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Conserved domains on  [gi|446520108|ref|WP_000597454|]
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ABC transporter substrate-binding protein [Escherichia coli]

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 ...
 7-335 2.41e-58

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 195.26  E-value: 2.41e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108   7 VLLSALVSCALISGCKEENKTNVSIEFMHSSveQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLP 86
Cdd:COG1653   11 ALALALAACGGGGSGAAAAAGKVTLTVWHTG--GGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  87 EVIETSHDYAKVM-DKEQLIDRKAVATViSNVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGLEEP 165
Cdd:COG1653   89 DVVQVDSGWLAEFaAAGALVPLDDLLDD-DGLDKDDFLPGALDAG-TYDGKLY-GVPFNTDTLGLYYNKDLFEKAGLDPP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 166 KNWQQLLDVAQKLNDPANkKYGIALPTAESvlteQSFSQFALSNQANVFNAEGKITLDTPEMMQALTYYRDLAAN--TMP 243
Cdd:COG1653  166 KTWDELLAAAKKLKAKDG-VYGFALGGKDG----AAWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKDgyVPP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 244 GSN--DIMEVKDAFMNGTAPMAIYSTYILLAVIKEGDPKNVGFV----VPTEKNSAVYGMLTSLTITAGqkTEETEAAEK 317
Cdd:COG1653  241 GALgtDWDDARAAFASGKAAMMINGSWALGALKDAAPDFDVGVAplpgGPGGKKPASVLGGSGLAIPKG--SKNPEAAWK 318

                        330
                 ....*....|....*...
gi 446520108 318 FVTFMEQADNIADWVMMS 335
Cdd:COG1653  319 FLKFLTSPEAQAKWDALQ 336
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 7-335 2.41e-58

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 195.26  E-value: 2.41e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108   7 VLLSALVSCALISGCKEENKTNVSIEFMHSSveQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLP 86
Cdd:COG1653   11 ALALALAACGGGGSGAAAAAGKVTLTVWHTG--GGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  87 EVIETSHDYAKVM-DKEQLIDRKAVATViSNVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGLEEP 165
Cdd:COG1653   89 DVVQVDSGWLAEFaAAGALVPLDDLLDD-DGLDKDDFLPGALDAG-TYDGKLY-GVPFNTDTLGLYYNKDLFEKAGLDPP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 166 KNWQQLLDVAQKLNDPANkKYGIALPTAESvlteQSFSQFALSNQANVFNAEGKITLDTPEMMQALTYYRDLAAN--TMP 243
Cdd:COG1653  166 KTWDELLAAAKKLKAKDG-VYGFALGGKDG----AAWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKDgyVPP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 244 GSN--DIMEVKDAFMNGTAPMAIYSTYILLAVIKEGDPKNVGFV----VPTEKNSAVYGMLTSLTITAGqkTEETEAAEK 317
Cdd:COG1653  241 GALgtDWDDARAAFASGKAAMMINGSWALGALKDAAPDFDVGVAplpgGPGGKKPASVLGGSGLAIPKG--SKNPEAAWK 318

                        330
                 ....*....|....*...
gi 446520108 318 FVTFMEQADNIADWVMMS 335
Cdd:COG1653  319 FLKFLTSPEAQAKWDALQ 336
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 31-357 2.06e-51

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: 177.60  E-value: 2.06e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  31 IEFMHSSvEQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSH-DYAKVMDKEQLIDrka 109
Cdd:cd13585    2 LTFWDWG-QPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGpWVPEFASNGALLD--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 110 VATVISNVGEGAFYDGVLRIVRTEDGSAWtGVPVSAWIGGIWYRKDVLAKAG--LEEPKNWQQLLDVAQKLNDPANKKYG 187
Cdd:cd13585   78 LDDYIEKDGLDDDFPPGLLDAGTYDGKLY-GLPFDADTLVLFYNKDLFDKAGpgPKPPWTWDELLEAAKKLTDKKGGQYG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 188 IALPTAESVLTEqsFSQFALSNQANVFNA-EGKITLDTPEMMQALTYYRDLAA-NTMPGS--NDIMEVKDAFMNGTAPMA 263
Cdd:cd13585  157 FALRGGSGGQTQ--WYPFLWSNGGDLLDEdDGKATLNSPEAVEALQFYVDLYKdGVAPSSatTGGDEAVDLFASGKVAMM 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 264 IYSTYILLAVIKEGDPKNVGFV-VPTEKNSAVYGMLTSLTITAGQKTEETEAAEKFVTFMEQADNIADWVMMSPGAALPV 342
Cdd:cd13585  235 IDGPWALGTLKDSKVKFKWGVApLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAA 314

                        330
                 ....*....|....*
gi 446520108 343 NKAVVTTATWKDNDV 357
Cdd:cd13585  315 AAASAAAPDAKPALA 329
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 39-327 1.57e-31

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: 122.14  E-value: 1.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108   39 EQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLP-EVIETSHDYAKVMDKeqlidrKAVATVISNV 117
Cdd:pfam01547   3 SLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAK------AGLLLPLDDY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  118 GEGAFYDGVLRivrtedgsaWTGVPVSAWIGGIWYRKDVLAKAGLEEPKNWQQLLDVAQKLNDpANKKYGIALPTAESVL 197
Cdd:pfam01547  77 VANYLVLGVPK---------LYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKE-KGKSPGGAGGGDASGT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  198 TEQSFSQFALSNQANVFNAEGKiTLDTPEMMQALTYYRDLAA---------NTMPGSNDIMEVKDAFMNGTAPMAIYSTY 268
Cdd:pfam01547 147 LGYFTLALLASLGGPLFDKDGG-GLDNPEAVDAITYYVDLYAkvlllkklkNPGVAGADGREALALFEQGKAAMGIVGPW 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446520108  269 ILLAVIKEGdpKNVGFVVPTEKNSAVYGMLTSLTITAG----------QKTEETEAAEKFVTFMEQADN 327
Cdd:pfam01547 226 AALAANKVK--LKVAFAAPAPDPKGDVGYAPLPAGKGGkgggyglaipKGSKNKEAAKKFLDFLTSPEA 292
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
31-345 3.73e-06

sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 49.03  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  31 IEFMHSsVEQERQAVISKLIARFEKENPgiTVKQVPVEEDAYNTKV---ITLSRSGSLPEVIETSHDYAKVMDKEQLIdr 107
Cdd:PRK10974  28 IPFWHS-MEGELGKEVDSLAQRFNASQP--DYKIVPVYKGNYEQSLaagIAAFRSGNAPAILQVYEVGTATMMASKAI-- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 108 KAVATVISNVG----EGAFYDGVLRIVRTEDGSAWTGVPVSAWIGGIWYRKDVLAKAGL---EEPKNWQQLLDVAQKLnd 180
Cdd:PRK10974 103 KPVYDVFKDAGipfdESQFVPTVAGYYSDAKTGHLLSQPFNSSTPVLYYNKDAFKKAGLdpeQPPKTWQDLAAYAAKL-- 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 181 panKKYGIALPTA---ESVLTEQSFSQF---ALSNQANVFN-AEGKITLDTPEMMQALTYYRDLAAN---TMPGSNDimE 250
Cdd:PRK10974 181 ---RAAGMKCGYAsgwQGWIQLENFSAWhglPFASKNNGFDgTDAVLEFNKPEQVKHIALLEEMNKKgdfTYVGRKD--E 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 251 VKDAFMNGTAPMAIYSTYIlLAVIKEGDPKN--VGFV-----VPTEKNSAVYGMlTSLTITAGQKTEETEAAEKFVTFME 323
Cdd:PRK10974 256 STEKFYNGDCAITTASSGS-LANIRKYAKFNygVGMMpydadVKGAPQNAIIGG-ASLWVMQGKDKETYKGVAKFLDFLA 333

                        330       340
                 ....*....|....*....|..
gi 446520108 324 QADNIADWVMMSpgAALPVNKA 345
Cdd:PRK10974 334 KPENAAEWHQKT--GYLPITTA 353
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 7-335 2.41e-58

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 195.26  E-value: 2.41e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108   7 VLLSALVSCALISGCKEENKTNVSIEFMHSSveQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLP 86
Cdd:COG1653   11 ALALALAACGGGGSGAAAAAGKVTLTVWHTG--GGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  87 EVIETSHDYAKVM-DKEQLIDRKAVATViSNVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGLEEP 165
Cdd:COG1653   89 DVVQVDSGWLAEFaAAGALVPLDDLLDD-DGLDKDDFLPGALDAG-TYDGKLY-GVPFNTDTLGLYYNKDLFEKAGLDPP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 166 KNWQQLLDVAQKLNDPANkKYGIALPTAESvlteQSFSQFALSNQANVFNAEGKITLDTPEMMQALTYYRDLAAN--TMP 243
Cdd:COG1653  166 KTWDELLAAAKKLKAKDG-VYGFALGGKDG----AAWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKDgyVPP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 244 GSN--DIMEVKDAFMNGTAPMAIYSTYILLAVIKEGDPKNVGFV----VPTEKNSAVYGMLTSLTITAGqkTEETEAAEK 317
Cdd:COG1653  241 GALgtDWDDARAAFASGKAAMMINGSWALGALKDAAPDFDVGVAplpgGPGGKKPASVLGGSGLAIPKG--SKNPEAAWK 318

                        330
                 ....*....|....*...
gi 446520108 318 FVTFMEQADNIADWVMMS 335
Cdd:COG1653  319 FLKFLTSPEAQAKWDALQ 336
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 31-357 2.06e-51

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: 177.60  E-value: 2.06e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  31 IEFMHSSvEQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSH-DYAKVMDKEQLIDrka 109
Cdd:cd13585    2 LTFWDWG-QPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGpWVPEFASNGALLD--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 110 VATVISNVGEGAFYDGVLRIVRTEDGSAWtGVPVSAWIGGIWYRKDVLAKAG--LEEPKNWQQLLDVAQKLNDPANKKYG 187
Cdd:cd13585   78 LDDYIEKDGLDDDFPPGLLDAGTYDGKLY-GLPFDADTLVLFYNKDLFDKAGpgPKPPWTWDELLEAAKKLTDKKGGQYG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 188 IALPTAESVLTEqsFSQFALSNQANVFNA-EGKITLDTPEMMQALTYYRDLAA-NTMPGS--NDIMEVKDAFMNGTAPMA 263
Cdd:cd13585  157 FALRGGSGGQTQ--WYPFLWSNGGDLLDEdDGKATLNSPEAVEALQFYVDLYKdGVAPSSatTGGDEAVDLFASGKVAMM 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 264 IYSTYILLAVIKEGDPKNVGFV-VPTEKNSAVYGMLTSLTITAGQKTEETEAAEKFVTFMEQADNIADWVMMSPGAALPV 342
Cdd:cd13585  235 IDGPWALGTLKDSKVKFKWGVApLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAA 314

                        330
                 ....*....|....*
gi 446520108 343 NKAVVTTATWKDNDV 357
Cdd:cd13585  315 AAASAAAPDAKPALA 329
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 31-378 1.11e-46

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: 165.16  E-value: 1.11e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  31 IEFMHSSvEQERQAVISKLIARFEKENPGITVKQVPVEEDAYN-TKVITLSRSGSLPEVIETSHDYAKvmdkeQLIDRKA 109
Cdd:cd14748    2 ITFWHGM-SGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTlTKLLAALAAGTAPDVAQVDASWVA-----QLADSGA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 110 VA---TVIS--NVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGL---EEPKNWQQLLDVAQKLNDP 181
Cdd:cd14748   76 LEpldDYIDkdGVDDDDFYPAALDAG-TYDGKLY-GLPFDTSTPVLYYNKDLFEEAGLdpeKPPKTWDELEEAAKKLKDK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 182 ANK--KYGIALPTAEsvlTEQSFSQFALSNQANVFNAE-GKITLDTPEMMQALTYYRDLAANT-MPGSNDIMEVKDAFMN 257
Cdd:cd14748  154 GGKtgRYGFALPPGD---GGWTFQALLWQNGGDLLDEDgGKVTFNSPEGVEALEFLVDLVGKDgVSPLNDWGDAQDAFIS 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 258 GTAPMAIYSTYILLAVIKEGDPKNVGFV---VPTEKNSAVYGMLTSLTITAGqKTEETEAAEKFVTFMEQADNIADWVMM 334
Cdd:cd14748  231 GKVAMTINGTWSLAGIRDKGAGFEYGVAplpAGKGKKGATPAGGASLVIPKG-SSKKKEAAWEFIKFLTSPENQAKWAKA 309

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 446520108 335 spGAALPVNKAVVttatwkdndvikalgELPNQLIGELPNIQVF 378
Cdd:cd14748  310 --TGYLPVRKSAA---------------EDPEEFLAENPNYKVA 336
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 30-367 1.92e-38

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: 142.90  E-value: 1.92e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  30 SIEFMHSSVEQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSH-----DYAKV------ 98
Cdd:cd14749    1 TITYWQYFTGDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPggwlaEFVKAglllpl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  99 --MDKEQLIDRKAVATVISNV-GEGAFYdgvlrivrtedgsawtGVPVSAWIGGIWYRKDVLAKAG-LEEPKNWQQLLDV 174
Cdd:cd14749   81 tdYLDPNGVDKRFLPGLADAVtFNGKVY----------------GIPFAARALALFYNKDLFEEAGgVKPPKTWDELIEA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 175 AQKLNDPANKKYGIALPTAESvlTEQSFSQFALSNQANVF---NAEGKITLDTPEMMQALTYYRDL----AANTMPGSND 247
Cdd:cd14749  145 AKKDKFKAKGQTGFGLLLGAQ--GGHWYFQYLVRQAGGGPlsdDGSGKATFNDPAFVQALQKLQDLvkagAFQEGFEGID 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 248 IMEVKDAFMNGTAPMAIYSTYILLAVIKEGDPKNVGFVVPTEKN-----SAVYGMLTSLTITAgqKTEETEAAEKFVTFM 322
Cdd:cd14749  223 YDDAGQAFAQGKAAMNIGGSWDLGAIKAGEPGGKIGVFPFPTVGkgaqtSTIGGSDWAIAISA--NGKKKEAAVKFLKYL 300

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 446520108 323 EQADNIADWVMMspGAALPVNKAVVTTATWKDNDVIKALGELPNQ 367
Cdd:cd14749  301 TSPEVMKQYLED--VGLLPAKEVVAKDEDPDPVAILGPFADVLNA 343
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
3-429 1.54e-36

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 138.16  E-value: 1.54e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108   3 KSKIVLLSALVSCALISGC---------KEENKTNVSIEFMHSsveQERQAVISKLIARFEKEnPGITVKQVPVEEDAYN 73
Cdd:COG2182    4 RLLAALALALALALALAACgsgssssgsSSAAGAGGTLTVWVD---DDEAEALEEAAAAFEEE-PGIKVKVVEVPWDDLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  74 TKVITLSRSGSLPEVIETSHDYAkvmdkEQLIDRKAVATVISNVGEGA-FYDGVLRIVrTEDGSAWtGVPVSAWIGGIWY 152
Cdd:COG2182   80 EKLTTAAPAGKGPDVFVGAHDWL-----GELAEAGLLAPLDDDLADKDdFLPAALDAV-TYDGKLY-GVPYAVETLALYY 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 153 RKDVLAKaglEEPKNWQQLLDVAQKLNDPAnkKYGIALPTAESvlteQSFSQFALSNQANVFNAEG----KITLDTPEMM 228
Cdd:COG2182  153 NKDLVKA---EPPKTWDELIAAAKKLTAAG--KYGLAYDAGDA----YYFYPFLAAFGGYLFGKDGddpkDVGLNSPGAV 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 229 QALTYYRDLAAN-TMPGSNDIMEVKDAFMNGTAPMAIYSTYIlLAVIKEGDPKNVGFV-VPTEKN-SAVYGMLTSLTITA 305
Cdd:COG2182  224 AALEYLKDLIKDgVLPADADYDAADALFAEGKAAMIINGPWA-AADLKKALGIDYGVApLPTLAGgKPAKPFVGVKGFGV 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 306 GQKTEETEAAEKFVTFMEQADNIADWVMMSPgaALPVNKAVVTTATWKDNDVIKALGElpnqligelpniQVFGAVGDKN 385
Cdd:COG2182  303 SAYSKNKEAAQEFAEYLTSPEAQKALFEATG--RIPANKAAAEDAEVKADPLIAAFAE------------QAEYAVPMPN 368

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 446520108 386 FTRMGDVtgSGVVSSMVHNVTVGKADLPGTLQASQKKLDELIEQ 429
Cdd:COG2182  369 IPEMGAV--WTPLGTALQAIASGKADPAEALDAAQKQIEAAIAQ 410
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 33-363 2.22e-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: 126.27  E-value: 2.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  33 FMHSSVEQErqaVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHD----YAKVMDKEQLIDRk 108
Cdd:cd14747    6 AMGNSAEAE---LLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTwvaeFAAMGALEDLTPY- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 109 avatVISNVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGLEE-PKNWQQLLDVAQKLNDPANKKYG 187
Cdd:cd14747   82 ----LEDLGGDKDLFPGLVDTG-TVDGKYY-GVPWYADTRALFYRTDLLKKAGGDEaPKTWDELEAAAKKIKADGPDVSG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 188 IALPTAESVltEQSFSQFALSNQANVFN-AEGKITLDTPEMMQALTYYRDLAANTMPGSNDIMEVKD---AFMNGTAPMa 263
Cdd:cd14747  156 FAIPGKNDV--WHNALPFVWGAGGDLATkDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSADveqAFANGKVAM- 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 264 IYSTYILLAVIKEGDP---KNVGFVV---PTEKNSAVYGMLTSLTITAGQKteETEAAEKFVTFMEQADNIADWVMMSpg 337
Cdd:cd14747  233 IISGPWEIGAIREAGPdlaGKWGVAPlpgGPGGGSPSFAGGSNLAVFKGSK--NKDLAWKFIEFLSSPENQAAYAKAT-- 308

                        330       340
                 ....*....|....*....|....*.
gi 446520108 338 AALPVNKAVVTTATWKDNDVIKALGE 363
Cdd:cd14747  309 GMLPANTSAWDDPSLANDPLLAVFAE 334
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 39-327 1.57e-31

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: 122.14  E-value: 1.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108   39 EQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLP-EVIETSHDYAKVMDKeqlidrKAVATVISNV 117
Cdd:pfam01547   3 SLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAK------AGLLLPLDDY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  118 GEGAFYDGVLRivrtedgsaWTGVPVSAWIGGIWYRKDVLAKAGLEEPKNWQQLLDVAQKLNDpANKKYGIALPTAESVL 197
Cdd:pfam01547  77 VANYLVLGVPK---------LYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKE-KGKSPGGAGGGDASGT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  198 TEQSFSQFALSNQANVFNAEGKiTLDTPEMMQALTYYRDLAA---------NTMPGSNDIMEVKDAFMNGTAPMAIYSTY 268
Cdd:pfam01547 147 LGYFTLALLASLGGPLFDKDGG-GLDNPEAVDAITYYVDLYAkvlllkklkNPGVAGADGREALALFEQGKAAMGIVGPW 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446520108  269 ILLAVIKEGdpKNVGFVVPTEKNSAVYGMLTSLTITAG----------QKTEETEAAEKFVTFMEQADN 327
Cdd:pfam01547 226 AALAANKVK--LKVAFAAPAPDPKGDVGYAPLPAGKGGkgggyglaipKGSKNKEAAKKFLDFLTSPEA 292
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 48-355 3.01e-26

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 107.11  E-value: 3.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108   48 KLIARFEKENpGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETS--HDYAKvmdkeQLIDRKAVATvISNVGEGAFYDG 125
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDLDVVWiaADQLA-----TLAEAGLLAD-LSDVDNLDDLPD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  126 VLRIVrTEDGsAWTGVPVSA-WIGGIWYRKDVLAKAGlEEPKNWQQLLDVAQKLNdpanKKYGIALPTAesvlteQSFSQ 204
Cdd:pfam13416  74 ALDAA-GYDG-KLYGVPYAAsTPTVLYYNKDLLKKAG-EDPKTWDELLAAAAKLK----GKTGLTDPAT------GWLLW 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  205 FALSNQANvFNAEGKITLDTPEmmqALTYYRDLAAN--TMPGSNDIMevkDAFMNGTAPMAIYSTYILLAVIKEGdpKNV 282
Cdd:pfam13416 141 ALLADGVD-LTDDGKGVEALDE---ALAYLKKLKDNgkVYNTGADAV---QLFANGEVAMTVNGTWAAAAAKKAG--KKL 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446520108  283 GFVVPteKNSAVYGMlTSLTITAGQKTEEtEAAEKFVTFMEQADNIADWVMMSPGaaLPVNKAVVTTATWKDN 355
Cdd:pfam13416 212 GAVVP--KDGSFLGG-KGLVVPAGAKDPR-LAALDFIKFLTSPENQAALAEDTGY--IPANKSAALSDEVKAD 278
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 31-423 7.81e-25

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: 105.07  E-value: 7.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  31 IEFMHSSVEQERQaVISKLIARFEKENPGITVK--QVPVEEDAYNTKVITLSRSGSLP------EVIETSHDYAKVMDKE 102
Cdd:cd14750    2 ITFAAGSDGQEGE-LLKKAIAAFEKKHPDIKVEieELPASSDDQRQQLVTALAAGSSApdvlglDVIWIPEFAEAGWLLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 103 QLIDRKAVatvisnvGEGAFYDGVLRiVRTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGLEEPKNWQQLLDVAQKLNDPA 182
Cdd:cd14750   81 LTEYLKEE-------EDDDFLPATVE-ANTYDGKLY-ALPWFTDAGLLYYRKDLLEKYGPEPPKTWDELLEAAKKRKAGE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 183 NKKYGIALPTAE-SVLTeQSFSQFALSNQANVFNAE-GKITLDTPEMMQALTYYRDLAANTM--PGSNDIME--VKDAFM 256
Cdd:cd14750  152 PGIWGYVFQGKQyEGLV-CNFLELLWSNGGDIFDDDsGKVTVDSPEALEALQFLRDLIGEGIspKGVLTYGEeeARAAFQ 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 257 NGTAPMAI--YSTYILLAVIKEGDPKNVGFV-VPTEKNSAVYGML--TSLTITAgqKTEETEAAEKFVTFMEQADNIADW 331
Cdd:cd14750  231 AGKAAFMRnwPYAYALLQGPESAVAGKVGVApLPAGPGGGSASTLggWNLAISA--NSKHKEAAWEFVKFLTSPEVQKRR 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 332 VMMspGAALPVNKAVVttatwKDNDVIKALGELPNQLIGEL-----PNIQVFGAVgdknftrmgdvtgSGVVSSMVHNVT 406
Cdd:cd14750  309 AIN--GGLPPTRRALY-----DDPEVLEAYPFLPALLEALEnavprPVTPKYPEV-------------STAIQIALSAAL 368

                        410
                 ....*....|....*..
gi 446520108 407 VGKADLPGTLQASQKKL 423
Cdd:cd14750  369 SGQATPEEALKQAQEKL 385
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 39-363 2.17e-23

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: 100.83  E-value: 2.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  39 EQERQAVISKLIARFEKENpGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHDYAKVMDKEQLIDRKAVATVISNVG 118
Cdd:cd13586    8 EDGELEYLKELAEEFEKKY-GIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLAVKIKN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 119 EGAFYDGVlrivrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAgleePKNWQQLLDVAQKLNDPANKKYGIALPTAESVLt 198
Cdd:cd13586   87 LPVALAAV-----TYNGKLY-GVPVSVETIALFYNKDLVPEP----PKTWEELIALAKKFNDKAGGKYGFAYDQTNPYF- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 199 eqsFSQFALSNQANVFNAEGK----ITLDTPEMMQALTYYRDL--AANTMPGSNDIMEVKDAFMNGTAPMAIYSTYILLA 272
Cdd:cd13586  156 ---SYPFLAAFGGYVFGENGGdptdIGLNNEGAVKGLKFIKDLkkKYKVLPPDLDYDIADALFKEGKAAMIINGPWDLAD 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 273 VIKEGDpkNVGF-VVPTEKNSAVYG-MLTSLTITAGQKTEETEAAEKFVTFMeqADNIADWVMMSPGAALPVNKAVVTTA 350
Cdd:cd13586  233 YKDAGI--NFGVaPLPTLPGGKQAApFVGVQGAFVSAYSKNKEAAVEFAEYL--TSDEAQLLLFEKTGRIPALKDALNDA 308

                        330
                 ....*....|...
gi 446520108 351 TWKDNDVIKALGE 363
Cdd:cd13586  309 AVKNDPLVKAFAE 321
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 30-360 1.03e-21

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: 95.91  E-value: 1.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  30 SIEFMHSSVEQErQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSH----DYAKvMDKEQLI 105
Cdd:cd14751    1 TITFWHTSSDEE-KVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIawvpEFAK-LGYLQPL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 106 DRKAVATVIsnvgeGAFYDGVLRIVRTEdGSAWtGVPVSAWIGGIWYRKDVLAKAGLEEPKNWQQLLDVAQKlNDPANKK 185
Cdd:cd14751   79 DGTPAFDDI-----VDYLPGPMETNRYN-GHYY-GVPQVTNTLALFYNKRLLEEAGTEVPKTMDELVAAAKA-IKKKKGR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 186 YGIALptaeSVLTEQSFSQFALSNQANVFNAEGK-ITLDTPEMMQALTYYRDL-----AANTMPGSNDIMevKDAFMNGT 259
Cdd:cd14751  151 YGLYI----SGDGPYWLLPFLWSFGGDLTDEKKAtGYLNSPESVRALETIVDLydegaITPCASGGYPNM--QDGFKSGR 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 260 APMAI---YSTYILLAVIKEGDPKNVGF----VVPTEKNSAVYGmlTSLTITAGQKTEetEAAEKFVTFMEQADNIAdwV 332
Cdd:cd14751  225 YAMIVngpWAYADILGGKEFKDPDNLGIapvpAGPGGSGSPVGG--EDLVIFKGSKNK--DAAWKFVKFMSSAEAQA--L 298

                        330       340
                 ....*....|....*....|....*...
gi 446520108 333 MMSPGAALPVNKAVVTTATWKDNDVIKA 360
Cdd:cd14751  299 TAAKLGLLPTRTSAYESPEVANNPMVAA 326
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 30-363 9.42e-21

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: 93.21  E-value: 9.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  30 SIEFMHSSVEQERQAvISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHDYAKVMDKEQLIDrkA 109
Cdd:cd13657    1 TITIWHALTGAEEDA-LQQIIDEFEAKYPVPNVKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLV--P 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 110 VATVISNVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAgleePKNWQQLLDVAQKLNDPANKKYGIA 189
Cdd:cd13657   78 ISDYLSEDDFENYLPTAVEAV-TYKGKVY-GLPEAYETVALIYNKALVDQP----PETTDELLAIMKDHTDPAAGSYGLA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 190 LPtaesVLTEQSFSQFALSNQANVFNAEG-KITLDTPEMMQALTYYRDLAANTMPGSNDIMEVKDAFMNGTAPMAIYSTY 268
Cdd:cd13657  152 YQ----VSDAYFVSAWIFGFGGYYFDDETdKPGLDTPETIKGIQFLKDFSWPYMPSDPSYNTQTSLFNEGKAAMIINGPW 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 269 ILLAVIKEGDpkNVGFV----VPTEKNSAVYGMLTSLTITAGQKTEETEAAEKFVTFMEQADNIAdwVMMSPGAALPVNK 344
Cdd:cd13657  228 FIGGIKAAGI--DLGVAplptVDGTNPPRPYSGVEGIYVTKYAERKNKEAALDFAKFFTTAEASK--ILADENGYVPAAT 303

                        330
                 ....*....|....*....
gi 446520108 345 AVVTTATWKDNDVIKALGE 363
Cdd:cd13657  304 NAYDDAEVAADPVIAAFKA 322
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 31-346 7.29e-15

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: 75.53  E-value: 7.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  31 IEFMHSSVEQERQAViSKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHDYAKVMdkeqlidrkAV 110
Cdd:cd13522    2 ITVWHQYDTGENQAV-NELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPF---------AA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 111 ATVISNVGEG---------AFYDGVlrivrTEDGSAWtGVPVSAWIGGIWYRKDVLAKaglEEPKNWQQLLDVAQKLNDP 181
Cdd:cd13522   72 AGLLAPLDEYvsksgkyapNTIAAM-----KLNGKLY-GVPVSVGAHLMYYNKKLVPK---NPPKTWQELIALAQGLKAK 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 182 AnkKYGIALPTAESVLteqsFSQFALSNQANVFNAEG---KITLDTPEMMQALTYYRDL--AANTMPGSNDIMEVKDAFM 256
Cdd:cd13522  143 N--VWGLVYNQNEPYF----FAAWIGGFGGQVFKANNgknNPTLDTPGAVEALQFLVDLksKYKIMPPETDYSIADALFK 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 257 NGTAPMAIYSTYIlLAVIKEGDPKNVGF----VVPTEKNSAVygMLTSLTITAGQKTEETEAAEKFVTFMEQADNIADWV 332
Cdd:cd13522  217 AGKAAMIINGPWD-LGDYRQALKINLGVaplpTFSGTKHAAP--FVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLF 293

                        330
                 ....*....|....
gi 446520108 333 MMSPGaaLPVNKAV 346
Cdd:cd13522  294 DDAGD--IPANLQA 305
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-346 8.53e-12

Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 66.09  E-value: 8.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108   1 MIKSKIVLLSALVSCALISGCkeenktnvsiefmHSSVEQERQAVIS--------KLIARFEKENpGITVKQVPVE--ED 70
Cdd:COG0687    1 MSRRSLLGLAAAALAAALAGG-------------APAAAAEGTLNVYnwggyidpDVLEPFEKET-GIKVVYDTYDsnEE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  71 AYnTKVITlsrSGSLPEVIETSHDYAKVMDKEQL---IDRKAvatvISNVgegAFYDGVLRIVRTEDGSAWtGVPVSAWI 147
Cdd:COG0687   67 ML-AKLRA---GGSGYDVVVPSDYFVARLIKAGLlqpLDKSK----LPNL---ANLDPRFKDPPFDPGNVY-GVPYTWGT 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 148 GGIWYRKDVLAkaglEEPKNWQQLLDvaqklndPANK-KYGIaLPTAESVLTeqsfsqFALsnqanvfNAEGK--ITLDT 224
Cdd:COG0687  135 TGIAYNTDKVK----EPPTSWADLWD-------PEYKgKVAL-LDDPREVLG------AAL-------LYLGYdpNSTDP 189

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 225 PEMMQALTYYRDLAANTMPGSNDIMEVKDAFMNGTAPMAIYSTYILLAVIKEGDPknVGFVVPTEKnsaVYGMLTSLTIT 304
Cdd:COG0687  190 ADLDAAFELLIELKPNVRAFWSDGAEYIQLLASGEVDLAVGWSGDALALRAEGPP--IAYVIPKEG---ALLWFDNMAIP 264

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 446520108 305 AGqkTEETEAAEKFVTFMEQADNIADWVMMSPGAalPVNKAV 346
Cdd:COG0687  265 KG--APNPDLAYAFINFMLSPEVAAALAEYVGYA--PPNKAA 302
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 55-331 1.43e-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: 1.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  55 KENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVI-----ETSHDYAK---VMDKEQLIDRKA--VATVISNVGEGAF-Y 123
Cdd:cd13580   29 EEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVvvndpQLSITLVKqgaLWDLTDYLDKYYpnLKKIIEQEGWDSAsV 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 124 DGVLrivrtedgsawTGVPVSAWIG---GIWYRKDVLAKAGLEEPKNWQQLLDVAQ--KLNDP----ANKKYGIALPtae 194
Cdd:cd13580  109 DGKI-----------YGIPRKRPLIgrnGLWIRKDWLDKLGLEVPKTLDELYEVAKafTEKDPdgngKKDTYGLTDT--- 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 195 SVLTEQSFSQFALS----NQANVFNAEGKITLD--TPEMMQALTYYRDLAAN--------TMPGSNdimeVKDAFMNGTA 260
Cdd:cd13580  175 KDLIGSGFTGLFGAfgapPNNWWKDEDGKLVPGsiQPEMKEALKFLKKLYKEglidpefaVNDGTK----ANEKFISGKA 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 261 PM---AIYSTYILLAVIKEGDPKNVGFVVPT------EKNSAVYGMLTSLTItAGQKTEETEAAEKFVTFM--EQADNIA 329
Cdd:cd13580  251 GIfvgNWWDPAWPQASLKKNDPDAEWVAVPIpsgpdgKYGVWAESGVNGFFV-IPKKSKKPEAILKLLDFLsdPEVQKLL 329


                 ..
gi 446520108 330 DW 331
Cdd:cd13580  330 DY 331
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 131-362 8.35e-09

ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 56.48  E-value: 8.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 131 RTEDGsAWTGVpvSAWIGGIWYRKDVLAKAGLeePKNWQQLLdvaqklnDPANK-KYGIALPTAEsvlteqSFSQFALSN 209
Cdd:COG1840   72 RDPDG-YWFGF--SVRARVIVYNTDLLKELGV--PKSWEDLL-------DPEYKgKIAMADPSSS------GTGYLLVAA 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 210 QANVFNAEgkitldtpemmQALTYYRDLAANT---MPGSNDIMevkDAFMNGTAPMAIYSTYILLAVIKEGDPknVGFVV 286
Cdd:COG1840  134 LLQAFGEE-----------KGWEWLKGLAANGarvTGSSSAVA---KAVASGEVAIGIVNSYYALRAKAKGAP--VEVVF 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446520108 287 PTEKNSA-VYGMLtsltITAGqkTEETEAAEKFVTFM--EQADNIadwvMMSPGAALPVNKAVVTTATWKDNDVIKALG 362
Cdd:COG1840  198 PEDGTLVnPSGAA----ILKG--APNPEAAKLFIDFLlsDEGQEL----LAEEGYEYPVRPDVEPPEGLPPLGELKLID 266
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 39-381 5.33e-07

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: 51.33  E-value: 5.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  39 EQERQAVISKLIARFEKENpGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHD-YAKVMDKEQLIDRKavatvISNV 117
Cdd:cd13658    8 EDKKMAFIKKIAKQYTKKT-GVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDrIGSAVLQGLLSPIK-----LSKD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 118 GEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAgleePKNWQQLLDVAQKLNDPANKKYGIaLPTAesvl 197
Cdd:cd13658   82 KKKGFTDQALKAL-TYDGKLY-GLPAAVETLALYYNKDLVKNA----PKTFDELEALAKDLTKEKGKQYGF-LADA---- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 198 TEQSFSQFALS-NQANVFNAEGK------ITLDTPEMMQALTYYRDLAANT-MPGSNDIMEVKDAFMNGTAPMAIYSTYI 269
Cdd:cd13658  151 TNFYYSYGLLAgNGGYIFKKNGSdldindIGLNSPGAVKAVKFLKKWYTEGyLPKGMTGDVIQGLFKEGKAAAVIDGPWA 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 270 LLAVIKEGdpKNVGFV-VPTEKNS-------AVYGMLTSltitagQKTEETEAAEKFVTFMEQADNIAD-WVMMSpgaAL 340
Cdd:cd13658  231 IQEYQEAG--VNYGVApLPTLPNGkpmapflGVKGWYLS------AYSKHKEWAQKFMEFLTSKENLKKrYDETN---EI 299

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 446520108 341 PVNKAVVTTATWKDNDVIKALGELPNQLIgELPNIQVFGAV 381
Cdd:cd13658  300 PPRKDVRSDPEIKNNPLTSAFAKQASRAV-PMPNIPEMGAV 339
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
31-345 3.73e-06

sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 49.03  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  31 IEFMHSsVEQERQAVISKLIARFEKENPgiTVKQVPVEEDAYNTKV---ITLSRSGSLPEVIETSHDYAKVMDKEQLIdr 107
Cdd:PRK10974  28 IPFWHS-MEGELGKEVDSLAQRFNASQP--DYKIVPVYKGNYEQSLaagIAAFRSGNAPAILQVYEVGTATMMASKAI-- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 108 KAVATVISNVG----EGAFYDGVLRIVRTEDGSAWTGVPVSAWIGGIWYRKDVLAKAGL---EEPKNWQQLLDVAQKLnd 180
Cdd:PRK10974 103 KPVYDVFKDAGipfdESQFVPTVAGYYSDAKTGHLLSQPFNSSTPVLYYNKDAFKKAGLdpeQPPKTWQDLAAYAAKL-- 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 181 panKKYGIALPTA---ESVLTEQSFSQF---ALSNQANVFN-AEGKITLDTPEMMQALTYYRDLAAN---TMPGSNDimE 250
Cdd:PRK10974 181 ---RAAGMKCGYAsgwQGWIQLENFSAWhglPFASKNNGFDgTDAVLEFNKPEQVKHIALLEEMNKKgdfTYVGRKD--E 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 251 VKDAFMNGTAPMAIYSTYIlLAVIKEGDPKN--VGFV-----VPTEKNSAVYGMlTSLTITAGQKTEETEAAEKFVTFME 323
Cdd:PRK10974 256 STEKFYNGDCAITTASSGS-LANIRKYAKFNygVGMMpydadVKGAPQNAIIGG-ASLWVMQGKDKETYKGVAKFLDFLA 333

                        330       340
                 ....*....|....*....|..
gi 446520108 324 QADNIADWVMMSpgAALPVNKA 345
Cdd:PRK10974 334 KPENAAEWHQKT--GYLPITTA 353
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 47-319 1.21e-04

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: 44.27  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  47 SKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIE-TSHDYAKVMDKE-QLID-----------RKAVatv 113
Cdd:cd13583   19 DWLIWKEIEEKTNVKFKRTPIPSSDYETKRSLLIASGDAPDIIPvLYPGEENEFVASgALLPisdyldympnyKKYV--- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 114 iSNVGEGAFYDgvlrIVRTEDGS--AWTGVPVSAWIGGIW-YRKDVLAKAGLEEPKNWQQLLDVAQKLNDpankKYGIAL 190
Cdd:cd13583   96 -EKWGLGKELA----TGRQSDGKyySLPGLHEDPGVQYSFlYRKDIFEKAGIKIPTTWDEFYAALKKLKE----KYPDSY 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 191 PTAESVLTEQSFSQFALSNQANVFNAEGKITLD-----------TPEMMQALTYYRDLAAN------TMPGSNDImeVKD 253
Cdd:cd13583  167 PYSDRWNSNALLLIAAPAFGTTAGWGFSNYTYDpdtdkfvygatTDEYKDMLQYFNKLYAEglldpeSFTQTDDQ--AKA 244

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446520108 254 AFMNG-----TAPMAIYSTYILLAVIKEGDPKNV-GFVVPTEKNSAVYgmlTSLTITAG-------QKTEETEAAEKFV 319
Cdd:cd13583  245 KFLNGksfviTTNPQTVDELQRNLRAADGGNYEVvSITPPAGPAGKAI---NGSRLENGfmisskaKDSKNFEALLQFL 320
PBP2_Fbp_like_2 cd13547
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 124-322 2.65e-04

Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270265 [Multi-domain]  Cd Length: 259  Bit Score: 42.59  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 124 DGVLRIVRTEDGSaWTGVPVSAwiGGIWYRKDvlaKAGLEEPKNWQQLLDvaqklndpANKKYGIALPTAesvlteqSFS 203
Cdd:cd13547   83 DAIPAPFYDKDGY-YYGTRLSA--MGIAYNTD---KVPEEAPKSWADLTK--------PKYKGQIVMPDP-------LYS 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 204 QFALSNQANVFNAEGkitldtpemmQALTYYRDLAAN--TMPGSNDimEVKDAFMNGTAPMAIYSTYILLAVIKEGDPkn 281
Cdd:cd13547  142 GAALDLVAALADKYG----------LGWEYFEKLKENgvKVEGGNG--QVLDAVASGERPAGVGVDYNALRAKEKGSP-- 207

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446520108 282 VGFVVPTEknsavyGMLTSLTITAGQK-TEETEAAEKFVTFM 322
Cdd:cd13547  208 LEVIYPEE------GTVVIPSPIAILKgSKNPEAAKAFVDFL 243
PBP2_Fbp_like_1 cd13544
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ...
 131-173 3.80e-04

Substrate binding domain of a putative ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270262 [Multi-domain]  Cd Length: 292  Bit Score: 42.20  E-value: 3.80e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446520108 131 RTEDGsAWTGVpvSAWIGGIWYRKDVLAKAGLEEPKNWQQLLD 173
Cdd:cd13544   87 KDPDG-YWTGI--YLGPLGFGVNTDELKEKGLPVPKSWEDLLN 126
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 33-187 1.10e-03

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: 41.29  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108  33 FMHSSVEQERQAVISKLiarfeKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHDYAKVM---------DKEQ 103
Cdd:cd13521   10 FNDNWVDDENWPVAKEI-----EKLTNVKLEIVAVTAATSQQKLNLMLASGDLPDIVGADYLKDKFIaygmegaflPLSK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 104 LIDRkavatvISNVGE--GAFYDGVLRIvRTEDGSAW---TGVPVSAWIGGIWYRKDVLAKAGLEEPKNWQQLLDVAQKL 178
Cdd:cd13521   85 YIDQ------YPNLKAffKQHPDVLRAS-TASDGKIYlipYEPPKDVPNQGYFIRKDWLDKLNLKTPKTLDELYNVLKAF 157


                 ....*....
gi 446520108 179 NDPANKKYG 187
Cdd:cd13521  158 KEKDPNGNG 166
PBP2_TbpA cd13545
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ...
 229-322 1.70e-03

Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding fold superfamily; Thiamin-binding protein TbpA is the periplasmic component of ABC-type transporter in E. coli, while the transmembrane permease and ATPase are ThiP and ThiQ, respectively. Thiamin (vitamin B1) is an essential confactor in all living systems that most prokaryotes, plants, and fungi can synthesized thiamin. However, in vertebrates, thiamine cannot be synthesized and must therefore be obtained through dietary absorption. In addition to thiamin biosynthesis, most organisms can import thiamin using specific transporters. After binding thiamine with high affinity, TbpA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The thiamine-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270263 [Multi-domain]  Cd Length: 269  Bit Score: 39.97  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520108 229 QALTYYRDLAANTMPGSNDIMEVKDAFMNGTAPMAI-YSTYILLAVIKEGDPKNVGFVVPTEKNSAVYGMltslTITAGQ 307
Cdd:cd13545  161 GYLEYWKKLKANGVTVTPGWSEAYGLFTTGEAPMVVsYATSPAYHVYYEKDLRYTAVIFPEGHYRQVEGA----GILKGA 236

                         90
                 ....*....|....*
gi 446520108 308 KteETEAAEKFVTFM 322
Cdd:cd13545  237 K--NPELAKKFVDFL 249
 
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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