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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712346021  44 NSVGAQVDHKIIGIDPGAGLMKATEKAMKDYDLKDWELVEGSSAAMTAALTQAYKDKKPIIVTGWTPHWMFSKFEMKYLE 123
Cdd:cd13639   101 LDHADKFGGKIVGIEPGAGLMKLTEEAIEEYGLLDYELVTSSTAAMLAELDRAIDNKEPIVVTGWSPHWMFAKYDLKYLE 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712346021 124 DPKGTFGKDEQIHTIVRKGLKDEHPSAYALLGKFSWTPADMEKVMLDIESGKKPEEAAAEWVKNNEATVNKWVE 197
Cdd:cd13639   181 DPKGVYGEAESIHTIARKGFEEDHPEAYEFLKNFKLTDEDLESLMLEIEDGGDPEEAAEEWIDENPDLVDEWLE 254

Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1712346021   1 MKKGTLKGLAVALGLSMVMAGCSNAGTPQGNQPAEGNTGT 40
Cdd:COG2182     1 MKRRLLAALALALALALALAACGSGSSSSGSSSAAGAGGT 40

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712346021  44 NSVGAQVDHKIIGIDPGAGLMKATEKAMKDYDLKDWELVEGSSAAMTAALTQAYKDKKPIIVTGWTPHWMFSKFEMKYLE 123
Cdd:cd13639   101 LDHADKFGGKIVGIEPGAGLMKLTEEAIEEYGLLDYELVTSSTAAMLAELDRAIDNKEPIVVTGWSPHWMFAKYDLKYLE 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712346021 124 DPKGTFGKDEQIHTIVRKGLKDEHPSAYALLGKFSWTPADMEKVMLDIESGKKPEEAAAEWVKNNEATVNKWVE 197
Cdd:cd13639   181 DPKGVYGEAESIHTIARKGFEEDHPEAYEFLKNFKLTDEDLESLMLEIEDGGDPEEAAEEWIDENPDLVDEWLE 254

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712346021  43 PNSVGAQVDHKIIGIDPGAGLMKATEKAMKDYDLKDWELVEGSSAAMTAALTQAYKDKKPIIVTGWTPHWMFSKFEMKYL 122
Cdd:pfam04069 112 ADDLELGFKGEFIGRPDGWGCMRSTEGLLKAYGLDKYELVEGSEAAMDALIYAAYKRGEPDVVYAWTPDWMIKKYDLVVL 191

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712346021 123 EDPKGTFGKDEQIHTIVRKGLKDEHPSAYALLGKFSWTPADMEKVMLDIE-SGKKPEEAAAEWVKN 187
Cdd:pfam04069 192 EDPKGLFPPAYNVVPVVRKGFAEKHPEVAAFLNKLSLDTEDLNELNAQVDvEGKDPEEVAKDWLAE 257

ABC-type proline/glycine betaine transport system, periplasmic component [Amino acid transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712346021 200 QPAEGKKLTLAYVAWDSEIASTNVVKTVLEqKLKYKVELSQVEAGPMWVGVSNGDVDGMVAAWLPTTHADYMEKLGKD-V 278
Cdd:COG2113    26 APGSCKTVTIADVGWTSATATTAVAKQILE-ELGYEVELVELDVPVTYQGLANGDIDVFLEAWLPTTHADYDEAYGDGkV 104

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1712346021 279 EDLGPNLQGTKLGLAVPAYM---EVNSIEDLKK 308
Cdd:COG2113   105 EDLGTNYEGAKQGLAVPKYVaepGIKSIADLKK 137

proline/glycine betaine ABC transporter substrate-binding protein ProX;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712346021  55 IGIDPGAGLMKATEKAMKDYDLKDW-ELVEGSSAAMTAALTQAYKDKKPIIVTGWTPHWMfsKFEMKYLED--------- 124
Cdd:PRK11119  155 TGCNPGWGCEAVINHQLKAYGLEDTvTHNQGNYAALMADTIARYKEGKPVLYYTWTPYWV--SDVLKPGKDvvwlqvpfs 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712346021 125 --PKGTFGKDE-------------QIHTIVRKGLKDEHPSAYALLGKFSWTPADMEKVMLDIESGKKPEE----AAAEWV 185
Cdd:PRK11119  233 slPGDQKNADTklpngknygfpvnTMHIVANKAFAEKNPAAAKLFEIMKLPLADINAQNLRMHEGESSEAdierHVDGWI 312

                         170
                  ....*....|..
gi 1712346021 186 KNNEATVNKWVE 197
Cdd:PRK11119  313 KAHQAQFDGWVK 324

Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1712346021   1 MKKGTLKGLAVALGLSMVMAGCSNAGTPQGNQPAEGNTGT 40
Cdd:COG2182     1 MKRRLLAALALALALALALAACGSGSSSSGSSSAAGAGGT 40

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712346021  44 NSVGAQVDHKIIGIDPGAGLMKATEKAMKDYDLKDWELVEGSSAAMTAALTQAYKDKKPIIVTGWTPHWMFSKFEMKYLE 123
Cdd:cd13639   101 LDHADKFGGKIVGIEPGAGLMKLTEEAIEEYGLLDYELVTSSTAAMLAELDRAIDNKEPIVVTGWSPHWMFAKYDLKYLE 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712346021 124 DPKGTFGKDEQIHTIVRKGLKDEHPSAYALLGKFSWTPADMEKVMLDIESGKKPEEAAAEWVKNNEATVNKWVE 197
Cdd:cd13639   181 DPKGVYGEAESIHTIARKGFEEDHPEAYEFLKNFKLTDEDLESLMLEIEDGGDPEEAAEEWIDENPDLVDEWLE 254

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712346021  43 PNSVGAQVDHKIIGIDPGAGLMKATEKAMKDYDLKDWELVEGSSAAMTAALTQAYKDKKPIIVTGWTPHWMFSKFEMKYL 122
Cdd:pfam04069 112 ADDLELGFKGEFIGRPDGWGCMRSTEGLLKAYGLDKYELVEGSEAAMDALIYAAYKRGEPDVVYAWTPDWMIKKYDLVVL 191

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712346021 123 EDPKGTFGKDEQIHTIVRKGLKDEHPSAYALLGKFSWTPADMEKVMLDIE-SGKKPEEAAAEWVKN 187
Cdd:pfam04069 192 EDPKGLFPPAYNVVPVVRKGFAEKHPEVAAFLNKLSLDTEDLNELNAQVDvEGKDPEEVAKDWLAE 257

Substrate binding domain of ABC-type choline transport system; the type 2 periplasmic binding protein fold; This subfamily is part of a high affinity multicomponent binding-protein-dependent transport system specific to choline and acetylcholine 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 choline and betaines. Choline is necessary for the biosynthesis of glycine betaine. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. In the case of the Sinorhizobium meliloti choline uptake system ChoVWX, ChoV is the nucleotide-binding domain that provides energy for the transport process via ATP hydrolysis, ChoW is the integral transmembrane protein that forms the substrate translaocation pathway, and ChoX is the substrate-binding domain. ChoX 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712346021  47 GAQVDHKIIGIDPGAGLMKATEKAMKD--YDLKDWELVEGSSAAMTAALTQAYKDKKPIIVTGWTPHWMFSKFEMKYLED 124
Cdd:cd13640   108 ADKFDGKIYGIEPGNDGNEIIQKMIDNntYGLGDWKLVESSEQGMLAQVERAIRNKEWIVFLGWEPHPMNVEFDIKYLDG 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712346021 125 PKGTFGKD---EQIHTIVRKGLKDEHPSAYALLGKFSWTPADMEKVMLDI-ESGKKPEEAAAEWVKNNEATVNKWVEGI 199
Cdd:cd13640   188 GDDYFGPNygaATVYTVTRKGYAEDCPNVAKLLSNLKFSVDMENQWMYEIlNKGRDPEDAAREWIKANPDVVDAWLDGV 266

ABC-type proline/glycine betaine transport system, periplasmic component [Amino acid transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712346021 200 QPAEGKKLTLAYVAWDSEIASTNVVKTVLEqKLKYKVELSQVEAGPMWVGVSNGDVDGMVAAWLPTTHADYMEKLGKD-V 278
Cdd:COG2113    26 APGSCKTVTIADVGWTSATATTAVAKQILE-ELGYEVELVELDVPVTYQGLANGDIDVFLEAWLPTTHADYDEAYGDGkV 104

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1712346021 279 EDLGPNLQGTKLGLAVPAYM---EVNSIEDLKK 308
Cdd:COG2113   105 EDLGTNYEGAKQGLAVPKYVaepGIKSIADLKK 137

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712346021 205 KKLTLAYVAWDSEIASTNVVKTVLEqKLKYKVELSQVEA-GPMWVGVSNGDVDGMVAAWLPTTHADYMEKL--GKDVEDL 281
Cdd:pfam04069   1 KTIVIGSKNWTEQEILANIAAQLLE-ALGYVVELVGLGSsAVLFAALASGDIDLYPEEWTGTTYEAYKKAVeeKLGLLVL 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1712346021 282 GPNLQGTKLGLAVPAYM----EVNSIEDLKK 308
Cdd:pfam04069  80 GPLGAGNTYGLAVPKYVaekpGIKSISDLAK 110

Substrate binding domain of osmoregulatory ABC-type glycine betaine/choline/L-proline transport system and related proteins; the type 2 periplasmic binding protein fold; This family is part of a high affinity multicomponent binding-protein-dependent ATP-binding cassette transport system specific to certain quaternary ammonium 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 betaines, choline, and L-proline. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712346021 206 KLTLAYVAWDSEIASTNVVKTVLEqKLKYKVELSQVEAGPMWVGVSNGDVDGMVAAWLPTTHADYMEKL-GKDVEDLGPN 284
Cdd:cd13535     1 TVKLAVPSWTGETATTHVLGTILE-ALGYTVDYVSLNNAVTFQSLANGDIDITVENWLPNHEDFYAKYVeGKKVVVLGQN 79

                          90       100
                  ....*....|....*....|...
gi 1712346021 285 LQGTKLGLAVPAYMEVNSIEDLK 307
Cdd:cd13535    80 LYGAKQGFAVPKKVAELNPITNI 102

Substrate binding domain of ABC-type choline transport system; the type 2 periplasmic binding protein fold; This subfamily is part of a high affinity multicomponent binding-protein-dependent transport system specific to choline and acetylcholine 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 choline and betaines. Choline is necessary for the biosynthesis of glycine betaine. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. In the case of the Sinorhizobium meliloti choline uptake system ChoVWX, ChoV is the nucleotide-binding domain that provides energy for the transport process via ATP hydrolysis, ChoW is the integral transmembrane protein that forms the substrate translaocation pathway, and ChoX is the substrate-binding domain. ChoX 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712346021 209 LAYVAWdSEIASTNVVKTVLEQKLKYKVELSQVEAGPMWVGVSNGDVDGMVAAWLPT---THADYMEKlgKDVEDLGPNL 285
Cdd:cd13640     4 FGDVGW-TDITVTTAVASQILEALGYETEVKELSVPIIYQGLANGDIDVFLGNWMPSqepMIDPYLEK--GSIEVVGTNL 80

                          90       100
                  ....*....|....*....|....*.
gi 1712346021 286 QGTKLGLAVPAYME---VNSIEDLKK 308
Cdd:cd13640    81 EGAKYTLAVPTYVYeagVKSFADLAK 106

Substrate binding domain of Escherichia coli betaine transport system-like; the type 2 periplasmic binding protein fold; This group includes the periplasmic substrate-binding protein ProX. ProX from the Escherichia coli ATP-binding cassette transport system ProU binds the compatible solutes glycine betaine and proline betaine with high affinity and specificity. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. The ProX 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712346021  55 IGIDPGAGLMKATEKAMKDYDLKDW-ELVEGSSAAMTAALTQAYKDKKPIIVTGWTPHWMFSKF----EMKYLEDPKgTF 129
Cdd:cd13638   131 TGCNPGWGCEKVIEHQLDAYGLRDTvNHNQGSYSALMADAIARYKQGKPVLYYTWTPNWVSNVLvpgkDVVWLEVPF-TA 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712346021 130 GKDEQ-------------------IHTIVRKGLKDEHPSAYALLGKFSWTPADMEKVMLDIESGKKPEEA----AAEWVK 186
Cdd:cd13638   210 LPGDQagattgvangknlgfpvndIRIVANKAFLEANPAAKKLFELVQIPLADISAQNLLMNQGEGSPEDirrhADEWIA 289

                         170
                  ....*....|
gi 1712346021 187 NNEATVNKWV 196
Cdd:cd13638   290 ANQDTFDGWI 299

Substrate binding domain of Escherichia coli betaine transport system-like; the type 2 periplasmic binding protein fold; This group includes the periplasmic substrate-binding protein ProX. ProX from the Escherichia coli ATP-binding cassette transport system ProU binds the compatible solutes glycine betaine and proline betaine with high affinity and specificity. Many microorganisms accumulate these compatible solutes in response to high osmolarity to offset the loss of cell water. The ProX 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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712346021 201 PAEGKKLTLAYVAWDSEIASTNVVKTVLEqKLKYKVELS-QVEAGPMWVGVSNGDVDGMVAAWLPtTHADYMEKLGKD 277
Cdd:cd13638     1 PGKGVTVRPAKSTWAEEYFQTEIVSKGLE-KLGYKVKEPkELDYPLFYVAVANGDADFWADHWFP-LHDPFFEKAGGD 76

Substrate-binding domain of ABC-type histidine transporter involves in betaine and proline uptake; the type 2 periplasmic-binding protein fold; This subfamily is part of a high affinity multicomponent binding-protein-dependent transport system specific to certain quaternary ammonium 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, proline betaine, choline, and carnitine. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712346021 206 KLTLAYVAWDSEIASTNVVKTVLEQKLKYKVELSQVEAGPMWVGVSNGDVDGMVAAWlPTTHADYMEKL---GKdVEDLG 282
Cdd:cd13641     1 PVTFADMNWDSAQFHNRIAGFILEHGYGCQVEVVPGSTPPTLTALARGDIDVAMELW-TDNISEAYNKAveeGK-VLDLG 78

                          90
                  ....*....|....*.
gi 1712346021 283 PNLQGTKLGLAVPAYM 298
Cdd:cd13641    79 TNFDDARQGWYVPTYV 94