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Conserved domains on  [gi|491605907|ref|WP_005463467|]
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MULTISPECIES: autoinducer 2-binding periplasmic protein LuxP [Vibrio]

Protein Classification

autoinducer 2-binding periplasmic protein LuxP( domain architecture ID 10156851)

autoinducer 2-binding periplasmic protein LuxP binds to the signaling molecule autoinducer 2 (AI-2), a furanosyl borate diester, (3a-methyl-5,6-dihydrofuro-[2,3d][1,3,2]dioxaborole-2,2,6, 6a-tetraol)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP1_LuxPQ_Quorum_Sensing cd06303
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ...
 40-358 0e+00

periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs; Periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs from other bacteria. The members of this group are highly homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea, and that are members of the type 1 periplasmic binding protein superfamily. The Vibrio harveyi AI-2 receptor consists of two polypeptides, LuxP and LuxQ: LuxP is a periplasmic binding protein that binds AI-2 by clamping it between two domains, LuxQ is an integral membrane protein belonging to the two-component sensor kinase family. Unlike AI-2 bound to the LsrB receptor in Salmonella typhimurium, the Vibrio harveyi AI-2 signaling molecule has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LuxPQ to control light production as well as its motility behavior.


:

Pssm-ID: 380526 [Multi-domain]  Cd Length: 320  Bit Score: 506.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907  40 EQKHLTDALAAAVRDDPVPIAPEKRHPLKISVVYPGQQISDYWIRNIDAFEKRLDKLNIDYQINQVFTRPNADIKQQSLS 119
Cdd:cd06303    1 EQRQLTEDFSERVRAPPVPAEVTQKRPVKIAVVYPGLQVSDYWRRSIVSFRKRLDELGIKYQLDEFFTRPGAEIRLQALQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 120 LMEALKSNSDYLIFTLDTTRHRKFVEHVLDSTKTKLILQNITTPVREWETRQPFMYVGFDHAEGSRELAVEFGKQFPKNT 199
Cdd:cd06303   81 IREMLKSDPDYLIFTLDALRHRRFVEILLDSGKPKLILQNITTPLRDWDNHQPLLYVGFDHAEGSRMLAKHFIKIFPEEG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 200 HYSVLYFSEGYISDIRGNTFIHQVNQDSQFELQSAYYTKATKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSEL 279
Cdd:cd06303  161 KYAILYLTEGYVSDQRGDTFIDEVARHSNLELVSAYYTDFDRESAREAARALLARHPDLDFIYACSTDIALGAIDALQEL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 280 GRE-DVMINGWGGGSAELDAILKGELDITVMRMNDDTGIAMAEAIKWDLEGKPVPTVYSGDFEVVTKSDSPERIEALRKR 358
Cdd:cd06303  241 GREtDIMINGWGGGSAELDALQKGGLDVTVMRMNDDNGIAMAEAIKLDLEGREVPTVYAGDFELVTKGDSPERIEALKKR 320
 
Name Accession Description Interval E-value
PBP1_LuxPQ_Quorum_Sensing cd06303
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ...
 40-358 0e+00

periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs; Periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs from other bacteria. The members of this group are highly homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea, and that are members of the type 1 periplasmic binding protein superfamily. The Vibrio harveyi AI-2 receptor consists of two polypeptides, LuxP and LuxQ: LuxP is a periplasmic binding protein that binds AI-2 by clamping it between two domains, LuxQ is an integral membrane protein belonging to the two-component sensor kinase family. Unlike AI-2 bound to the LsrB receptor in Salmonella typhimurium, the Vibrio harveyi AI-2 signaling molecule has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LuxPQ to control light production as well as its motility behavior.


Pssm-ID: 380526 [Multi-domain]  Cd Length: 320  Bit Score: 506.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907  40 EQKHLTDALAAAVRDDPVPIAPEKRHPLKISVVYPGQQISDYWIRNIDAFEKRLDKLNIDYQINQVFTRPNADIKQQSLS 119
Cdd:cd06303    1 EQRQLTEDFSERVRAPPVPAEVTQKRPVKIAVVYPGLQVSDYWRRSIVSFRKRLDELGIKYQLDEFFTRPGAEIRLQALQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 120 LMEALKSNSDYLIFTLDTTRHRKFVEHVLDSTKTKLILQNITTPVREWETRQPFMYVGFDHAEGSRELAVEFGKQFPKNT 199
Cdd:cd06303   81 IREMLKSDPDYLIFTLDALRHRRFVEILLDSGKPKLILQNITTPLRDWDNHQPLLYVGFDHAEGSRMLAKHFIKIFPEEG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 200 HYSVLYFSEGYISDIRGNTFIHQVNQDSQFELQSAYYTKATKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSEL 279
Cdd:cd06303  161 KYAILYLTEGYVSDQRGDTFIDEVARHSNLELVSAYYTDFDRESAREAARALLARHPDLDFIYACSTDIALGAIDALQEL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 280 GRE-DVMINGWGGGSAELDAILKGELDITVMRMNDDTGIAMAEAIKWDLEGKPVPTVYSGDFEVVTKSDSPERIEALRKR 358
Cdd:cd06303  241 GREtDIMINGWGGGSAELDALQKGGLDVTVMRMNDDNGIAMAEAIKLDLEGREVPTVYAGDFELVTKGDSPERIEALKKR 320
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 44-347 6.27e-32

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


Pssm-ID: 441483 [Multi-domain]  Cd Length: 307  Bit Score: 121.96  E-value: 6.27e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907  44 LTDALAAAVRDDPVPIAPEKRhPLKISVVYPGQQiSDYWIRNIDAFEKRLDKLNIDYQinqvFTRPNADIKQQSLSLMEA 123
Cdd:COG1879   12 LALALAACGSAAAEAAAAAAK-GKTIGFVVKTLG-NPFFVAVRKGAEAAAKELGVELI----VVDAEGDAAKQISQIEDL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 124 LKSNSDYLIFT-LDTTRHRKFVEHVLDStKTKLILQNITTPvreweTRQPFMYVGFDHAEGSRELAVEFGKQFPKNTHYS 202
Cdd:COG1879   86 IAQGVDAIIVSpVDPDALAPALKKAKAA-GIPVVTVDSDVD-----GSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 203 VLYFSEGYISDI-RGNTFIHQVNQDSQFELQSAYYTKATKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGR 281
Cdd:COG1879  160 ILTGSPGAPAANeRTDGFKEALKEYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGR 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491605907 282 E-DVMINGWGGGSAELDAILKGELDITVMRMNDDTG-IAMAEAIKWdLEGKPVPTVYSGDFEVVTKSD 347
Cdd:COG1879  240 KgDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGyLAVDAALKL-LKGKEVPKEILTPPVLVTKEN 306
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 69-331 5.20e-10

Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433182 [Multi-domain]  Cd Length: 259  Bit Score: 59.25  E-value: 5.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907   69 ISVVYPGQQIsDYWIRNIDAFEKRLDKLNIDYQinqVFTRPNADIKQQSLSLMEALKSNSDYLIFTLDttrHRKFVEHVL 148
Cdd:pfam13407   1 IGVVPKSTGN-PFFQAAEEGAEEAAKELGGEVI---VVGPAEADAAEQVAQIEDAIAQGVDAIIVAPV---DPTALAPVL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907  149 DstktKLILQNIttPV----REWETRQPFMYVGFDHAEGSRELAVEFGKQFPKNTHYSVLYFSEGYISDIRGNTFIHQVN 224
Cdd:pfam13407  74 K----KAKDAGI--PVvtfdSDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907  225 QDSQFELQ---SAYYTKATKQSGYEAAKASLKKYPD-VEFIYACSTDVALGAVEALSELGR-EDVMINGWGGGSAELDAI 299
Cdd:pfam13407 148 KEKYPGIKvvaEVEGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLaGKVVVTGFDATPEALEAI 227

                         250       260       270
                  ....*....|....*....|....*....|..
gi 491605907  300 LKGELDITVMRMNDDTGIAMAEAIKWDLEGKP 331
Cdd:pfam13407 228 KDGTIDATVLQDPYGQGYAAVELAAALLKGKK 259
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
252-345 1.82e-07

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 52.01  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 252 LKKYPDVEFIYACSTDVALGAVEALSELGREDVMINGWGGGSAELDAILKGELDITVMRMNDDTGIAMAEAIKWDLEGKP 331
Cdd:PRK10653 202 LTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGIKAVNRGKLAATIAQQPDQIGAIGVETADKVLKGEK 281

                         90
                 ....*....|....
gi 491605907 332 VPTVYSGDFEVVTK 345
Cdd:PRK10653 282 VEAKIPVDLKLVTK 295
 
Name Accession Description Interval E-value
PBP1_LuxPQ_Quorum_Sensing cd06303
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ...
 40-358 0e+00

periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs; Periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs from other bacteria. The members of this group are highly homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea, and that are members of the type 1 periplasmic binding protein superfamily. The Vibrio harveyi AI-2 receptor consists of two polypeptides, LuxP and LuxQ: LuxP is a periplasmic binding protein that binds AI-2 by clamping it between two domains, LuxQ is an integral membrane protein belonging to the two-component sensor kinase family. Unlike AI-2 bound to the LsrB receptor in Salmonella typhimurium, the Vibrio harveyi AI-2 signaling molecule has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LuxPQ to control light production as well as its motility behavior.


Pssm-ID: 380526 [Multi-domain]  Cd Length: 320  Bit Score: 506.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907  40 EQKHLTDALAAAVRDDPVPIAPEKRHPLKISVVYPGQQISDYWIRNIDAFEKRLDKLNIDYQINQVFTRPNADIKQQSLS 119
Cdd:cd06303    1 EQRQLTEDFSERVRAPPVPAEVTQKRPVKIAVVYPGLQVSDYWRRSIVSFRKRLDELGIKYQLDEFFTRPGAEIRLQALQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 120 LMEALKSNSDYLIFTLDTTRHRKFVEHVLDSTKTKLILQNITTPVREWETRQPFMYVGFDHAEGSRELAVEFGKQFPKNT 199
Cdd:cd06303   81 IREMLKSDPDYLIFTLDALRHRRFVEILLDSGKPKLILQNITTPLRDWDNHQPLLYVGFDHAEGSRMLAKHFIKIFPEEG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 200 HYSVLYFSEGYISDIRGNTFIHQVNQDSQFELQSAYYTKATKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSEL 279
Cdd:cd06303  161 KYAILYLTEGYVSDQRGDTFIDEVARHSNLELVSAYYTDFDRESAREAARALLARHPDLDFIYACSTDIALGAIDALQEL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 280 GRE-DVMINGWGGGSAELDAILKGELDITVMRMNDDTGIAMAEAIKWDLEGKPVPTVYSGDFEVVTKSDSPERIEALRKR 358
Cdd:cd06303  241 GREtDIMINGWGGGSAELDALQKGGLDVTVMRMNDDNGIAMAEAIKLDLEGREVPTVYAGDFELVTKGDSPERIEALKKR 320
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
 68-342 1.50e-34

periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.


Pssm-ID: 380478 [Multi-domain]  Cd Length: 268  Bit Score: 128.07  E-value: 1.50e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907  68 KISVVYPGQQiSDYWIRNIDAFEKRLDKLNIDYQINQvftrPNADIKQQsLSLME-ALKSNSDYLIFT-LDTTRHRKFVE 145
Cdd:cd01536    1 KIGVVVKDLT-NPFWVAVKKGAEAAAKELGVELVVLD----AQGDVAKQ-ISQIEdLIAQGVDAIIIApVDSEALVPAVK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 146 HVLDStKTKLILQNITTPVREwetrQPFMYVGFDHAEGSRELAVEFGKQFPKNTHYSVLYFSEG-YISDIRGNTFIHQVN 224
Cdd:cd01536   75 KANAA-GIPVVAVDTDIDGGG----DVVAFVGTDNYEAGKLAGEYLAEALGGKGKVAILEGPPGsSTAIDRTKGFKEALK 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 225 QDSQFELQSAYYTKATKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGR-EDVMINGWGGGSAELDAILKGE 303
Cdd:cd01536  150 KYPDIEIVAEQPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRtGDIKIVGVDGTPEALKAIKDGE 229

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 491605907 304 LDITVMRMNDDTGIAMAEAIKWDLEGKPVPTVYSGDFEV 342
Cdd:cd01536  230 LDATVAQDPYLQGYLAVEAAVKLLNGEKVPKEILTPVTL 268
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 44-347 6.27e-32

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


Pssm-ID: 441483 [Multi-domain]  Cd Length: 307  Bit Score: 121.96  E-value: 6.27e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907  44 LTDALAAAVRDDPVPIAPEKRhPLKISVVYPGQQiSDYWIRNIDAFEKRLDKLNIDYQinqvFTRPNADIKQQSLSLMEA 123
Cdd:COG1879   12 LALALAACGSAAAEAAAAAAK-GKTIGFVVKTLG-NPFFVAVRKGAEAAAKELGVELI----VVDAEGDAAKQISQIEDL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 124 LKSNSDYLIFT-LDTTRHRKFVEHVLDStKTKLILQNITTPvreweTRQPFMYVGFDHAEGSRELAVEFGKQFPKNTHYS 202
Cdd:COG1879   86 IAQGVDAIIVSpVDPDALAPALKKAKAA-GIPVVTVDSDVD-----GSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 203 VLYFSEGYISDI-RGNTFIHQVNQDSQFELQSAYYTKATKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGR 281
Cdd:COG1879  160 ILTGSPGAPAANeRTDGFKEALKEYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGR 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491605907 282 E-DVMINGWGGGSAELDAILKGELDITVMRMNDDTG-IAMAEAIKWdLEGKPVPTVYSGDFEVVTKSD 347
Cdd:COG1879  240 KgDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGyLAVDAALKL-LKGKEVPKEILTPPVLVTKEN 306
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
 68-354 2.51e-16

periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally.


Pssm-ID: 380532 [Multi-domain]  Cd Length: 285  Bit Score: 78.41  E-value: 2.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907  68 KISVVYPGQQiSDYWIRNIDAFEKRLDKLNIDYqinqVFTRPNADIKQQSLSLMEALKSNSDYLIFT-LDTTRhrkfVEH 146
Cdd:cd06309    1 TVGFSQAGSE-SPWRVANTKSIKEAAKKRGYEL----VYTDANQDQEKQINDIRDLIAQGVDAILISpIDATG----WDP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 147 VLDSTKTK---LILQNITTPVR---EWETrqpfmYVGFDH-AEGsrELAVEF-GKQF-PKNTHYSVLYFSEG-YISDIRG 216
Cdd:cd06309   72 VLKEAKDAgipVILVDRTIDGEdgsLYVT-----FIGSDFvEEG--RRAAEWlVKNYkGGKGNVVELQGTAGsSVAIDRS 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 217 NTFIHQVNQDSQFEL---QSAYYTKATkqsGYEAAKASLKKYP-DVEFIYACSTDVALGAVEALSELGR---EDVMINGW 289
Cdd:cd06309  145 KGFREVIKKHPNIKIvasQSGNFTREK---GQKVMENLLQAGPgDIDVIYAHNDDMALGAIQALKEAGLkpgKDVLVVGI 221

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491605907 290 GGGSAELDAILKGELDITVmRMNDDTGIAMAEAIKWDLEGKPVPTVYSGDFEVVTKSDSPERIEA 354
Cdd:cd06309  222 DGQKDALEAIKAGELNATV-ECNPLFGPTAFDTIAKLLAGEKVPKLIIVEERLFDKDNAAEELEP 285
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
 79-346 1.49e-13

periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis; Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding.


Pssm-ID: 380543 [Multi-domain]  Cd Length: 283  Bit Score: 69.98  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907  79 SDYWIRNIDAFEKRLDKLNIDYQinqVFTRPNADIKQQSLSLMEAL--KSNSDYLIFTLDTTrhrKFVEHVLDSTKTKLI 156
Cdd:cd06320   11 NPFWVAMKDGIEAEAKKLGVKVD---VQAAPSETDTQGQLNLLETMlnKGYDAILVSPISDT---NLIPPIEKANKKGIP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 157 LQNITTPVREWETRQPFM----YVGFDHAEGSRELAVEFGKQFPKNTHYSVLyfsEG----YISDIRGNTFIHQVNQDSQ 228
Cdd:cd06320   85 VINLDDAVDADALKKAGGkvtsFIGTDNVAAGALAAEYIAEKLPGGGKVAII---EGlpgnAAAEARTKGFKETFKKAPG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 229 FEL---QSAYY--TKAtkqsgYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGRE-DVMINGWGGGSAELDAILKG 302
Cdd:cd06320  162 LKLvasQPADWdrTKA-----LDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKTgKVLVVGTDGIPEAKKSIKAG 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 491605907 303 ELDITVMRMNDDTGIAMAEAIKWDLEGKPVPTVYSGDFEVVTKS 346
Cdd:cd06320  237 ELTATVAQYPYLEGAMAVEAALRLLQGQKVPAVVATPQALITKD 280
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 68-308 3.95e-12

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380547 [Multi-domain]  Cd Length: 317  Bit Score: 66.47  E-value: 3.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907  68 KISVVYPGQQISDYWIRNIDAFEKRLDKLNIDYQinqVFTRPNADIKQQSLsLMEALKSNS--DYLIFTLDTTRHRKFVE 145
Cdd:cd06324    1 RVVFINPGKEDEPFWQNVTRFMQAAAKDLGIELE---VLYANRNRFKMLEL-AEELLARPPkpDYLILVNEKGVAPELLE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 146 hVLDSTKTKLILQNITTPVREWET----RQPFMY----VGFDHAEGSRELA---VEFGKQFPKNTHYSVLYFS---EGYI 211
Cdd:cd06324   77 -LAEQAKIPVFLINNDLTDEERALlgkpREKFKYwlgsIVPDNEQAGYLLAkalIKAARKKSDDGKIRVLAISgdkSTPA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 212 SDIRGNTFIHQVNQDSQFELQSAYYTKATKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGR---EDVMING 288
Cdd:cd06324  156 SILREQGLRDALAEHPDVTLLQIVYANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLkpgKDVLVGG 235

                        250       260
                 ....*....|....*....|
gi 491605907 289 WGGGSAELDAILKGELDITV 308
Cdd:cd06324  236 IDWSPEALQAVKDGELTASV 255
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 69-331 5.20e-10

Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433182 [Multi-domain]  Cd Length: 259  Bit Score: 59.25  E-value: 5.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907   69 ISVVYPGQQIsDYWIRNIDAFEKRLDKLNIDYQinqVFTRPNADIKQQSLSLMEALKSNSDYLIFTLDttrHRKFVEHVL 148
Cdd:pfam13407   1 IGVVPKSTGN-PFFQAAEEGAEEAAKELGGEVI---VVGPAEADAAEQVAQIEDAIAQGVDAIIVAPV---DPTALAPVL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907  149 DstktKLILQNIttPV----REWETRQPFMYVGFDHAEGSRELAVEFGKQFPKNTHYSVLYFSEGYISDIRGNTFIHQVN 224
Cdd:pfam13407  74 K----KAKDAGI--PVvtfdSDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907  225 QDSQFELQ---SAYYTKATKQSGYEAAKASLKKYPD-VEFIYACSTDVALGAVEALSELGR-EDVMINGWGGGSAELDAI 299
Cdd:pfam13407 148 KEKYPGIKvvaEVEGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLaGKVVVTGFDATPEALEAI 227

                         250       260       270
                  ....*....|....*....|....*....|..
gi 491605907  300 LKGELDITVMRMNDDTGIAMAEAIKWDLEGKP 331
Cdd:pfam13407 228 KDGTIDATVLQDPYGQGYAAVELAAALLKGKK 259
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 100-345 1.43e-09

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380661 [Multi-domain]  Cd Length: 274  Bit Score: 58.38  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 100 YQINQVFTRPNA--DIKQQSLSLMEALKSNSDYLIFT-LDTTRHRKFVEHVLDStKTKLILqnITTPVrewETRQPFMYV 176
Cdd:cd20006   30 YGVDLEFLGPESeeDIDGQIELIEEAIAQKPDAIVLAaSDYDRLVEAVERAKKA-GIPVIT--IDSPV---NSKKADSFV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 177 GFDHAEGSRELAVEFGKQFPKNTHYSVLYFSEGYISDI-RGNTFIHQVNQDSQFELQSAYYTKATKQSGYEAAKASLKKY 255
Cdd:cd20006  104 ATDNYEAGKKAGEKLASLLGEKGKVAIVSFVKGSSTAIeREEGFKQALAEYPNIKIVETEYCDSDEEKAYEITKELLSKY 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 256 PDVEFIYACSTDVALGAVEALSELGRED-VMINGWGGGSAELDAILKGELDITVMRMNDDTG-IAMAEAIKwDLEGKPVP 333
Cdd:cd20006  184 PDINGIVALNEQSTLGAARALKELGLGGkVKVVGFDSSVEEIQLLEEGIIDALVVQNPFNMGyLSVQAAVD-LLNGKKIP 262

                        250
                 ....*....|..
gi 491605907 334 TVYSGDFEVVTK 345
Cdd:cd20006  263 KRIDTGSVVITK 274
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
 179-344 5.03e-09

D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ribose binding protein (ttRBP); Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group are belonging to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.


Pssm-ID: 380622 [Multi-domain]  Cd Length: 272  Bit Score: 56.56  E-value: 5.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 179 DHAEGSRELAVEFGKQFPKNTHYSVLYFSEGYI-SDIRGNTFIHQVNQDSQFELQSAYYTKATKQSGYEAAKASLKKYPD 257
Cdd:cd19967  103 DNYQGAVLLAQYFVKLMGEKGLYVELLGKESDTnAQLRSQGFHSVIDQYPELKMVAQQSADWDRTEAFEKMESILQANPD 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 258 VEFIYACSTDVALGAVEALSELGR-EDVMINGWGGGSAELDAILKGELDITVMRMNDDTGIAMAEAIKWDLEG--KPVPT 334
Cdd:cd19967  183 IKGVICGNDEMALGAIAALKAAGRaGDVIIVGFDGSNDVRDAIKEGKISATVLQPAKLIARLAVEQADQYLKGgsTGKEE 262

                        170
                 ....*....|
gi 491605907 335 VYSGDFEVVT 344
Cdd:cd19967  263 KQLFDCVLIT 272
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
 241-344 6.20e-09

periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs; Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis D-ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group belong to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.


Pssm-ID: 380546 [Multi-domain]  Cd Length: 268  Bit Score: 56.15  E-value: 6.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 241 KQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGREDVMINGWGGGSAELDAILKGELDITVMRMNDDTG-IAM 319
Cdd:cd06323  165 RTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGRKDVIVVGFDGTPDAVKAVKDGKLAATVAQQPEEMGaKAV 244

                         90       100
                 ....*....|....*....|....*
gi 491605907 320 AEAIKWdLEGKPVPTVYSGDFEVVT 344
Cdd:cd06323  245 ETADKY-LKGEKVPKKIPVPLKLVT 268
PBP1_ABC_sugar_binding-like cd06316
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 244-346 1.14e-08

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380539 [Multi-domain]  Cd Length: 294  Bit Score: 55.71  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 244 GYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGREDVMI--NGWGGGSAeLDAILKGELDITVMRMNDDTGIAMAE 321
Cdd:cd06316  173 AEEVASAMLTANPDIDGIYVSWDTPALGVISALRAAGRSDIKIttVDLGTEIA-LDMAKGGNVKGIGAQRPYDQGVAEAL 251

                         90       100
                 ....*....|....*....|....*
gi 491605907 322 AIKWDLEGKPVPTVYSGDFEVVTKS 346
Cdd:cd06316  252 AAALALLGKEVPPFIGVPPLAVTKD 276
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 207-295 3.51e-08

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380534 [Multi-domain]  Cd Length: 270  Bit Score: 53.91  E-value: 3.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 207 SEGYISDIRGNTFIHQVNQDSQFELQSAYYTKATKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGREDVMI 286
Cdd:cd06311  131 SSGSVNEERVAGFKEVIKGNPGIKILAMQAGDWTREDGLKVAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAGRTDIKV 210


                 ....*....
gi 491605907 287 NGWGGGSAE 295
Cdd:cd06311  211 MTGGGGSQE 219
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 244-344 8.99e-08

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380627 [Multi-domain]  Cd Length: 269  Bit Score: 52.83  E-value: 8.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 244 GYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGRE-DVMINGWGGGSAELDAILKGELDITVMRMNDDTG-IAMAE 321
Cdd:cd19972  168 GFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLDhKIWVVGFDGDVAGLKAVKDGVLDATMTQQTQKMGrLAVDS 247

                         90       100
                 ....*....|....*....|...
gi 491605907 322 AIKWdLEGKPVPTVYSGDFEVVT 344
Cdd:cd19972  248 AIDL-LNGKAVPKEQLQDAVLTT 269
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
252-345 1.82e-07

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 52.01  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 252 LKKYPDVEFIYACSTDVALGAVEALSELGREDVMINGWGGGSAELDAILKGELDITVMRMNDDTGIAMAEAIKWDLEGKP 331
Cdd:PRK10653 202 LTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGIKAVNRGKLAATIAQQPDQIGAIGVETADKVLKGEK 281

                         90
                 ....*....|....
gi 491605907 332 VPTVYSGDFEVVTK 345
Cdd:PRK10653 282 VEAKIPVDLKLVTK 295
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 175-344 2.20e-07

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380662 [Multi-domain]  Cd Length: 271  Bit Score: 51.47  E-value: 2.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 175 YVGFDHAEGSRELAVEFGKQFPKNTHYSVLYFSEGYIS-DIRGNTFIHQVNQDSQFELQSAYYTKATKQSGYEAAKASLK 253
Cdd:cd20007  100 QIASDNVAGGALAAEALAELIGGKGKVLVINSTPGVSTtDARVKGFAEEMKKYPGIKVLGVQYSENDPAKAASIVAAALQ 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 254 KYPDVEFIYACSTDVALGAVEALSELGRED-VMINGWGGGSAELDAILKGELDITVMRMNDDTG-IAMAEAIKWdLEGKP 331
Cdd:cd20007  180 ANPDLAGIFGTNTFSAEGAAAALRNAGKTGkVKVVGFDASPAQVEQLKAGTIDALIAQKPAEIGyLAVEQAVAA-LTGKP 258

                        170
                 ....*....|...
gi 491605907 332 VPTVYSGDFEVVT 344
Cdd:cd20007  259 VPKDILTPFVVIT 271
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
 125-343 2.59e-07

ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of TreR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380484 [Multi-domain]  Cd Length: 259  Bit Score: 51.34  E-value: 2.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 125 KSNSDYLIF--TLDTTRHRKfvehvldstktklILQNITTPV----REWETrqpFMYVGFDHAEGSRELavefGKQFPKN 198
Cdd:cd01542   53 RQKVDGIILfaTEITDEHRK-------------ALKKLKIPVvvlgQEHEG---FSCVYHDDYGAGKLL----GEYLLKK 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 199 THYSVLYFSEGYiSDI-----RGNTFIHQVNqDSQFELQSAYYTKATKQSGYEAAKASLKKYPDVefIYACSTD-VALGA 272
Cdd:cd01542  113 GHKNIAYIGVDE-EDIavgvaRKQGYLDALK-EHGIDEVEIVETDFSMESGYEAAKELLKENKPD--AIICATDnIALGA 188

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491605907 273 VEALSELGR---EDVMINGWGGGsaELDAILKGELdITVMRMNDDTGIAMAEAIKWDLEGKPVPTVYSGDFEVV 343
Cdd:cd01542  189 IKALRELGIkipEDISVAGFGGY--DLSEFVSPSL-TTVKFDYEEAGEKAAELLLDMIEGEKVPKKQKLPYELI 259
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 240-326 2.96e-07

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 51.21  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 240 TKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGRE-DVMINGWGGGSAELDAILKGELDITVM----RMNDD 314
Cdd:cd06319  168 TVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTgDILVVGFDGDPEALDLIKDGKLDGTVAqqpfGMGAR 247

                         90
                 ....*....|..
gi 491605907 315 TGIAMAEAIKWD 326
Cdd:cd06319  248 AVELAIQALNGD 259
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
 165-308 4.20e-07

periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.


Pssm-ID: 380623 [Multi-domain]  Cd Length: 271  Bit Score: 50.85  E-value: 4.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 165 REWETRQPFMYVGFDHAEGSRELAVEFGKQFPKNTHYSVLYFSEGYISDI-RGNTFIHQVNQDSQFEL---QSAYYTKAT 240
Cdd:cd19968   88 RRAEGAAPVPHVGADNVAGGREVAKFVVDKLPNGAKVIELTGTPGSSPAIdRTKGFHEELAAGPKIKVvfeQTGNFERDE 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 241 KQSGYEAAKASLKKYPDVefIYACSTDVALGAVEALSE--LGREDVMINGWGGGSAELDAILKGELDITV 308
Cdd:cd19968  168 GLTVMENILTSLPGPPDA--IICANDDMALGAIEAMRAagLDLKKVKVIGFDAVPDALQAIKDGELYATV 235
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
 252-345 6.41e-06

periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group includes periplasmic D-threitol-binding protein ThpA and xylitol/L-sorbitol-binding protein XypA, which are part of sugar ABC-type transport systems. Both ThpA and XypA share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.


Pssm-ID: 380536 [Multi-domain]  Cd Length: 277  Bit Score: 47.26  E-value: 6.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 252 LKKYPD-VEFIYACSTDVALGAVEALSELGREDVMINGWGGGSAELDAILKGELDITVMrmnDD------TGIAMAEAIk 324
Cdd:cd06313  176 LQAYGDeIDGIIAQNDDMALGALQAVKAAGRDDIPVVGIDGIEDALQAVKSGELIATVL---QDaeaqgkGAVEVAVDA- 251

                         90       100
                 ....*....|....*....|.
gi 491605907 325 wdLEGKPVPTVYSGDFEVVTK 345
Cdd:cd06313  252 --VKGEGVEKKYYIPFVLVTK 270
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 175-347 6.47e-06

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380540 [Multi-domain]  Cd Length: 281  Bit Score: 47.37  E-value: 6.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 175 YVGFDHAEGSRELAVEFGKQFPKNTHYS----VLYFSEGYISDIRGNTFIHQVNQDSQFELQSAYYTKATKQSGYEAAKA 250
Cdd:cd06317   98 QVGVDNLEGGKEIGKYAADYIKAELGGQakigVVGALSSLIQNQRQKGFEEALKANPGVEIVATVDGQNVQEKALSAAEN 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 251 SLKKYPDVEFIYACSTDVALGAVEALSELGRE-DVMINGWgGGSAEL------DAILKGELDITVMRMNDDTGIAMAEAI 323
Cdd:cd06317  178 LLTANPDLDAIYATGEPALLGAVAAVRSQGRQgKIKVFGW-DLTKQAiflgidEGVLQAVVQQDPEKMGYEAVKAAVKAI 256

                        170       180
                 ....*....|....*....|....
gi 491605907 324 KwdleGKPVPTVYSGDFEVVTKSD 347
Cdd:cd06317  257 K----GEDVEKTIDVPPTIVTKEN 276
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
 240-333 7.28e-06

periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail.


Pssm-ID: 380531 [Multi-domain]  Cd Length: 268  Bit Score: 46.77  E-value: 7.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 240 TKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGRED-VMINGWGGGSAELD-AILKGELDITVmrMND---D 314
Cdd:cd06308  165 LRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGREKeIKIIGVDGLPEAGEkAVKDGILAATF--LYPtggK 242

                         90
                 ....*....|....*....
gi 491605907 315 TGIAMAEAIkwdLEGKPVP 333
Cdd:cd06308  243 EAIEAALKI---LNGEKVP 258
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 68-344 1.22e-05

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380533 [Multi-domain]  Cd Length: 272  Bit Score: 46.18  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907  68 KISVVYPGQQiSDYWIRNIDAFEKRLDKLNidYQINQVFTRPNADIKQQSLSLMEALKSNSDYLIFT-LDTTrhrKFVEH 146
Cdd:cd06310    1 KIGVVLKGTT-SAFWRTVREGAEAAAKDLG--VKIIFVGPESEEDVAGQNSLLEELINKKPDAIVVApLDSE---DLVDP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 147 VLDSTKTKLILQNITTPVrewETRQPFMYVGFDHAEGSRELAVEFGKQFPKNTHYSVLYFSEGYIS-DIRGNTFIHQVNQ 225
Cdd:cd06310   75 LKDAKDKGIPVIVIDSGI---KGDAYLSYIATDNYAAGRLAAQKLAEALGGKGKVAVLSLTAGNSTtDQREEGFKEYLKK 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 226 DSQ-FELQSAYYTKATKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGRED-VMINGWGGGSAELDAILKGE 303
Cdd:cd06310  152 HPGgIKVLASQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGqIKIVGFDSQEELLDALKNGK 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 491605907 304 LDITVMRMNDDTGIAMAEAIKWDLEGKPVPTVYSGDFEVVT 344
Cdd:cd06310  232 IDALVVQNPYEIGYEGIKLALKLLKGEEVPKNIDTGAELIT 272
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
 207-345 1.38e-05

periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily; Periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. ABP is only involved in transport contrary to other related sugar-binding proteins such as the glucose/galactose-binding protein (GGBP) and the ribose-binding protein (RBP), both of which are involved in chemotaxis as well as transport. The periplasmic ABP consists of two alpha/beta globular domains connected by a three-stranded hinge, a Venus flytrap-like domain, which undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, ABP is homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380482 [Multi-domain]  Cd Length: 294  Bit Score: 46.13  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 207 SEGYISDIRGNTF----IHQVNQDSQFelqsayytkatKQSGYEAAKASLKKYPDVE--FIYACSTDVALGAVEALSE-- 278
Cdd:cd01540  149 TDGAKDALKAAGFpedqIFQAPYKGTD-----------TEGAFNAANAVITAHPEVKhwLVVGCNDEGVLGAVRALEQag 217

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491605907 279 LGREDVMINGWGGGSAELDAILKGEldiTVMRMN-----DDTGIAMAEA-IKWDLEGKPVPTVYSGDFEVVTK 345
Cdd:cd01540  218 FDAEDIIGVGIGGYLAADEEFKKQP---TGFKASlyispDKHGYIAAEElYNWITDGKPPPAETLTDGVIVTR 287
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
 241-323 1.43e-05

periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380481 [Multi-domain]  Cd Length: 302  Bit Score: 46.42  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 241 KQSGYEAAKASLKKYPD-VEFIYACSTDVALGAVEALSELGREDVMINGW----G-GGSAE-LDAILKGELDITVmrMND 313
Cdd:cd01539  183 RAQAKDKMDAWLSKYGDkIELVIANNDDMALGAIEALKAAGYNTGDGDKYipvfGvDATPEaLEAIKEGKMLGTV--LND 260

                         90
                 ....*....|
gi 491605907 314 dtGIAMAEAI 323
Cdd:cd01539  261 --AKAQAKAI 268
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 172-342 1.51e-05

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380625 [Multi-domain]  Cd Length: 275  Bit Score: 46.09  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 172 PFMYVGFDHAEGSRELAVEFGKQFPKNTHYSVLyfsEG----YISDIRGNTFihqvnQDSQFE-------LQSAYYtKAT 240
Cdd:cd19970  104 NVPFVGPDNRQGAYLAGDYLAKKLGKGGKVAII---EGipgaDNAQQRKAGF-----LKAFEEagmkivaSQSANW-EID 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 241 KqsGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGR-EDVMINGWGGGSAELDAILKGELDITVMRMNDDTGiam 319
Cdd:cd19970  175 E--ANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKaGKVLVVGFDNIPAVRPLLKDGKMLATIDQHPAKQA--- 249

                        170       180
                 ....*....|....*....|....*.
gi 491605907 320 AEAIKWDLE---GKPVPTVYSGDFEV 342
Cdd:cd19970  250 VYGIEYALKmlnGEEVPGWVKTPVEL 275
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
225-343 1.89e-05

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 46.02  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 225 QDSQFELQSAYYTKATKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGRE-DVMINGWGGGSAELDAILKGE 303
Cdd:PRK09701 184 KASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTgKVLVVGTDGIPEARKMVEAGQ 263

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 491605907 304 LDITVMRMNDDTGIA----MAEAIKwdlEGKPVPTVYSGDFEVV 343
Cdd:PRK09701 264 MTATVAQNPADIGATglklMVDAEK---SGKVIPLDKAPEFKLV 304
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
 144-291 5.78e-05

ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators; This group represents the ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of GntR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding, which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380489 [Multi-domain]  Cd Length: 269  Bit Score: 44.02  E-value: 5.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 144 VEHvldSTKTKLILQNITTPVRE-WE-TRQPF-MYVGFDHAEGSRELA---VEFGKQfpknthySVLYFSEGYISDIRG- 216
Cdd:cd01575   64 TEH---TPATRKLLRAAGIPVVEtWDlPDDPIdMAVGFSNFAAGRAMArhlIERGYR-------RIAFVGARLDGDSRAr 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 217 ---NTFiHQVNQDSQFELQSAYYTK--ATKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGR---EDVMING 288
Cdd:cd01575  134 qrlEGF-RDALAEAGLPLPLVLLVElpSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIrvpGDIAIAG 212


                 ...
gi 491605907 289 WGG 291
Cdd:cd01575  213 FGD 215
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
 173-344 6.53e-05

periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP).


Pssm-ID: 380537 [Multi-domain]  Cd Length: 271  Bit Score: 44.11  E-value: 6.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 173 FMYVGFDHAEGSRELAVEFGKQFPKNThySVLYFSEGYISD-----IRGntFIHQVNQDSQFELQSAYYTKATKQSGYEA 247
Cdd:cd06314   97 LAYIGTDNYEAGREAGELMKKALPGGG--KVAIITGGLGADnlnerIQG--FKDALKGSPGIEIVDPLSDNDDIAKAVQN 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 248 AKASLKKYPDVEFIYACSTDVALGAVEALSELGR-EDVMINGWGGGSAELDAILKGELDITVM----RMNDDTGIAMAEA 322
Cdd:cd06314  173 VEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKvGKVKIVGFDTLPETLQGIKDGVIAATVGqrpyEMGYLSVKLLYKL 252

                        170       180
                 ....*....|....*....|..
gi 491605907 323 IKwdlEGKPVPTVYSGDFEVVT 344
Cdd:cd06314  253 LK---GGKPVPDVIDTGVDVVT 271
PBP1_LacI-like cd06287
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 242-286 9.06e-05

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380510 [Multi-domain]  Cd Length: 268  Bit Score: 43.56  E-value: 9.06e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 491605907 242 QSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGR---EDVMI 286
Cdd:cd06287  163 RAGYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRsvpEDLMV 210
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 246-346 9.28e-05

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 43.77  E-value: 9.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 246 EAAKASLKKYPDVEFIYACSTDVALGAVEALSELGRE-DVMINGWGGGSAELDAILKGELDITV----MRMNDDTGIAMA 320
Cdd:cd20005  173 DIAKAILQANPDLKGIYATNEGAAIGVANALKEMGKLgKIKVVGFDSGEAQIDAIKNGVIAGSVtqnpYGMGYKTVKAAV 252

                         90       100
                 ....*....|....*....|....*.
gi 491605907 321 EAIKwdlEGKPVPTVYSGdFEVVTKS 346
Cdd:cd20005  253 KALK---GEEVEKLIDTG-AKWYDKD 274
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 193-333 9.52e-05

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380626 [Multi-domain]  Cd Length: 267  Bit Score: 43.34  E-value: 9.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 193 KQFPKNTHYSVLYFSEGYISDIRGNTFIHQVNQDSQFELQSAYYTKATKQSGYEAAKASLKKYPDVEFIYACSTDVALGA 272
Cdd:cd19971  117 KKLPEGAKIAVLDHPTAESCVDRIDGFLDAIKKNPKFEVVAQQDGKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGA 196

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491605907 273 VEALSELGRE-DVMINGWGGGSAELDAILKGELDITVMRMNDDTGIAMAEAIKWDLEGKPVP 333
Cdd:cd19971  197 LAALKAAGKLgDILVYGVDGSPDAKAAIKDGKMTATAAQSPIEIGKKAVETAYKILNGEKVE 258
PBP1_CelR cd06295
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ...
 236-288 2.50e-04

ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators; This group includes the ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators. The binding of CelR to the celE promoter is inhibited specifically by cellobiose. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380518 [Multi-domain]  Cd Length: 273  Bit Score: 42.24  E-value: 2.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491605907 236 YTKATKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGR---EDVMING 288
Cdd:cd06295  163 SCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGIsvpGDVAVVG 218
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
 240-337 3.73e-04

similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Proteins similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. The sugar-binding domain of the periplasmic proteins in this group is also homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR), DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380528 [Multi-domain]  Cd Length: 273  Bit Score: 41.90  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 240 TKQSGYEAAKASLKKYPDVEF--IYACSTDVALGAVEALSELGREDVMINGWGGGSAELDAILKGELDITVMRMNDDT-- 315
Cdd:cd06305  165 TAADAQTQVEALLKKYPEGGIdaIWAAWDEPAKGAVQALEEAGRTDIKVYGVDISNQDLELMADEGSPWVATAAQDPAli 244

                         90       100
                 ....*....|....*....|..
gi 491605907 316 GIAMAEAIKWDLEGKPVPTVYS 337
Cdd:cd06305  245 GTVAVRNVARKLAGEDLPDKYS 266
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 230-344 5.03e-04

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380544 [Multi-domain]  Cd Length: 270  Bit Score: 41.51  E-value: 5.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 230 ELQSAYYTKATKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGREDVMINGWgGGSAELDAILKGELDITVM 309
Cdd:cd06321  153 KLVDDQNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDDIVITSV-DGSPEAVAALKREGSPFIA 231

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491605907 310 RMNDD------TGIAMAEAIKWDLEgkPVPTVYSGDFEVVT 344
Cdd:cd06321  232 TAAQDpydmarKAVELALKILNGQE--PAPELVLIPSTLVT 270
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 203-333 7.59e-04

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380659 [Multi-domain]  Cd Length: 273  Bit Score: 40.68  E-value: 7.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 203 VLYFSEGYIS-DIRGNTFIHQVNQDSQ-FELQSAYYTKATKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELG 280
Cdd:cd20004  128 LLRLAKGSAStTDRERGFLEALKKLAPgLKVVDDQYAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLG 207

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491605907 281 RED--VMInGWGGGSAELDAILKGELDITVM----RMNDDTGIAMAEAIKwdleGKPVP 333
Cdd:cd20004  208 LAGkvKFI-GFDASDLLLDALRAGEISALVVqdpyRMGYLGVKTAVAALR----GKPVP 261
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 244-333 7.61e-04

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380545 [Multi-domain]  Cd Length: 270  Bit Score: 40.72  E-value: 7.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 244 GYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGRED-VMINGWGGGSAELDAILKGELDITVMRMN-DDTGIAMAE 321
Cdd:cd06322  168 ALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKEDkIKVIGFDGNPEAIKAIAKGGKIKADIAQQpDKIGQETVE 247

                         90
                 ....*....|..
gi 491605907 322 AIKWDLEGKPVP 333
Cdd:cd06322  248 AIVKYLAGETVE 259
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
240-291 1.02e-03

DNA-binding transcriptional regulator, LacI/PurR family [Transcription];


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 40.57  E-value: 1.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491605907 240 TKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGR---EDVMINGWGG 291
Cdd:COG1609  222 SAESGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLrvpEDVSVVGFDD 276
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
 235-286 1.13e-03

ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily; Ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily. In most cases, ligands are monosaccharide including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the domain sugar binding changes the DNA binding activity of the repressor domain.


Pssm-ID: 380491 [Multi-domain]  Cd Length: 264  Bit Score: 40.19  E-value: 1.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491605907 235 YYTKATKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGR---EDVMI 286
Cdd:cd06267  155 VEGDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLrvpEDISV 209
PBP1_LsrB_Quorum_Sensing-like cd20001
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
 235-330 1.20e-03

ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380656  Cd Length: 296  Bit Score: 40.34  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 235 YYTKATKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGRED-VMINGWGGGSAELDAILKGelDITVMRMND 313
Cdd:cd20001  162 VETNDDSETAYEKAKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLQGkIAVVGTGLPSVAGEYLEDG--TIDYIQFWD 239

                         90
                 ....*....|....*....
gi 491605907 314 --DTGIAMAEAIKWDLEGK 330
Cdd:cd20001  240 paDAGYAMNALAVMVLEGE 258
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
 242-289 2.99e-03

ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of LacI is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380488 [Multi-domain]  Cd Length: 265  Bit Score: 38.72  E-value: 2.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491605907 242 QSGYEAAKAsLKKYPDVEFIYACSTDVALGAVEALSELGR---EDVMINGW 289
Cdd:cd01574  160 ASGYRAGRR-LLDDGPVTAVFAANDQMALGALRALHERGLrvpEDVSVVGF 209
PBP1_AglR-like cd20010
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ...
 168-335 3.07e-03

Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380665 [Multi-domain]  Cd Length: 269  Bit Score: 39.07  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 168 ETRQPFMYVGFDHAEGSRELA---VEFGKQ------FPKNTHYSVLyFSEGYISDIRGntfiHQVNQDSQFELQSAyytk 238
Cdd:cd20010   92 ESGAPYAWVDIDNEGAFRRATrrlLALGHRriallnGPEELNFAHQ-RRDGYRAALAE----AGLPVDPALVREGP---- 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 239 ATKQSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGRE---DVMINGWGGGSAELDAILKGeldITVMRMN-DD 314
Cdd:cd20010  163 LTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSpgkDVSVIGHDDLLPALEYFSPP---LTTTRSSlRD 239

                        170       180
                 ....*....|....*....|.
gi 491605907 315 TGIAMAEAIKWDLEGKPVPTV 335
Cdd:cd20010  240 AGRRLAEMLLALIDGEPAAEL 260
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
 242-288 7.63e-03

ligand-binding domain of putative DNA transcription regulators highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380630 [Multi-domain]  Cd Length: 269  Bit Score: 37.54  E-value: 7.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 491605907 242 QSGYEAAKASLKKYPDVEFIYACSTDVALGAVEALSELG---REDVMING 288
Cdd:cd19975  163 KSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGirvPEDISVIG 212
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
 242-288 8.24e-03

ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380507 [Multi-domain]  Cd Length: 267  Bit Score: 37.52  E-value: 8.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491605907 242 QSGYEAAKA--SLKKYPDVefIYACSTDVALGAVEALSELGR---EDVMING 288
Cdd:cd06284  161 EAGYAAARAllALPERPTA--IFCASDELAIGAIKALRRAGLrvpEDVSVIG 210
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 71-308 9.32e-03

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380535 [Multi-domain]  Cd Length: 272  Bit Score: 37.60  E-value: 9.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907  71 VVYPGQQISDYW----IRNIDAFEKrldKLNIDYQINQVftrPNADIKQQSLSLMEALKSNSDYLIFTLdttrhrkFVEH 146
Cdd:cd06312    3 YVISHGSPSDPFwsvvKKGAKDAAK---DLGVTVQYLGP---QNNDIADQARLIEQAIAAKPDGIIVTI-------PDPD 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 147 VLDSTKTKLILQNIttPV-------REWETRQP-FMYVGFDHAEGSRELAVEFGKQFPKN----THYSVLYFSE----GY 210
Cdd:cd06312   70 ALEPALKRAVAAGI--PViainsgdDRSKERLGaLTYVGQDEYLAGQAAGERALEAGPKNalcvNHEPGNPGLEarckGF 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491605907 211 ISDIRGNTFIHQVNQDSQfelqsaYYTKATkqsgyEAAKASLKKYPDVEFIYACSTDVALGAVEALSELGREDVMINGWG 290
Cdd:cd06312  148 ADAFKGAGILVELLDVGG------DPTEAQ-----EAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLKGKVKIGTF 216

                        250
                 ....*....|....*....
gi 491605907 291 GGSAE-LDAILKGELDITV 308
Cdd:cd06312  217 DLSPEtLEAIKDGKILFAI 235
 
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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