVKN---LGSNYVQHQAMLGGDIDISAtRYSGTDLT--STLGREAEKD 109
Cdd:cd13616     1 PVVVGSKIDTEGALLGNMIVLALEA----HGFPVEDktgLGTTPVVRKALLSGEIDLYP-EYTGNGAFffPEADDPVWKD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 110 PEKALHIVQQDFKKKFNYKWFDSYGFDNTYAFTVTKELAEKGNYETISDLK---KDADKLKLGVDNAWLKRKgDGYPGFK 186
Cdd:cd13616    76 ARKGYETVKELDAKNNGLVWLDPAPANNTWAIAVRRDLAEKNNLKTLADLAayvNEGGAFKLAASAEFVERP-DALPAFE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 187 QEYGFSFGS----TFPMqiGLVYDAVKNGKMDI-----VLAYSTDGRIKAYDLKLLKDDKRFFPPYDCSPVVPEKVLKEH 257
Cdd:cd13616   155 KAYGFKLSKdqlvILSG--GNTAQTEQAAAQGTsgvnaAMAYGTDGAIAALGLVVLEDPKGAQPVYAPAPVVRQEVLEAY 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1772215112 258 PELKETINKLIGKIDTETMQELNYEVDGKLKEPSVVAAEFLK 299
Cdd:cd13616   233 PEIAEILKPVFATLDLKTLQELNARIAVEGESAEDVARDYLK 274
PBP2_ProX_like cd13606
Bacterial substrate-binding protein ProX of ABC-type osmoregulated transporter and its related ...
35-299 1.12e-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: 136.93  E-value: 1.12e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  35 TIKIGAQNLTESEILANMISLLIEhDTDLNTVLVKNLGSNYVQHQAMLGGDIDISAtRYSGTDLTSTLGREAEKDPEKal 114
Cdd:cd13606     1 TVVVGSADFPESEILAEIYAQALE-AAGVKVTRKLNIGSREVYLPALEDGSIDLVP-EYTGNLLQYLDKDATATDPEE-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 115 hiVQQDFKKKF--NYKWFDSYGFDNTYAFTVTKELAEKGNYETISDLKKDADKLKLGVDNAWLKRKGdGYPGFKQEYGFS 192
Cdd:cd13606    77 --VYAALKAALpeGLEVLDPSPAEDKDALVVTKETAEKYGLKSIADLAPVAGELTLGGPPEFKTRPY-GLPGLKEVYGVT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 193 FGSTFPMQIG--LVYDAVKNGKMDIVLAYSTDGRIKAYDLKLLKDDKRFFPPYDCSPVVPEKVLkeHPELKETINKLIGK 270
Cdd:cd13606   154 FKEFKPLDAGgpLTVKALKDGTVQVANIFTTDPAIADNGLVVLEDPKNLFPAQNVVPLVRKAKL--DDKAADALNAVSAK 231
                         250       260
                  ....*....|....*....|....*....
gi 1772215112 271 IDTETMQELNYEVDGKLKEPSVVAAEFLK 299
Cdd:cd13606   232 LTTEDLTELNKQVVGDKADPADVAKEWLK 260
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
12-260 1.73e-04

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


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 42.30  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  12 VMLVFSLLISGCALPGlGGASDKTIKIGAQNLTESEILAnmisLLIEH----DTDLNtVLVKNLGSNYVQHQAMLGGDID 87
Cdd:COG0715     1 LAALAALALAACSAAA-AAAEKVTLRLGWLPNTDHAPLY----VAKEKgyfkKEGLD-VELVEFAGGAAALEALAAGQAD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112  88 ISATrysgtDLTSTLGREAEKDPEKALHIVQQDfkkkfnykwfdsygfdNTYAFTVTKelaeKGNYETISDLK-Kdadkl 166
Cdd:COG0715    75 FGVA-----GAPPALAARAKGAPVKAVAALSQS----------------GGNALVVRK----DSGIKSLADLKgK----- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1772215112 167 KLGV-----DNAWLKRkgdgypgFKQEYGFSFGS-TF-PMQIGLVYDAVKNGKMDIVLAYSTDGR--IKAYDLKLLKDDK 237
Cdd:COG0715   125 KVAVpggstSHYLLRA-------LLAKAGLDPKDvEIvNLPPPDAVAALLAGQVDAAVVWEPFESqaEKKGGGRVLADSA 197
                         250       260
                  ....*....|....*....|....
gi 1772215112 238 RFFPPYDCSP-VVPEKVLKEHPEL 260
Cdd:COG0715   198 DLVPGYPGDVlVASEDFLEENPEA 221
PBP2_OpuAC_like cd13639
Substrate binding domain of Lactococcus lactis ABC-type transporter OpuA and related proteins; ...
227-301 6.54e-03

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: 37.52  E-value: 6.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1772215112 227 AYDLKLLKDDKRFFPPYDCSPVVPEKVLKE-HPELKETINKLigKIDTETMQELNYEVDgKLKEPSVVAAEFLKKH 301
Cdd:cd13639   173 KYDLKYLEDPKGVYGEAESIHTIARKGFEEdHPEAYEFLKNF--KLTDEDLESLMLEIE-DGGDPEEAAEEWIDEN 245
 
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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