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Conserved domains on  [gi|446520088|ref|WP_000597434|]
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ABC transporter substrate-binding protein [Shigella flexneri]

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 ...
 7-332 1.03e-58

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 196.03  E-value: 1.03e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088   7 VLLSALVSCALISGCKEENKTHVSIEFMHSSveQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLP 86
Cdd:COG1653   11 ALALALAACGGGGSGAAAAAGKVTLTVWHTG--GGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  87 EVIETSHDYAKVM-DKEQLIDRKAVATViSNVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGLEEP 165
Cdd:COG1653   89 DVVQVDSGWLAEFaAAGALVPLDDLLDD-DGLDKDDFLPGALDAG-TYDGKLY-GVPFNTDTLGLYYNKDLFEKAGLDPP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 166 KNWQQLLDVAQKLNDPANkKYGIALPTAESvlteQSFSQFALSNQANVFNAEGKITLDTPEMMQALTYYRDLAAN--TMP 243
Cdd:COG1653  166 KTWDELLAAAKKLKAKDG-VYGFALGGKDG----AAWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKDgyVPP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 244 GSN--DIMEVKDAFMNGTAPMAIYSTYILPAVIKEGDPKNVGFV----VPTEKNSAVYGMLTSLTITAGQK-TEAAEKFV 316
Cdd:COG1653  241 GALgtDWDDARAAFASGKAAMMINGSWALGALKDAAPDFDVGVAplpgGPGGKKPASVLGGSGLAIPKGSKnPEAAWKFL 320

                        330
                 ....*....|....*.
gi 446520088 317 TFMEQADNIADWVMMS 332
Cdd:COG1653  321 KFLTSPEAQAKWDALQ 336
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 7-332 1.03e-58

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 196.03  E-value: 1.03e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088   7 VLLSALVSCALISGCKEENKTHVSIEFMHSSveQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLP 86
Cdd:COG1653   11 ALALALAACGGGGSGAAAAAGKVTLTVWHTG--GGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  87 EVIETSHDYAKVM-DKEQLIDRKAVATViSNVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGLEEP 165
Cdd:COG1653   89 DVVQVDSGWLAEFaAAGALVPLDDLLDD-DGLDKDDFLPGALDAG-TYDGKLY-GVPFNTDTLGLYYNKDLFEKAGLDPP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 166 KNWQQLLDVAQKLNDPANkKYGIALPTAESvlteQSFSQFALSNQANVFNAEGKITLDTPEMMQALTYYRDLAAN--TMP 243
Cdd:COG1653  166 KTWDELLAAAKKLKAKDG-VYGFALGGKDG----AAWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKDgyVPP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 244 GSN--DIMEVKDAFMNGTAPMAIYSTYILPAVIKEGDPKNVGFV----VPTEKNSAVYGMLTSLTITAGQK-TEAAEKFV 316
Cdd:COG1653  241 GALgtDWDDARAAFASGKAAMMINGSWALGALKDAAPDFDVGVAplpgGPGGKKPASVLGGSGLAIPKGSKnPEAAWKFL 320

                        330
                 ....*....|....*.
gi 446520088 317 TFMEQADNIADWVMMS 332
Cdd:COG1653  321 KFLTSPEAQAKWDALQ 336
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 31-354 1.39e-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: 180.68  E-value: 1.39e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  31 IEFMHSSvEQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSH-DYAKVMDKEQLIDrka 109
Cdd:cd13585    2 LTFWDWG-QPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGpWVPEFASNGALLD--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 110 VATVISNVGEGAFYDGVLRIVRTEDGSAWtGVPVSAWIGGIWYRKDVLAKAG--LEEPKNWQQLLDVAQKLNDPANKKYG 187
Cdd:cd13585   78 LDDYIEKDGLDDDFPPGLLDAGTYDGKLY-GLPFDADTLVLFYNKDLFDKAGpgPKPPWTWDELLEAAKKLTDKKGGQYG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 188 IALPTAESVLTEqsFSQFALSNQANVFNA-EGKITLDTPEMMQALTYYRDLAA-NTMPGS--NDIMEVKDAFMNGTAPMA 263
Cdd:cd13585  157 FALRGGSGGQTQ--WYPFLWSNGGDLLDEdDGKATLNSPEAVEALQFYVDLYKdGVAPSSatTGGDEAVDLFASGKVAMM 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 264 IYSTYILPAVIKEGDPKNVGFVV----PTEKNSAVYGMlTSLTITAG-QKTEAAEKFVTFMEQADNIADWVMMSPGAALP 338
Cdd:cd13585  235 IDGPWALGTLKDSKVKFKWGVAPlpagPGGKRASVLGG-WGLAISKNsKHPEAAWKFIKFLTSKENQLKLGGAAGPAALA 313

                        330
                 ....*....|....*.
gi 446520088 339 VNKAVVTTATWKDNDV 354
Cdd:cd13585  314 AAAASAAAPDAKPALA 329
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 39-324 6.09e-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: 120.21  E-value: 6.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088   39 EQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLP-EVIETSHDYAKVMDKeqlidrKAVATVISNV 117
Cdd:pfam01547   3 SLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAK------AGLLLPLDDY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  118 GEGAFYDGVLRivrtedgsaWTGVPVSAWIGGIWYRKDVLAKAGLEEPKNWQQLLDVAQKLNDpANKKYGIALPTAESVL 197
Cdd:pfam01547  77 VANYLVLGVPK---------LYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKE-KGKSPGGAGGGDASGT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  198 TEQSFSQFALSNQANVFNAEGKiTLDTPEMMQALTYYRDLAA---------NTMPGSNDIMEVKDAFMNGTAPMAIYSTY 268
Cdd:pfam01547 147 LGYFTLALLASLGGPLFDKDGG-GLDNPEAVDAITYYVDLYAkvlllkklkNPGVAGADGREALALFEQGKAAMGIVGPW 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446520088  269 -----------ILPAVIKEGDPKNVG-FVVPTEKNSAVYGmlTSLTITAG-QKTEAAEKFVTFMEQADN 324
Cdd:pfam01547 226 aalaankvklkVAFAAPAPDPKGDVGyAPLPAGKGGKGGG--YGLAIPKGsKNKEAAKKFLDFLTSPEA 292
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
31-342 1.03e-04

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 44.41  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  31 IEFMHSsVEQERQAVISKLIARFEKENPgiTVKQVPVEEDAYNTKV---ITLSRSGSLPEVIETSHDYAKVMDKEQLIdr 107
Cdd:PRK10974  28 IPFWHS-MEGELGKEVDSLAQRFNASQP--DYKIVPVYKGNYEQSLaagIAAFRSGNAPAILQVYEVGTATMMASKAI-- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 108 KAVATVISNVG----EGAFYDGVLRIVRTEDGSAWTGVPVSAWIGGIWYRKDVLAKAGL---EEPKNWQQLLDVAQKLnd 180
Cdd:PRK10974 103 KPVYDVFKDAGipfdESQFVPTVAGYYSDAKTGHLLSQPFNSSTPVLYYNKDAFKKAGLdpeQPPKTWQDLAAYAAKL-- 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 181 panKKYGIALPTA---ESVLTEQSFSQF---ALSNQANVFN-AEGKITLDTPEMMQALTYYRDLAAN---TMPGSNDimE 250
Cdd:PRK10974 181 ---RAAGMKCGYAsgwQGWIQLENFSAWhglPFASKNNGFDgTDAVLEFNKPEQVKHIALLEEMNKKgdfTYVGRKD--E 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 251 VKDAFMNGTAPMAIYSTYILpAVIKEGDPKN--VGFV-----VPTEKNSAVYGMlTSLTITAGQKTE---AAEKFVTFME 320
Cdd:PRK10974 256 STEKFYNGDCAITTASSGSL-ANIRKYAKFNygVGMMpydadVKGAPQNAIIGG-ASLWVMQGKDKEtykGVAKFLDFLA 333

                        330       340
                 ....*....|....*....|..
gi 446520088 321 QADNIADWVMMSpgAALPVNKA 342
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 ...
 7-332 1.03e-58

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 196.03  E-value: 1.03e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088   7 VLLSALVSCALISGCKEENKTHVSIEFMHSSveQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLP 86
Cdd:COG1653   11 ALALALAACGGGGSGAAAAAGKVTLTVWHTG--GGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  87 EVIETSHDYAKVM-DKEQLIDRKAVATViSNVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGLEEP 165
Cdd:COG1653   89 DVVQVDSGWLAEFaAAGALVPLDDLLDD-DGLDKDDFLPGALDAG-TYDGKLY-GVPFNTDTLGLYYNKDLFEKAGLDPP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 166 KNWQQLLDVAQKLNDPANkKYGIALPTAESvlteQSFSQFALSNQANVFNAEGKITLDTPEMMQALTYYRDLAAN--TMP 243
Cdd:COG1653  166 KTWDELLAAAKKLKAKDG-VYGFALGGKDG----AAWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKDgyVPP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 244 GSN--DIMEVKDAFMNGTAPMAIYSTYILPAVIKEGDPKNVGFV----VPTEKNSAVYGMLTSLTITAGQK-TEAAEKFV 316
Cdd:COG1653  241 GALgtDWDDARAAFASGKAAMMINGSWALGALKDAAPDFDVGVAplpgGPGGKKPASVLGGSGLAIPKGSKnPEAAWKFL 320

                        330
                 ....*....|....*.
gi 446520088 317 TFMEQADNIADWVMMS 332
Cdd:COG1653  321 KFLTSPEAQAKWDALQ 336
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 31-354 1.39e-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: 180.68  E-value: 1.39e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  31 IEFMHSSvEQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSH-DYAKVMDKEQLIDrka 109
Cdd:cd13585    2 LTFWDWG-QPAETAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGpWVPEFASNGALLD--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 110 VATVISNVGEGAFYDGVLRIVRTEDGSAWtGVPVSAWIGGIWYRKDVLAKAG--LEEPKNWQQLLDVAQKLNDPANKKYG 187
Cdd:cd13585   78 LDDYIEKDGLDDDFPPGLLDAGTYDGKLY-GLPFDADTLVLFYNKDLFDKAGpgPKPPWTWDELLEAAKKLTDKKGGQYG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 188 IALPTAESVLTEqsFSQFALSNQANVFNA-EGKITLDTPEMMQALTYYRDLAA-NTMPGS--NDIMEVKDAFMNGTAPMA 263
Cdd:cd13585  157 FALRGGSGGQTQ--WYPFLWSNGGDLLDEdDGKATLNSPEAVEALQFYVDLYKdGVAPSSatTGGDEAVDLFASGKVAMM 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 264 IYSTYILPAVIKEGDPKNVGFVV----PTEKNSAVYGMlTSLTITAG-QKTEAAEKFVTFMEQADNIADWVMMSPGAALP 338
Cdd:cd13585  235 IDGPWALGTLKDSKVKFKWGVAPlpagPGGKRASVLGG-WGLAISKNsKHPEAAWKFIKFLTSKENQLKLGGAAGPAALA 313

                        330
                 ....*....|....*.
gi 446520088 339 VNKAVVTTATWKDNDV 354
Cdd:cd13585  314 AAAASAAAPDAKPALA 329
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 31-375 3.89e-47

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: 165.93  E-value: 3.89e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  31 IEFMHSSvEQERQAVISKLIARFEKENPGITVKQVPVEEDAYN-TKVITLSRSGSLPEVIETSHDYAKvmdkeQLIDRKA 109
Cdd:cd14748    2 ITFWHGM-SGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTlTKLLAALAAGTAPDVAQVDASWVA-----QLADSGA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 110 VA---TVIS--NVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGL---EEPKNWQQLLDVAQKLNDP 181
Cdd:cd14748   76 LEpldDYIDkdGVDDDDFYPAALDAG-TYDGKLY-GLPFDTSTPVLYYNKDLFEEAGLdpeKPPKTWDELEEAAKKLKDK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 182 ANK--KYGIALPTAEsvlTEQSFSQFALSNQANVFNAE-GKITLDTPEMMQALTYYRDLAANT-MPGSNDIMEVKDAFMN 257
Cdd:cd14748  154 GGKtgRYGFALPPGD---GGWTFQALLWQNGGDLLDEDgGKVTFNSPEGVEALEFLVDLVGKDgVSPLNDWGDAQDAFIS 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 258 GTAPMAIYSTYILPAVIKEGDPKNVGFV---VPTEKNSAVYGMLTSLTITAG--QKTEAAEKFVTFMEQADNIADWVMMs 332
Cdd:cd14748  231 GKVAMTINGTWSLAGIRDKGAGFEYGVAplpAGKGKKGATPAGGASLVIPKGssKKKEAAWEFIKFLTSPENQAKWAKA- 309

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 446520088 333 pGAALPVNKAVVttatwkdndvikalgELPNQLIGELPNIQVF 375
Cdd:cd14748  310 -TGYLPVRKSAA---------------EDPEEFLAENPNYKVA 336
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 30-364 2.66e-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: 145.22  E-value: 2.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  30 SIEFMHSSVEQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSH-----DYAKV------ 98
Cdd:cd14749    1 TITYWQYFTGDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPggwlaEFVKAglllpl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  99 --MDKEQLIDRKAVATVISNV-GEGAFYdgvlrivrtedgsawtGVPVSAWIGGIWYRKDVLAKAG-LEEPKNWQQLLDV 174
Cdd:cd14749   81 tdYLDPNGVDKRFLPGLADAVtFNGKVY----------------GIPFAARALALFYNKDLFEEAGgVKPPKTWDELIEA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 175 AQKLNDPANKKYGIALPTAESvlTEQSFSQFALSNQANVF---NAEGKITLDTPEMMQALTYYRDL----AANTMPGSND 247
Cdd:cd14749  145 AKKDKFKAKGQTGFGLLLGAQ--GGHWYFQYLVRQAGGGPlsdDGSGKATFNDPAFVQALQKLQDLvkagAFQEGFEGID 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 248 IMEVKDAFMNGTAPMAIYSTYILPAVIKEGDPKNVGFVVPTEKN-----SAVYGMLTSLTITA-GQKTEAAEKFVTFMEQ 321
Cdd:cd14749  223 YDDAGQAFAQGKAAMNIGGSWDLGAIKAGEPGGKIGVFPFPTVGkgaqtSTIGGSDWAIAISAnGKKKEAAVKFLKYLTS 302

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 446520088 322 ADNIADWVMMspGAALPVNKAVVTTATWKDNDVIKALGELPNQ 364
Cdd:cd14749  303 PEVMKQYLED--VGLLPAKEVVAKDEDPDPVAILGPFADVLNA 343
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
3-426 1.65e-35

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 135.46  E-value: 1.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088   3 KSKIVLLSALVSCALISGCKEENKTH---------VSIEFMHSsveQERQAVISKLIARFEKEnPGITVKQVPVEEDAYN 73
Cdd:COG2182    4 RLLAALALALALALALAACGSGSSSSgsssaagagGTLTVWVD---DDEAEALEEAAAAFEEE-PGIKVKVVEVPWDDLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  74 TKVITLSRSGSLPEVIETSHDYAkvmdkEQLIDRKAVATVISNVGEGA-FYDGVLRIVrTEDGSAWtGVPVSAWIGGIWY 152
Cdd:COG2182   80 EKLTTAAPAGKGPDVFVGAHDWL-----GELAEAGLLAPLDDDLADKDdFLPAALDAV-TYDGKLY-GVPYAVETLALYY 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 153 RKDVLAKaglEEPKNWQQLLDVAQKLNDPAnkKYGIALPTAESvlteQSFSQFALSNQANVFNAEG----KITLDTPEMM 228
Cdd:COG2182  153 NKDLVKA---EPPKTWDELIAAAKKLTAAG--KYGLAYDAGDA----YYFYPFLAAFGGYLFGKDGddpkDVGLNSPGAV 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 229 QALTYYRDLAAN-TMPGSNDIMEVKDAFMNGTAPMAIYSTYILPAvIKEGDPKNVGFV----VPTEKNSAVYGMLTSLTI 303
Cdd:COG2182  224 AALEYLKDLIKDgVLPADADYDAADALFAEGKAAMIINGPWAAAD-LKKALGIDYGVAplptLAGGKPAKPFVGVKGFGV 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 304 TAGQK-TEAAEKFVTFMEQADNIADWVMMSPgaALPVNKAVVTTATWKDNDVIKALGElpnqligelpniQVFGAVGDKN 382
Cdd:COG2182  303 SAYSKnKEAAQEFAEYLTSPEAQKALFEATG--RIPANKAAAEDAEVKADPLIAAFAE------------QAEYAVPMPN 368

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 446520088 383 FTRMGDVtgSGVVSSMVHNVTVGKADLPGTLQASQKKLDELIEQ 426
Cdd:COG2182  369 IPEMGAV--WTPLGTALQAIASGKADPAEALDAAQKQIEAAIAQ 410
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 33-360 7.73e-33

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: 127.43  E-value: 7.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  33 FMHSSVEQErqaVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHD----YAKVMDKEQLIDRk 108
Cdd:cd14747    6 AMGNSAEAE---LLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTwvaeFAAMGALEDLTPY- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 109 avatVISNVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGLEE-PKNWQQLLDVAQKLNDPANKKYG 187
Cdd:cd14747   82 ----LEDLGGDKDLFPGLVDTG-TVDGKYY-GVPWYADTRALFYRTDLLKKAGGDEaPKTWDELEAAAKKIKADGPDVSG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 188 IALPTAESVltEQSFSQFALSNQANVFN-AEGKITLDTPEMMQALTYYRDLAANTMPGSNDIMEVKD---AFMNGTAPMa 263
Cdd:cd14747  156 FAIPGKNDV--WHNALPFVWGAGGDLATkDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSADveqAFANGKVAM- 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 264 IYSTYILPAVIKEGDP---KNVGFVV---PTEKNSAVYGMLTSLTITAG-QKTEAAEKFVTFMEQADNIADWVMMSpgAA 336
Cdd:cd14747  233 IISGPWEIGAIREAGPdlaGKWGVAPlpgGPGGGSPSFAGGSNLAVFKGsKNKDLAWKFIEFLSSPENQAAYAKAT--GM 310

                        330       340
                 ....*....|....*....|....
gi 446520088 337 LPVNKAVVTTATWKDNDVIKALGE 360
Cdd:cd14747  311 LPANTSAWDDPSLANDPLLAVFAE 334
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 39-324 6.09e-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: 120.21  E-value: 6.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088   39 EQERQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLP-EVIETSHDYAKVMDKeqlidrKAVATVISNV 117
Cdd:pfam01547   3 SLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAK------AGLLLPLDDY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  118 GEGAFYDGVLRivrtedgsaWTGVPVSAWIGGIWYRKDVLAKAGLEEPKNWQQLLDVAQKLNDpANKKYGIALPTAESVL 197
Cdd:pfam01547  77 VANYLVLGVPK---------LYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKE-KGKSPGGAGGGDASGT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  198 TEQSFSQFALSNQANVFNAEGKiTLDTPEMMQALTYYRDLAA---------NTMPGSNDIMEVKDAFMNGTAPMAIYSTY 268
Cdd:pfam01547 147 LGYFTLALLASLGGPLFDKDGG-GLDNPEAVDAITYYVDLYAkvlllkklkNPGVAGADGREALALFEQGKAAMGIVGPW 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446520088  269 -----------ILPAVIKEGDPKNVG-FVVPTEKNSAVYGmlTSLTITAG-QKTEAAEKFVTFMEQADN 324
Cdd:pfam01547 226 aalaankvklkVAFAAPAPDPKGDVGyAPLPAGKGGKGGG--YGLAIPKGsKNKEAAKKFLDFLTSPEA 292
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 48-352 2.22e-26

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 107.49  E-value: 2.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088   48 KLIARFEKENpGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETS--HDYAKvmdkeQLIDRKAVATvISNVGEGAFYDG 125
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDLDVVWiaADQLA-----TLAEAGLLAD-LSDVDNLDDLPD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  126 VLRIVrTEDGsAWTGVPVSA-WIGGIWYRKDVLAKAGlEEPKNWQQLLDVAQKLNdpanKKYGIALPTAesvlteQSFSQ 204
Cdd:pfam13416  74 ALDAA-GYDG-KLYGVPYAAsTPTVLYYNKDLLKKAG-EDPKTWDELLAAAAKLK----GKTGLTDPAT------GWLLW 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  205 FALSNQANvFNAEGKITLDTPEmmqALTYYRDLAAN--TMPGSNDIMevkDAFMNGTAPMAIYSTYILPAVIKEGdpKNV 282
Cdd:pfam13416 141 ALLADGVD-LTDDGKGVEALDE---ALAYLKKLKDNgkVYNTGADAV---QLFANGEVAMTVNGTWAAAAAKKAG--KKL 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446520088  283 GFVVPteKNSAVYGMlTSLTITAGQKTE--AAEKFVTFMEQADNIADWVMMSPGaaLPVNKAVVTTATWKDN 352
Cdd:pfam13416 212 GAVVP--KDGSFLGG-KGLVVPAGAKDPrlAALDFIKFLTSPENQAALAEDTGY--IPANKSAALSDEVKAD 278
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 31-420 8.31e-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: 8.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  31 IEFMHSSVEQERQaVISKLIARFEKENPGITVK--QVPVEEDAYNTKVITLSRSGSLP------EVIETSHDYAKVMDKE 102
Cdd:cd14750    2 ITFAAGSDGQEGE-LLKKAIAAFEKKHPDIKVEieELPASSDDQRQQLVTALAAGSSApdvlglDVIWIPEFAEAGWLLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 103 QLIDRKAVatvisnvGEGAFYDGVLRiVRTEDGSAWtGVPVSAWIGGIWYRKDVLAKAGLEEPKNWQQLLDVAQKLNDPA 182
Cdd:cd14750   81 LTEYLKEE-------EDDDFLPATVE-ANTYDGKLY-ALPWFTDAGLLYYRKDLLEKYGPEPPKTWDELLEAAKKRKAGE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 183 NKKYGIALPTAE-SVLTeQSFSQFALSNQANVFNAE-GKITLDTPEMMQALTYYRDLAANTM--PGSNDIME--VKDAFM 256
Cdd:cd14750  152 PGIWGYVFQGKQyEGLV-CNFLELLWSNGGDIFDDDsGKVTVDSPEALEALQFLRDLIGEGIspKGVLTYGEeeARAAFQ 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 257 NGTAPMAIYSTYILPAVIKEGDP--KNVGFV-VPTEKNSAVYGML--TSLTITAG-QKTEAAEKFVTFMEQADNIADWVM 330
Cdd:cd14750  231 AGKAAFMRNWPYAYALLQGPESAvaGKVGVApLPAGPGGGSASTLggWNLAISANsKHKEAAWEFVKFLTSPEVQKRRAI 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 331 MspGAALPVNKAVVttatwKDNDVIKALGELPNQLIGEL-----PNIQVFGAVgdknftrmgdvtgSGVVSSMVHNVTVG 405
Cdd:cd14750  311 N--GGLPPTRRALY-----DDPEVLEAYPFLPALLEALEnavprPVTPKYPEV-------------STAIQIALSAALSG 370

                        410
                 ....*....|....*
gi 446520088 406 KADLPGTLQASQKKL 420
Cdd:cd14750  371 QATPEEALKQAQEKL 385
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 39-360 2.67e-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: 100.45  E-value: 2.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  39 EQERQAVISKLIARFEKENpGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHDYAKVMDKEQLIDRKAVATVISNVG 118
Cdd:cd13586    8 EDGELEYLKELAEEFEKKY-GIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLAVKIKN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 119 EGAFYDGVlrivrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAgleePKNWQQLLDVAQKLNDPANKKYGIALPTAESVLt 198
Cdd:cd13586   87 LPVALAAV-----TYNGKLY-GVPVSVETIALFYNKDLVPEP----PKTWEELIALAKKFNDKAGGKYGFAYDQTNPYF- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 199 eqsFSQFALSNQANVFNAEGK----ITLDTPEMMQALTYYRDL--AANTMPGSNDIMEVKDAFMNGTAPMAIYSTYILPA 272
Cdd:cd13586  156 ---SYPFLAAFGGYVFGENGGdptdIGLNNEGAVKGLKFIKDLkkKYKVLPPDLDYDIADALFKEGKAAMIINGPWDLAD 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 273 VIKEGDpkNVGfVVPTEKNSAVYGMLTSLTITA------GQKTEAAEKFVTFMeqADNIADWVMMSPGAALPVNKAVVTT 346
Cdd:cd13586  233 YKDAGI--NFG-VAPLPTLPGGKQAAPFVGVQGafvsaySKNKEAAVEFAEYL--TSDEAQLLLFEKTGRIPALKDALND 307

                        330
                 ....*....|....
gi 446520088 347 ATWKDNDVIKALGE 360
Cdd:cd13586  308 AAVKNDPLVKAFAE 321
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 30-357 2.58e-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: 94.75  E-value: 2.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  30 SIEFMHSSVEQErQAVISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSH----DYAKvMDKEQLI 105
Cdd:cd14751    1 TITFWHTSSDEE-KVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIawvpEFAK-LGYLQPL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 106 DRKAVATVIsnvgeGAFYDGVLRIVRTEdGSAWtGVPVSAWIGGIWYRKDVLAKAGLEEPKNWQQLLDVAQKlNDPANKK 185
Cdd:cd14751   79 DGTPAFDDI-----VDYLPGPMETNRYN-GHYY-GVPQVTNTLALFYNKRLLEEAGTEVPKTMDELVAAAKA-IKKKKGR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 186 YGIALptaeSVLTEQSFSQFALSNQANVFNAEGK-ITLDTPEMMQALTYYRDL-----AANTMPGSNDIMevKDAFMNGT 259
Cdd:cd14751  151 YGLYI----SGDGPYWLLPFLWSFGGDLTDEKKAtGYLNSPESVRALETIVDLydegaITPCASGGYPNM--QDGFKSGR 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 260 APMAI---YSTYILPAVIKEGDPKNVGF----VVPTEKNSAVYGmlTSLTITAGQK-TEAAEKFVTFMEQADNIAdwVMM 331
Cdd:cd14751  225 YAMIVngpWAYADILGGKEFKDPDNLGIapvpAGPGGSGSPVGG--EDLVIFKGSKnKDAAWKFVKFMSSAEAQA--LTA 300

                        330       340
                 ....*....|....*....|....*.
gi 446520088 332 SPGAALPVNKAVVTTATWKDNDVIKA 357
Cdd:cd14751  301 AKLGLLPTRTSAYESPEVANNPMVAA 326
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 30-360 1.64e-20

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: 92.44  E-value: 1.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  30 SIEFMHSSVEQERQAvISKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHDYAKVMDKEQLIDrkA 109
Cdd:cd13657    1 TITIWHALTGAEEDA-LQQIIDEFEAKYPVPNVKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLV--P 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 110 VATVISNVGEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAgleePKNWQQLLDVAQKLNDPANKKYGIA 189
Cdd:cd13657   78 ISDYLSEDDFENYLPTAVEAV-TYKGKVY-GLPEAYETVALIYNKALVDQP----PETTDELLAIMKDHTDPAAGSYGLA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 190 LPtaesVLTEQSFSQFALSNQANVFNAEG-KITLDTPEMMQALTYYRDLAANTMPGSNDIMEVKDAFMNGTAPMAIYSTY 268
Cdd:cd13657  152 YQ----VSDAYFVSAWIFGFGGYYFDDETdKPGLDTPETIKGIQFLKDFSWPYMPSDPSYNTQTSLFNEGKAAMIINGPW 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 269 ILPAVIKEGDpkNVGfVVPTEKNSAVYGM-------LTSLTITAGQKT-EAAEKFVTFMEQADNIAdwVMMSPGAALPVN 340
Cdd:cd13657  228 FIGGIKAAGI--DLG-VAPLPTVDGTNPPrpysgveGIYVTKYAERKNkEAALDFAKFFTTAEASK--ILADENGYVPAA 302

                        330       340
                 ....*....|....*....|
gi 446520088 341 KAVVTTATWKDNDVIKALGE 360
Cdd:cd13657  303 TNAYDDAEVAADPVIAAFKA 322
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 31-343 6.81e-16

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: 78.61  E-value: 6.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  31 IEFMHSSVEQERQAViSKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHDYAKVMdkeqlidrkAV 110
Cdd:cd13522    2 ITVWHQYDTGENQAV-NELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPF---------AA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 111 ATVISNVGEG---------AFYDGVlrivrTEDGSAWtGVPVSAWIGGIWYRKDVLAKaglEEPKNWQQLLDVAQKLNDP 181
Cdd:cd13522   72 AGLLAPLDEYvsksgkyapNTIAAM-----KLNGKLY-GVPVSVGAHLMYYNKKLVPK---NPPKTWQELIALAQGLKAK 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 182 AnkKYGIALPTAESVLteqsFSQFALSNQANVFNAEG---KITLDTPEMMQALTYYRDL--AANTMPGSNDIMEVKDAFM 256
Cdd:cd13522  143 N--VWGLVYNQNEPYF----FAAWIGGFGGQVFKANNgknNPTLDTPGAVEALQFLVDLksKYKIMPPETDYSIADALFK 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 257 NGTAPMAIYSTYILpAVIKEGDPKNVGF----VVPTEKNSAVY-GMLTSLTITAGQKTEAAEKFVTFMEQADNIADWVMM 331
Cdd:cd13522  217 AGKAAMIINGPWDL-GDYRQALKINLGVaplpTFSGTKHAAPFvGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDD 295

                        330
                 ....*....|..
gi 446520088 332 SPGaaLPVNKAV 343
Cdd:cd13522  296 AGD--IPANLQA 305
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-343 9.81e-12

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 65.70  E-value: 9.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088   1 MIKSKIVLLSALVSCALISGCkeenkthvsiefmHSSVEQERQAVIS--------KLIARFEKENpGITVKQVPVE--ED 70
Cdd:COG0687    1 MSRRSLLGLAAAALAAALAGG-------------APAAAAEGTLNVYnwggyidpDVLEPFEKET-GIKVVYDTYDsnEE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  71 AYnTKVITlsrSGSLPEVIETSHDYAKVMDKEQL---IDRKAvatvISNVgegAFYDGVLRIVRTEDGSAWtGVPVSAWI 147
Cdd:COG0687   67 ML-AKLRA---GGSGYDVVVPSDYFVARLIKAGLlqpLDKSK----LPNL---ANLDPRFKDPPFDPGNVY-GVPYTWGT 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 148 GGIWYRKDVLAkaglEEPKNWQQLLDvaqklndPANK-KYGIaLPTAESVLTeqsfsqFALsnqanvfNAEGK--ITLDT 224
Cdd:COG0687  135 TGIAYNTDKVK----EPPTSWADLWD-------PEYKgKVAL-LDDPREVLG------AAL-------LYLGYdpNSTDP 189

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 225 PEMMQALTYYRDLAANTMPGSNDIMEVKDAFMNGTAPMAIYSTYILPAVIKEGDPknVGFVVPTEKnsaVYGMLTSLTIT 304
Cdd:COG0687  190 ADLDAAFELLIELKPNVRAFWSDGAEYIQLLASGEVDLAVGWSGDALALRAEGPP--IAYVIPKEG---ALLWFDNMAIP 264

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 446520088 305 AG-QKTEAAEKFVTFMEQADNIADWVMMSPGAalPVNKAV 343
Cdd:COG0687  265 KGaPNPDLAYAFINFMLSPEVAAALAEYVGYA--PPNKAA 302
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 28-280 2.04e-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: 65.43  E-value: 2.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  28 HVSIEFMHSSVEQERQAVISKLIArfEKENPGITVKQVPVeeDAYNTKVITLSRSGSLPEVI-----ETSHDYAK---VM 99
Cdd:cd13580    6 TIVANLGGNPKPDPDDNPYTKYLE--EKTNIDVKVKWVPD--SSYDEKLNLALASGDLPDIVvvndpQLSITLVKqgaLW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 100 DKEQLIDRKA--VATVISNVGEGAF-YDGVLrivrtedgsawTGVPVSAWIG---GIWYRKDVLAKAGLEEPKNWQQLLD 173
Cdd:cd13580   82 DLTDYLDKYYpnLKKIIEQEGWDSAsVDGKI-----------YGIPRKRPLIgrnGLWIRKDWLDKLGLEVPKTLDELYE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 174 VAQ--KLNDP----ANKKYGIALPtaeSVLTEQSFSQFALS----NQANVFNAEGKITLD--TPEMMQALTYYRDLAAN- 240
Cdd:cd13580  151 VAKafTEKDPdgngKKDTYGLTDT---KDLIGSGFTGLFGAfgapPNNWWKDEDGKLVPGsiQPEMKEALKFLKKLYKEg 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 446520088 241 -------TMPGSNdimeVKDAFMNGTAPM---AIYSTYILPAVIKEGDPK 280
Cdd:cd13580  228 lidpefaVNDGTK----ANEKFISGKAGIfvgNWWDPAWPQASLKKNDPD 273
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 131-359 6.12e-08

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 53.79  E-value: 6.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 131 RTEDGsAWTGVpvSAWIGGIWYRKDVLAKAGLeePKNWQQLLdvaqklnDPANK-KYGIALPTAEsvlteqSFSQFALSN 209
Cdd:COG1840   72 RDPDG-YWFGF--SVRARVIVYNTDLLKELGV--PKSWEDLL-------DPEYKgKIAMADPSSS------GTGYLLVAA 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 210 QANVFNAEgkitldtpemmQALTYYRDLAANT---MPGSNDIMevkDAFMNGTAPMAIYSTYILPAVIKEGDPknVGFVV 286
Cdd:COG1840  134 LLQAFGEE-----------KGWEWLKGLAANGarvTGSSSAVA---KAVASGEVAIGIVNSYYALRAKAKGAP--VEVVF 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446520088 287 PTEKNSA-VYGMLtsltITAG-QKTEAAEKFVTFM--EQADNIadwvMMSPGAALPVNKAVVTTATWKDNDVIKALG 359
Cdd:COG1840  198 PEDGTLVnPSGAA----ILKGaPNPEAAKLFIDFLlsDEGQEL----LAEEGYEYPVRPDVEPPEGLPPLGELKLID 266
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 39-378 9.28e-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: 50.56  E-value: 9.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  39 EQERQAVISKLIARFEKENpGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHD-YAKVMDKEQLIDRKavatvISNV 117
Cdd:cd13658    8 EDKKMAFIKKIAKQYTKKT-GVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDrIGSAVLQGLLSPIK-----LSKD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 118 GEGAFYDGVLRIVrTEDGSAWtGVPVSAWIGGIWYRKDVLAKAgleePKNWQQLLDVAQKLNDPANKKYGIaLPTAesvl 197
Cdd:cd13658   82 KKKGFTDQALKAL-TYDGKLY-GLPAAVETLALYYNKDLVKNA----PKTFDELEALAKDLTKEKGKQYGF-LADA---- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 198 TEQSFSQFALS-NQANVFNAEGK------ITLDTPEMMQALTYYRDLAANT-MPGSNDIMEVKDAFMNGTAPMAIYSTYI 269
Cdd:cd13658  151 TNFYYSYGLLAgNGGYIFKKNGSdldindIGLNSPGAVKAVKFLKKWYTEGyLPKGMTGDVIQGLFKEGKAAAVIDGPWA 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 270 LPAVIKEGdpKNVGFV-VPTEKNS-------AVYGMLTSltiTAGQKTEAAEKFVTFMEQADNIAD-WVMMSpgaALPVN 340
Cdd:cd13658  231 IQEYQEAG--VNYGVApLPTLPNGkpmapflGVKGWYLS---AYSKHKEWAQKFMEFLTSKENLKKrYDETN---EIPPR 302

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 446520088 341 KAVVTTATWKDNDVIKALGELPNQLIgELPNIQVFGAV 378
Cdd:cd13658  303 KDVRSDPEIKNNPLTSAFAKQASRAV-PMPNIPEMGAV 339
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
31-342 1.03e-04

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 44.41  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  31 IEFMHSsVEQERQAVISKLIARFEKENPgiTVKQVPVEEDAYNTKV---ITLSRSGSLPEVIETSHDYAKVMDKEQLIdr 107
Cdd:PRK10974  28 IPFWHS-MEGELGKEVDSLAQRFNASQP--DYKIVPVYKGNYEQSLaagIAAFRSGNAPAILQVYEVGTATMMASKAI-- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 108 KAVATVISNVG----EGAFYDGVLRIVRTEDGSAWTGVPVSAWIGGIWYRKDVLAKAGL---EEPKNWQQLLDVAQKLnd 180
Cdd:PRK10974 103 KPVYDVFKDAGipfdESQFVPTVAGYYSDAKTGHLLSQPFNSSTPVLYYNKDAFKKAGLdpeQPPKTWQDLAAYAAKL-- 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 181 panKKYGIALPTA---ESVLTEQSFSQF---ALSNQANVFN-AEGKITLDTPEMMQALTYYRDLAAN---TMPGSNDimE 250
Cdd:PRK10974 181 ---RAAGMKCGYAsgwQGWIQLENFSAWhglPFASKNNGFDgTDAVLEFNKPEQVKHIALLEEMNKKgdfTYVGRKD--E 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 251 VKDAFMNGTAPMAIYSTYILpAVIKEGDPKN--VGFV-----VPTEKNSAVYGMlTSLTITAGQKTE---AAEKFVTFME 320
Cdd:PRK10974 256 STEKFYNGDCAITTASSGSL-ANIRKYAKFNygVGMMpydadVKGAPQNAIIGG-ASLWVMQGKDKEtykGVAKFLDFLA 333

                        330       340
                 ....*....|....*....|..
gi 446520088 321 QADNIADWVMMSpgAALPVNKA 342
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 ...
 47-282 1.31e-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: 43.88  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  47 SKLIARFEKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIE-TSHDYAKVMDKE-QLID-----------RKAVatv 113
Cdd:cd13583   19 DWLIWKEIEEKTNVKFKRTPIPSSDYETKRSLLIASGDAPDIIPvLYPGEENEFVASgALLPisdyldympnyKKYV--- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 114 iSNVGEGAFYDgvlrIVRTEDGS--AWTGVPVSAWIGGIW-YRKDVLAKAGLEEPKNWQQLLDVAQKLNDpankKYGIAL 190
Cdd:cd13583   96 -EKWGLGKELA----TGRQSDGKyySLPGLHEDPGVQYSFlYRKDIFEKAGIKIPTTWDEFYAALKKLKE----KYPDSY 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 191 PTAESVLTEQSFSQFALSNQANVFNAEGKITLD-----------TPEMMQALTYYRDLAAN------TMPGSNDImeVKD 253
Cdd:cd13583  167 PYSDRWNSNALLLIAAPAFGTTAGWGFSNYTYDpdtdkfvygatTDEYKDMLQYFNKLYAEglldpeSFTQTDDQ--AKA 244

                        250       260       270
                 ....*....|....*....|....*....|....
gi 446520088 254 AFMNG-----TAPMAIYSTYILPAVIKEGDPKNV 282
Cdd:cd13583  245 KFLNGksfviTTNPQTVDELQRNLRAADGGNYEV 278
PBP2_Fbp_like_1 cd13544
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ...
 131-173 3.56e-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: 3.56e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446520088 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 1.06e-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: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088  33 FMHSSVEQERQAVISKLiarfeKENPGITVKQVPVEEDAYNTKVITLSRSGSLPEVIETSHDYAKVM---------DKEQ 103
Cdd:cd13521   10 FNDNWVDDENWPVAKEI-----EKLTNVKLEIVAVTAATSQQKLNLMLASGDLPDIVGADYLKDKFIaygmegaflPLSK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 104 LIDRkavatvISNVGE--GAFYDGVLRIvRTEDGSAW---TGVPVSAWIGGIWYRKDVLAKAGLEEPKNWQQLLDVAQKL 178
Cdd:cd13521   85 YIDQ------YPNLKAffKQHPDVLRAS-TASDGKIYlipYEPPKDVPNQGYFIRKDWLDKLNLKTPKTLDELYNVLKAF 157


                 ....*....
gi 446520088 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 ...
 229-319 2.27e-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: 39.59  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 229 QALTYYRDLAANTMPGSNDIMEVKDAFMNGTAPMAI-YSTYILPAVIKEGDPKNVGFVVPTEKNSAVYGMltslTITAGQ 307
Cdd:cd13545  161 GYLEYWKKLKANGVTVTPGWSEAYGLFTTGEAPMVVsYATSPAYHVYYEKDLRYTAVIFPEGHYRQVEGA----GILKGA 236

                         90
                 ....*....|...
gi 446520088 308 K-TEAAEKFVTFM 319
Cdd:cd13545  237 KnPELAKKFVDFL 249
PBP2_Fbp_like_2 cd13547
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 124-319 5.14e-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: 38.36  E-value: 5.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 124 DGVLRIVRTEDGSaWTGVPVSAwiGGIWYRKDvlaKAGLEEPKNWQQLLDvaqklndpANKKYGIALPTAesvlteqSFS 203
Cdd:cd13547   83 DAIPAPFYDKDGY-YYGTRLSA--MGIAYNTD---KVPEEAPKSWADLTK--------PKYKGQIVMPDP-------LYS 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520088 204 QFALSNQANVFNAEGkitldtpemmQALTYYRDLAAN--TMPGSNDimEVKDAFMNGTAPMAIYSTYILPAVIKEGDPkn 281
Cdd:cd13547  142 GAALDLVAALADKYG----------LGWEYFEKLKENgvKVEGGNG--QVLDAVASGERPAGVGVDYNALRAKEKGSP-- 207

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446520088 282 VGFVVPTEKNSAVygmlTS-LTITAGQK-TEAAEKFVTFM 319
Cdd:cd13547  208 LEVIYPEEGTVVI----PSpIAILKGSKnPEAAKAFVDFL 243
 
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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