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Conserved domains on  [gi|1130619298]
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Chain A, Substrate-binding region of ABC-type glycine betaine transport system

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 ...
22-295 5.21e-159

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: 444.08  E-value: 5.21e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  22 QVAVSSKIDTEGGVLGNIILTVLNANGIKTTDRIQLGATPVVRKAITAGEIDIYPEYTGNAAFFFNKADDPLWKDPAKAY 101
Cdd:cd13616     1 PVVVGSKIDTEGALLGNMIVLALEAHGFPVEDKTGLGTTPVVRKALLSGEIDLYPEYTGNGAFFFPEADDPVWKDARKGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 102 ETAKKLDYDANKIVWLTPSPANNTWGIAVRKDVANENKLASLSDFGKYIAGGGKVVLAASSEFVNSAAALPAFQTAYGFT 181
Cdd:cd13616    81 ETVKELDAKNNGLVWLDPAPANNTWAIAVRRDLAEKNNLKTLADLAAYVNEGGAFKLAASAEFVERPDALPAFEKAYGFK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 182 LKPDQLITLSGGDTAATIAAAANQTNGANAAMVYGTDGGIAPSGLVVLEDDKHVQPVYQPAPIIREEVLKKDPKIEELLK 261
Cdd:cd13616   161 LSKDQLVILSGGNTAQTEQAAAQGTSGVNAAMAYGTDGAIAALGLVVLEDPKGAQPVYAPAPVVRQEVLEAYPEIAEILK 240
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1130619298 262 PVFEKLDLTTLQDLNGRVQLGGEPAKAVAEDFLK 295
Cdd:cd13616   241 PVFATLDLKTLQELNARIAVEGESAEDVARDYLK 274
 
Name Accession Description Interval E-value
PBP2_OsmF cd13616
Substrate-binding domain OsmF of an osmoregulated ABC-type transporter; the type 2 ...
22-295 5.21e-159

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: 444.08  E-value: 5.21e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  22 QVAVSSKIDTEGGVLGNIILTVLNANGIKTTDRIQLGATPVVRKAITAGEIDIYPEYTGNAAFFFNKADDPLWKDPAKAY 101
Cdd:cd13616     1 PVVVGSKIDTEGALLGNMIVLALEAHGFPVEDKTGLGTTPVVRKALLSGEIDLYPEYTGNGAFFFPEADDPVWKDARKGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 102 ETAKKLDYDANKIVWLTPSPANNTWGIAVRKDVANENKLASLSDFGKYIAGGGKVVLAASSEFVNSAAALPAFQTAYGFT 181
Cdd:cd13616    81 ETVKELDAKNNGLVWLDPAPANNTWAIAVRRDLAEKNNLKTLADLAAYVNEGGAFKLAASAEFVERPDALPAFEKAYGFK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 182 LKPDQLITLSGGDTAATIAAAANQTNGANAAMVYGTDGGIAPSGLVVLEDDKHVQPVYQPAPIIREEVLKKDPKIEELLK 261
Cdd:cd13616   161 LSKDQLVILSGGNTAQTEQAAAQGTSGVNAAMAYGTDGAIAALGLVVLEDPKGAQPVYAPAPVVRQEVLEAYPEIAEILK 240
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1130619298 262 PVFEKLDLTTLQDLNGRVQLGGEPAKAVAEDFLK 295
Cdd:cd13616   241 PVFATLDLKTLQELNARIAVEGESAEDVARDYLK 274
OsmF COG1732
Periplasmic glycine betaine/choline-binding (lipo)protein of an ABC-type transport system ...
23-297 6.48e-108

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: 315.16  E-value: 6.48e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  23 VAVSSKIDTEGGVLGNIILTVLNANGIKTTDRIQLGATPVVRKAITAGEIDIYPEYTGNAAFFFNKADDPlwKDPAKAYE 102
Cdd:COG1732    32 IVVGSKNFTEQEILAEIYAQALEAAGLKVERKLNLGGTEVVRQALKSGEIDLYPEYTGTALTTYLKEDPI--TDPEEVYE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 103 TAKKLDYDANKIVWLTPSPANNTWGIAVRKDVANENKLASLSDFGKYIaggGKVVLAASSEFVNSAAALPAFQTAYGFTL 182
Cdd:COG1732   110 AVKEALPEKNGLTWLDPAGFNNTYALAVTKETAEKYGLKTISDLAKVA---GELTLGADPEFAERPDGLPGLKKAYGFEF 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 183 KpdQLITLSGGdtaatIAAAANQTNGANAAMVYGTDGGIAPSGLVVLEDDKHVQPVYQPAPIIREEVLKKDPKIEELLKP 262
Cdd:COG1732   187 K--EVKPMDTG-----LTYTALANGQVDVADAYTTDGRIAALDLVVLEDDKNFFPPYNAAPLVRKEVLEKYPELAEVLNK 259
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1130619298 263 VFEKLDLTTLQDLNGRVQLGGEPAKAVAEDFLKKN 297
Cdd:COG1732   260 LSGKLTTETMQELNYQVDVDGEDPADVAREFLKEK 294
OpuAC pfam04069
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity ...
23-296 8.99e-47

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: 157.87  E-value: 8.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  23 VAVSSKIDTEGGVLGNIILTVLNANGIKTtDRIQLGATPVVRKAITAGEIDIYP-EYTGNAafffnkaddplwkdpakaY 101
Cdd:pfam04069   3 IVIGSKNWTEQEILANIAAQLLEALGYVV-ELVGLGSSAVLFAALASGDIDLYPeEWTGTT------------------Y 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 102 ETAKKLDYDANKIVWLTPSPANNTWGIAVRKDVANENKLASLSDFGKYiagGGKVVLAASSEFVNSAAALPAFQT----- 176
Cdd:pfam04069  64 EAYKKAVEEKLGLLVLGPLGAGNTYGLAVPKYVAEKPGIKSISDLAKP---ADDLELGFKGEFIGRPDGWGCMRStegll 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 177 -AYGFTlkpdqLITLSGGDTAATIAAAAN--QTNGANAAMVYGTDGGIAPSGLVVLEDDKHVQ-PVYQPAPIIREEVLKK 252
Cdd:pfam04069 141 kAYGLD-----KYELVEGSEAAMDALIYAayKRGEPDVVYAWTPDWMIKKYDLVVLEDPKGLFpPAYNVVPVVRKGFAEK 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1130619298 253 DPKIEELLKPVfeKLDLTTLQDLNGRVQLGGEPAKAVAEDFLKK 296
Cdd:pfam04069 216 HPEVAAFLNKL--SLDTEDLNELNAQVDVEGKDPEEVAKDWLAE 257
 
Name Accession Description Interval E-value
PBP2_OsmF cd13616
Substrate-binding domain OsmF of an osmoregulated ABC-type transporter; the type 2 ...
22-295 5.21e-159

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: 444.08  E-value: 5.21e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  22 QVAVSSKIDTEGGVLGNIILTVLNANGIKTTDRIQLGATPVVRKAITAGEIDIYPEYTGNAAFFFNKADDPLWKDPAKAY 101
Cdd:cd13616     1 PVVVGSKIDTEGALLGNMIVLALEAHGFPVEDKTGLGTTPVVRKALLSGEIDLYPEYTGNGAFFFPEADDPVWKDARKGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 102 ETAKKLDYDANKIVWLTPSPANNTWGIAVRKDVANENKLASLSDFGKYIAGGGKVVLAASSEFVNSAAALPAFQTAYGFT 181
Cdd:cd13616    81 ETVKELDAKNNGLVWLDPAPANNTWAIAVRRDLAEKNNLKTLADLAAYVNEGGAFKLAASAEFVERPDALPAFEKAYGFK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 182 LKPDQLITLSGGDTAATIAAAANQTNGANAAMVYGTDGGIAPSGLVVLEDDKHVQPVYQPAPIIREEVLKKDPKIEELLK 261
Cdd:cd13616   161 LSKDQLVILSGGNTAQTEQAAAQGTSGVNAAMAYGTDGAIAALGLVVLEDPKGAQPVYAPAPVVRQEVLEAYPEIAEILK 240
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1130619298 262 PVFEKLDLTTLQDLNGRVQLGGEPAKAVAEDFLK 295
Cdd:cd13616   241 PVFATLDLKTLQELNARIAVEGESAEDVARDYLK 274
OsmF COG1732
Periplasmic glycine betaine/choline-binding (lipo)protein of an ABC-type transport system ...
23-297 6.48e-108

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: 315.16  E-value: 6.48e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  23 VAVSSKIDTEGGVLGNIILTVLNANGIKTTDRIQLGATPVVRKAITAGEIDIYPEYTGNAAFFFNKADDPlwKDPAKAYE 102
Cdd:COG1732    32 IVVGSKNFTEQEILAEIYAQALEAAGLKVERKLNLGGTEVVRQALKSGEIDLYPEYTGTALTTYLKEDPI--TDPEEVYE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 103 TAKKLDYDANKIVWLTPSPANNTWGIAVRKDVANENKLASLSDFGKYIaggGKVVLAASSEFVNSAAALPAFQTAYGFTL 182
Cdd:COG1732   110 AVKEALPEKNGLTWLDPAGFNNTYALAVTKETAEKYGLKTISDLAKVA---GELTLGADPEFAERPDGLPGLKKAYGFEF 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 183 KpdQLITLSGGdtaatIAAAANQTNGANAAMVYGTDGGIAPSGLVVLEDDKHVQPVYQPAPIIREEVLKKDPKIEELLKP 262
Cdd:COG1732   187 K--EVKPMDTG-----LTYTALANGQVDVADAYTTDGRIAALDLVVLEDDKNFFPPYNAAPLVRKEVLEKYPELAEVLNK 259
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1130619298 263 VFEKLDLTTLQDLNGRVQLGGEPAKAVAEDFLKKN 297
Cdd:COG1732   260 LSGKLTTETMQELNYQVDVDGEDPADVAREFLKEK 294
PBP2_osmoprotectants cd13528
Substrate-binding domain of osmoregulatory ABC-type transporters; the type 2 ...
23-295 1.65e-83

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: 252.13  E-value: 1.65e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  23 VAVSSKIDTEGGVLGNIILTVLNANG-IKTTDRIQLGATPVVRKAITAGEIDIYPEYTGNAAFFFNKADDPlWKDPAKAY 101
Cdd:cd13528     2 IVVGSKNFTEQYILGEMLAQLLEANTdLTVERKLNLGGTEVAFNALKNGDIDLYVEYTGTALLTILKEDAP-ITDPEEVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 102 ETAKKLDYDANKIVWLTPSPANNTWGIAVRKDVANENKLASLSDfgkYIAGGGKVVLAASSEFVNSAAALPAFQTAYGFT 181
Cdd:cd13528    81 EKVKKEYEEKFGLTWLDPLGFNNTYALAVRKDTAEKYGLKTISD---LAPHSDQLVFGADPEFYERSDGLPGLKKTYGFD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 182 LKpdqliTLSGGDTAATIAAAANQTngANAAMVYGTDGGIAPSGLVVLEDDKHVQPVYQPAPIIREEVLKKDPKIEELLK 261
Cdd:cd13528   158 FK-----EVKTMDPGLTYEALDNGE--VDVIDAFSTDGRIKAFDLVVLEDDKNFFPPYNAAPVVREDVLKKHPELEEVLN 230
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1130619298 262 PVFEKLDLTTLQDLNGRVQLGGEPAKAVAEDFLK 295
Cdd:cd13528   231 KLSGKLTDETMQQLNYQVDVEGKDPEEVARDFLK 264
PBP2_YehZ cd13611
Substrate-binding domain YehZ of an osmoregulated ABC-type transporter; the type 2 ...
23-295 3.99e-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: 235.94  E-value: 3.99e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  23 VAVSSKIDTEGGVLGNIILTVLNANGIKTTDRIQLGATPVVRKAITAGEIDIYPEYTGNAAFFFNKADDPLwKDPAKAYE 102
Cdd:cd13611     2 ITVGSKDFTEQLILGKITVQALQAAGADVTDKTNLGGSASARQALENGQVDVYWEYTGTAWITYLGHTEPI-LDPQEQYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 103 TAKKLDYdANKIVWLTPSPANNTWGIAVRKDVANENKLASLSDFGKYIAGGGKVVLAASSEFVNSAAALPAFQTAYGFTL 182
Cdd:cd13611    81 AVKDLDA-EKGLVWLDPAPLNNTYALAMREATAEELGITTLSDLALAKLPPGDRTFCVDAEFASRPDGLPPLLEAYGFEF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 183 KPDQLITLSGGdtaatiaAAANQT-NGA-NAAMVYGTDGGIAPSGLVVLEDDKHVQPVYQPAPIIREEVLKKDPKIEELL 260
Cdd:cd13611   160 PRANVRQMDTG-------LVYTATaNGQcDFGEVFTTDGRIKALDLVVLEDDKGFFPAYNAAPVVRTEVLDAHPELAEIL 232
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1130619298 261 KPVFEKLDLTTLQDLNGRVQLGGEPAKAVAEDFLK 295
Cdd:cd13611   233 NPISAKLDNDTMQELNARVDVDGEDPADVARDWLV 267
PBP2_QAT_like cd13614
Substrate-binding domain of quaternary amine ABC-type transporter; the type 2 ...
23-295 2.98e-62

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: 197.99  E-value: 2.98e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  23 VAVSSKIDTEGGVLGNIILTVLNANGIKTTDRIQLGATPVVRKAITAGEIDIYPEYTGNAAFFFNKAddPLWKDPAKAYE 102
Cdd:cd13614     2 IRVGSKNFTEQFILGEMYALALEDAGIKVERKLNLGGTLIAHQALVNGEIDLYPEYTGTALLTVLKG--EPSSDAKQVYK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 103 TAKKLDYDANKIVWLTPSPANNTWGIAVRKDVANENKLASLSDFGKyiaGGGKVVLAASSEFVNSAAALPAFQTAYG-FT 181
Cdd:cd13614    80 TVKDAYAEQFQLTWLEPAPFNNTYALVMTRETAEKYGIKTLSDLAK---AAGELVFGGGPEFQDREDGLPGLKAKYGaFD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 182 LKPDQLITLSGGDTAATIAAAANQTNGanaamvYGTDGGIAPSGLVVLEDDKHVQPVYQPAPIIREEVLKKDPKIEELLK 261
Cdd:cd13614   157 FKEFVQVDPLGLRYQALAQGQIDVAVG------FGTDGQIAAYGLVVLEDDKNLFPPYQVAPVVRQDVLDANPKIAEVLN 230
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1130619298 262 PVFEKLDLTTLQDLNGRVQLGGEPAKAVAEDFLK 295
Cdd:cd13614   231 KLSALLDNETMQRLNYEVDGNKREPKDVAREFLK 264
PBP2_ProWY cd13615
Substrate-binding domain of ABC-type osmoregulated transporter; the type 2 periplasmic-binding ...
23-295 2.69e-56

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: 182.64  E-value: 2.69e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  23 VAVSSKIDTEGGVLGNIILTVLNANGIKTTDRIQLGATpVVRKAITAGEIDIYPEYTGNAAFFFNKAddPLWKDPAKAYE 102
Cdd:cd13615     2 IRVGSKDFTENLIVAEIYALALEDAGYKVKRKPNISSS-VVHQALTSGQIDLYPEYTGTGLLAVLKK--EAITDPQKVYA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 103 TAKKlDYDAN-KIVWLTPSPANNTWGIAVRKDVANENKLASLSDFGKyiaGGGKVVLAASSEFVNSAAALPAFQTAYG-F 180
Cdd:cd13615    79 TVKD-GYAKKfNLVWLDYAPANDGQGLVIRTSVAKKYGIKTISDLQK---NASQIRFASQGEFDQREDGLPGLEKVYGkF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 181 TLKPDQLItlsggDTAATIAAAANqtNGANAAMVYGTDGGIAPSGLVVLEDDKHVQPVYQPAPIIREEVLKKDPKIEELL 260
Cdd:cd13615   155 SFKSTKVY-----DNGLKYQVLAN--DKADITPAYTTEGQLDTSKFTLLKDDKHVWPPYNLAPVVRKDVLKANPKIASAL 227
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1130619298 261 KPVFEKLDLTTLQDLNGRVQLGGEPAKAVAEDFLK 295
Cdd:cd13615   228 NKVSAKLTTKTLTQLNAKVDVDKQEYADVAKDFYL 262
PBP2_Opu_like_1 cd13609
Substrate-binding domain of putative ABC-type osmoprotectant uptake system; the type 2 ...
22-295 9.74e-52

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: 170.86  E-value: 9.74e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  22 QVAVSSKIDTEGGVLGNIILTVLNAN-GIKTTDRIQLGATPVVRKAITAGEIDIYPEYTGNAafFFNKADDPLWKDPAKA 100
Cdd:cd13609     1 TIVIGSKNFTEQLILGNMYADLIEANtDIKVERKLNLGGSSVCFSALKNGDIDMYVDYTGTI--LVNILKEPPISDPDEV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 101 YETAKKLDYDANKIVWLTPSPANNTWGIAVRKDVANENKLASLSDFGKYiagGGKVVLAASSEFVNSAAALPAFQTAYGF 180
Cdd:cd13609    79 YNTVKELMKEKYNLEVLKPLGFNNTYTLAVRKETAEKYNLKTISDLAKV---SDELTLGCTLEFLNREDGLPGLEKTYGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 181 TLKpdQLITLSGGdtAATIAAAANQTNGANAamvYGTDGGIAPSGLVVLEDDKHVQPVYQPAPIIREEVLKKDPKIEELL 260
Cdd:cd13609   156 NFK--DVKGLDGS--LRYTALENGEVDVIDA---FSTDGLLKKFDLVVLEDDKNFFPPYYAVPLVREETLEKYPELEDVL 228
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1130619298 261 KPVFEKLDLTTLQDLNGRVQLGGEPAKAVAEDFLK 295
Cdd:cd13609   229 NKLAGKISEETMRELNYKVDELGKDPEDVAHEFLV 263
OpuAC pfam04069
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity ...
23-296 8.99e-47

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: 157.87  E-value: 8.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  23 VAVSSKIDTEGGVLGNIILTVLNANGIKTtDRIQLGATPVVRKAITAGEIDIYP-EYTGNAafffnkaddplwkdpakaY 101
Cdd:pfam04069   3 IVIGSKNWTEQEILANIAAQLLEALGYVV-ELVGLGSSAVLFAALASGDIDLYPeEWTGTT------------------Y 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 102 ETAKKLDYDANKIVWLTPSPANNTWGIAVRKDVANENKLASLSDFGKYiagGGKVVLAASSEFVNSAAALPAFQT----- 176
Cdd:pfam04069  64 EAYKKAVEEKLGLLVLGPLGAGNTYGLAVPKYVAEKPGIKSISDLAKP---ADDLELGFKGEFIGRPDGWGCMRStegll 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 177 -AYGFTlkpdqLITLSGGDTAATIAAAAN--QTNGANAAMVYGTDGGIAPSGLVVLEDDKHVQ-PVYQPAPIIREEVLKK 252
Cdd:pfam04069 141 kAYGLD-----KYELVEGSEAAMDALIYAayKRGEPDVVYAWTPDWMIKKYDLVVLEDPKGLFpPAYNVVPVVRKGFAEK 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1130619298 253 DPKIEELLKPVfeKLDLTTLQDLNGRVQLGGEPAKAVAEDFLKK 296
Cdd:pfam04069 216 HPEVAAFLNKL--SLDTEDLNELNAQVDVEGKDPEEVAKDWLAE 257
PBP2_ProX_like cd13606
Bacterial substrate-binding protein ProX of ABC-type osmoregulated transporter and its related ...
31-295 1.28e-43

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: 149.64  E-value: 1.28e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  31 TEGGVLGNIILTVLNANGIKTTDRIQLGATPVVRKAITAGEIDIYPEYTGNAAFFFNKADDPlwKDPAKAYET-AKKLDy 109
Cdd:cd13606    10 PESEILAEIYAQALEAAGVKVTRKLNIGSREVYLPALEDGSIDLVPEYTGNLLQYLDKDATA--TDPEEVYAAlKAALP- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 110 daNKIVWLTPSPANNTWGIAVRKDVANENKLASLSDFGKYiagGGKVVLAASSEFVNSAAALPAFQTAYGftLKPDQLIT 189
Cdd:cd13606    87 --EGLEVLDPSPAEDKDALVVTKETAEKYGLKSIADLAPV---AGELTLGGPPEFKTRPYGLPGLKEVYG--VTFKEFKP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 190 LSGGDTAATIAAAANQTNGANaamVYGTDGGIAPSGLVVLEDDKHVQPVYQPAPIIREEVLkkDPKIEELLKPVFEKLDL 269
Cdd:cd13606   160 LDAGGPLTVKALKDGTVQVAN---IFTTDPAIADNGLVVLEDPKNLFPAQNVVPLVRKAKL--DDKAADALNAVSAKLTT 234
                         250       260
                  ....*....|....*....|....*.
gi 1130619298 270 TTLQDLNGRVQLGGEPAKAVAEDFLK 295
Cdd:cd13606   235 EDLTELNKQVVGDKADPADVAKEWLK 260
PBP2_ChoS cd13610
Substrate-binding domain ChoS of an osmoregulated ABC-type transporter and related proteins; ...
22-295 2.34e-43

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: 149.28  E-value: 2.34e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  22 QVAVSSKIDTEGGVLGNI--ILTVLNANGIKTTDRIQLGATPVVRKAITAGEIDIYPEYTGNAAFFFNKaDDPLWKDPAK 99
Cdd:cd13610     1 SIVIAGKLGSEPDILINMykLLIEEETPDLQVTLKPNFGKTSFLFNALKSGDIDIYPEFTGTVLETLLK-EPPKSNDPME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 100 AYETAKKLDYDANKIVWLTPSPANNTWGIAVRKDVANENKLASLSDFGKYIAgggKVVLAASSEFVNSAAALPAFQTAYG 179
Cdd:cd13610    80 VYEQARDGLAKQYQLTYLKPMAYNNTYALAVKKEFAKQHNLKTISDLQKVQD---KLKAGFTLEFMDREDGYKGLQKAYG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 180 FTLKpdqliTLSGGDTAATIAAAANQTNGANAamvYGTDGGIAPSGLVVLEDDKHVQPVYQPAPIIREEVLKKDPKIEEL 259
Cdd:cd13610   157 LNFN-----VKSMEPALRYQAINNGQVNVIDA---YSTDSEIKQYDLVVLKDDKHLFPPYQGAPLMREEFLKKHPELVKA 228
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1130619298 260 LKPVFEKLDLTTLQDLNGRVQLGGEPAKAVAEDFLK 295
Cdd:cd13610   229 LNKLAGKITDEEMQEMNYRVDVKHKSAAKVAKEYLQ 264
PBP2_Opu_like_2 cd13613
Substrate-binding domain of putative ABC-type osmoprotectant uptake system; the type 2 ...
22-295 3.34e-41

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: 143.63  E-value: 3.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  22 QVAVSSKIDTEGGVLGNIILTVLNANGIKTTDR-IQLGATPVVRKAITAGEIDIYPEYTGNAafFFNKADDPLWKDPAKA 100
Cdd:cd13613     1 RIIIGSKNFTEQVILGELLAQQIEARTDLKVERrFNLGGTFICHQALLSGAIDAYVEYTGTA--LTAILKQPPIRDPQRV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 101 YETAKKLDYDANKIVWLTPSPANNTWGIAVRKDVANENKLASLSDFGKYIAGggkVVLAASSEFVNSAAALPAFQTAYGF 180
Cdd:cd13613    79 YEQVKQLYADRFGLEVMPPLGFENTFAILVRGEDARKLGLKTLSDAAPYTPG---WRAGFGYEFLERADGYPGLAKTYGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 181 -TLKPDQLITLSggdtAATIAAAANQTN--GANAamvygTDGGIAPSGLVVLEDDKHVQPVYQPAPIIREEVLKKDPKIE 257
Cdd:cd13613   156 kFAKTPRVMDLG----LLYRALAQKQVDliAGNS-----TDGLIAALDLVILEDDRHYFPPYQAVPVVRQATLAKYPELR 226
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1130619298 258 ELLKPVFEKLDLTTLQDLNGRVQLGGEPAKAVAEDFLK 295
Cdd:cd13613   227 TAIAELAGKISAETMQQMNYQVDGEHRDVAEVAREFLK 264
PBP2_AfProX_like cd13607
Substrate-binding protein ProX of ABC-type osmoregulatory transporter from Archaeoglobus ...
22-295 4.49e-41

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: 143.11  E-value: 4.49e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  22 QVAVSSKIDTEGGVLGNIILTVLNANGIKTTDRIQLGATPVVRKAITAGEIDIYPEYTGNAAFffNKADDPLWKDPAKAY 101
Cdd:cd13607     1 TVVIGSKTFTEQYILAEMIAQLLEEAGYPAEHREGLGGTRVLFEALKSGEIDVYVEYTGTLYA--EILKRPETWDPAAVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 102 ETAKKLDYDANkIVWLTPSPANNTWGIAVRKDVANENKLASLSDFGKYIAgggKVVLAASSEFVNSAAALPAFQTAYGFT 181
Cdd:cd13607    79 AELKEALAERG-IVVAGPLGFENTYALAMREDRAEALGIRTISDLLARAP---DLRFGFDPEFLDRPDGWPALRRVYGLP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 182 LKpdqliTLSGGDTAATIAAAANqtNGANAAMVYGTDGGIAPSGLVVLEDDKHVQPVYQPAPIIREEVLKKDPKIEELLK 261
Cdd:cd13607   155 FK-----EVRGLDHTLAYRALKS--GQVDVIDAYTTDARIDAYDLRVLEDDRGAFPPYDAVLLYRADLAERAPKAVAALR 227
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1130619298 262 PVFEKLDLTTLQDLNGRVQLGGEPAKAVAEDFLK 295
Cdd:cd13607   228 RLEGRIDADTMRALNAQVDLEKRSEAEVAAEFLA 261
PBP2_ProWX cd13612
Substrate-binding protein ProWX of ABC-type osmoregulated transporter and its related proteins; ...
25-298 2.75e-39

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: 138.52  E-value: 2.75e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  25 VSSKIDTEGGVLGNII---------LTVLNANGIKttdriqlGATPVVRKAITAGEIDIYPEYTGNAAFFFNKADDPlwk 95
Cdd:cd13612     4 IATKPMTEQYILGEMLkqlieqdtdLKVELTKGVG-------GGTSNIHPAMVKGEFDLYPEYTGTGWLFVLKKDGT--- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  96 DPAKAYETAKKLDYDANKIVWLTPSPANNTWGIAVRKDVANENKLASLSDFGKYiagGGKVVLAASSEFVNSAAALPAFQ 175
Cdd:cd13612    74 YSEELFDQLQKEYEEKYNLTWLGLYGFNNTYGLAVRKELAEKYNLKTYSDLAKV---SNQLVFGAEYDFFEREDGYDALQ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 176 TAYGFTLKP--DQLITLSggdtaaTIAAAANQTNGANaamVYGTDGGIAPSGLVVLEDDKHVQPVYQPAPIIREEVLKKD 253
Cdd:cd13612   151 KAYGFNFKKtvDMDIGLK------YQAIESGKVDVIN---VFTTDGQLSDADIVVLEDDKGFFPSYYAGTVVREETLEKY 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1130619298 254 PKIEELLKPVFEKLDLTTLQDLNGRVQLGGEPAKAVAEDFLKKNG 298
Cdd:cd13612   222 PELEDVLEKLTGLISDEDMAEMNYQVEIEKKDPKDVAKEFLEEKG 266
PBP2_OpuCC_like cd13608
Substrate-binding protein OpuCC of ABC-type osmoregulatory transporter and related proteins; ...
22-295 2.20e-37

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: 133.52  E-value: 2.20e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298  22 QVAVSSKIDTEGGVLGNIILTVLNAN-GIKTTDRIQLGATPVVRKAITAGEIDI-YPEYTGNAafFFNKADDPLWKDPAK 99
Cdd:cd13608     1 TIRIGSQSTTESQILAEMVKQLIEHYtDLKVELINNLGSSTVQHQAMLNGDANIsAARYTGTD--LTGELGMEPIKDPEK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 100 AYETAKKLDYDANKIVWLTPSPANNTWGIAVRKDVANENKLASLSDFGKYIAgggKVVLAASSEFVN-SAAALPAFQTAY 178
Cdd:cd13608    79 ALKVVQKEFQKRFDQTWFDSYGFANTYAFMVTKEFAEKYNLKKVSDLKKVAD---NLKLGVDTSWLNrKGDGYPGFKETY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1130619298 179 GFTLK---PDQlITLsggdtaatiAAAANQTNGANAAMVYGTDGGIAPSGLVVLEDDKHVQPVYQPAPIIREEVLKKDPK 255
Cdd:cd13608   156 GFDFGtvyPMQ-IGL---------VYDAVASGKMDVVLGYSTDGRIKSYDLVVLEDDKQFFPPYDASPVATNEILKKYPE 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1130619298 256 IEELLKPVFEKLDLTTLQDLNGRV-QLGGEPAKaVAEDFLK 295
Cdd:cd13608   226 LEEILEKLEGKISTETMQELNYQVdNDLKEPSV-VAKEFLE 265
 
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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