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Conserved domains on  [gi|498422089|ref|WP_010729375|]
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MULTISPECIES: ABC transporter substrate-binding protein [Enterococcus]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 10194397)

ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of one or more from a variety of substrates including sugars, ions, peptides, and drugs, among others; belongs to the type 2 periplasmic binding protein (PBP2) fold superfamily; similar to Streptococcus pneumoniae substrate-binding protein FusA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
45-529 0e+00

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


:

Pssm-ID: 270299 [Multi-domain]  Cd Length: 490  Bit Score: 541.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  45 KVSLKMMSQSAPLAPnDPNDKLIFQRLEEETNLHIDWTNYSSD-FAEKRNLDIASGDLPDAIFNAAAGDYDLLNWAESGV 123
Cdd:cd13581    1 KVTLTIFVRKSPLVE-DYNENLFFKRLEEKTGIKIEWETVPEDaWAEKKNLMLASGDLPDAFLGAGASDADLMTYGKQGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 124 IVPIEDLIEDYMPNLKKIFDENPEYRQMSTAPDGHIYSMPWIEELGEGkesihTVNGMAWINKEWLDNLGLEMPQTTDQL 203
Cdd:cd13581   80 FLPLEDLIDKYAPNLKALFDENPDIKAAITAPDGHIYALPSVNECYHC-----SYGQRMWINKKWLDKLGLEMPTTTDEL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 204 MTVLEAFKTQDPNGNGEADEIPFSFI-NNGGNEDLKFLMGAFGLGDND--DHLVVDNDGQVQFTANKEGYKEAIKYFNEM 280
Cdd:cd13581  155 YEVLKAFKEQDPNGNGKADEIPLSFSgLNGGTDDPAFLLNSFGINDGGygGYGFVVKDGKVIYTATDPEYKEALAYLNKL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 281 NNKGLIDKEAFEQDWNTYVAKGK--EHKYGVYFTWDKANITGAD--DSYDVLPVLAGPDGTKHVTRTNGMGFSRDRFVIT 356
Cdd:cd13581  235 YKEGLIDPEAFTQDYDQLAAKGKasTAKVGVFFGWDPGLFFGEEryEQYVPLPPLKGPNGDQLAWVGNSSGYGRGGFVIT 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 357 SANKNLELTARWIDKMYEPLQSVQNNWGTYGDEAQANIFEL--KDGMLKHLPLEGTAPGELRQKTEAGGPLAVLDSYYGT 434
Cdd:cd13581  315 SKNKNPEAAIRWADFLYSPEGSLQANFGPEGEDWEKNPDGEygVDGPPAAYKILEPSEGEQNVAWADGGPGAIPDEYRLK 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 435 VTTMPDD--AKWRLDLMHDTYLPYITEDNiYPRVFLEKEETDRLAKIETDMWDYIYRKRAEWITGGKIDEEWEEYLAELE 512
Cdd:cd13581  395 QVTDEDMdeAEARLDEAKKYYEPYAPPDN-SPPPALLDEEAEKISTIQTDINNYIEQKRAKFITGGGDDKEWDAYVKQLE 473
                        490
                 ....*....|....*..
gi 498422089 513 RVGLEEWIQIKQTGYDN 529
Cdd:cd13581  474 KMGLDEYLEIYQKAYDR 490
 
Name Accession Description Interval E-value
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
45-529 0e+00

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270299 [Multi-domain]  Cd Length: 490  Bit Score: 541.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  45 KVSLKMMSQSAPLAPnDPNDKLIFQRLEEETNLHIDWTNYSSD-FAEKRNLDIASGDLPDAIFNAAAGDYDLLNWAESGV 123
Cdd:cd13581    1 KVTLTIFVRKSPLVE-DYNENLFFKRLEEKTGIKIEWETVPEDaWAEKKNLMLASGDLPDAFLGAGASDADLMTYGKQGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 124 IVPIEDLIEDYMPNLKKIFDENPEYRQMSTAPDGHIYSMPWIEELGEGkesihTVNGMAWINKEWLDNLGLEMPQTTDQL 203
Cdd:cd13581   80 FLPLEDLIDKYAPNLKALFDENPDIKAAITAPDGHIYALPSVNECYHC-----SYGQRMWINKKWLDKLGLEMPTTTDEL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 204 MTVLEAFKTQDPNGNGEADEIPFSFI-NNGGNEDLKFLMGAFGLGDND--DHLVVDNDGQVQFTANKEGYKEAIKYFNEM 280
Cdd:cd13581  155 YEVLKAFKEQDPNGNGKADEIPLSFSgLNGGTDDPAFLLNSFGINDGGygGYGFVVKDGKVIYTATDPEYKEALAYLNKL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 281 NNKGLIDKEAFEQDWNTYVAKGK--EHKYGVYFTWDKANITGAD--DSYDVLPVLAGPDGTKHVTRTNGMGFSRDRFVIT 356
Cdd:cd13581  235 YKEGLIDPEAFTQDYDQLAAKGKasTAKVGVFFGWDPGLFFGEEryEQYVPLPPLKGPNGDQLAWVGNSSGYGRGGFVIT 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 357 SANKNLELTARWIDKMYEPLQSVQNNWGTYGDEAQANIFEL--KDGMLKHLPLEGTAPGELRQKTEAGGPLAVLDSYYGT 434
Cdd:cd13581  315 SKNKNPEAAIRWADFLYSPEGSLQANFGPEGEDWEKNPDGEygVDGPPAAYKILEPSEGEQNVAWADGGPGAIPDEYRLK 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 435 VTTMPDD--AKWRLDLMHDTYLPYITEDNiYPRVFLEKEETDRLAKIETDMWDYIYRKRAEWITGGKIDEEWEEYLAELE 512
Cdd:cd13581  395 QVTDEDMdeAEARLDEAKKYYEPYAPPDN-SPPPALLDEEAEKISTIQTDINNYIEQKRAKFITGGGDDKEWDAYVKQLE 473
                        490
                 ....*....|....*..
gi 498422089 513 RVGLEEWIQIKQTGYDN 529
Cdd:cd13581  474 KMGLDEYLEIYQKAYDR 490
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
1-375 7.81e-35

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 134.40  E-value: 7.81e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089   1 MKaKWMLPIVFTSVLILGACGGSKEKSKSSpdyelenvsfplKEKVSLKMMSQSAPLAPNdpNDKLI--FQrlEEETNLH 78
Cdd:COG1653    1 MR-RLALALAAALALALAACGGGGSGAAAA------------AGKVTLTVWHTGGGEAAA--LEALIkeFE--AEHPGIK 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  79 IDWTNYSS-DFAEKRNLDIASGDLPDAIFnaaAGDYDLLNWAESGVIVPIEDLIEDYMPNLKKIFdenPEYRQMSTaPDG 157
Cdd:COG1653   64 VEVESVPYdDYRTKLLTALAAGNAPDVVQ---VDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFL---PGALDAGT-YDG 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 158 HIYSMPWieelgegkesihTVNGMA-WINKEWLDNLGLEMPQTTDQLMTVLEAFKTQDpngngeaDEIPFSFinnGGNED 236
Cdd:COG1653  137 KLYGVPF------------NTDTLGlYYNKDLFEKAGLDPPKTWDELLAAAKKLKAKD-------GVYGFAL---GGKDG 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 237 LKFLMGAFGLGDNddhlVVDNDGQVQFtaNKEGYKEAIKYFNEMNNKGLIDKEAFEQDWNTYVAKGKEHKYGVYF--TWD 314
Cdd:COG1653  195 AAWLDLLLSAGGD----LYDEDGKPAF--DSPEAVEALEFLKDLVKDGYVPPGALGTDWDDARAAFASGKAAMMIngSWA 268
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498422089 315 KANITGADDS--YDVLPVLAGPDGTKHVTRTNGMGfsrdrFVITSANKNLELTARWIDKMYEP 375
Cdd:COG1653  269 LGALKDAAPDfdVGVAPLPGGPGGKKPASVLGGSG-----LAIPKGSKNPEAAWKFLKFLTSP 326
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
72-375 1.22e-10

Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.


Pssm-ID: 460248 [Multi-domain]  Cd Length: 294  Bit Score: 62.43  E-value: 1.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089   72 EEETNLHIDWTNYSSD-FAEKRNLDIASGDLPDAIFnaAAGDYDLLNWAESGVIVPIEDLIEDYMPNlkkifdenpeyrq 150
Cdd:pfam01547  19 KEHPGIKVEVESVGSGsLAQKLTTAIAAGDGPADVF--ASDNDWIAELAKAGLLLPLDDYVANYLVL------------- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  151 mstaPDGHIYSMPWieelgegkesiHTVNGMAWINKEWLDNLGLEMPQTTDQLMTVLEAFKTQDPNGNGEAdeiPFSFIN 230
Cdd:pfam01547  84 ----GVPKLYGVPL-----------AAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAG---GGDASG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  231 NGGNEDLKFLMGAFGLGDNDDHLVVDNDGQVQFTANkegykEAIKYFNEMNNKGLIDKEAFEQDWNTYVAKGKEHKYGVY 310
Cdd:pfam01547 146 TLGYFTLALLASLGGPLFDKDGGGLDNPEAVDAITY-----YVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMG 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  311 FTWDKANITGADDSYDVLPVLAGPDGTKHVTRT-----NGMGFSRDRFVITSANKNLELTARWIDKMYEP 375
Cdd:pfam01547 221 IVGPWAALAANKVKLKVAFAAPAPDPKGDVGYAplpagKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSP 290
 
Name Accession Description Interval E-value
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
45-529 0e+00

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270299 [Multi-domain]  Cd Length: 490  Bit Score: 541.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  45 KVSLKMMSQSAPLAPnDPNDKLIFQRLEEETNLHIDWTNYSSD-FAEKRNLDIASGDLPDAIFNAAAGDYDLLNWAESGV 123
Cdd:cd13581    1 KVTLTIFVRKSPLVE-DYNENLFFKRLEEKTGIKIEWETVPEDaWAEKKNLMLASGDLPDAFLGAGASDADLMTYGKQGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 124 IVPIEDLIEDYMPNLKKIFDENPEYRQMSTAPDGHIYSMPWIEELGEGkesihTVNGMAWINKEWLDNLGLEMPQTTDQL 203
Cdd:cd13581   80 FLPLEDLIDKYAPNLKALFDENPDIKAAITAPDGHIYALPSVNECYHC-----SYGQRMWINKKWLDKLGLEMPTTTDEL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 204 MTVLEAFKTQDPNGNGEADEIPFSFI-NNGGNEDLKFLMGAFGLGDND--DHLVVDNDGQVQFTANKEGYKEAIKYFNEM 280
Cdd:cd13581  155 YEVLKAFKEQDPNGNGKADEIPLSFSgLNGGTDDPAFLLNSFGINDGGygGYGFVVKDGKVIYTATDPEYKEALAYLNKL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 281 NNKGLIDKEAFEQDWNTYVAKGK--EHKYGVYFTWDKANITGAD--DSYDVLPVLAGPDGTKHVTRTNGMGFSRDRFVIT 356
Cdd:cd13581  235 YKEGLIDPEAFTQDYDQLAAKGKasTAKVGVFFGWDPGLFFGEEryEQYVPLPPLKGPNGDQLAWVGNSSGYGRGGFVIT 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 357 SANKNLELTARWIDKMYEPLQSVQNNWGTYGDEAQANIFEL--KDGMLKHLPLEGTAPGELRQKTEAGGPLAVLDSYYGT 434
Cdd:cd13581  315 SKNKNPEAAIRWADFLYSPEGSLQANFGPEGEDWEKNPDGEygVDGPPAAYKILEPSEGEQNVAWADGGPGAIPDEYRLK 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 435 VTTMPDD--AKWRLDLMHDTYLPYITEDNiYPRVFLEKEETDRLAKIETDMWDYIYRKRAEWITGGKIDEEWEEYLAELE 512
Cdd:cd13581  395 QVTDEDMdeAEARLDEAKKYYEPYAPPDN-SPPPALLDEEAEKISTIQTDINNYIEQKRAKFITGGGDDKEWDAYVKQLE 473
                        490
                 ....*....|....*..
gi 498422089 513 RVGLEEWIQIKQTGYDN 529
Cdd:cd13581  474 KMGLDEYLEIYQKAYDR 490
PBP2_AlgQ1_2 cd13584
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 ...
61-528 5.58e-68

Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 periplasmic binding fold; This group represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria such as Sphingomonas sp. A1. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that includes alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270302 [Multi-domain]  Cd Length: 481  Bit Score: 226.94  E-value: 5.58e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  61 DPNDKLI--FQRLEEETNLHIDWTNYS--SDFAEKRNLDIASGDLPDAIFNAAAGDYD-LLNWAESGVIVPIEDLIEDYM 135
Cdd:cd13584   14 WPNDNDLpvYKEMERKTNVKLNFVANPvaQNSQEQFNLMMASGQLPDIIGGDWLKDKGgFEKYGEDGAFLPLNDLIDQYA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 136 PNLKKIFDENPEYRQMSTAPDGHIYSMPWIEELGEGKESIHTVngmawINKEWLDNLGLEMPQTTDQLMTVLEAFKTQDP 215
Cdd:cd13584   94 PNLKKFLDEHPDVKKAITTDDGNIYGFPYLPDGDVAKEARGYF-----IRKDWLDKLGLKTPSTIDEWYTVLKAFKERDP 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 216 NGNGEADEIPFSFINNGGNEDLKFLmGAFGLgdNDDHLVVdnDGQVQFTANKEGYKEAIKYFNEMNNKGLIDKEAF---- 291
Cdd:cd13584  169 NGNGKADEVPLILTKPGYDETGRLI-NAWGA--YMDFYQE--NGKVKYGPLEPGFKDFLKTMNQWYKEGLIDPDFFtrka 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 292 ---EQDWNTYVAKGKEHKYGVYFTWDKANITGADDSYDVL----PVLAGpdGTKHVTRTNGMGFSRDRFVITSANKNLEL 364
Cdd:cd13584  244 karEQNIMNGNIGGFTHDWFASTGTFNLALLKNVPDFKLVavppPVLNK--GQTPYEEDSRQIAKGDGAAITASNKNPVL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 365 TARWIDKMYEPLQSVQNNWGTYGDEaqaniFELKDGMLKHLPLEGTAPgelrqkteaGGPLAVLDSYYGTVTTMPD---- 440
Cdd:cd13584  322 AIKWLDYAYSEEGRLLSNFGVEGES-----YTIKNGKPVFTDDVLKDP---------QPLVNALSLYYGAQIPGGFwqdy 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 441 --DAKWRLDLMHDTYLPYITEDNIY--PRVFLEKEETDRLAKIETDMWDYIYRKRAEWITGGK-IDEEWEEYLAELERVG 515
Cdd:cd13584  388 eyEEQWTTPEALESKDIYAKNKYVMplPPVTLTEEERSIYDSIMTDIDTYVNEMGQKWIMGKEdADDNWDEYQKKLKSLG 467
                        490
                 ....*....|...
gi 498422089 516 LEEWIQIKQTGYD 528
Cdd:cd13584  468 LYEALEIQQAAYD 480
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
45-528 2.14e-61

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This family represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria and related proteins. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. In Sphingomonas sp. A1, the transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins AlgQ1 and AlgQ2. Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270239 [Multi-domain]  Cd Length: 483  Bit Score: 209.62  E-value: 2.14e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  45 KVSLKMMSQSAPLAPNDPNDKLIfQRLEEETNLHIDWT-NYSSDFAEKRNLDIASGDLPDaIFNAAAGDYDLLNWAESGV 123
Cdd:cd13521    1 PLTLSVLMAFNDNWVDDENWPVA-KEIEKLTNVKLEIVaVTAATSQQKLNLMLASGDLPD-IVGADYLKDKFIAYGMEGA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 124 IVPIEDLIEDYmPNLKKIFDENPEYRQMSTAPDGHIYSMPWIEELGegkesihTVNGMAWINKEWLDNLGLEMPQTTDQL 203
Cdd:cd13521   79 FLPLSKYIDQY-PNLKAFFKQHPDVLRASTASDGKIYLIPYEPPKD-------VPNQGYFIRKDWLDKLNLKTPKTLDEL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 204 MTVLEAFKTQDPNGNGEADEIPfsFINNGGNEDLKFLMG----AFGLGDNDDHLVVDNdGQVQFTANKEGYKEAIKYFNE 279
Cdd:cd13521  151 YNVLKAFKEKDPNGNGKADEIP--FIDRDPLYGAFRLINswgaRSAGGSTDSDWYEDN-GKFKHPFASEEYKDGMKYMNK 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 280 MNNKGLIDKEAFEQDWNTYVAKGKEHKYGVY-FTW------DKANITGADDSYDVLPVLAGPDGTKHVTRTNGMGFSRDR 352
Cdd:cd13521  228 LYTEGLIDKESFTQKDDQAEQKFSNGKLGGFtHNWfasdnlFTAQLGKEKPMYILLPIAPAGNVKGRREEDSPGYTGPDG 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 353 FVITSANKNLELTARWIDKMYEPLQSVQNNWGTYG-----DEAQANIF-------ELKDGMLKHLPleGTAPGELRQKTE 420
Cdd:cd13521  308 VAISKKAKNPVAALKFFDWLASEEGRELANFGIEGvhynkDNGKKRTKdpvkksdQPGDNQLYDLP--AFIKGGFWNEYT 385
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 421 AGGPLAVLDSYYGTVTTMPDDAKwrldlmhdtylPYITEDNIYPrVFLEKEETDRLAKIETDMWDYIYRKRAEWITGGKI 500
Cdd:cd13521  386 YPRPQWGVLTGDSARLPIDMYIK-----------PKYSPPKPEG-ANLTIEEREQVSIDNTELKDIMMEMTQKWIMGTKE 453
                        490       500
                 ....*....|....*....|....*....
gi 498422089 501 -DEEWEEYLAELERVGLEEWIQIKQTGYD 528
Cdd:cd13521  454 kDEEWDAYQEQLKSAGLYQVTEEVQKAYD 482
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
44-521 1.75e-59

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 204.10  E-value: 1.75e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  44 EKVSLKMMSQSAPLAPNDPNDKLIFQRLEEETN--LHIDWTNySSDFAEKRNLDIASGDLPDAIFnaAAGDYDLLNWAES 121
Cdd:cd13580    1 EPVTITIVANLGGNPKPDPDDNPYTKYLEEKTNidVKVKWVP-DSSYDEKLNLALASGDLPDIVV--VNDPQLSITLVKQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 122 GVIVPIEDLIEDYMPNLKKIFDENPEyrqMSTAPDGHIYSMPWIEELGEGkesihtvNGMaWINKEWLDNLGLEMPQTTD 201
Cdd:cd13580   78 GALWDLTDYLDKYYPNLKKIIEQEGW---DSASVDGKIYGIPRKRPLIGR-------NGL-WIRKDWLDKLGLEVPKTLD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 202 QLMTVLEAFKTQDPNGNGEADEIPFSFINNGGNEDLKFLMGAFGLGDNDDHlvVDNDGQVQFTANKEGYKEAIKYFNEMN 281
Cdd:cd13580  147 ELYEVAKAFTEKDPDGNGKKDTYGLTDTKDLIGSGFTGLFGAFGAPPNNWW--KDEDGKLVPGSIQPEMKEALKFLKKLY 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 282 NKGLIDKEAFEQDWNTYVAKGKEHKYGVYF-TWDKANITGA-------DDSYDVLPVLAGPDGTKHVTRTNGMGfsrDRF 353
Cdd:cd13580  225 KEGLIDPEFAVNDGTKANEKFISGKAGIFVgNWWDPAWPQAslkkndpDAEWVAVPIPSGPDGKYGVWAESGVN---GFF 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 354 VITSANKNLELTARWIDKMYEPLQSVQNNWGTYGDEaqaniFELKDGMlKHLPLEGT--APGELRQKTEAGGPLAVLDSY 431
Cdd:cd13580  302 VIPKKSKKPEAILKLLDFLSDPEVQKLLDYGIEGVH-----YTVKDGG-PVNIIPPDkqEVGDATLDYFQGSLALEKYKL 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 432 YGTVTTMPDDAKWRLDLMHDTYLPYITEDNIY--PRVFLEKEETDRLAKIETDMWDYIYRkraeWITGGKIDEEWEEYLA 509
Cdd:cd13580  376 TNNGERKSDAKKEALDERVVNANDEENENIAVgpPTETLVSPTEKYGATLDKLEDDAFTK----IIMGQIPLDEFDKFVE 451
                        490
                 ....*....|..
gi 498422089 510 ELERVGLEEWIQ 521
Cdd:cd13580  452 EWKKSGGDEITK 463
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
45-527 2.77e-40

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 152.13  E-value: 2.77e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  45 KVSLKMMSQSAPLAPNDpNDKLIFQRLEEETNLHIDWTNY-SSDFAEKRNLDIASGDLPDaIFNAAAGDYDLlNWAESGV 123
Cdd:cd13583    1 PLTLSMMYRDHPNYPVK-DDWLIWKEIEEKTNVKFKRTPIpSSDYETKRSLLIASGDAPD-IIPVLYPGEEN-EFVASGA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 124 IVPIEDLIeDYMPNLKKIFDENPEYRQMSTA--PDGHIYSMPWIEELGEGkesihtvnGMAW-INKEWLDNLGLEMPQTT 200
Cdd:cd13583   78 LLPISDYL-DYMPNYKKYVEKWGLGKELATGrqSDGKYYSLPGLHEDPGV--------QYSFlYRKDIFEKAGIKIPTTW 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 201 DQLMTVLEAFKTQDPngngeaDEIPFSFINNGGNEDLKFLMGAFG--LGDNDDHLVVDNDGQVQFTANKEGYKEAIKYFN 278
Cdd:cd13583  149 DEFYAALKKLKEKYP------DSYPYSDRWNSNALLLIAAPAFGTtaGWGFSNYTYDPDTDKFVYGATTDEYKDMLQYFN 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 279 EMNNKGLIDKEAFEQDWNTYVAK---GK----EHKYGVYFT--WDKANITGADDSYDVLPVLAGPDGtKHVTR---TNGM 346
Cdd:cd13583  223 KLYAEGLLDPESFTQTDDQAKAKflnGKsfviTTNPQTVDElqRNLRAADGGNYEVVSITPPAGPAG-KAINGsrlENGF 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 347 GFSrdrfVITSANKNLELTARWIDKMYEPLQSVQNNWGTYG-----DEAQANIFELKDGMLKHLPlegtaPGELRQKTEA 421
Cdd:cd13583  302 MIS----SKAKDSKNFEALLQFLDWLYSDEGQELATWGVEGetytkEGDGKVYLADSNTPALNPS-----GTKLLQKDFG 372
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 422 GGPLAVLDSYYGTV---TTMPDDAKWrldlmHDTYLPYITEDNIYPRVFLEKEETDRLAKIETDMWDYIYRKRAEWITGG 498
Cdd:cd13583  373 FSDGVFTDGGGTSGklsEMTPEEAEF-----NDTMLENRKPVPPIPPPPMTEEELEQLSLLETPLKDFVDEMTAKFITGK 447
                        490       500
                 ....*....|....*....|....*....
gi 498422089 499 KIDEEWEEYLAELERVGLEEWIQIKQTGY 527
Cdd:cd13583  448 RSMDEWDAFVAEVKKLGLDQLLDIYNDAY 476
PBP2_AlgQ_like_3 cd13582
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
46-528 2.36e-37

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270300 [Multi-domain]  Cd Length: 504  Bit Score: 144.39  E-value: 2.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  46 VSLKMMSQSAPLAPNDPNDKlIFQRLEEETNLHIDWTNYSSDFAEKRNLDIASGDLPDAIFnaAAGDYDLLnwAESGVIV 125
Cdd:cd13582    2 ITFTFFSADSNATPDDFKTP-VAKKITELTGVTLEIEYLVGGEKQKIGLMIASGDLPDLIY--AKGDTDKL--IEAGALV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 126 PIEDLIEDYMPNLKKIFDENPEyRQMSTaPDGHIYSMPwieeLGEGKESIHTVNGMAWINKEWLDNLGLEMPQTTDQLMT 205
Cdd:cd13582   77 PLDDLIEKYGPNIKKWYGDYLL-KKLRS-EDGHIYYLP----NYRVEDAPWYPNGGFWLQHDVLKELGYPKIKTLDDYEN 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 206 VLEAFKTQDPNGNGEaDEIPFSFINnggnEDLKFLMG----AFGLG-DNDDHLVVDND-GQVQFTANKEGYKEAIKYFNE 279
Cdd:cd13582  151 LIKDYKKKYPTINGQ-PTIGFTALT----DDWRFLISvtnpAFLAGyPNDGEVYVDPKtLKAKFHYTRPYYKEYYKWLNE 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 280 MNNKGLIDKEAFEQDWNTYVAK----------GKEHKYGVYFTWDKANitGADDSYDVLPVLAGPDGTKHVTRTNGMGFS 349
Cdd:cd13582  226 LWNEGLLDKESFTQKYDQYLAKiasgrvlgfyDAGWDIGNAITALKAK--GKDERLYAYYPVAVGVDDKDYNYGDPGYLG 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 350 RDRFVITSANKNLELTARWIDKMYEPLQSVQNNWGTYGDEaqaniFELKDGMLKHLPLEGTA----PGELRQKT------ 419
Cdd:cd13582  304 GDGIAITKSCKDPERAFKFLDWLASEEAQKLINWGIEGVD-----YDVDDGKRVYLTEEMAAknkdPDYTKKTGigkywy 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 420 ---EAGGPLAvlDSYYGTVTTMPDDAKWRLDLMHDTYLPYITE-----------------DNIYPrvflEKEETDRLAKI 479
Cdd:cd13582  379 fppRKGGKFS--DGTGNSPTPDPEEEYIYTAVEKKVKAAYKAElwkdmfppfeefpvkpyGYAWP----IGIPDESIAII 452
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 498422089 480 ETDMWDYIYRKRAEWITG--GKIDEEWEEYLAELERVGLEEWIQIKQTGYD 528
Cdd:cd13582  453 NQKASDITRKYIPKAIMAkpDDFDSIWDEYLKDLEKAGYKKLEEYYTKQIK 503
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
1-375 7.81e-35

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 134.40  E-value: 7.81e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089   1 MKaKWMLPIVFTSVLILGACGGSKEKSKSSpdyelenvsfplKEKVSLKMMSQSAPLAPNdpNDKLI--FQrlEEETNLH 78
Cdd:COG1653    1 MR-RLALALAAALALALAACGGGGSGAAAA------------AGKVTLTVWHTGGGEAAA--LEALIkeFE--AEHPGIK 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  79 IDWTNYSS-DFAEKRNLDIASGDLPDAIFnaaAGDYDLLNWAESGVIVPIEDLIEDYMPNLKKIFdenPEYRQMSTaPDG 157
Cdd:COG1653   64 VEVESVPYdDYRTKLLTALAAGNAPDVVQ---VDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFL---PGALDAGT-YDG 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 158 HIYSMPWieelgegkesihTVNGMA-WINKEWLDNLGLEMPQTTDQLMTVLEAFKTQDpngngeaDEIPFSFinnGGNED 236
Cdd:COG1653  137 KLYGVPF------------NTDTLGlYYNKDLFEKAGLDPPKTWDELLAAAKKLKAKD-------GVYGFAL---GGKDG 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 237 LKFLMGAFGLGDNddhlVVDNDGQVQFtaNKEGYKEAIKYFNEMNNKGLIDKEAFEQDWNTYVAKGKEHKYGVYF--TWD 314
Cdd:COG1653  195 AAWLDLLLSAGGD----LYDEDGKPAF--DSPEAVEALEFLKDLVKDGYVPPGALGTDWDDARAAFASGKAAMMIngSWA 268
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498422089 315 KANITGADDS--YDVLPVLAGPDGTKHVTRTNGMGfsrdrFVITSANKNLELTARWIDKMYEP 375
Cdd:COG1653  269 LGALKDAAPDfdVGVAPLPGGPGGKKPASVLGGSG-----LAIPKGSKNPEAAWKFLKFLTSP 326
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
57-369 8.12e-19

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270303 [Multi-domain]  Cd Length: 383  Bit Score: 88.23  E-value: 8.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  57 LAPNDPNDKLIFQRL-----EEETNLHIDWTNYSSDFAEKR-NLDIASGDLPDAIFNaaaGDYDLLNWAESGVIVPIEDL 130
Cdd:cd13585    5 WDWGQPAETAALKKLidafeKENPGVKVEVVPVPYDDYWTKlTTAAAAGTAPDVFYV---DGPWVPEFASNGALLDLDDY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 131 IEDYmpNLKKIFDENPEYrqmSTAPDGHIYSMPWieelgegkesihTVNGMA-WINKEWLDNLG--LEMPQTTDQLMTVL 207
Cdd:cd13585   82 IEKD--GLDDDFPPGLLD---AGTYDGKLYGLPF------------DADTLVlFYNKDLFDKAGpgPKPPWTWDELLEAA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 208 EAFKtqdpngNGEADEIPFSF-INNGGNEDLKFLMGAFGlGDnddhLVVDNDGQVQFtaNKEGYKEAIKYFNEMNNKGLI 286
Cdd:cd13585  145 KKLT------DKKGGQYGFALrGGSGGQTQWYPFLWSNG-GD----LLDEDDGKATL--NSPEAVEALQFYVDLYKDGVA 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 287 --DKEAFEQDWNTYVAKGkehKYGVYFT--WDKANIT--GADDSYDVLPVLAGPDGTKhVTRTNGMGfsrdrFVITSANK 360
Cdd:cd13585  212 psSATTGGDEAVDLFASG---KVAMMIDgpWALGTLKdsKVKFKWGVAPLPAGPGGKR-ASVLGGWG-----LAISKNSK 282

                 ....*....
gi 498422089 361 NLELTARWI 369
Cdd:cd13585  283 HPEAAWKFI 291
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-396 2.74e-17

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 83.85  E-value: 2.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089   1 MKAKWM--LPIVFTSVLILGACGGSKEKSKSSPDYElenvsfplkEKVSLKMMSqsaplapnDPNDKLIFQRL----EEE 74
Cdd:COG2182    1 MKRRLLaaLALALALALALAACGSGSSSSGSSSAAG---------AGGTLTVWV--------DDDEAEALEEAaaafEEE 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  75 TNLHIDWTNYS-SDFAEKRNLDIASGDLPDAIFnaaaGDYDLL-NWAESGVIVPIEDLIE---DYMPNLKKIFdenpEYr 149
Cdd:COG2182   64 PGIKVKVVEVPwDDLREKLTTAAPAGKGPDVFV----GAHDWLgELAEAGLLAPLDDDLAdkdDFLPAALDAV----TY- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 150 qmstapDGHIYSMPWieelgegkesihTVNGMA-WINKewlDNLGLEMPQTTDQLMTVLEAFKTqdpngngeADEIPFSF 228
Cdd:COG2182  135 ------DGKLYGVPY------------AVETLAlYYNK---DLVKAEPPKTWDELIAAAKKLTA--------AGKYGLAY 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 229 inNGGNedlkF-----LMGAFG---LGDNDdhlvvDNDGQVQFtaNKEGYKEAIKYFNEMNNKGLIDKEAfeqDWNTYVA 300
Cdd:COG2182  186 --DAGD----AyyfypFLAAFGgylFGKDG-----DDPKDVGL--NSPGAVAALEYLKDLIKDGVLPADA---DYDAADA 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 301 KGKEHKYGVYFT--WDKANITGA-DDSYDVLPVLAGPDGTKHVTRTNGMGfsrdrFVITSANKNLELTARWID------- 370
Cdd:COG2182  250 LFAEGKAAMIINgpWAAADLKKAlGIDYGVAPLPTLAGGKPAKPFVGVKG-----FGVSAYSKNKEAAQEFAEyltspea 324
                        410       420       430
                 ....*....|....*....|....*....|....
gi 498422089 371 --KMYE------PLQSVQNNWGTYGDEAQANIFE 396
Cdd:COG2182  325 qkALFEatgripANKAAAEDAEVKADPLIAAFAE 358
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
72-375 1.22e-10

Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.


Pssm-ID: 460248 [Multi-domain]  Cd Length: 294  Bit Score: 62.43  E-value: 1.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089   72 EEETNLHIDWTNYSSD-FAEKRNLDIASGDLPDAIFnaAAGDYDLLNWAESGVIVPIEDLIEDYMPNlkkifdenpeyrq 150
Cdd:pfam01547  19 KEHPGIKVEVESVGSGsLAQKLTTAIAAGDGPADVF--ASDNDWIAELAKAGLLLPLDDYVANYLVL------------- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  151 mstaPDGHIYSMPWieelgegkesiHTVNGMAWINKEWLDNLGLEMPQTTDQLMTVLEAFKTQDPNGNGEAdeiPFSFIN 230
Cdd:pfam01547  84 ----GVPKLYGVPL-----------AAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAG---GGDASG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  231 NGGNEDLKFLMGAFGLGDNDDHLVVDNDGQVQFTANkegykEAIKYFNEMNNKGLIDKEAFEQDWNTYVAKGKEHKYGVY 310
Cdd:pfam01547 146 TLGYFTLALLASLGGPLFDKDGGGLDNPEAVDAITY-----YVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMG 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  311 FTWDKANITGADDSYDVLPVLAGPDGTKHVTRT-----NGMGFSRDRFVITSANKNLELTARWIDKMYEP 375
Cdd:pfam01547 221 IVGPWAALAANKVKLKVAFAAPAPDPKGDVGYAplpagKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSP 290
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
96-348 2.59e-10

The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold; This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270451 [Multi-domain]  Cd Length: 385  Bit Score: 62.31  E-value: 2.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  96 IASGDLPDAIFNAAAGdydLLNWAESGVIVPIEDLIEDYMPNLKKIFdenPEYRQMSTaPDGHIYSMPWieelgegkesi 175
Cdd:cd14748   51 LAAGTAPDVAQVDASW---VAQLADSGALEPLDDYIDKDGVDDDDFY---PAALDAGT-YDGKLYGLPF----------- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 176 HTVNGMAWINKEWLDNLGL---EMPQTTDQLMTVLEAFKTQDpngnGEADEIPFSFINNGGNEDLKFLMGAFGlGDnddh 252
Cdd:cd14748  113 DTSTPVLYYNKDLFEEAGLdpeKPPKTWDELEEAAKKLKDKG----GKTGRYGFALPPGDGGWTFQALLWQNG-GD---- 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 253 LVVDNDGQVQFtANKEGyKEAIKYFNEM-NNKGLIDKEAFEQDWNTYVAKgkehKYGVYF--TWDKANITGADDSYDV-- 327
Cdd:cd14748  184 LLDEDGGKVTF-NSPEG-VEALEFLVDLvGKDGVSPLNDWGDAQDAFISG----KVAMTIngTWSLAGIRDKGAGFEYgv 257
                        250       260
                 ....*....|....*....|...
gi 498422089 328 --LPVlagPDGTKHVTRTNGMGF 348
Cdd:cd14748  258 apLPA---GKGKKGATPAGGASL 277
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
59-442 3.32e-09

The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; possesses type 2 periplasmic binding fold; This group represents the periplasmic component of an ABC transport system XBP1 that shows preference for xylo-oligosaccharides in the order of xylotriose > xylobiose > xylotetraose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270452 [Multi-domain]  Cd Length: 388  Bit Score: 58.93  E-value: 3.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  59 PNDPNDKLIFQRLEEE-----TNLHIDWTNYSSD-FAEKRNLDIASGDLPDAIFNAAAGDYDllNWAESGVIVPIEDlie 132
Cdd:cd14749    8 FTGDTKKKYMDELIADfekenPNIKVKVVVFPYDnYKTKLKTAVAAGEGPDVFNLWPGGWLA--EFVKAGLLLPLTD--- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 133 dYMPNLKKIFDENPEYRQMSTApDGHIYSMPwieelgegkesiHTVNGMA-WINKEWLDNLG-LEMPQTTDQLMTVLEAF 210
Cdd:cd14749   83 -YLDPNGVDKRFLPGLADAVTF-NGKVYGIP------------FAARALAlFYNKDLFEEAGgVKPPKTWDELIEAAKKD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 211 KtqdpngNGEADEIPFSFINNGGNEDLKFLMGAFGLGDNDDHlvvdNDGQVQFTANKEGYKEAIKYFNEMNNKGLIDKEA 290
Cdd:cd14749  149 K------FKAKGQTGFGLLLGAQGGHWYFQYLVRQAGGGPLS----DDGSGKATFNDPAFVQALQKLQDLVKAGAFQEGF 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 291 FEQDWNTYVAKGKEHKYGVYF--TWDKANITG--ADDSYDV--LPVLAGPDGTKHVtrtngmGFSRDRFVITSANKNLEL 364
Cdd:cd14749  219 EGIDYDDAGQAFAQGKAAMNIggSWDLGAIKAgePGGKIGVfpFPTVGKGAQTSTI------GGSDWAIAISANGKKKEA 292
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498422089 365 TARWIDKMYEPLqsVQNNWGTYGDEAQANifelKDGMLKHLPLEGTAPGELRQKTEAGGPLAVLDSYYGTVTTMPDDA 442
Cdd:cd14749  293 AVKFLKYLTSPE--VMKQYLEDVGLLPAK----EVVAKDEDPDPVAILGPFADVLNAAGSTPFLDEYWPAAAQVHKDA 364
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
67-316 2.30e-06

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 49.33  E-value: 2.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089   67 IFQRLEEETNLHIDWTNYSS-DFAEKRNLDIASGDLPDAIFNAAAGDyDLLNWAESGVIVPIEDLiedymPNLKKIFDEN 145
Cdd:pfam13416   2 LAKAFEKKTGVTVEVEPQASnDLQAKLLAAAAAGNAPDLDVVWIAAD-QLATLAEAGLLADLSDV-----DNLDDLPDAL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  146 PEYRqmstaPDGHIYSMPWIEElgegkesihTVNGMAWiNKEWLDNLGLEmPQTTDQLMTVLEAFK-----TQDPNGNge 220
Cdd:pfam13416  76 DAAG-----YDGKLYGVPYAAS---------TPTVLYY-NKDLLKKAGED-PKTWDELLAAAAKLKgktglTDPATGW-- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  221 adeipfsfinnggnedlkFLMGAFGLGDNDDHLVVDNDGQVQFTANKEGYKEAIKYFN--EMNNKGLIDKEA---FEQDW 295
Cdd:pfam13416 138 ------------------LLWALLADGVDLTDDGKGVEALDEALAYLKKLKDNGKVYNtgADAVQLFANGEVamtVNGTW 199
                         250       260
                  ....*....|....*....|.
gi 498422089  296 NTYVAKGKEHKYGVYFTWDKA 316
Cdd:pfam13416 200 AAAAAKKAGKKLGAVVPKDGS 220
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
106-288 1.71e-05

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold; This group represents the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270453 [Multi-domain]  Cd Length: 385  Bit Score: 47.29  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 106 FNAAAGDYDLLN----W----AESGVIVPIEDLIEDympnlKKIFDENPEYRQMSTApDGHIYSMPWieelgegkesiHT 177
Cdd:cd14750   52 LAAGSSAPDVLGldviWipefAEAGWLLPLTEYLKE-----EEDDDFLPATVEANTY-DGKLYALPW-----------FT 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 178 VNGMAWINKEWLDNLGLEMPQTTDQLMTVLEAFKTQDPngngeaDEIPFSFinNGGN-EDL--KFLM--GAFGlgdndDH 252
Cdd:cd14750  115 DAGLLYYRKDLLEKYGPEPPKTWDELLEAAKKRKAGEP------GIWGYVF--QGKQyEGLvcNFLEllWSNG-----GD 181
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 498422089 253 LVVDNDGQVqfTANKEGYKEAIKYFNEMNNKGLIDK 288
Cdd:cd14750  182 IFDDDSGKV--TVDSPEALEALQFLRDLIGEGISPK 215
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
61-338 3.46e-05

The periplasmic binding component of ABC transport system specific for maltodextrin; This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270375 [Multi-domain]  Cd Length: 368  Bit Score: 46.22  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  61 DPNDKLIFQRLEEETNLHIDWTNYSSDFAEKRNLD------IASGDLPDAIFNAaagdYD-LLNWAESGVIVPIED-LIE 132
Cdd:cd13657    9 TGAEEDALQQIIDEFEAKYPVPNVKVPFEKKPDLQnklltaIPAGEGPDLFIWA----HDwIGQFAEAGLLVPISDyLSE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 133 DYMPNLKKIFDENPEYrqmstapDGHIYSMPwieelgegkESIHTVngMAWINKEWLDNLglemPQTTDQLMTVLEAFKT 212
Cdd:cd13657   85 DDFENYLPTAVEAVTY-------KGKVYGLP---------EAYETV--ALIYNKALVDQP----PETTDELLAIMKDHTD 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 213 QDPNGNGEADEIP----FSFINNGgnedlkflMGAFGLGDNDDHLVVDNDGQVQftankegykeAIKYFNEMNNKGLidk 288
Cdd:cd13657  143 PAAGSYGLAYQVSdayfVSAWIFG--------FGGYYFDDETDKPGLDTPETIK----------GIQFLKDFSWPYM--- 201
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 498422089 289 eAFEQDWNTYVAKGKEHKYGVYFT--WDKANITGADDSYDVLPvLAGPDGTK 338
Cdd:cd13657  202 -PSDPSYNTQTSLFNEGKAAMIINgpWFIGGIKAAGIDLGVAP-LPTVDGTN 251
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
63-337 2.23e-03

The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold; This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270454 [Multi-domain]  Cd Length: 376  Bit Score: 40.44  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089  63 NDKLI--FQRleEETNLHIDWTNYSSDFAE-KRNLDIASGDLPDaIFNAAAGdydllnW----AESGVIVPIEDLIEDYm 135
Cdd:cd14751   16 YEKLIpaFEK--EYPKIKVKAVRVPFDGLHnQIKTAAAGGQAPD-VMRADIA------WvpefAKLGYLQPLDGTPAFD- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 136 pNLKKIFDEnpeyrQMSTAP-DGHIYSMPwieelgegkesiHTVNGMAWI-NKEWLDNLGLEMPQTTDQLMTVLEAF-KT 212
Cdd:cd14751   86 -DIVDYLPG-----PMETNRyNGHYYGVP------------QVTNTLALFyNKRLLEEAGTEVPKTMDELVAAAKAIkKK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498422089 213 QDPNGNGEADEIPFSFinnggnedLKFLMGaFGlGDnddhlvVDNDGQVQFTANKEGYKEAIKYFNEMNNKGLIDKEAfe 292
Cdd:cd14751  148 KGRYGLYISGDGPYWL--------LPFLWS-FG-GD------LTDEKKATGYLNSPESVRALETIVDLYDEGAITPCA-- 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 498422089 293 QDWNTYVAKG-KEHKYGVYFT--WDKANITG-----ADDSYDVLPVLAGPDGT 337
Cdd:cd14751  210 SGGYPNMQDGfKSGRYAMIVNgpWAYADILGgkefkDPDNLGIAPVPAGPGGS 262
 
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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