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Conserved domains on  [gi|507083855|ref|WP_016154603|]
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MULTISPECIES: ABC transporter substrate-binding protein [Citrobacter]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 11447308)

ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of one or more from a variety of substrates including carbohydrates

Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
PubMed:  26517916|24638992|25750732|26517916
SCOP:  3000083
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-334 1.72e-48

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 169.07  E-value: 1.72e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855   1 MRvvKLAKLTAcVLFAFCISGCGPDDKKSA-ETAKTPIKMWvAPNENEEAFWNTMVKEWNKDPAHTPVEFTPIPAASSsE 79
Cdd:COG1653    1 MR--RLALALA-AALALALAACGGGGSGAAaAAGKVTLTVW-HTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDY-R 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  80 EAIMNALASGTEPDISsNIFIGFASQLVEIGQLEDLSKMSGFNELVNNRQMGKIIPAWQLNGEQHVLPIYINPIVWWWRG 159
Cdd:COG1653   76 TKLLTALAAGNAPDVV-QVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 160 DLLKQYGFDhVPTRYDELYQLAERRAADNNGYVIQMTAGKNWWerWFDFIplyyAQNGGKPYLAGHQATFADPAGQAVLT 239
Cdd:COG1653  155 DLFEKAGLD-PPKTWDELLAAAKKLKAKDGVYGFALGGKDGAA--WLDLL----LSAGGDLYDEDGKPAFDSPEAVEALE 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 240 FMGKVFNSKWS-----SYDFTAADDPLATGQVLASARGPWDIARYHKQYPEIlkTLQIGPMLTEKGDAHPYTFGDSKGVV 314
Cdd:COG1653  228 FLKDLVKDGYVppgalGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDF--DVGVAPLPGGPGGKKPASVLGGSGLA 305

                        330       340
                 ....*....|....*....|
gi 507083855 315 IFSSSKRKAQAWAFIQWVFN 334
Cdd:COG1653  306 IPKGSKNPEAAWKFLKFLTS 325
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-334 1.72e-48

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 169.07  E-value: 1.72e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855   1 MRvvKLAKLTAcVLFAFCISGCGPDDKKSA-ETAKTPIKMWvAPNENEEAFWNTMVKEWNKDPAHTPVEFTPIPAASSsE 79
Cdd:COG1653    1 MR--RLALALA-AALALALAACGGGGSGAAaAAGKVTLTVW-HTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDY-R 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  80 EAIMNALASGTEPDISsNIFIGFASQLVEIGQLEDLSKMSGFNELVNNRQMGKIIPAWQLNGEQHVLPIYINPIVWWWRG 159
Cdd:COG1653   76 TKLLTALAAGNAPDVV-QVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 160 DLLKQYGFDhVPTRYDELYQLAERRAADNNGYVIQMTAGKNWWerWFDFIplyyAQNGGKPYLAGHQATFADPAGQAVLT 239
Cdd:COG1653  155 DLFEKAGLD-PPKTWDELLAAAKKLKAKDGVYGFALGGKDGAA--WLDLL----LSAGGDLYDEDGKPAFDSPEAVEALE 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 240 FMGKVFNSKWS-----SYDFTAADDPLATGQVLASARGPWDIARYHKQYPEIlkTLQIGPMLTEKGDAHPYTFGDSKGVV 314
Cdd:COG1653  228 FLKDLVKDGYVppgalGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDF--DVGVAPLPGGPGGKKPASVLGGSGLA 305

                        330       340
                 ....*....|....*....|
gi 507083855 315 IFSSSKRKAQAWAFIQWVFN 334
Cdd:COG1653  306 IPKGSKNPEAAWKFLKFLTS 325
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 37-422 6.60e-40

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: 146.67  E-value: 6.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  37 IKMWVAPNENEEAFWNTMVKEWNKDPAHTPVEFTPIPAASSSEEAIMNALASGTEPDISSnIFIGFASQLVEIGQLEDLS 116
Cdd:cd14748    2 ITFWHGMSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTLTKLLAALAAGTAPDVAQ-VDASWVAQLADSGALEPLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 117 ---KMSGFNelvnnrqMGKIIPAW----QLNGEQHVLPIYINPIVWWWRGDLLKQYGFD--HVPTRYDELYQLAERRAAD 187
Cdd:cd14748   81 dyiDKDGVD-------DDDFYPAAldagTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDpeKPPKTWDELEEAAKKLKDK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 188 NNGYVIQMTAGKNWWERWFdFIPLYYaQNGGKPYLA-GHQATFADPAGQAVLTFMGK-VFNSKWSSYDFT-AADDPLATG 264
Cdd:cd14748  154 GGKTGRYGFALPPGDGGWT-FQALLW-QNGGDLLDEdGGKVTFNSPEGVEALEFLVDlVGKDGVSPLNDWgDAQDAFISG 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 265 QVLASARGPWDIArYHKQYPEILKtLQIGPMLTEKGDAhPYTFGDSKGVVIFS-SSKRKAQAWAFIQWvFNNAEHDRSWL 343
Cdd:cd14748  232 KVAMTINGTWSLA-GIRDKGAGFE-YGVAPLPAGKGKK-GATPAGGASLVIPKgSSKKKEAAWEFIKF-LTSPENQAKWA 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 344 ELTGMPPARSDLMSNPlfVNYFEKNP-LEKAIASYVDVALPPAATTQTTEIQRSMTQMLEQVIFNHADPAATLDKSAQEI 422
Cdd:cd14748  308 KATGYLPVRKSAAEDP--EEFLAENPnYKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 42-336 2.33e-17

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: 82.08  E-value: 2.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855   42 APNENEEAFWNTMVKEWNKDPAHTPVEFTPIPAASSSEEAIMNALASGTEPDISsNIFIGFASQLVEIGQLEDLSKMSGF 121
Cdd:pfam01547   1 AASLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPADVF-ASDNDWIAELAKAGLLLPLDDYVAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  122 NelvnnrqmgkiipAWQLNGEQHVLPIYINPIVWWWRGDLLKQYGFDhVPTRYDELYQLAERraADNNGYVIQMTAGKNW 201
Cdd:pfam01547  80 Y-------------LVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLD-PPKTWDELLEAAKK--LKEKGKSPGGAGGGDA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  202 WERWFDFIPLYYAQNGGkPYLAGHQATFADPAGQAVLTFMGKVF----------NSKWSSYDFTAADDPLATGQVLASAR 271
Cdd:pfam01547 144 SGTLGYFTLALLASLGG-PLFDKDGGGLDNPEAVDAITYYVDLYakvlllkklkNPGVAGADGREALALFEQGKAAMGIV 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507083855  272 GPWDIARYHKQYPeilKTLQIGPMLTEKGD----AHPYTFGDSKGV---VIFSSSKRKAQAWAFIQWVFNNA 336
Cdd:pfam01547 223 GPWAALAANKVKL---KVAFAAPAPDPKGDvgyaPLPAGKGGKGGGyglAIPKGSKNKEAAKKFLDFLTSPE 291
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-334 1.72e-48

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 169.07  E-value: 1.72e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855   1 MRvvKLAKLTAcVLFAFCISGCGPDDKKSA-ETAKTPIKMWvAPNENEEAFWNTMVKEWNKDPAHTPVEFTPIPAASSsE 79
Cdd:COG1653    1 MR--RLALALA-AALALALAACGGGGSGAAaAAGKVTLTVW-HTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDY-R 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  80 EAIMNALASGTEPDISsNIFIGFASQLVEIGQLEDLSKMSGFNELVNNRQMGKIIPAWQLNGEQHVLPIYINPIVWWWRG 159
Cdd:COG1653   76 TKLLTALAAGNAPDVV-QVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 160 DLLKQYGFDhVPTRYDELYQLAERRAADNNGYVIQMTAGKNWWerWFDFIplyyAQNGGKPYLAGHQATFADPAGQAVLT 239
Cdd:COG1653  155 DLFEKAGLD-PPKTWDELLAAAKKLKAKDGVYGFALGGKDGAA--WLDLL----LSAGGDLYDEDGKPAFDSPEAVEALE 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 240 FMGKVFNSKWS-----SYDFTAADDPLATGQVLASARGPWDIARYHKQYPEIlkTLQIGPMLTEKGDAHPYTFGDSKGVV 314
Cdd:COG1653  228 FLKDLVKDGYVppgalGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDF--DVGVAPLPGGPGGKKPASVLGGSGLA 305

                        330       340
                 ....*....|....*....|
gi 507083855 315 IFSSSKRKAQAWAFIQWVFN 334
Cdd:COG1653  306 IPKGSKNPEAAWKFLKFLTS 325
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 37-422 6.60e-40

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: 146.67  E-value: 6.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  37 IKMWVAPNENEEAFWNTMVKEWNKDPAHTPVEFTPIPAASSSEEAIMNALASGTEPDISSnIFIGFASQLVEIGQLEDLS 116
Cdd:cd14748    2 ITFWHGMSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTLTKLLAALAAGTAPDVAQ-VDASWVAQLADSGALEPLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 117 ---KMSGFNelvnnrqMGKIIPAW----QLNGEQHVLPIYINPIVWWWRGDLLKQYGFD--HVPTRYDELYQLAERRAAD 187
Cdd:cd14748   81 dyiDKDGVD-------DDDFYPAAldagTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDpeKPPKTWDELEEAAKKLKDK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 188 NNGYVIQMTAGKNWWERWFdFIPLYYaQNGGKPYLA-GHQATFADPAGQAVLTFMGK-VFNSKWSSYDFT-AADDPLATG 264
Cdd:cd14748  154 GGKTGRYGFALPPGDGGWT-FQALLW-QNGGDLLDEdGGKVTFNSPEGVEALEFLVDlVGKDGVSPLNDWgDAQDAFISG 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 265 QVLASARGPWDIArYHKQYPEILKtLQIGPMLTEKGDAhPYTFGDSKGVVIFS-SSKRKAQAWAFIQWvFNNAEHDRSWL 343
Cdd:cd14748  232 KVAMTINGTWSLA-GIRDKGAGFE-YGVAPLPAGKGKK-GATPAGGASLVIPKgSSKKKEAAWEFIKF-LTSPENQAKWA 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 344 ELTGMPPARSDLMSNPlfVNYFEKNP-LEKAIASYVDVALPPAATTQTTEIQRSMTQMLEQVIFNHADPAATLDKSAQEI 422
Cdd:cd14748  308 KATGYLPVRKSAAEDP--EEFLAENPnYKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 37-422 1.38e-39

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: 146.01  E-value: 1.38e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  37 IKMWVAPNENEEAFWNTMVKEWNKdpAHT--PVEFTPIPAASSsEEAIMNALASGTEPDISsNIFIGFASQLVEIGQLED 114
Cdd:cd13585    2 LTFWDWGQPAETAALKKLIDAFEK--ENPgvKVEVVPVPYDDY-WTKLTTAAAAGTAPDVF-YVDGPWVPEFASNGALLD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 115 LSKMSGfNELVNNRQMGKIIPAWQLNGEQHVLPIYINPIVWWWRGDLLKQYG-FDHVPTRYDELYQLAERRAADNNG-YV 192
Cdd:cd13585   78 LDDYIE-KDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGpGPKPPWTWDELLEAAKKLTDKKGGqYG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 193 IQMTAGKNWWERWFDFIplyyAQNGGKPYLAGH-QATFADPAGQAVLTFMGKVFNSKWS----SYDFTAADDPLATGQVL 267
Cdd:cd13585  157 FALRGGSGGQTQWYPFL----WSNGGDLLDEDDgKATLNSPEAVEALQFYVDLYKDGVApssaTTGGDEAVDLFASGKVA 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 268 ASARGPWDIARYHKQYPEilKTLQIGPMLTEKGdAHPYTFGDSKGVVIFSSSKRKAQAWAFIQWvFNNAEHDRSWleLTG 347
Cdd:cd13585  233 MMIDGPWALGTLKDSKVK--FKWGVAPLPAGPG-GKRASVLGGWGLAISKNSKHPEAAWKFIKF-LTSKENQLKL--GGA 306

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507083855 348 MPPARSDLMSNPLFVNYFEKNPLEKAIASYVDVALPPAATTQTTEIQRSMTQMLEQVIFN--HADPAATLDKSAQEI 422
Cdd:cd13585  307 AGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGalGKSPEEALKEAAKEI 383
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 37-427 2.96e-32

Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. 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: 270450 [Multi-domain]  Cd Length: 386  Bit Score: 125.89  E-value: 2.96e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  37 IKMWVAPNENEEAFWNTMVKEWNKDPAHTPVEFTPIPAASSSEEaIMNALASGTEPDISS--NIFI-GFASQlveiGQLE 113
Cdd:cd14747    2 LTVWAMGNSAEAELLKELADEFEKENPGIEVKVQVLPWGDAHTK-ITTAAASGDGPDVVQlgNTWVaEFAAM----GALE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 114 DLS-----KMSGFNELVNNRQMGkiipawQLNGEQHVLPIYINPIVWWWRGDLLKQYGFDHVPTRYDELYQLAER-RAAD 187
Cdd:cd14747   77 DLTpyledLGGDKDLFPGLVDTG------TVDGKYYGVPWYADTRALFYRTDLLKKAGGDEAPKTWDELEAAAKKiKADG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 188 NNGYVIQMTAGKNWWERWFDFIplyyAQNGGKpYLAGHQ--ATFADPAGQAVLTFMGKVFNSKWSS----YDFTAADDPL 261
Cdd:cd14747  151 PDVSGFAIPGKNDVWHNALPFV----WGAGGD-LATKDKwkATLDSPEAVAGLEFYTSLYQKGLSPkstlENSADVEQAF 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 262 ATGQVLASARGPWDIARYHKQYPEILKTLQIGPMLTEKGDAHPYTFGDSKgVVIFSSSKRKAQAWAFIQWVFNNaEHDRS 341
Cdd:cd14747  226 ANGKVAMIISGPWEIGAIREAGPDLAGKWGVAPLPGGPGGGSPSFAGGSN-LAVFKGSKNKDLAWKFIEFLSSP-ENQAA 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 342 WLELTGMPPARSDLMSNPlfvnYFEKNPLEKAIASYVDVALPPAATTQTTEIQRSMTQMLEQVIFNH-ADPAATLDKSAQ 420
Cdd:cd14747  304 YAKATGMLPANTSAWDDP----SLANDPLLAVFAEQLKTGKATPATPEWGEIEAELVLVLEEVWIGVgADVEDALDKAAA 379


                 ....*..
gi 507083855 421 EINTLLA 427
Cdd:cd14747  380 EINEILN 386
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 43-428 1.40e-28

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: 115.55  E-value: 1.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  43 PNENEEAFWNTMVKEWNKDPAHTPVEFTPIPAASSSEEAIMnALASGTEPDISSNIFIGFASQLVEIGQLEDLSKMsgfn 122
Cdd:cd14749    9 TGDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKT-AVAAGEGPDVFNLWPGGWLAEFVKAGLLLPLTDY---- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 123 eLVNNRQMGKIIP----AWQLNGEQHVLPIYINPIVWWWRGDLLKQYGFDHVPTRYDELYQLAERRAADNNGYVIQMTAG 198
Cdd:cd14749   84 -LDPNGVDKRFLPgladAVTFNGKVYGIPFAARALALFYNKDLFEEAGGVKPPKTWDELIEAAKKDKFKAKGQTGFGLLL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 199 KNWWERWfdFIPLYYAQNGGKPY--LAGHQATFADPAGQAVLTFM-----GKVFNSKWSSYDFTAADDPLATGQVLASAR 271
Cdd:cd14749  163 GAQGGHW--YFQYLVRQAGGGPLsdDGSGKATFNDPAFVQALQKLqdlvkAGAFQEGFEGIDYDDAGQAFAQGKAAMNIG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 272 GPWDIARYHKQypEILKTLQIGPMLTEKGDAHP-YTFGDSKGVVIFSSSKRKAQAWAFIQWvFNNAEHDRSWLELTGMPP 350
Cdd:cd14749  241 GSWDLGAIKAG--EPGGKIGVFPFPTVGKGAQTsTIGGSDWAIAISANGKKKEAAVKFLKY-LTSPEVMKQYLEDVGLLP 317

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507083855 351 ARSDLMSNPLFVNYFEKNPLEKAIASY-VDVALPPAATTQTTEIQRSMTQMLEQVIfnhadpaaTLDKSAQEINTLLAK 428
Cdd:cd14749  318 AKEVVAKDEDPDPVAILGPFADVLNAAgSTPFLDEYWPAAAQVHKDAVQKLLTGKI--------DPEQVVKQAQSAAAK 388
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 36-422 4.45e-20

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: 91.20  E-value: 4.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  36 PIKMWVAPNENEEAFWNTMVKEWNKDPAHTPVEFTPIPA-ASSSEEAIMNALASG-TEPDI-SSNIFIgfASQLVEIGQL 112
Cdd:cd14750    1 TITFAAGSDGQEGELLKKAIAAFEKKHPDIKVEIEELPAsSDDQRQQLVTALAAGsSAPDVlGLDVIW--IPEFAEAGWL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 113 EDLSkmSGFNELVNNRQMGKIIPAWQLNGEQHVLPIYINPIVWWWRGDLLKQYGfDHVPTRYDELYQLAERRAADNN--- 189
Cdd:cd14750   79 LPLT--EYLKEEEDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYG-PEPPKTWDELLEAAKKRKAGEPgiw 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 190 GYVIQmtaGKNWWERWFDFIPLYYAQNG-------GKPylaghqaTFADPAGQAVLTFMGKVFNSKWS-----SYDFTAA 257
Cdd:cd14750  156 GYVFQ---GKQYEGLVCNFLELLWSNGGdifdddsGKV-------TVDSPEALEALQFLRDLIGEGISpkgvlTYGEEEA 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 258 DDPLATGQVLASARGPWDIARYHKQYPEILKTLQIGPMLTEKGDAHPYTFGdSKGVVIFSSSKRKAQAWAFIQWVFNNAE 337
Cdd:cd14750  226 RAAFQAGKAAFMRNWPYAYALLQGPESAVAGKVGVAPLPAGPGGGSASTLG-GWNLAISANSKHKEAAWEFVKFLTSPEV 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 338 HDRSWLELtGMPPARSDLMSNPLFVnyfEKNPLEKAIASYVDVALPPAATTQTTEIQRSMTQMLEQVIFNHADPAATLDK 417
Cdd:cd14750  305 QKRRAING-GLPPTRRALYDDPEVL---EAYPFLPALLEALENAVPRPVTPKYPEVSTAIQIALSAALSGQATPEEALKQ 380


                 ....*
gi 507083855 418 SAQEI 422
Cdd:cd14750  381 AQEKL 385
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 37-423 2.04e-19

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: 89.36  E-value: 2.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  37 IKMWVAPNENEEAFWNTMVKEWNKDPAHTPVEFTPIPAASSSEEAIMNAlASGTEPDISsNIFIGFASQLVEIGQLEDLS 116
Cdd:cd14751    2 ITFWHTSSDEEKVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAA-AGGQAPDVM-RADIAWVPEFAKLGYLQPLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 117 KMSGFNElvnnrqMGKIIPA----WQLNGEQHVLPIYINPIVWWWRGDLLKQYGFDhVPTRYDELYQLAERRAADNNGYV 192
Cdd:cd14751   80 GTPAFDD------IVDYLPGpmetNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTE-VPKTMDELVAAAKAIKKKKGRYG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 193 IQMTAGKNWWerwfdFIPLYYAQNGGKPYLAGHQATFADPAGQAVLTFMGKVFNSK----WSSYDFTAADDPLATGQVLA 268
Cdd:cd14751  153 LYISGDGPYW-----LLPFLWSFGGDLTDEKKATGYLNSPESVRALETIVDLYDEGaitpCASGGYPNMQDGFKSGRYAM 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 269 SARGPWDIARYHKQYPEILK-TLQIGPMLTEKGDAHPYTFGDSkgVVIFSSSKRKAQAWAFIQWVfNNAEHDRSWLELTG 347
Cdd:cd14751  228 IVNGPWAYADILGGKEFKDPdNLGIAPVPAGPGGSGSPVGGED--LVIFKGSKNKDAAWKFVKFM-SSAEAQALTAAKLG 304

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507083855 348 MPPARSDLMSNPLFVNyfekNPLEKAIASYVDVALPPAATTQTTEIQRSMTQMLEQVIFNHADPAATLDKSAQEIN 423
Cdd:cd14751  305 LLPTRTSAYESPEVAN----NPMVAAFKPALETAVPRPPIPEWGELFEPLTLAFAKVLRGEKSPREALDEAAKQWD 376
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 37-422 1.04e-18

The periplasmic-binding component of ABC transport systems specific for maltose and related oligosaccharides; possess type 2 periplasmic binding fold; This family represents the periplasmic binding component of ABC transport systems involved in uptake of oligosaccharides including maltose, trehalose, maltodextrin, and cyclodextrin. Members of this family 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: 270240 [Multi-domain]  Cd Length: 368  Bit Score: 87.08  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  37 IKMWVAPNENEEAFWNTMVKEWNKDPAHTPVEFTPIPAASSSEEaIMNALASGTEPDIssnIFIGFAS--QLVEIGQLED 114
Cdd:cd13522    2 ITVWHQYDTGENQAVNELIAKFEKAYPGITVEVTYQDTEARRQF-FSTAAAGGKGPDV---VFGPSDSlgPFAAAGLLAP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 115 LSKMSGFNELVNNrqmgKIIPAWQLNGEQHVLPIYINPIVWWWRGDLLKqygfDHVPTRYDELYQLAER-RAADNNGYVI 193
Cdd:cd13522   78 LDEYVSKSGKYAP----NTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVP----KNPPKTWQELIALAQGlKAKNVWGLVY 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 194 QMTAGknwwerwFDFIPLYYAqNGGKPYLAGHQA---TFADPAGQAVLTFM-GKVFNSKW--SSYDFTAADDPLATGQVL 267
Cdd:cd13522  150 NQNEP-------YFFAAWIGG-FGGQVFKANNGKnnpTLDTPGAVEALQFLvDLKSKYKImpPETDYSIADALFKAGKAA 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 268 ASARGPWDIARYHKQypeiLK-TLQIGPMLTEKGDAHPYTFGDSKGVVIFSSSKRKAQAWAFIQWVFNNAEHDRSWLELT 346
Cdd:cd13522  222 MIINGPWDLGDYRQA----LKiNLGVAPLPTFSGTKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAG 297

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507083855 347 GMpPARSDLMSNPLFVNyfekNPLEKAIASYVDVALPPAATTQTTEIQRSMTQMLEQVIFNHADPAATLDKSAQEI 422
Cdd:cd13522  298 DI-PANLQAYESPAVQN----KPAQKASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQQEA 368
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 42-336 2.33e-17

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: 82.08  E-value: 2.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855   42 APNENEEAFWNTMVKEWNKDPAHTPVEFTPIPAASSSEEAIMNALASGTEPDISsNIFIGFASQLVEIGQLEDLSKMSGF 121
Cdd:pfam01547   1 AASLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPADVF-ASDNDWIAELAKAGLLLPLDDYVAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  122 NelvnnrqmgkiipAWQLNGEQHVLPIYINPIVWWWRGDLLKQYGFDhVPTRYDELYQLAERraADNNGYVIQMTAGKNW 201
Cdd:pfam01547  80 Y-------------LVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLD-PPKTWDELLEAAKK--LKEKGKSPGGAGGGDA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  202 WERWFDFIPLYYAQNGGkPYLAGHQATFADPAGQAVLTFMGKVF----------NSKWSSYDFTAADDPLATGQVLASAR 271
Cdd:pfam01547 144 SGTLGYFTLALLASLGG-PLFDKDGGGLDNPEAVDAITYYVDLYakvlllkklkNPGVAGADGREALALFEQGKAAMGIV 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507083855  272 GPWDIARYHKQYPeilKTLQIGPMLTEKGD----AHPYTFGDSKGV---VIFSSSKRKAQAWAFIQWVFNNA 336
Cdd:pfam01547 223 GPWAALAANKVKL---KVAFAAPAPDPKGDvgyaPLPAGKGGKGGGyglAIPKGSKNKEAAKKFLDFLTSPE 291
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 39-422 1.85e-15

The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold; This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. 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: 270376 [Multi-domain]  Cd Length: 372  Bit Score: 77.52  E-value: 1.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  39 MWVAPNEnEEAFWNTMVKEWNKDpAHTPVEFTPIPAASSSEEAIMNALAsGTEPDI--SSNIFIGfasQLVEIGQLEDL- 115
Cdd:cd13658    4 VWVDEDK-KMAFIKKIAKQYTKK-TGVKVKLVEVDQLDQLEKLSLDGPA-GKGPDVmvAPHDRIG---SAVLQGLLSPIk 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 116 ---SKMSGFNElvnnrqmgKIIPAWQLNGEQHVLPIYINPIVWWWRGDLLKQygfdhVPTRYDELYQLAERRAADNNGYV 192
Cdd:cd13658   78 lskDKKKGFTD--------QALKALTYDGKLYGLPAAVETLALYYNKDLVKN-----APKTFDELEALAKDLTKEKGKQY 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 193 IQMTAGKNWWERWFdfiplYYAQNGGkpYLAGHQATFADPaGQAVLTFMGKVFNSKWSSYDFTAADDPLAT--------- 263
Cdd:cd13658  145 GFLADATNFYYSYG-----LLAGNGG--YIFKKNGSDLDI-NDIGLNSPGAVKAVKFLKKWYTEGYLPKGMtgdviqglf 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 264 --GQVLASARGPWDIaryhKQYPEILKTLQIGPMLTEKGDAHPYTFGDSKGVVIFSSSKRKAQAWAFIQWVfNNAEHDRS 341
Cdd:cd13658  217 keGKAAAVIDGPWAI----QEYQEAGVNYGVAPLPTLPNGKPMAPFLGVKGWYLSAYSKHKEWAQKFMEFL-TSKENLKK 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 342 WLELTGMPPARSDLMSNPLFVNyfekNPLEKAIASYVDVALPPAATTQTTEIQRSMTQMLEQVIFNHADPAATLDKSAQE 421
Cdd:cd13658  292 RYDETNEIPPRKDVRSDPEIKN----NPLTSAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKTPKQALNDAVND 367


                 .
gi 507083855 422 I 422
Cdd:cd13658  368 I 368
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 37-422 8.99e-15

The periplasmic-binding component of ABC transport systems specific for maltose and related polysaccharides; possess type 2 periplasmic binding fold; This subfamily represents the periplasmic binding component of ABC transport systems involved in uptake of polysaccharides including maltose, maltodextrin, and cyclodextrin. Members of this family 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: 270304 [Multi-domain]  Cd Length: 367  Bit Score: 75.41  E-value: 8.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  37 IKMWVAPNENEEAFwNTMVKEWNKDpAHTPVEFTPIPAASSSEeAIMNALASGTEPDIssniFIG---FASQLVEIGQLE 113
Cdd:cd13586    2 ITVWTDEDGELEYL-KELAEEFEKK-YGIKVEVVYVDSGDTRE-KFITAGPAGKGPDV----FFGphdWLGELAAAGLLA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 114 DLSKMSGfnelVNNRQMGKIIPAWQLNGEQHVLPIYINPIVWWWRGDLLKQygfdhVPTRYDELYQLAERRA-ADNNGYV 192
Cdd:cd13586   75 PIPEYLA----VKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPE-----PPKTWEELIALAKKFNdKAGGKYG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 193 IQMTAGKNWWerWFDFIPLY----YAQNGGKPylagHQATFADPAGQAVLTF---MGKVFNSKWSSYDFTAADDPLATGQ 265
Cdd:cd13586  146 FAYDQTNPYF--SYPFLAAFggyvFGENGGDP----TDIGLNNEGAVKGLKFikdLKKKYKVLPPDLDYDIADALFKEGK 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 266 VLASARGPWDIARYhkqypEILK-TLQIGPMLTEKGDAHPYTFGDSKGVVIFSSSKRKAQAWAFIQWVFNNAEHDRSWlE 344
Cdd:cd13586  220 AAMIINGPWDLADY-----KDAGiNFGVAPLPTLPGGKQAAPFVGVQGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLF-E 293

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507083855 345 LTGMPPARSDLMSNPLFVNyfekNPLEKAIASYVDVALPPAATTQTTEIQRSMTQMLEQVIFNHADPAATLDKSAQEI 422
Cdd:cd13586  294 KTGRIPALKDALNDAAVKN----DPLVKAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEEAAKDAVAAI 367
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 54-354 3.71e-12

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 66.28  E-value: 3.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855   54 MVKEWNKDpahTPVEFTPIPAASS-SEEAIMNALASGTEPDISSNIF-IGFASQLVEIGQLEDLSKMSGFNELVnnrqmg 131
Cdd:pfam13416   2 LAKAFEKK---TGVTVEVEPQASNdLQAKLLAAAAAGNAPDLDVVWIaADQLATLAEAGLLADLSDVDNLDDLP------ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  132 KIIPAWQLNGEQHVLPIYIN-PIVWWWRGDLLKQYGFDhvPTRYDELYQLAErraaDNNGYVIQMTAGKNWWErWFDFIp 210
Cdd:pfam13416  73 DALDAAGYDGKLYGVPYAAStPTVLYYNKDLLKKAGED--PKTWDELLAAAA----KLKGKTGLTDPATGWLL-WALLA- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  211 lyyaqnGGKPYlagHQATFADPAGQAVLTFMGK-VFNSKWSSYDfTAADDPLATGQVLASARGPWDIARYHKQYPEIlkt 289
Cdd:pfam13416 145 ------DGVDL---TDDGKGVEALDEALAYLKKlKDNGKVYNTG-ADAVQLFANGEVAMTVNGTWAAAAAKKAGKKL--- 211

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507083855  290 lqigpmltekGDAHP--YTFGDSKGVVIFSSSKRKAQ-AWAFIQWVfNNAEHDRSWLELTGMPPARSD 354
Cdd:pfam13416 212 ----------GAVVPkdGSFLGGKGLVVPAGAKDPRLaALDFIKFL-TSPENQAALAEDTGYIPANKS 268
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 52-337 1.64e-11

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: 65.81  E-value: 1.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  52 NTMVKEWNKDpahTPVEFTPIPAASSSEEAIMN-ALASGTEPDISSNIFIGFASQLVEIGQLEDLSKM--------SGFN 122
Cdd:cd13580   22 NPYTKYLEEK---TNIDVKVKWVPDSSYDEKLNlALASGDLPDIVVVNDPQLSITLVKQGALWDLTDYldkyypnlKKII 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 123 ELVNNRQM---GKI--IPAWQLNGEQHVLpiyinpivwWWRGDLLKQYGFDhVPTRYDELYQLAerRA-----ADNNGY- 191
Cdd:cd13580   99 EQEGWDSAsvdGKIygIPRKRPLIGRNGL---------WIRKDWLDKLGLE-VPKTLDELYEVA--KAftekdPDGNGKk 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 192 -VIQMTAGKNWWERWFD--------FIPLYYAQNGGKPYLAGHQatfadPAGQAVLTFMGKVFNSKWSSYDF-----TAA 257
Cdd:cd13580  167 dTYGLTDTKDLIGSGFTglfgafgaPPNNWWKDEDGKLVPGSIQ-----PEMKEALKFLKKLYKEGLIDPEFavndgTKA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 258 DDPLATGQVLASARGPWDIARYHKQYPEIL---KTLQIGPMLTEKGDAHPYTFGDSKGVVIFSSSKRKAQA------WAF 328
Cdd:cd13580  242 NEKFISGKAGIFVGNWWDPAWPQASLKKNDpdaEWVAVPIPSGPDGKYGVWAESGVNGFFVIPKKSKKPEAilklldFLS 321


                 ....*....
gi 507083855 329 IQWVFNNAE 337
Cdd:cd13580  322 DPEVQKLLD 330
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 36-422 1.09e-09

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: 59.70  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  36 PIKMWVAPNENEEAFWNTMVKEWNKDpahTPVEFTPIP--AASSSEEAIMNALASGTEPDIssnifIGFA----SQLVEI 109
Cdd:cd13657    1 TITIWHALTGAEEDALQQIIDEFEAK---YPVPNVKVPfeKKPDLQNKLLTAIPAGEGPDL-----FIWAhdwiGQFAEA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 110 GQLEDLSKMsgFNELVNNRQMGKIIPAWQLNGEQHVLPIYINPIVWWWRGDLLKQygfdhVPTRYDELYQLAERRAADNN 189
Cdd:cd13657   73 GLLVPISDY--LSEDDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQ-----PPETTDELLAIMKDHTDPAA 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 190 G-YVIQMTAGKNWWERWF--DFIPLYYAQNGGKPylaGHQATFADPAGQAVLTFmgkvfnskwsSYDFTAADDPLAT--- 263
Cdd:cd13657  146 GsYGLAYQVSDAYFVSAWifGFGGYYFDDETDKP---GLDTPETIKGIQFLKDF----------SWPYMPSDPSYNTqts 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 264 ----GQVLASARGPWDIARyhkqypeiLKTLQIG------PMLTEKGDAHPYTFGDSKGVVIFSSSKRKAQAWAFIQWvF 333
Cdd:cd13657  213 lfneGKAAMIINGPWFIGG--------IKAAGIDlgvaplPTVDGTNPPRPYSGVEGIYVTKYAERKNKEAALDFAKF-F 283

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 334 NNAEHDRSWLELTGMPPARSDLMSNPLFVNYfeknPLEKAIASYVDVALPPAATTQTTEIQRSMTQMLEQVIFNHADPAA 413
Cdd:cd13657  284 TTAEASKILADENGYVPAATNAYDDAEVAAD----PVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQE 359


                 ....*....
gi 507083855 414 TLDKSAQEI 422
Cdd:cd13657  360 ALAAAQQEI 368
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 40-333 7.14e-06

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: 48.22  E-value: 7.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  40 WVAPNENEEAfwNTMVKEWNKDpAHTPVEFTPIPAASSSEEaiMNA-LASGTEPDIS-----SNIFIGFASQlveiGQLE 113
Cdd:cd13521   10 FNDNWVDDEN--WPVAKEIEKL-TNVKLEIVAVTAATSQQK--LNLmLASGDLPDIVgadylKDKFIAYGME----GAFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 114 DLSKMsgFNELVNNRQMGKIIPAWQLN-----GEQHVLPIYINPIVW----WWRGDLLKQYGFdHVPTRYDELYQLAER- 183
Cdd:cd13521   81 PLSKY--IDQYPNLKAFFKQHPDVLRAstasdGKIYLIPYEPPKDVPnqgyFIRKDWLDKLNL-KTPKTLDELYNVLKAf 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 184 RAADNNGY---VIQMTAGKNWWERWFDFIPLYYAQNGGKP-----YLAGHQ--ATFADPAGQAVLTFMGK-----VFNSK 248
Cdd:cd13521  158 KEKDPNGNgkaDEIPFIDRDPLYGAFRLINSWGARSAGGStdsdwYEDNGKfkHPFASEEYKDGMKYMNKlytegLIDKE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855 249 WSSYDFTAADDPLATGQVLASARGPWDIARYHKQYP--EILKTLQIGPMLteKGDAHPYTFGDSK------GVVIFSSSK 320
Cdd:cd13521  238 SFTQKDDQAEQKFSNGKLGGFTHNWFASDNLFTAQLgkEKPMYILLPIAP--AGNVKGRREEDSPgytgpdGVAISKKAK 315

                        330
                 ....*....|...
gi 507083855 321 RKAQAWAFIQWVF 333
Cdd:cd13521  316 NPVAALKFFDWLA 328
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 43-179 1.86e-05

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: 46.58  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855  43 PNENEEAFWNTMVKEWNkdpahtpVEFTPIPAASSSEEAIMNAL-ASGTEPDISSNIFIGFASQLVEIGQLEDLS----K 117
Cdd:cd13583   15 PVKDDWLIWKEIEEKTN-------VKFKRTPIPSSDYETKRSLLiASGDAPDIIPVLYPGEENEFVASGALLPISdyldY 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507083855 118 MSGFNELVNNRQMGKIIPAW-QLNGEQHVLPIY-INPIV---WWWRGDLLKQYGFDhVPTRYDELYQ 179
Cdd:cd13583   88 MPNYKKYVEKWGLGKELATGrQSDGKYYSLPGLhEDPGVqysFLYRKDIFEKAGIK-IPTTWDEFYA 153
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 5-89 5.98e-03

ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism];


Pssm-ID: 441483 [Multi-domain]  Cd Length: 307  Bit Score: 38.37  E-value: 5.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083855   5 KLAKLTACVLFAFCISGCGPDDKKSAETAKTPIKMWVAPNENEEAFWNTMVKEWNKDPAHTPVEFTPIPAASSSE---EA 81
Cdd:COG1879    2 RLALLAAVLALALALAACGSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAkqiSQ 81


                 ....*...
gi 507083855  82 IMNALASG 89
Cdd:COG1879   82 IEDLIAQG 89
 
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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