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Conserved domains on  [gi|16129271|ref|NP_415826|]
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putative ABC transporter periplasmic binding protein YcjN [Escherichia coli str. K-12 substr. MG1655]

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 3.36e-59

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 197.19  E-value: 3.36e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271   7 VLLSALVSCALISGCKEENKTNVSIEFMHSSveQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLP 86
Cdd:COG1653  11 ALALALAACGGGGSGAAAAAGKVTLTVWHTG--GGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAP 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  87 EVIETSHDYAKVM-DKEQLIDRKAVATViSNVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGLEEP 165
Cdd:COG1653  89 DVVQVDSGWLAEFaAAGALVPLDDLLDD-DGLDKDDFLPGALDAG-TYDGKLY-GVPFNTDTLGLYYNKDLFEKAGLDPP 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 166 KNWQQLLDVAQKLNDPANkKYGIALPTAESvlteQSFSQFALSNQANVFNAEGKITLDTPEMMQALTYYRDL----TANT 241
Cdd:COG1653 166 KTWDELLAAAKKLKAKDG-VYGFALGGKDG----AAWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLvkdgYVPP 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 242 MPGSNDIMEVKDAFMNGTAPMAIYSTYILPAVIKEGDPKNVGFV----VPTEKNSAVYGMLTSLTITAGqkTEETEAAEK 317
Cdd:COG1653 241 GALGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDFDVGVAplpgGPGGKKPASVLGGSGLAIPKG--SKNPEAAWK 318

                       330
                ....*....|....*...
gi 16129271 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 3.36e-59

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 197.19  E-value: 3.36e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271   7 VLLSALVSCALISGCKEENKTNVSIEFMHSSveQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLP 86
Cdd:COG1653  11 ALALALAACGGGGSGAAAAAGKVTLTVWHTG--GGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAP 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  87 EVIETSHDYAKVM-DKEQLIDRKAVATViSNVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGLEEP 165
Cdd:COG1653  89 DVVQVDSGWLAEFaAAGALVPLDDLLDD-DGLDKDDFLPGALDAG-TYDGKLY-GVPFNTDTLGLYYNKDLFEKAGLDPP 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 166 KNWQQLLDVAQKLNDPANkKYGIALPTAESvlteQSFSQFALSNQANVFNAEGKITLDTPEMMQALTYYRDL----TANT 241
Cdd:COG1653 166 KTWDELLAAAKKLKAKDG-VYGFALGGKDG----AAWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLvkdgYVPP 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 242 MPGSNDIMEVKDAFMNGTAPMAIYSTYILPAVIKEGDPKNVGFV----VPTEKNSAVYGMLTSLTITAGqkTEETEAAEK 317
Cdd:COG1653 241 GALGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDFDVGVAplpgGPGGKKPASVLGGSGLAIPKG--SKNPEAAWK 318

                       330
                ....*....|....*...
gi 16129271 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 3.88e-52

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: 179.52  E-value: 3.88e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  31 IEFMHSSvEQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSH-DYAKVMDKEQLIDrka 109
Cdd:cd13585   2 LTFWDWG-QPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGpWVPEFASNGALLD--- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 110 VATVISNVGEGAFYDGVLRIVRTEDGSAWtGVPVSAWIGGIWYRKDVLAKAG--LEEPKNWQQLLDVAQKLNDPANKKYG 187
Cdd:cd13585  78 LDDYIEKDGLDDDFPPGLLDAGTYDGKLY-GLPFDADTLVLFYNKDLFDKAGpgPKPPWTWDELLEAAKKLTDKKGGQYG 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 188 IALPTAESVLTEqsFSQFALSNQANVFNA-EGKITLDTPEMMQALTYYRDLTA-NTMPGS--NDIMEVKDAFMNGTAPMA 263
Cdd:cd13585 157 FALRGGSGGQTQ--WYPFLWSNGGDLLDEdDGKATLNSPEAVEALQFYVDLYKdGVAPSSatTGGDEAVDLFASGKVAMM 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 264 IYSTYILPAVIKEGDPKNVGFV-VPTEKNSAVYGMLTSLTITAGQKTEETEAAEKFVTFMEQADNIADWVMMSPGAALPV 342
Cdd:cd13585 235 IDGPWALGTLKDSKVKFKWGVApLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAA 314

                       330
                ....*....|....*
gi 16129271 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 1.62e-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: 121.75  E-value: 1.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271    39 EQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLP-EVIETSHDYAKVMDKeqlidrKAVATVISNV 117
Cdd:pfam01547   3 SLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAK------AGLLLPLDDY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271   118 GEGAFYDGVLRivrtedgsaWTGVPVSAWIGGIWYRKDVLAKAGLEEPKNWQQLLDVAQKLNDpANKKYGIALPTAESVL 197
Cdd:pfam01547  77 VANYLVLGVPK---------LYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKE-KGKSPGGAGGGDASGT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271   198 TEQSFSQFALSNQANVFNAEGKiTLDTPEMMQALTYYRDLTA---------NTMPGSNDIMEVKDAFMNGTAPMAIYSTY 268
Cdd:pfam01547 147 LGYFTLALLASLGGPLFDKDGG-GLDNPEAVDAITYYVDLYAkvlllkklkNPGVAGADGREALALFEQGKAAMGIVGPW 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129271   269 -----------ILPAVIKEGDPKNVG-FVVPTEKNSAVYGmltsLTITAGQKTEETEAAEKFVTFMEQADN 327
Cdd:pfam01547 226 aalaankvklkVAFAAPAPDPKGDVGyAPLPAGKGGKGGG----YGLAIPKGSKNKEAAKKFLDFLTSPEA 292
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
31-345 9.06e-06

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 47.87  E-value: 9.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271   31 IEFMHSsVEQERQAVISKLIARFEKENPgiTVKQVPVEEDAYNTKV---ITLSRSGSLPEVIETSHDYAKVMDKEQLIdr 107
Cdd:PRK10974  28 IPFWHS-MEGELGKEVDSLAQRFNASQP--DYKIVPVYKGNYEQSLaagIAAFRSGNAPAILQVYEVGTATMMASKAI-- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  108 KAVATVISNVG----EGAFYDGVLRIVRTEDGSAWTGVPVSAWIGGIWYRKDVLAKAGL---EEPKNWQQLLDVAQKLnd 180
Cdd:PRK10974 103 KPVYDVFKDAGipfdESQFVPTVAGYYSDAKTGHLLSQPFNSSTPVLYYNKDAFKKAGLdpeQPPKTWQDLAAYAAKL-- 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  181 panKKYGIALPTA---ESVLTEQSFSQF---ALSNQANVFN-AEGKITLDTPEMMQALTYYRDLTAN---TMPGSNDimE 250
Cdd:PRK10974 181 ---RAAGMKCGYAsgwQGWIQLENFSAWhglPFASKNNGFDgTDAVLEFNKPEQVKHIALLEEMNKKgdfTYVGRKD--E 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  251 VKDAFMNGTAPMAIYSTYILpAVIKEGDPKN--VGFV-----VPTEKNSAVYGMlTSLTITAGQKTEETEAAEKFVTFME 323
Cdd:PRK10974 256 STEKFYNGDCAITTASSGSL-ANIRKYAKFNygVGMMpydadVKGAPQNAIIGG-ASLWVMQGKDKETYKGVAKFLDFLA 333

                        330       340
                 ....*....|....*....|..
gi 16129271  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 3.36e-59

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 197.19  E-value: 3.36e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271   7 VLLSALVSCALISGCKEENKTNVSIEFMHSSveQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLP 86
Cdd:COG1653  11 ALALALAACGGGGSGAAAAAGKVTLTVWHTG--GGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAP 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  87 EVIETSHDYAKVM-DKEQLIDRKAVATViSNVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGLEEP 165
Cdd:COG1653  89 DVVQVDSGWLAEFaAAGALVPLDDLLDD-DGLDKDDFLPGALDAG-TYDGKLY-GVPFNTDTLGLYYNKDLFEKAGLDPP 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 166 KNWQQLLDVAQKLNDPANkKYGIALPTAESvlteQSFSQFALSNQANVFNAEGKITLDTPEMMQALTYYRDL----TANT 241
Cdd:COG1653 166 KTWDELLAAAKKLKAKDG-VYGFALGGKDG----AAWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLvkdgYVPP 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 242 MPGSNDIMEVKDAFMNGTAPMAIYSTYILPAVIKEGDPKNVGFV----VPTEKNSAVYGMLTSLTITAGqkTEETEAAEK 317
Cdd:COG1653 241 GALGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDFDVGVAplpgGPGGKKPASVLGGSGLAIPKG--SKNPEAAWK 318

                       330
                ....*....|....*...
gi 16129271 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 3.88e-52

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: 179.52  E-value: 3.88e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  31 IEFMHSSvEQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSH-DYAKVMDKEQLIDrka 109
Cdd:cd13585   2 LTFWDWG-QPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGpWVPEFASNGALLD--- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 110 VATVISNVGEGAFYDGVLRIVRTEDGSAWtGVPVSAWIGGIWYRKDVLAKAG--LEEPKNWQQLLDVAQKLNDPANKKYG 187
Cdd:cd13585  78 LDDYIEKDGLDDDFPPGLLDAGTYDGKLY-GLPFDADTLVLFYNKDLFDKAGpgPKPPWTWDELLEAAKKLTDKKGGQYG 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 188 IALPTAESVLTEqsFSQFALSNQANVFNA-EGKITLDTPEMMQALTYYRDLTA-NTMPGS--NDIMEVKDAFMNGTAPMA 263
Cdd:cd13585 157 FALRGGSGGQTQ--WYPFLWSNGGDLLDEdDGKATLNSPEAVEALQFYVDLYKdGVAPSSatTGGDEAVDLFASGKVAMM 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 264 IYSTYILPAVIKEGDPKNVGFV-VPTEKNSAVYGMLTSLTITAGQKTEETEAAEKFVTFMEQADNIADWVMMSPGAALPV 342
Cdd:cd13585 235 IDGPWALGTLKDSKVKFKWGVApLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAA 314

                       330
                ....*....|....*
gi 16129271 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; ...
 31-423 2.17e-48

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: 169.40  E-value: 2.17e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  31 IEFMHSSvEQERQAVISKLIARFEKENPGITVKQVPVEEDAYN-TKVITLSRSGSLPEVIETSHDYAKvmdkeQLIDRKA 109
Cdd:cd14748   2 ITFWHGM-SGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTlTKLLAALAAGTAPDVAQVDASWVA-----QLADSGA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 110 VA---TVIS--NVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGL---EEPKNWQQLLDVAQKLNDP 181
Cdd:cd14748  76 LEpldDYIDkdGVDDDDFYPAALDAG-TYDGKLY-GLPFDTSTPVLYYNKDLFEEAGLdpeKPPKTWDELEEAAKKLKDK 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 182 ANK--KYGIALPTAEsvlTEQSFSQFALSNQANVFNAE-GKITLDTPEMMQALTYYRDLTANT-MPGSNDIMEVKDAFMN 257
Cdd:cd14748 154 GGKtgRYGFALPPGD---GGWTFQALLWQNGGDLLDEDgGKVTFNSPEGVEALEFLVDLVGKDgVSPLNDWGDAQDAFIS 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 258 GTAPMAIYSTYILPAVIKEGDPKNVGFV---VPTEKNSAVYGMLTSLTITAGqKTEETEAAEKFVTFMEQADNIADWVMM 334
Cdd:cd14748 231 GKVAMTINGTWSLAGIRDKGAGFEYGVAplpAGKGKKGATPAGGASLVIPKG-SSKKKEAAWEFIKFLTSPENQAKWAKA 309

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 335 spGAALPVNKAVVttatwkdndvikalgELPNQLIGELPNIQVFGAVGDKNFTRMGDVTGSGVVSSMVHN----VTVGKA 410
Cdd:cd14748 310 --TGYLPVRKSAA---------------EDPEEFLAENPNYKVAVDQLDYAKPWGPPVPNGAEIRDELNEaleaALLGKK 372

                       410
                ....*....|...
gi 16129271 411 DLSTTLQASQKKL 423
Cdd:cd14748 373 TPEEALKEAQEKI 385
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 30-367 2.19e-39

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: 145.60  E-value: 2.19e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  30 SIEFMHSSVEQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSH-----DYAKV------ 98
Cdd:cd14749   1 TITYWQYFTGDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPggwlaEFVKAglllpl 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  99 --MDKEQLIDRKAVATVISNV-GEGAFYdgvlrivrtedgsawtGVPVSAWIGGIWYRKDVLAKAG-LEEPKNWQQLLDV 174
Cdd:cd14749  81 tdYLDPNGVDKRFLPGLADAVtFNGKVY----------------GIPFAARALALFYNKDLFEEAGgVKPPKTWDELIEA 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 175 AQKLNDPANKKYGIALPTAESvlTEQSFSQFALSNQANVF---NAEGKITLDTPEMMQALTYYRDL-TANTMP---GSND 247
Cdd:cd14749 145 AKKDKFKAKGQTGFGLLLGAQ--GGHWYFQYLVRQAGGGPlsdDGSGKATFNDPAFVQALQKLQDLvKAGAFQegfEGID 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 248 IMEVKDAFMNGTAPMAIYSTYILPAVIKEGDPKNVGFVVPTEKN-----SAVYGMLTSLTITAgqKTEETEAAEKFVTFM 322
Cdd:cd14749 223 YDDAGQAFAQGKAAMNIGGSWDLGAIKAGEPGGKIGVFPFPTVGkgaqtSTIGGSDWAIAISA--NGKKKEAAVKFLKYL 300

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 16129271 323 EQADNIADWVMMspGAALPVNKAVVTTATWKDNDVIKALGELPNQ 367
Cdd:cd14749 301 TSPEVMKQYLED--VGLLPAKEVVAKDEDPDPVAILGPFADVLNA 343
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
3-429 3.31e-38

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 142.78  E-value: 3.31e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271   3 KSKIVLLSALVSCALISGC---------KEENKTNVSIEFMHSsveQERQAVISKLIARFEKEnPGITVKQVPVEEDAYN 73
Cdd:COG2182   4 RLLAALALALALALALAACgsgssssgsSSAAGAGGTLTVWVD---DDEAEALEEAAAAFEEE-PGIKVKVVEVPWDDLR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  74 TKVITLSRSGSLPEVIETSHDYAkvmdkEQLIDRKAVATVISNVGEGA-FYDGVLRIVrTEDGSAWtGVPVSAWIGGIWY 152
Cdd:COG2182  80 EKLTTAAPAGKGPDVFVGAHDWL-----GELAEAGLLAPLDDDLADKDdFLPAALDAV-TYDGKLY-GVPYAVETLALYY 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 153 RKDVLAKaglEEPKNWQQLLDVAQKLNDPAnkKYGIALPTAESvlteQSFSQFALSNQANVFNAEG----KITLDTPEMM 228
Cdd:COG2182 153 NKDLVKA---EPPKTWDELIAAAKKLTAAG--KYGLAYDAGDA----YYFYPFLAAFGGYLFGKDGddpkDVGLNSPGAV 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 229 QALTYYRDLTAN-TMPGSNDIMEVKDAFMNGTAPMAIYSTYILPAvIKEGDPKNVGFV-VPTEKN-SAVYGMLTSLTITA 305
Cdd:COG2182 224 AALEYLKDLIKDgVLPADADYDAADALFAEGKAAMIINGPWAAAD-LKKALGIDYGVApLPTLAGgKPAKPFVGVKGFGV 302

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 306 GQKTEETEAAEKFVTFMEQADNIADWVMMSPgaALPVNKAVVTTATWKDNDVIKALGElpnqligelpniQVFGAVGDKN 385
Cdd:COG2182 303 SAYSKNKEAAQEFAEYLTSPEAQKALFEATG--RIPANKAAAEDAEVKADPLIAAFAE------------QAEYAVPMPN 368

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 16129271 386 FTRMGDVtgSGVVSSMVHNVTVGKADLSTTLQASQKKLDELIEQ 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 3.38e-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: 3.38e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  33 FMHSSVEQErqaVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHD----YAKVMDKEQLIDRk 108
Cdd:cd14747   6 AMGNSAEAE---LLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTwvaeFAAMGALEDLTPY- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 109 avatVISNVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGLEE-PKNWQQLLDVAQKLNDPANKKYG 187
Cdd:cd14747  82 ----LEDLGGDKDLFPGLVDTG-TVDGKYY-GVPWYADTRALFYRTDLLKKAGGDEaPKTWDELEAAAKKIKADGPDVSG 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 188 IALPTAESVltEQSFSQFALSNQANVFN-AEGKITLDTPEMMQALTYYRDLTANTMPGSNDIMEVKD---AFMNGTAPMa 263
Cdd:cd14747 156 FAIPGKNDV--WHNALPFVWGAGGDLATkDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSADveqAFANGKVAM- 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 264 IYSTYILPAVIKEGDP---KNVGFVV---PTEKNSAVYGMLTSLTITAGQKteETEAAEKFVTFMEQADNIADWVMMSpg 337
Cdd:cd14747 233 IISGPWEIGAIREAGPdlaGKWGVAPlpgGPGGGSPSFAGGSNLAVFKGSK--NKDLAWKFIEFLSSPENQAAYAKAT-- 308

                       330       340
                ....*....|....*....|....*.
gi 16129271 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 1.62e-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: 121.75  E-value: 1.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271    39 EQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLP-EVIETSHDYAKVMDKeqlidrKAVATVISNV 117
Cdd:pfam01547   3 SLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAK------AGLLLPLDDY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271   118 GEGAFYDGVLRivrtedgsaWTGVPVSAWIGGIWYRKDVLAKAGLEEPKNWQQLLDVAQKLNDpANKKYGIALPTAESVL 197
Cdd:pfam01547  77 VANYLVLGVPK---------LYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKE-KGKSPGGAGGGDASGT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271   198 TEQSFSQFALSNQANVFNAEGKiTLDTPEMMQALTYYRDLTA---------NTMPGSNDIMEVKDAFMNGTAPMAIYSTY 268
Cdd:pfam01547 147 LGYFTLALLASLGGPLFDKDGG-GLDNPEAVDAITYYVDLYAkvlllkklkNPGVAGADGREALALFEQGKAAMGIVGPW 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129271   269 -----------ILPAVIKEGDPKNVG-FVVPTEKNSAVYGmltsLTITAGQKTEETEAAEKFVTFMEQADN 327
Cdd:pfam01547 226 aalaankvklkVAFAAPAPDPKGDVGyAPLPAGKGGKGGG----YGLAIPKGSKNKEAAKKFLDFLTSPEA 292
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 48-355 9.25e-27

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 108.65  E-value: 9.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271    48 KLIARFEKENpGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETS--HDYAKvmdkeQLIDRKAVATvISNVGEGAFYDG 125
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDLDVVWiaADQLA-----TLAEAGLLAD-LSDVDNLDDLPD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271   126 VLRIVrTEDGsAWTGVPVSA-WIGGIWYRKDVLAKAGlEEPKNWQQLLDVAQKLNdpanKKYGIALPTAesvlteQSFSQ 204
Cdd:pfam13416  74 ALDAA-GYDG-KLYGVPYAAsTPTVLYYNKDLLKKAG-EDPKTWDELLAAAAKLK----GKTGLTDPAT------GWLLW 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271   205 FALSNQANvFNAEGKITLDTPEmmqALTYYRDLTAN--TMPGSNDIMevkDAFMNGTAPMAIYSTYILPAVIKEGdpKNV 282
Cdd:pfam13416 141 ALLADGVD-LTDDGKGVEALDE---ALAYLKKLKDNgkVYNTGADAV---QLFANGEVAMTVNGTWAAAAAKKAG--KKL 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129271   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 4.45e-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: 105.84  E-value: 4.45e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  31 IEFMHSSVEQERQaVISKLIARFEKENPGITVK--QVPVEEDAYNTKVITLSRSGSLP------EVIETSHDYAKVMDKE 102
Cdd:cd14750   2 ITFAAGSDGQEGE-LLKKAIAAFEKKHPDIKVEieELPASSDDQRQQLVTALAAGSSApdvlglDVIWIPEFAEAGWLLP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 103 QLIDRKAVatvisnvGEGAFYDGVLRiVRTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGLEEPKNWQQLLDVAQKLNDPA 182
Cdd:cd14750  81 LTEYLKEE-------EDDDFLPATVE-ANTYDGKLY-ALPWFTDAGLLYYRKDLLEKYGPEPPKTWDELLEAAKKRKAGE 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 183 NKKYGIALPTAE-SVLTeQSFSQFALSNQANVFNAE-GKITLDTPEMMQALTYYRDLTANTM--PGSNDIME--VKDAFM 256
Cdd:cd14750 152 PGIWGYVFQGKQyEGLV-CNFLELLWSNGGDIFDDDsGKVTVDSPEALEALQFLRDLIGEGIspKGVLTYGEeeARAAFQ 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 257 NGTAPMAIYSTYILPAVIKEGDP--KNVGFV-VPTEKNSAVYGML--TSLTITAgqKTEETEAAEKFVTFMEQADNIADW 331
Cdd:cd14750 231 AGKAAFMRNWPYAYALLQGPESAvaGKVGVApLPAGPGGGSASTLggWNLAISA--NSKHKEAAWEFVKFLTSPEVQKRR 308

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 332 VMMspGAALPVNKAVVttatwKDNDVIKALGELPNQLIGEL-----PNIQVFGAVgdknftrmgdvtgSGVVSSMVHNVT 406
Cdd:cd14750 309 AIN--GGLPPTRRALY-----DDPEVLEAYPFLPALLEALEnavprPVTPKYPEV-------------STAIQIALSAAL 368

                       410
                ....*....|....*..
gi 16129271 407 VGKADLSTTLQASQKKL 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 5.94e-24

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: 102.37  E-value: 5.94e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  39 EQERQAVISKLIARFEKENpGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHDYAKVMDKEQLIDRKAVATVISNVG 118
Cdd:cd13586   8 EDGELEYLKELAEEFEKKY-GIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLAVKIKN 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 119 EGAFYDGVlrivrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAgleePKNWQQLLDVAQKLNDPANKKYGIALPTAESVLt 198
Cdd:cd13586  87 LPVALAAV-----TYNGKLY-GVPVSVETIALFYNKDLVPEP----PKTWEELIALAKKFNDKAGGKYGFAYDQTNPYF- 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 199 eqsFSQFALSNQANVFNAEGK----ITLDTPEMMQALTYYRDL--TANTMPGSNDIMEVKDAFMNGTAPMAIYSTYILPA 272
Cdd:cd13586 156 ---SYPFLAAFGGYVFGENGGdptdIGLNNEGAVKGLKFIKDLkkKYKVLPPDLDYDIADALFKEGKAAMIINGPWDLAD 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 273 VIKEGDpkNVGF-VVPTEKNSAVYG-MLTSLTITAGQKTEETEAAEKFVTFMeqADNIADWVMMSPGAALPVNKAVVTTA 350
Cdd:cd13586 233 YKDAGI--NFGVaPLPTLPGGKQAApFVGVQGAFVSAYSKNKEAAVEFAEYL--TSDEAQLLLFEKTGRIPALKDALNDA 308

                       330
                ....*....|...
gi 16129271 351 TWKDNDVIKALGE 363
Cdd:cd13586 309 AVKNDPLVKAFAE 321
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 30-363 4.84e-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: 93.98  E-value: 4.84e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  30 SIEFMHSSVEQERQAvISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHDYAKVMDKEQLIDrkA 109
Cdd:cd13657   1 TITIWHALTGAEEDA-LQQIIDEFEAKYPVPNVKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLV--P 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 110 VATVISNVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAgleePKNWQQLLDVAQKLNDPANKKYGIA 189
Cdd:cd13657  78 ISDYLSEDDFENYLPTAVEAV-TYKGKVY-GLPEAYETVALIYNKALVDQP----PETTDELLAIMKDHTDPAAGSYGLA 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 190 LPtaesVLTEQSFSQFALSNQANVFNAEG-KITLDTPEMMQALTYYRDLTANTMPGSNDIMEVKDAFMNGTAPMAIYSTY 268
Cdd:cd13657 152 YQ----VSDAYFVSAWIFGFGGYYFDDETdKPGLDTPETIKGIQFLKDFSWPYMPSDPSYNTQTSLFNEGKAAMIINGPW 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 269 ILPAVIKEGDpkNVGFV----VPTEKNSAVYGMLTSLTITAGQKTEETEAAEKFVTFMEQADNIAdwVMMSPGAALPVNK 344
Cdd:cd13657 228 FIGGIKAAGI--DLGVAplptVDGTNPPRPYSGVEGIYVTKYAERKNKEAALDFAKFFTTAEASK--ILADENGYVPAAT 303

                       330
                ....*....|....*....
gi 16129271 345 AVVTTATWKDNDVIKALGE 363
Cdd:cd13657 304 NAYDDAEVAADPVIAAFKA 322
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 30-360 9.94e-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: 93.21  E-value: 9.94e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  30 SIEFMHSSVEQErQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSH----DYAKvMDKEQLI 105
Cdd:cd14751   1 TITFWHTSSDEE-KVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIawvpEFAK-LGYLQPL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 106 DRKAVATVIsnvgeGAFYDGVLRIVRTEdGSAWtGVPVSAWIGGIWYRKDVLAKAGLEEPKNWQQLLDVAQKlNDPANKK 185
Cdd:cd14751  79 DGTPAFDDI-----VDYLPGPMETNRYN-GHYY-GVPQVTNTLALFYNKRLLEEAGTEVPKTMDELVAAAKA-IKKKKGR 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 186 YGIALptaeSVLTEQSFSQFALSNQANVFNAEGK-ITLDTPEMMQALTYYRDLTAN-----TMPGSNDIMevKDAFMNGT 259
Cdd:cd14751 151 YGLYI----SGDGPYWLLPFLWSFGGDLTDEKKAtGYLNSPESVRALETIVDLYDEgaitpCASGGYPNM--QDGFKSGR 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 260 APMAI---YSTYILPAVIKEGDPKNVGF----VVPTEKNSAVYGmlTSLTITAGQKTEetEAAEKFVTFMEQADNIAdwV 332
Cdd:cd14751 225 YAMIVngpWAYADILGGKEFKDPDNLGIapvpAGPGGSGSPVGG--EDLVIFKGSKNK--DAAWKFVKFMSSAEAQA--L 298

                       330       340
                ....*....|....*....|....*...
gi 16129271 333 MMSPGAALPVNKAVVTTATWKDNDVIKA 360
Cdd:cd14751 299 TAAKLGLLPTRTSAYESPEVANNPMVAA 326
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 31-346 2.49e-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: 77.07  E-value: 2.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  31 IEFMHSSVEQERQAViSKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHDYAKVMdkeqlidrkAV 110
Cdd:cd13522   2 ITVWHQYDTGENQAV-NELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPF---------AA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 111 ATVISNVGEG---------AFYDGVlrivrTEDGSAWtGVPVSAWIGGIWYRKDVLAKaglEEPKNWQQLLDVAQKLNDP 181
Cdd:cd13522  72 AGLLAPLDEYvsksgkyapNTIAAM-----KLNGKLY-GVPVSVGAHLMYYNKKLVPK---NPPKTWQELIALAQGLKAK 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 182 AnkKYGIALPTAESVLteqsFSQFALSNQANVFNAEG---KITLDTPEMMQALTYYRDL--TANTMPGSNDIMEVKDAFM 256
Cdd:cd13522 143 N--VWGLVYNQNEPYF----FAAWIGGFGGQVFKANNgknNPTLDTPGAVEALQFLVDLksKYKIMPPETDYSIADALFK 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 257 NGTAPMAIYSTYILpAVIKEGDPKNVGF----VVPTEKNSAVygMLTSLTITAGQKTEETEAAEKFVTFMEQADNIADWV 332
Cdd:cd13522 217 AGKAAMIINGPWDL-GDYRQALKINLGVaplpTFSGTKHAAP--FVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLF 293

                       330
                ....*....|....
gi 16129271 333 MMSPGaaLPVNKAV 346
Cdd:cd13522 294 DDAGD--IPANLQA 305
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 55-331 1.56e-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: 1.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  55 KENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVI-----ETSHDYAK---VMDKEQLIDRKA--VATVISNVGEGAF-Y 123
Cdd:cd13580  29 EEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVvvndpQLSITLVKqgaLWDLTDYLDKYYpnLKKIIEQEGWDSAsV 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 124 DGVLrivrtedgsawTGVPVSAWIG---GIWYRKDVLAKAGLEEPKNWQQLLDVAQ--KLNDP----ANKKYGIALPtae 194
Cdd:cd13580 109 DGKI-----------YGIPRKRPLIgrnGLWIRKDWLDKLGLEVPKTLDELYEVAKafTEKDPdgngKKDTYGLTDT--- 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 195 SVLTEQSFSQFALS----NQANVFNAEGKITLD--TPEMMQALTYYRDLTAN--------TMPGSNdimeVKDAFMNGTA 260
Cdd:cd13580 175 KDLIGSGFTGLFGAfgapPNNWWKDEDGKLVPGsiQPEMKEALKFLKKLYKEglidpefaVNDGTK----ANEKFISGKA 250

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 261 PM---AIYSTYILPAVIKEGDPKNVGFVVPT------EKNSAVYGMLTSLTItAGQKTEETEAAEKFVTFM--EQADNIA 329
Cdd:cd13580 251 GIfvgNWWDPAWPQASLKKNDPDAEWVAVPIpsgpdgKYGVWAESGVNGFFV-IPKKSKKPEAILKLLDFLsdPEVQKLL 329


                ..
gi 16129271 330 DW 331
Cdd:cd13580 330 DY 331
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-346 5.98e-11

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 63.39  E-value: 5.98e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271   1 MIKSKIVLLSALVSCALISGCkeenktnvsiefmHSSVEQERQAVIS--------KLIARFEKENpGITVKQVPVE--ED 70
Cdd:COG0687   1 MSRRSLLGLAAAALAAALAGG-------------APAAAAEGTLNVYnwggyidpDVLEPFEKET-GIKVVYDTYDsnEE 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  71 AYnTKVITlsrSGSLPEVIETSHDYAKVMDKEQL---IDRKAvatvISNVgegAFYDGVLRIVRTEDGSAWtGVPVSAWI 147
Cdd:COG0687  67 ML-AKLRA---GGSGYDVVVPSDYFVARLIKAGLlqpLDKSK----LPNL---ANLDPRFKDPPFDPGNVY-GVPYTWGT 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 148 GGIWYRKDVLAkaglEEPKNWQQLLDvaqklndPANK-KYGIaLPTAESVLTeqsfsqFALsnqanvfNAEGK--ITLDT 224
Cdd:COG0687 135 TGIAYNTDKVK----EPPTSWADLWD-------PEYKgKVAL-LDDPREVLG------AAL-------LYLGYdpNSTDP 189

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 225 PEMMQALTYYRDLTANTMPGSNDIMEVKDAFMNGTAPMAIYSTYILPAVIKEGDPknVGFVVPTEKnsaVYGMLTSLTIT 304
Cdd:COG0687 190 ADLDAAFELLIELKPNVRAFWSDGAEYIQLLASGEVDLAVGWSGDALALRAEGPP--IAYVIPKEG---ALLWFDNMAIP 264

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 16129271 305 AGqkTEETEAAEKFVTFMEQADNIADWVMMSPGAalPVNKAV 346
Cdd:COG0687 265 KG--APNPDLAYAFINFMLSPEVAAALAEYVGYA--PPNKAA 302
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 39-381 3.07e-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: 52.10  E-value: 3.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  39 EQERQAVISKLIARFEKENpGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHD-YAKVMDKEQLIDRKavatvISNV 117
Cdd:cd13658   8 EDKKMAFIKKIAKQYTKKT-GVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDrIGSAVLQGLLSPIK-----LSKD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 118 GEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAgleePKNWQQLLDVAQKLNDPANKKYGIaLPTAesvl 197
Cdd:cd13658  82 KKKGFTDQALKAL-TYDGKLY-GLPAAVETLALYYNKDLVKNA----PKTFDELEALAKDLTKEKGKQYGF-LADA---- 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 198 TEQSFSQFALS-NQANVFNAEGK------ITLDTPEMMQALTYYRDLTANT-MPGSNDIMEVKDAFMNGTAPMAIYSTYI 269
Cdd:cd13658 151 TNFYYSYGLLAgNGGYIFKKNGSdldindIGLNSPGAVKAVKFLKKWYTEGyLPKGMTGDVIQGLFKEGKAAAVIDGPWA 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 270 LPAVIKEGdpKNVGFV-VPTEKNS-------AVYGMLTSltitagQKTEETEAAEKFVTFMEQADNIAD-WVMMSpgaAL 340
Cdd:cd13658 231 IQEYQEAG--VNYGVApLPTLPNGkpmapflGVKGWYLS------AYSKHKEWAQKFMEFLTSKENLKKrYDETN---EI 299

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 16129271 341 PVNKAVVTTATWKDNDVIKALGELPNQLIgELPNIQVFGAV 381
Cdd:cd13658 300 PPRKDVRSDPEIKNNPLTSAFAKQASRAV-PMPNIPEMGAV 339
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 131-362 4.73e-07

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 51.09  E-value: 4.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 131 RTEDGsAWTGVpvSAWIGGIWYRKDVLAKAGLeePKNWQQLLdvaqklnDPANK-KYGIALPTAEsvlteqSFSQFALSN 209
Cdd:COG1840  72 RDPDG-YWFGF--SVRARVIVYNTDLLKELGV--PKSWEDLL-------DPEYKgKIAMADPSSS------GTGYLLVAA 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 210 QANVFNAEgkitldtpemmQALTYYRDLTANT---MPGSNDIMevkDAFMNGTAPMAIYSTYILPAVIKEGDPknVGFVV 286
Cdd:COG1840 134 LLQAFGEE-----------KGWEWLKGLAANGarvTGSSSAVA---KAVASGEVAIGIVNSYYALRAKAKGAP--VEVVF 197

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129271 287 PTEKNSA-VYGMLtsltITAGqkTEETEAAEKFVTFM--EQADNIadwvMMSPGAALPVNKAVVTTATWKDNDVIKALG 362
Cdd:COG1840 198 PEDGTLVnPSGAA----ILKG--APNPEAAKLFIDFLlsDEGQEL----LAEEGYEYPVRPDVEPPEGLPPLGELKLID 266
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
31-345 9.06e-06

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 47.87  E-value: 9.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271   31 IEFMHSsVEQERQAVISKLIARFEKENPgiTVKQVPVEEDAYNTKV---ITLSRSGSLPEVIETSHDYAKVMDKEQLIdr 107
Cdd:PRK10974  28 IPFWHS-MEGELGKEVDSLAQRFNASQP--DYKIVPVYKGNYEQSLaagIAAFRSGNAPAILQVYEVGTATMMASKAI-- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  108 KAVATVISNVG----EGAFYDGVLRIVRTEDGSAWTGVPVSAWIGGIWYRKDVLAKAGL---EEPKNWQQLLDVAQKLnd 180
Cdd:PRK10974 103 KPVYDVFKDAGipfdESQFVPTVAGYYSDAKTGHLLSQPFNSSTPVLYYNKDAFKKAGLdpeQPPKTWQDLAAYAAKL-- 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  181 panKKYGIALPTA---ESVLTEQSFSQF---ALSNQANVFN-AEGKITLDTPEMMQALTYYRDLTAN---TMPGSNDimE 250
Cdd:PRK10974 181 ---RAAGMKCGYAsgwQGWIQLENFSAWhglPFASKNNGFDgTDAVLEFNKPEQVKHIALLEEMNKKgdfTYVGRKD--E 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  251 VKDAFMNGTAPMAIYSTYILpAVIKEGDPKN--VGFV-----VPTEKNSAVYGMlTSLTITAGQKTEETEAAEKFVTFME 323
Cdd:PRK10974 256 STEKFYNGDCAITTASSGSL-ANIRKYAKFNygVGMMpydadVKGAPQNAIIGG-ASLWVMQGKDKETYKGVAKFLDFLA 333

                        330       340
                 ....*....|....*....|..
gi 16129271  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 4.98e-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: 45.43  E-value: 4.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  47 SKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIE-TSHDYAKVMDKE-QLID-----------RKAVatv 113
Cdd:cd13583  19 DWLIWKEIEEKTNVKFKRTPIPSSDYETKRSLLIASGDAPDIIPvLYPGEENEFVASgALLPisdyldympnyKKYV--- 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 114 iSNVGEGAFYDgvlrIVRTEDGS--AWTGVPVSAWIGGIW-YRKDVLAKAGLEEPKNWQQLLDVAQKLNDpankKYGIAL 190
Cdd:cd13583  96 -EKWGLGKELA----TGRQSDGKyySLPGLHEDPGVQYSFlYRKDIFEKAGIKIPTTWDEFYAALKKLKE----KYPDSY 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 191 PTAESVLTEQSFSQFALSNQANVFNAEGKITLD-----------TPEMMQALTYYRDLTAN------TMPGSNDImeVKD 253
Cdd:cd13583 167 PYSDRWNSNALLLIAAPAFGTTAGWGFSNYTYDpdtdkfvygatTDEYKDMLQYFNKLYAEglldpeSFTQTDDQ--AKA 244

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129271 254 AFMNG-----TAPMAIYSTYILPAVIKEGDPKNV-GFVVPTEKNSAVYgmlTSLTITAG-------QKTEETEAAEKFV 319
Cdd:cd13583 245 KFLNGksfviTTNPQTVDELQRNLRAADGGNYEVvSITPPAGPAGKAI---NGSRLENGfmisskaKDSKNFEALLQFL 320
PBP2_Fbp_like_1 cd13544
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ...
 131-173 3.57e-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: 3.57e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 16129271 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 1.11e-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: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271  33 FMHSSVEQERQAVISKLiarfeKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHDYAKVM---------DKEQ 103
Cdd:cd13521  10 FNDNWVDDENWPVAKEI-----EKLTNVKLEIVAVTAATSQQKLNLMLASGDLPDIVGADYLKDKFIaygmegaflPLSK 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 104 LIDRkavatvISNVGE--GAFYDGVLRIvRTEDGSAW---TGVPVSAWIGGIWYRKDVLAKAGLEEPKNWQQLLDVAQKL 178
Cdd:cd13521  85 YIDQ------YPNLKAffKQHPDVLRAS-TASDGKIYlipYEPPKDVPNQGYFIRKDWLDKLNLKTPKTLDELYNVLKAF 157


                ....*....
gi 16129271 179 NDPANKKYG 187
Cdd:cd13521 158 KEKDPNGNG 166
PBP2_Fbp_like_2 cd13547
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 124-322 8.06e-03

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: 37.97  E-value: 8.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 124 DGVLRIVRTEDGSaWTGVPVSAwiGGIWYRKDvlaKAGLEEPKNWQQLLDvaqklndpANKKYGIALPTAesvlteqSFS 203
Cdd:cd13547  83 DAIPAPFYDKDGY-YYGTRLSA--MGIAYNTD---KVPEEAPKSWADLTK--------PKYKGQIVMPDP-------LYS 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 204 QFALSNQANVFNAEGkitldtpemmQALTYYRDLTAN--TMPGSNDimEVKDAFMNGTAPMAIYSTYILPAVIKEGDPkn 281
Cdd:cd13547 142 GAALDLVAALADKYG----------LGWEYFEKLKENgvKVEGGNG--QVLDAVASGERPAGVGVDYNALRAKEKGSP-- 207

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 16129271 282 VGFVVPTEknsavyGMLTSLTITAGQK-TEETEAAEKFVTFM 322
Cdd:cd13547 208 LEVIYPEE------GTVVIPSPIAILKgSKNPEAAKAFVDFL 243
PBP2_TbpA cd13545
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ...
 229-322 9.15e-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: 37.66  E-value: 9.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129271 229 QALTYYRDLTANTMPGSNDIMEVKDAFMNGTAPMAI-YSTYILPAVIKEGDPKNVGFVVPTEKNSAVYGMltslTITAGQ 307
Cdd:cd13545 161 GYLEYWKKLKANGVTVTPGWSEAYGLFTTGEAPMVVsYATSPAYHVYYEKDLRYTAVIFPEGHYRQVEGA----GILKGA 236

                        90
                ....*....|....*
gi 16129271 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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