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Conserved domains on  [gi|513037883|ref|WP_016505943|]
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ABC transporter substrate-binding protein [Salmonella enterica]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP2_OsmF cd13616
Substrate-binding domain OsmF of an osmoregulated ABC-type transporter; the type 2 ...
26-307 1.75e-174

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: 483.76  E-value: 1.75e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  26 PVTVGSKIDTEGALLGNMILQVLESHGVKTVNKIQLGTTPVVRGAITAGELDIYPaageldiypEYTGNGAFFFKDENDP 105
Cdd:cd13616    1 PVVVGSKIDTEGALLGNMIVLALEAHGFPVEDKTGLGTTPVVRKALLSGEIDLYP---------EYTGNGAFFFPEADDP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 106 AWKNAKQGFEKVKKLDAEQNKLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLSRYLKEGGTFKLAASAEFIERADALP 185
Cdd:cd13616   72 VWKDARKGYETVKELDAKNNGLVWLDPAPANNTWAIAVRRDLAEKNNLKTLADLAAYVNEGGAFKLAASAEFVERPDALP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 186 AFEKAYDFTLNQNQLLSLAGGDTAVTIKAAAQQTSGVNAAMAYGTDGPVAALGLQTLSDPKGVQPIYAPAPVVRESVLQA 265
Cdd:cd13616  152 AFEKAYGFKLSKDQLVILSGGNTAQTEQAAAQGTSGVNAAMAYGTDGAIAALGLVVLEDPKGAQPVYAPAPVVRQEVLEA 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 513037883 266 YPQIADWLQPVFASLDEKTLQQLNARIAVEGLDAKKVAADYL 307
Cdd:cd13616  232 YPEIAEILKPVFATLDLKTLQELNARIAVEGESAEDVARDYL 273
 
Name Accession Description Interval E-value
PBP2_OsmF cd13616
Substrate-binding domain OsmF of an osmoregulated ABC-type transporter; the type 2 ...
26-307 1.75e-174

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: 483.76  E-value: 1.75e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  26 PVTVGSKIDTEGALLGNMILQVLESHGVKTVNKIQLGTTPVVRGAITAGELDIYPaageldiypEYTGNGAFFFKDENDP 105
Cdd:cd13616    1 PVVVGSKIDTEGALLGNMIVLALEAHGFPVEDKTGLGTTPVVRKALLSGEIDLYP---------EYTGNGAFFFPEADDP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 106 AWKNAKQGFEKVKKLDAEQNKLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLSRYLKEGGTFKLAASAEFIERADALP 185
Cdd:cd13616   72 VWKDARKGYETVKELDAKNNGLVWLDPAPANNTWAIAVRRDLAEKNNLKTLADLAAYVNEGGAFKLAASAEFVERPDALP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 186 AFEKAYDFTLNQNQLLSLAGGDTAVTIKAAAQQTSGVNAAMAYGTDGPVAALGLQTLSDPKGVQPIYAPAPVVRESVLQA 265
Cdd:cd13616  152 AFEKAYGFKLSKDQLVILSGGNTAQTEQAAAQGTSGVNAAMAYGTDGAIAALGLVVLEDPKGAQPVYAPAPVVRQEVLEA 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 513037883 266 YPQIADWLQPVFASLDEKTLQQLNARIAVEGLDAKKVAADYL 307
Cdd:cd13616  232 YPEIAEILKPVFATLDLKTLQELNARIAVEGESAEDVARDYL 273
OsmF COG1732
Periplasmic glycine betaine/choline-binding (lipo)protein of an ABC-type transport system ...
6-310 1.09e-109

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: 320.17  E-value: 1.09e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883   6 LWVSSLALLATVSLPLQAAS--PVTVGSKIDTEGALLGNMILQVLESHGVKTVNKIQLGTTPVVRGAITAGELDIYPaag 83
Cdd:COG1732    9 LALAAALALAGCGLASAAAAgdTIVVGSKNFTEQEILAEIYAQALEAAGLKVERKLNLGGTEVVRQALKSGEIDLYP--- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  84 eldiypEYTGNGAFFFkDENDPAwKNAKQGFEKVKKLDAEQNKLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLSRYL 163
Cdd:COG1732   86 ------EYTGTALTTY-LKEDPI-TDPEEVYEAVKEALPEKNGLTWLDPAGFNNTYALAVTKETAEKYGLKTISDLAKVA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 164 KEggtFKLAASAEFIERADALPAFEKAYDFTLNQNQLLSLAggdtavtIKAAAQQTSGVNAAMAYGTDGPVAALGLQTLS 243
Cdd:COG1732  158 GE---LTLGADPEFAERPDGLPGLKKAYGFEFKEVKPMDTG-------LTYTALANGQVDVADAYTTDGRIAALDLVVLE 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 513037883 244 DPKGVQPIYAPAPVVRESVLQAYPQIADWLQPVFASLDEKTLQQLNARIAVEGLDAKKVAADYLRQK 310
Cdd:COG1732  228 DDKNFFPPYNAAPLVRKEVLEKYPELAEVLNKLSGKLTTETMQELNYQVDVDGEDPADVAREFLKEK 294
OpuAC pfam04069
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity ...
26-309 3.76e-55

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: 179.83  E-value: 3.76e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883   26 PVTVGSKIDTEGALLGNMILQVLESHGVKtVNKIQLGTTPVVRGAITAGELDIYPAageldiypEYTGNGafffkdendp 105
Cdd:pfam04069   2 TIVIGSKNWTEQEILANIAAQLLEALGYV-VELVGLGSSAVLFAALASGDIDLYPE--------EWTGTT---------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  106 awknakqgFEKVKKLDAEQNKLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLSRYlkeGGTFKLAASAEFIERADALP 185
Cdd:pfam04069  63 --------YEAYKKAVEEKLGLLVLGPLGAGNTYGLAVPKYVAEKPGIKSISDLAKP---ADDLELGFKGEFIGRPDGWG 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  186 ------AFEKAYDFTLNQNQLLSLAGGDTAvtIKAAAQQTSgVNAAMAYGTDGPVAALGLQTLSDPKGVQ-PIYAPAPVV 258
Cdd:pfam04069 132 cmrsteGLLKAYGLDKYELVEGSEAAMDAL--IYAAYKRGE-PDVVYAWTPDWMIKKYDLVVLEDPKGLFpPAYNVVPVV 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 513037883  259 RESVLQAYPQIADWLQPVfaSLDEKTLQQLNARIAVEGLDAKKVAADYLRQ 309
Cdd:pfam04069 209 RKGFAEKHPEVAAFLNKL--SLDTEDLNELNAQVDVEGKDPEEVAKDWLAE 257
 
Name Accession Description Interval E-value
PBP2_OsmF cd13616
Substrate-binding domain OsmF of an osmoregulated ABC-type transporter; the type 2 ...
26-307 1.75e-174

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: 483.76  E-value: 1.75e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  26 PVTVGSKIDTEGALLGNMILQVLESHGVKTVNKIQLGTTPVVRGAITAGELDIYPaageldiypEYTGNGAFFFKDENDP 105
Cdd:cd13616    1 PVVVGSKIDTEGALLGNMIVLALEAHGFPVEDKTGLGTTPVVRKALLSGEIDLYP---------EYTGNGAFFFPEADDP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 106 AWKNAKQGFEKVKKLDAEQNKLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLSRYLKEGGTFKLAASAEFIERADALP 185
Cdd:cd13616   72 VWKDARKGYETVKELDAKNNGLVWLDPAPANNTWAIAVRRDLAEKNNLKTLADLAAYVNEGGAFKLAASAEFVERPDALP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 186 AFEKAYDFTLNQNQLLSLAGGDTAVTIKAAAQQTSGVNAAMAYGTDGPVAALGLQTLSDPKGVQPIYAPAPVVRESVLQA 265
Cdd:cd13616  152 AFEKAYGFKLSKDQLVILSGGNTAQTEQAAAQGTSGVNAAMAYGTDGAIAALGLVVLEDPKGAQPVYAPAPVVRQEVLEA 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 513037883 266 YPQIADWLQPVFASLDEKTLQQLNARIAVEGLDAKKVAADYL 307
Cdd:cd13616  232 YPEIAEILKPVFATLDLKTLQELNARIAVEGESAEDVARDYL 273
OsmF COG1732
Periplasmic glycine betaine/choline-binding (lipo)protein of an ABC-type transport system ...
6-310 1.09e-109

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: 320.17  E-value: 1.09e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883   6 LWVSSLALLATVSLPLQAAS--PVTVGSKIDTEGALLGNMILQVLESHGVKTVNKIQLGTTPVVRGAITAGELDIYPaag 83
Cdd:COG1732    9 LALAAALALAGCGLASAAAAgdTIVVGSKNFTEQEILAEIYAQALEAAGLKVERKLNLGGTEVVRQALKSGEIDLYP--- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  84 eldiypEYTGNGAFFFkDENDPAwKNAKQGFEKVKKLDAEQNKLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLSRYL 163
Cdd:COG1732   86 ------EYTGTALTTY-LKEDPI-TDPEEVYEAVKEALPEKNGLTWLDPAGFNNTYALAVTKETAEKYGLKTISDLAKVA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 164 KEggtFKLAASAEFIERADALPAFEKAYDFTLNQNQLLSLAggdtavtIKAAAQQTSGVNAAMAYGTDGPVAALGLQTLS 243
Cdd:COG1732  158 GE---LTLGADPEFAERPDGLPGLKKAYGFEFKEVKPMDTG-------LTYTALANGQVDVADAYTTDGRIAALDLVVLE 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 513037883 244 DPKGVQPIYAPAPVVRESVLQAYPQIADWLQPVFASLDEKTLQQLNARIAVEGLDAKKVAADYLRQK 310
Cdd:COG1732  228 DDKNFFPPYNAAPLVRKEVLEKYPELAEVLNKLSGKLTTETMQELNYQVDVDGEDPADVAREFLKEK 294
PBP2_osmoprotectants cd13528
Substrate-binding domain of osmoregulatory ABC-type transporters; the type 2 ...
26-308 7.62e-97

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: 286.42  E-value: 7.62e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  26 PVTVGSKIDTEGALLGNMILQVLESHGVKTVN-KIQLGTTPVVRGAITAGELDIYPaageldiypEYTGNGAFFFKDEND 104
Cdd:cd13528    1 TIVVGSKNFTEQYILGEMLAQLLEANTDLTVErKLNLGGTEVAFNALKNGDIDLYV---------EYTGTALLTILKEDA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 105 PaWKNAKQGFEKVKKLDAEQNKLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLsryLKEGGTFKLAASAEFIERADAL 184
Cdd:cd13528   72 P-ITDPEEVYEKVKKEYEEKFGLTWLDPLGFNNTYALAVRKDTAEKYGLKTISDL---APHSDQLVFGADPEFYERSDGL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 185 PAFEKAYDFTLNQNQLLslaggDTAVTIKAAAQQTsgVNAAMAYGTDGPVAALGLQTLSDPKGVQPIYAPAPVVRESVLQ 264
Cdd:cd13528  148 PGLKKTYGFDFKEVKTM-----DPGLTYEALDNGE--VDVIDAFSTDGRIKAFDLVVLEDDKNFFPPYNAAPVVREDVLK 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 513037883 265 AYPQIADWLQPVFASLDEKTLQQLNARIAVEGLDAKKVAADYLR 308
Cdd:cd13528  221 KHPELEEVLNKLSGKLTDETMQQLNYQVDVEGKDPEEVARDFLK 264
PBP2_YehZ cd13611
Substrate-binding domain YehZ of an osmoregulated ABC-type transporter; the type 2 ...
26-308 2.83e-77

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: 236.71  E-value: 2.83e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  26 PVTVGSKIDTEGALLGNMILQVLESHGVKTVNKIQLGTTPVVRGAITAGELDIYPaageldiypEYTGNGAFFFKDENDP 105
Cdd:cd13611    1 TITVGSKDFTEQLILGKITVQALQAAGADVTDKTNLGGSASARQALENGQVDVYW---------EYTGTAWITYLGHTEP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 106 AwKNAKQGFEKVKKLDAEQNkLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLSRYLKEGGTFKLAASAEFIERADALP 185
Cdd:cd13611   72 I-LDPQEQYEAVKDLDAEKG-LVWLDPAPLNNTYALAMREATAEELGITTLSDLALAKLPPGDRTFCVDAEFASRPDGLP 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 186 AFEKAYDFTLNQNQLLSLaggDTAVTIKAAAQQTsgVNAAMAYGTDGPVAALGLQTLSDPKGVQPIYAPAPVVRESVLQA 265
Cdd:cd13611  150 PLLEAYGFEFPRANVRQM---DTGLVYTATANGQ--CDFGEVFTTDGRIKALDLVVLEDDKGFFPAYNAAPVVRTEVLDA 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 513037883 266 YPQIADWLQPVFASLDEKTLQQLNARIAVEGLDAKKVAADYLR 308
Cdd:cd13611  225 HPELAEILNPISAKLDNDTMQELNARVDVDGEDPADVARDWLV 267
PBP2_QAT_like cd13614
Substrate-binding domain of quaternary amine ABC-type transporter; the type 2 ...
26-308 3.64e-65

Substrate-binding domain of quaternary amine ABC-type transporter; the type 2 periplasmic-binding protein fold; This group includes the periplasmic substrate-binding component of a putative quaternary amine ABC transport system that is predicted to be involved in uptake of osmoprotectants (also termed compatible solutes) such as betaine, choline, proline betaine, carnitine, and L-proline. The relative substrate preference of this group is not known. To counteract the efflux of water, many microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270332  Cd Length: 264  Bit Score: 205.70  E-value: 3.64e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  26 PVTVGSKIDTEGALLGNMILQVLESHGVKTVNKIQLGTTPVVRGAITAGELDIYPaageldiypEYTGNGAFFFKDEndP 105
Cdd:cd13614    1 AIRVGSKNFTEQFILGEMYALALEDAGIKVERKLNLGGTLIAHQALVNGEIDLYP---------EYTGTALLTVLKG--E 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 106 AWKNAKQGFEKVKKLDAEQNKLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLSrylKEGGTFKLAASAEFIERADALP 185
Cdd:cd13614   70 PSSDAKQVYKTVKDAYAEQFQLTWLEPAPFNNTYALVMTRETAEKYGIKTLSDLA---KAAGELVFGGGPEFQDREDGLP 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 186 AFEKAYDFtLNQNQLLSLAGGdtAVTIKAAAQQTSGVnaAMAYGTDGPVAALGLQTLSDPKGVQPIYAPAPVVRESVLQA 265
Cdd:cd13614  147 GLKAKYGA-FDFKEFVQVDPL--GLRYQALAQGQIDV--AVGFGTDGQIAAYGLVVLEDDKNLFPPYQVAPVVRQDVLDA 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 513037883 266 YPQIADWLQPVFASLDEKTLQQLNARIAVEGLDAKKVAADYLR 308
Cdd:cd13614  222 NPKIAEVLNKLSALLDNETMQRLNYEVDGNKREPKDVAREFLK 264
OpuAC pfam04069
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity ...
26-309 3.76e-55

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: 179.83  E-value: 3.76e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883   26 PVTVGSKIDTEGALLGNMILQVLESHGVKtVNKIQLGTTPVVRGAITAGELDIYPAageldiypEYTGNGafffkdendp 105
Cdd:pfam04069   2 TIVIGSKNWTEQEILANIAAQLLEALGYV-VELVGLGSSAVLFAALASGDIDLYPE--------EWTGTT---------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  106 awknakqgFEKVKKLDAEQNKLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLSRYlkeGGTFKLAASAEFIERADALP 185
Cdd:pfam04069  63 --------YEAYKKAVEEKLGLLVLGPLGAGNTYGLAVPKYVAEKPGIKSISDLAKP---ADDLELGFKGEFIGRPDGWG 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  186 ------AFEKAYDFTLNQNQLLSLAGGDTAvtIKAAAQQTSgVNAAMAYGTDGPVAALGLQTLSDPKGVQ-PIYAPAPVV 258
Cdd:pfam04069 132 cmrsteGLLKAYGLDKYELVEGSEAAMDAL--IYAAYKRGE-PDVVYAWTPDWMIKKYDLVVLEDPKGLFpPAYNVVPVV 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 513037883  259 RESVLQAYPQIADWLQPVfaSLDEKTLQQLNARIAVEGLDAKKVAADYLRQ 309
Cdd:pfam04069 209 RKGFAEKHPEVAAFLNKL--SLDTEDLNELNAQVDVEGKDPEEVAKDWLAE 257
PBP2_Opu_like_1 cd13609
Substrate-binding domain of putative ABC-type osmoprotectant uptake system; the type 2 ...
27-308 3.03e-53

Substrate-binding domain of putative ABC-type osmoprotectant uptake system; the type 2 periplasmic-binding protein fold; This group includes the periplasmic substrate-binding component of a putative ABC transport system that is predicted to be involved in uptake of osmoprotectants (also termed compatible solutes) such as betaine, choline, proline betaine, carnitine, and L-proline. The relative substrate preference of this group is not known. To counteract the efflux of water, many microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270327  Cd Length: 263  Bit Score: 175.10  E-value: 3.03e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  27 VTVGSKIDTEGALLGNMILQVLESH-GVKTVNKIQLGTTPVVRGAITAGELDIYPaageldiypEYTGNG-AFFFKDEND 104
Cdd:cd13609    2 IVIGSKNFTEQLILGNMYADLIEANtDIKVERKLNLGGSSVCFSALKNGDIDMYV---------DYTGTIlVNILKEPPI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 105 pawKNAKQGFEKVKKLDAEQNKLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLSRYlkeGGTFKLAASAEFIERADAL 184
Cdd:cd13609   73 ---SDPDEVYNTVKELMKEKYNLEVLKPLGFNNTYTLAVRKETAEKYNLKTISDLAKV---SDELTLGCTLEFLNREDGL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 185 PAFEKAYDftLNQNQLLSLAGGdtavtIKAAAQQTSGVNAAMAYGTDGPVAALGLQTLSDPKGVQPIYAPAPVVRESVLQ 264
Cdd:cd13609  147 PGLEKTYG--LNFKDVKGLDGS-----LRYTALENGEVDVIDAFSTDGLLKKFDLVVLEDDKNFFPPYYAVPLVREETLE 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 513037883 265 AYPQIADWLQPVFASLDEKTLQQLNARIAVEGLDAKKVAADYLR 308
Cdd:cd13609  220 KYPELEDVLNKLAGKISEETMRELNYKVDELGKDPEDVAHEFLV 263
PBP2_ProWY cd13615
Substrate-binding domain of ABC-type osmoregulated transporter; the type 2 periplasmic-binding ...
26-307 1.39e-52

Substrate-binding domain of ABC-type osmoregulated transporter; the type 2 periplasmic-binding protein fold; Osmoprotectant binding lipoprotein ProWY of Streptococcus thermophilus is predicted to be involved in uptake of compatible solutes such as choline, L-proline and glycine betaine, but the relative substrate preference is not known. To counteract the efflux of water, microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. ProWY belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270333  Cd Length: 262  Bit Score: 173.40  E-value: 1.39e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  26 PVTVGSKIDTEGALLGNMILQVLESHGVKTVNKIQLGTTpVVRGAITAGELDIYPaageldiypEYTGNGAFFFKDEndP 105
Cdd:cd13615    1 AIRVGSKDFTENLIVAEIYALALEDAGYKVKRKPNISSS-VVHQALTSGQIDLYP---------EYTGTGLLAVLKK--E 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 106 AWKNAKQGFEKVKKLDAEQNKLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLSrylKEGGTFKLAASAEFIERADALP 185
Cdd:cd13615   69 AITDPQKVYATVKDGYAKKFNLVWLDYAPANDGQGLVIRTSVAKKYGIKTISDLQ---KNASQIRFASQGEFDQREDGLP 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 186 AFEKAY-DFTLNQNQLLslaggDTAVTIKAAAQQTSgvNAAMAYGTDGPVAALGLQTLSDPKGVQPIYAPAPVVRESVLQ 264
Cdd:cd13615  146 GLEKVYgKFSFKSTKVY-----DNGLKYQVLANDKA--DITPAYTTEGQLDTSKFTLLKDDKHVWPPYNLAPVVRKDVLK 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 513037883 265 AYPQIADWLQPVFASLDEKTLQQLNARIAVEGLDAKKVAADYL 307
Cdd:cd13615  219 ANPKIASALNKVSAKLTTKTLTQLNAKVDVDKQEYADVAKDFY 261
PBP2_ProWX cd13612
Substrate-binding protein ProWX of ABC-type osmoregulated transporter and its related proteins; ...
26-311 8.79e-45

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: 153.16  E-value: 8.79e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  26 PVTVGSKIDTEGALLGNMILQVLESHGVKTVNKIQlgttpvvrgAITAGELDIYPA--AGELDIYPEYTGNGAFFF--KD 101
Cdd:cd13612    1 TIHIATKPMTEQYILGEMLKQLIEQDTDLKVELTK---------GVGGGTSNIHPAmvKGEFDLYPEYTGTGWLFVlkKD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 102 ENDPAWKnakqgFEKVKKLDAEQNKLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLSRYlkeGGTFKLAASAEFIERA 181
Cdd:cd13612   72 GTYSEEL-----FDQLQKEYEEKYNLTWLGLYGFNNTYGLAVRKELAEKYNLKTYSDLAKV---SNQLVFGAEYDFFERE 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 182 DALPAFEKAYDFTLNQNQllslaggDTAVTIKAAAQQTSGVNAAMAYGTDGPVAALGLQTLSDPKGVQPIYAPAPVVRES 261
Cdd:cd13612  144 DGYDALQKAYGFNFKKTV-------DMDIGLKYQAIESGKVDVINVFTTDGQLSDADIVVLEDDKGFFPSYYAGTVVREE 216
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 513037883 262 VLQAYPQIADWLQPVFASLDEKTLQQLNARIAVEGLDAKKVAADYLRQKG 311
Cdd:cd13612  217 TLEKYPELEDVLEKLTGLISDEDMAEMNYQVEIEKKDPKDVAKEFLEEKG 266
PBP2_Opu_like_2 cd13613
Substrate-binding domain of putative ABC-type osmoprotectant uptake system; the type 2 ...
26-307 3.44e-43

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: 149.03  E-value: 3.44e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  26 PVTVGSKIDTEGALLGNMILQVLESHGVKTVN-KIQLGTTPVVRGAITAGELDIYPaageldiypEYTGNG--AFFFKde 102
Cdd:cd13613    1 RIIIGSKNFTEQVILGELLAQQIEARTDLKVErRFNLGGTFICHQALLSGAIDAYV---------EYTGTAltAILKQ-- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 103 ndPAWKNAKQGFEKVKKLDAEQNKLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLSRYLKeggTFKLAASAEFIERAD 182
Cdd:cd13613   70 --PPIRDPQRVYEQVKQLYADRFGLEVMPPLGFENTFAILVRGEDARKLGLKTLSDAAPYTP---GWRAGFGYEFLERAD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 183 ALPAFEKAYDFTLNQnqllSLAGGDTAVTIKAAAQQTsgVNAAMAYGTDGPVAALGLQTLSDPKGVQPIYAPAPVVRESV 262
Cdd:cd13613  145 GYPGLAKTYGLKFAK----TPRVMDLGLLYRALAQKQ--VDLIAGNSTDGLIAALDLVILEDDRHYFPPYQAVPVVRQAT 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 513037883 263 LQAYPQiadwLQPVFASLDEK----TLQQLNARIAVEGLDAKKVAADYL 307
Cdd:cd13613  219 LAKYPE----LRTAIAELAGKisaeTMQQMNYQVDGEHRDVAEVAREFL 263
PBP2_AfProX_like cd13607
Substrate-binding protein ProX of ABC-type osmoregulatory transporter from Archaeoglobus ...
26-308 3.04e-42

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: 146.57  E-value: 3.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  26 PVTVGSKIDTEGALLGNMILQVLESHGVKTVNKIQLGTTPVVRGAItageldiypAAGELDIYPEYTG---NGAFFFKDE 102
Cdd:cd13607    1 TVVIGSKTFTEQYILAEMIAQLLEEAGYPAEHREGLGGTRVLFEAL---------KSGEIDVYVEYTGtlyAEILKRPET 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 103 NDPAwknakQGFEKVKKLDAEQNkLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLSRYLKEggtFKLAASAEFIERAD 182
Cdd:cd13607   72 WDPA-----AVLAELKEALAERG-IVVAGPLGFENTYALAMREDRAEALGIRTISDLLARAPD---LRFGFDPEFLDRPD 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 183 ALPAFEKAYDFTLNQnqllsLAGGDTAVTIKAAAQQTsgVNAAMAYGTDGPVAALGLQTLSDPKGVQPIYAPAPVVRESV 262
Cdd:cd13607  143 GWPALRRVYGLPFKE-----VRGLDHTLAYRALKSGQ--VDVIDAYTTDARIDAYDLRVLEDDRGAFPPYDAVLLYRADL 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 513037883 263 LQAYPQIADWLQPVFASLDEKTLQQLNARIAVEGLDAKKVAADYLR 308
Cdd:cd13607  216 AERAPKAVAALRRLEGRIDADTMRALNAQVDLEKRSEAEVAAEFLA 261
PBP2_ChoS cd13610
Substrate-binding domain ChoS of an osmoregulated ABC-type transporter and related proteins; ...
27-307 3.84e-42

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: 146.20  E-value: 3.84e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  27 VTVGSKIDTEGALLGNMILQVLESHGVK-TVN-KIQLGTTPVVRGAITAGELDIYPaageldiypEYTGnGAFFFKDEND 104
Cdd:cd13610    2 IVIAGKLGSEPDILINMYKLLIEEETPDlQVTlKPNFGKTSFLFNALKSGDIDIYP---------EFTG-TVLETLLKEP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 105 PAWKNAKQGFEKVKKLDAEQNKLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLSRYLKEggtFKLAASAEFIERADAL 184
Cdd:cd13610   72 PKSNDPMEVYEQARDGLAKQYQLTYLKPMAYNNTYALAVKKEFAKQHNLKTISDLQKVQDK---LKAGFTLEFMDREDGY 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 185 PAFEKAYDFTLNqnqLLSLaggDTAVTIKAAAQQTsgVNAAMAYGTDGPVAALGLQTLSDPKGVQPIYAPAPVVRESVLQ 264
Cdd:cd13610  149 KGLQKAYGLNFN---VKSM---EPALRYQAINNGQ--VNVIDAYSTDSEIKQYDLVVLKDDKHLFPPYQGAPLMREEFLK 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 513037883 265 AYPQIADWLQPVFASLDEKTLQQLNARIAVEGLDAKKVAADYL 307
Cdd:cd13610  221 KHPELVKALNKLAGKITDEEMQEMNYRVDVKHKSAAKVAKEYL 263
PBP2_OpuCC_like cd13608
Substrate-binding protein OpuCC of ABC-type osmoregulatory transporter and related proteins; ...
26-308 8.72e-38

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: 135.06  E-value: 8.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  26 PVTVGSKIDTEGALLGNMILQVLESH---GVKTVNKiqLGTTPVVRGAITAGELDIypaageldIYPEYTG---NGAFFF 99
Cdd:cd13608    1 TIRIGSQSTTESQILAEMVKQLIEHYtdlKVELINN--LGSSTVQHQAMLNGDANI--------SAARYTGtdlTGELGM 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 100 KDENDPawknaKQGFEKVKKLDAEQNKLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLSRYLKEggtFKLAASAEFIE 179
Cdd:cd13608   71 EPIKDP-----EKALKVVQKEFQKRFDQTWFDSYGFANTYAFMVTKEFAEKYNLKKVSDLKKVADN---LKLGVDTSWLN 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 180 R-ADALPAFEKAYDFTLNQnqllsLAGGDTAVTIKAAAQQTsgVNAAMAYGTDGPVAALGLQTLSDPKGVQPIYAPAPVV 258
Cdd:cd13608  143 RkGDGYPGFKETYGFDFGT-----VYPMQIGLVYDAVASGK--MDVVLGYSTDGRIKSYDLVVLEDDKQFFPPYDASPVA 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 513037883 259 RESVLQAYPQIADWLQPVFASLDEKTLQQLNARIAVEGLDAKKVAADYLR 308
Cdd:cd13608  216 TNEILKKYPELEEILEKLEGKISTETMQELNYQVDNDLKEPSVVAKEFLE 265
PBP2_ProX_like cd13606
Bacterial substrate-binding protein ProX of ABC-type osmoregulated transporter and its related ...
26-308 4.22e-34

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: 125.37  E-value: 4.22e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883  26 PVTVGSKIDTEGALLGNMILQVLESHGVKTVNKIQLGTTPVVRGAITAGEldiypaageLDIYPEYTGNGAFFFKDENDP 105
Cdd:cd13606    1 TVVVGSADFPESEILAEIYAQALEAAGVKVTRKLNIGSREVYLPALEDGS---------IDLVPEYTGNLLQYLDKDATA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 106 AWKNAKQGfEKVKKLDAEqnkLVWLTPAPANNTWTIAVRQDIAEKNKLSSLADLSrylKEGGTFKLAASAEFIERADALP 185
Cdd:cd13606   72 TDPEEVYA-ALKAALPEG---LEVLDPSPAEDKDALVVTKETAEKYGLKSIADLA---PVAGELTLGGPPEFKTRPYGLP 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513037883 186 AFEKAYDFTLNQNQLLSLAGgdtAVTIKAAAQQTsgVNAAMAYGTDGPVAALGLQTLSDPKGVQPIYAPAPVVRESVLQa 265
Cdd:cd13606  145 GLKEVYGVTFKEFKPLDAGG---PLTVKALKDGT--VQVANIFTTDPAIADNGLVVLEDPKNLFPAQNVVPLVRKAKLD- 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 513037883 266 yPQIADWLQPVFASLDEKTLQQLNARIAVEGLDAKKVAADYLR 308
Cdd:cd13606  219 -DKAADALNAVSAKLTTEDLTELNKQVVGDKADPADVAKEWLK 260
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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