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Conserved domains on  [gi|147831352|emb|CAN02308|]
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putative sugar ABC transporter, substrate-binding protein [Clavibacter michiganensis subsp. michiganensis NCPPB 382]

Protein Classification

type 2 periplasmic-binding domain-containing protein( domain architecture ID 229383)

type 2 periplasmic-binding protein (PBP2) is typically comprised of two globular subdomains connected by a flexible hinge; it binds its ligand in the cleft between these domains in a manner resembling a Venus flytrap; similar to the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Periplasmic_Binding_Protein_Type_2 super family cl21456
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 66-447 1.47e-69

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically 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 origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. 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. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


The actual alignment was detected with superfamily member cd14748:

Pssm-ID: 473866 [Multi-domain]  Cd Length: 385  Bit Score: 226.02  E-value: 1.47e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  66 ITWWTTHPGQTSDLEAQFAADFLAK-TGITVNVVTGGaSYDEIAQKLQAAAGTDSMPDMVNASDTWWFRYMVNKQSIAMD 144
Cdd:cd14748    2 ITFWHGMSGPDGKALEELVDEFNKShPDIKVKAVYQG-SYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 145 GLMSHLGFEVDDFNKVFLDDYLYNGARYAVPYARSTPIFYYDKSIWQKAGL-PDRAPDTWAELEEWAPAImKVTGGNPAV 223
Cdd:cd14748   81 DYIDKDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLdPEKPPKTWDELEEAAKKL-KDKGGKTGR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 224 R--LPQGSIGTWAMSNVLWGRGGQY--SDGWDLKLDQPETLEAAGYARGLVFDSKIANVAAASGDTAvDFAGGLAPCTIA 299
Cdd:cd14748  160 YgfALPPGDGGWTFQALLWQNGGDLldEDGGKVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQD-AFISGKVAMTIN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 300 SAGAVG-IVTASAKFPIGTGVLPGGPQGQ-FVPTGGTGLaVIGSKTKEQQLAAAMFIKHLTEVDQQVALAKKTGYAPSRT 377
Cdd:cd14748  239 GTWSLAgIRDKGAGFEYGVAPLPAGKGKKgATPAGGASL-VIPKGSSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRK 317

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 378 SAGEstDLTGFWASNPAFRTVYDSLEHVRSQDWARTLIPNGDTYLQQPWSQILTQDADPAAVFPAAATQL 447
Cdd:cd14748  318 SAAE--DPEEFLAENPNYKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
 
Name Accession Description Interval E-value
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 66-447 1.47e-69

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: 226.02  E-value: 1.47e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  66 ITWWTTHPGQTSDLEAQFAADFLAK-TGITVNVVTGGaSYDEIAQKLQAAAGTDSMPDMVNASDTWWFRYMVNKQSIAMD 144
Cdd:cd14748    2 ITFWHGMSGPDGKALEELVDEFNKShPDIKVKAVYQG-SYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 145 GLMSHLGFEVDDFNKVFLDDYLYNGARYAVPYARSTPIFYYDKSIWQKAGL-PDRAPDTWAELEEWAPAImKVTGGNPAV 223
Cdd:cd14748   81 DYIDKDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLdPEKPPKTWDELEEAAKKL-KDKGGKTGR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 224 R--LPQGSIGTWAMSNVLWGRGGQY--SDGWDLKLDQPETLEAAGYARGLVFDSKIANVAAASGDTAvDFAGGLAPCTIA 299
Cdd:cd14748  160 YgfALPPGDGGWTFQALLWQNGGDLldEDGGKVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQD-AFISGKVAMTIN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 300 SAGAVG-IVTASAKFPIGTGVLPGGPQGQ-FVPTGGTGLaVIGSKTKEQQLAAAMFIKHLTEVDQQVALAKKTGYAPSRT 377
Cdd:cd14748  239 GTWSLAgIRDKGAGFEYGVAPLPAGKGKKgATPAGGASL-VIPKGSSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRK 317

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 378 SAGEstDLTGFWASNPAFRTVYDSLEHVRSQDWARTLIPNGDTYLQQPWSQILTQDADPAAVFPAAATQL 447
Cdd:cd14748  318 SAAE--DPEEFLAENPNYKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 23-366 2.26e-47

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 167.14  E-value: 2.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  23 LKLGAVLGGTAMLAACSGPSVGGDTAAtaapdtdwdgiqPATDITWWTTHPGQTSDLEAqFAADFLAKT-GITVNVVTGG 101
Cdd:COG1653    4 LALALAAALALALAACGGGGSGAAAAA------------GKVTLTVWHTGGGEAAALEA-LIKEFEAEHpGIKVEVESVP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 102 asYDEIAQKLQAAAGTDSMPDMVNASDTWWFRYMVNKQSIAMDGLMSHLGFEVDDFNKVFLDDYLYNGARYAVPYARSTP 181
Cdd:COG1653   71 --YDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 182 IFYYDKSIWQKAGLPdrAPDTWAELEEWAPAIMKVTGGNPavrLPQGSIGTWAMSNVLWGRGGQ-YSDGWDLKLDQPETL 260
Cdd:COG1653  149 GLYYNKDLFEKAGLD--PPKTWDELLAAAKKLKAKDGVYG---FALGGKDGAAWLDLLLSAGGDlYDEDGKPAFDSPEAV 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 261 EAAGYARGLVfDSKIANVAAAS---GDTAVDFAGGLAPCTIASAGAVG-IVTASAKFPIGTGVLPGGPQG--QFVPTGGT 334
Cdd:COG1653  224 EALEFLKDLV-KDGYVPPGALGtdwDDARAAFASGKAAMMINGSWALGaLKDAAPDFDVGVAPLPGGPGGkkPASVLGGS 302

                        330       340       350
                 ....*....|....*....|....*....|..
gi 147831352 335 GLAVigSKTKEQQLAAAMFIKHLTEVDQQVAL 366
Cdd:COG1653  303 GLAI--PKGSKNPEAAWKFLKFLTSPEAQAKW 332
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 82-395 3.82e-39

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 142.54  E-value: 3.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352   82 QFAADFLAKTGITVNVVTGGasYDEIAQKLQAAAGTDSMPDM-VNASDTWWFRYMVNKQSIAmdgLMSHLgFEVDDFNKv 160
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQA--SNDLQAKLLAAAAAGNAPDLdVVWIAADQLATLAEAGLLA---DLSDV-DNLDDLPD- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  161 FLDDYLYNGARYAVPYARSTP-IFYYDKSIWQKAGLPdraPDTWAELEEWAPAIMKVTGgnpavrLPQGSIGtwamsnvl 239
Cdd:pfam13416  74 ALDAAGYDGKLYGVPYAASTPtVLYYNKDLLKKAGED---PKTWDELLAAAAKLKGKTG------LTDPATG-------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  240 WGRGGQYSDGWDLKLD---QPETLEAAGYARGLVFDSKIANvaaASGDTAVDFAGGLAPCTIASAGAVgIVTASAKFPIG 316
Cdd:pfam13416 137 WLLWALLADGVDLTDDgkgVEALDEALAYLKKLKDNGKVYN---TGADAVQLFANGEVAMTVNGTWAA-AAAKKAGKKLG 212

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 147831352  317 TGVLPGGPqgqfvPTGGTGLaVIGSKTKEQQLAAAMFIKHLTEVDQQVALAKKTGYAPSRTSAgestDLTGFWASNPAF 395
Cdd:pfam13416 213 AVVPKDGS-----FLGGKGL-VVPAGAKDPRLAALDFIKFLTSPENQAALAEDTGYIPANKSA----ALSDEVKADPAL 281
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
168-393 2.81e-15

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 77.53  E-value: 2.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 168 NGARYAVPYARSTPIFYYDKSIWQKAGL-PDRAPDTWAELEEWAPAIMK-------VTGGNPAVRLPQGSigTWAMSNVL 239
Cdd:PRK10974 134 TGHLLSQPFNSSTPVLYYNKDAFKKAGLdPEQPPKTWQDLAAYAAKLRAagmkcgyASGWQGWIQLENFS--AWHGLPFA 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 240 WGRGGqySDGWD--LKLDQPETLEAAGYARGLVFDSKIANVAAASGDTAvDFAGGLAPCTIASAGAVGIVTASAKFPIGT 317
Cdd:PRK10974 212 SKNNG--FDGTDavLEFNKPEQVKHIALLEEMNKKGDFTYVGRKDESTE-KFYNGDCAITTASSGSLANIRKYAKFNYGV 288

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 318 GVLP------GGPQGQFVptGGTGLAVIGSKTKEQQLAAAMFIKHLTEVDQQVALAKKTGYAPSRTSAGESTDLTGFWAS 391
Cdd:PRK10974 289 GMMPydadvkGAPQNAII--GGASLWVMQGKDKETYKGVAKFLDFLAKPENAAEWHQKTGYLPITTAAYDLTREQGFYEK 366


                 ..
gi 147831352 392 NP 393
Cdd:PRK10974 367 NP 368
 
Name Accession Description Interval E-value
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 66-447 1.47e-69

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: 226.02  E-value: 1.47e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  66 ITWWTTHPGQTSDLEAQFAADFLAK-TGITVNVVTGGaSYDEIAQKLQAAAGTDSMPDMVNASDTWWFRYMVNKQSIAMD 144
Cdd:cd14748    2 ITFWHGMSGPDGKALEELVDEFNKShPDIKVKAVYQG-SYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 145 GLMSHLGFEVDDFNKVFLDDYLYNGARYAVPYARSTPIFYYDKSIWQKAGL-PDRAPDTWAELEEWAPAImKVTGGNPAV 223
Cdd:cd14748   81 DYIDKDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLdPEKPPKTWDELEEAAKKL-KDKGGKTGR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 224 R--LPQGSIGTWAMSNVLWGRGGQY--SDGWDLKLDQPETLEAAGYARGLVFDSKIANVAAASGDTAvDFAGGLAPCTIA 299
Cdd:cd14748  160 YgfALPPGDGGWTFQALLWQNGGDLldEDGGKVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQD-AFISGKVAMTIN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 300 SAGAVG-IVTASAKFPIGTGVLPGGPQGQ-FVPTGGTGLaVIGSKTKEQQLAAAMFIKHLTEVDQQVALAKKTGYAPSRT 377
Cdd:cd14748  239 GTWSLAgIRDKGAGFEYGVAPLPAGKGKKgATPAGGASL-VIPKGSSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRK 317

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 378 SAGEstDLTGFWASNPAFRTVYDSLEHVRSQDWARTLIPNGDTYLQQPWSQILTQDADPAAVFPAAATQL 447
Cdd:cd14748  318 SAAE--DPEEFLAENPNYKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 23-366 2.26e-47

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 167.14  E-value: 2.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  23 LKLGAVLGGTAMLAACSGPSVGGDTAAtaapdtdwdgiqPATDITWWTTHPGQTSDLEAqFAADFLAKT-GITVNVVTGG 101
Cdd:COG1653    4 LALALAAALALALAACGGGGSGAAAAA------------GKVTLTVWHTGGGEAAALEA-LIKEFEAEHpGIKVEVESVP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 102 asYDEIAQKLQAAAGTDSMPDMVNASDTWWFRYMVNKQSIAMDGLMSHLGFEVDDFNKVFLDDYLYNGARYAVPYARSTP 181
Cdd:COG1653   71 --YDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 182 IFYYDKSIWQKAGLPdrAPDTWAELEEWAPAIMKVTGGNPavrLPQGSIGTWAMSNVLWGRGGQ-YSDGWDLKLDQPETL 260
Cdd:COG1653  149 GLYYNKDLFEKAGLD--PPKTWDELLAAAKKLKAKDGVYG---FALGGKDGAAWLDLLLSAGGDlYDEDGKPAFDSPEAV 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 261 EAAGYARGLVfDSKIANVAAAS---GDTAVDFAGGLAPCTIASAGAVG-IVTASAKFPIGTGVLPGGPQG--QFVPTGGT 334
Cdd:COG1653  224 EALEFLKDLV-KDGYVPPGALGtdwDDARAAFASGKAAMMINGSWALGaLKDAAPDFDVGVAPLPGGPGGkkPASVLGGS 302

                        330       340       350
                 ....*....|....*....|....*....|..
gi 147831352 335 GLAVigSKTKEQQLAAAMFIKHLTEVDQQVAL 366
Cdd:COG1653  303 GLAI--PKGSKNPEAAWKFLKFLTSPEAQAKW 332
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
19-450 2.00e-44

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 160.12  E-value: 2.00e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  19 RRSVLKLGAVLGGTAMLAACSGPSVGGDTAATAAPdtdwdgiqpATDITWWttHPGQTSDLEAQFAADFLAKTGITVNVV 98
Cdd:COG2182    3 RRLLAALALALALALALAACGSGSSSSGSSSAAGA---------GGTLTVW--VDDDEAEALEEAAAAFEEEPGIKVKVV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  99 TGGasYDEIAQKLQAAAGTDSMPDMVNASDTWWFRYMVNKQSIAMDGLMShlgfEVDDFNKVFLDDYLYNGARYAVPYAR 178
Cdd:COG2182   72 EVP--WDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLA----DKDDFLPAALDAVTYDGKLYGVPYAV 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 179 STPIFYYDKSIWqkaglPDRAPDTWAELEEWAPAImkVTGGNPAVRLPQGSigTWAMSNVLWGRGGQY-----SDGWDLK 253
Cdd:COG2182  146 ETLALYYNKDLV-----KAEPPKTWDELIAAAKKL--TAAGKYGLAYDAGD--AYYFYPFLAAFGGYLfgkdgDDPKDVG 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 254 LDQPETLEAAGYARGLvFDSKIANVAAASGDTAVDFAGGLAPCTIASAGAVGIVTASAKFPIGTGVLPGGPQGQ-FVPTG 332
Cdd:COG2182  217 LNSPGAVAALEYLKDL-IKDGVLPADADYDAADALFAEGKAAMIINGPWAAADLKKALGIDYGVAPLPTLAGGKpAKPFV 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 333 GTGLAVIGSKTKEQQLAAAmFIKHLTEVDQQVALAKKTGYAPSRTSAGESTDLtgfwASNPAFRTVYDSLEHVRsqdwAR 412
Cdd:COG2182  296 GVKGFGVSAYSKNKEAAQE-FAEYLTSPEAQKALFEATGRIPANKAAAEDAEV----KADPLIAAFAEQAEYAV----PM 366

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 147831352 413 TLIPNGDTY---LQQPWSQILTQDADPAAVFPAAATQLTSA 450
Cdd:COG2182  367 PNIPEMGAVwtpLGTALQAIASGKADPAEALDAAQKQIEAA 407
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 82-395 3.82e-39

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 142.54  E-value: 3.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352   82 QFAADFLAKTGITVNVVTGGasYDEIAQKLQAAAGTDSMPDM-VNASDTWWFRYMVNKQSIAmdgLMSHLgFEVDDFNKv 160
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQA--SNDLQAKLLAAAAAGNAPDLdVVWIAADQLATLAEAGLLA---DLSDV-DNLDDLPD- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  161 FLDDYLYNGARYAVPYARSTP-IFYYDKSIWQKAGLPdraPDTWAELEEWAPAIMKVTGgnpavrLPQGSIGtwamsnvl 239
Cdd:pfam13416  74 ALDAAGYDGKLYGVPYAASTPtVLYYNKDLLKKAGED---PKTWDELLAAAAKLKGKTG------LTDPATG-------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  240 WGRGGQYSDGWDLKLD---QPETLEAAGYARGLVFDSKIANvaaASGDTAVDFAGGLAPCTIASAGAVgIVTASAKFPIG 316
Cdd:pfam13416 137 WLLWALLADGVDLTDDgkgVEALDEALAYLKKLKDNGKVYN---TGADAVQLFANGEVAMTVNGTWAA-AAAKKAGKKLG 212

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 147831352  317 TGVLPGGPqgqfvPTGGTGLaVIGSKTKEQQLAAAMFIKHLTEVDQQVALAKKTGYAPSRTSAgestDLTGFWASNPAF 395
Cdd:pfam13416 213 AVVPKDGS-----FLGGKGL-VVPAGAKDPRLAALDFIKFLTSPENQAALAEDTGYIPANKSA----ALSDEVKADPAL 281
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 66-438 3.48e-37

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: 140.23  E-value: 3.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  66 ITWWTTHPGQTSDLEAQFAADFLAK-TGITVNVVtgGASYDEIAQKLQAAAGTDSMPDMVNAsDTWWFRYMVNKQSIA-M 143
Cdd:cd13585    2 LTFWDWGQPAETAALKKLIDAFEKEnPGVKVEVV--PVPYDDYWTKLTTAAAAGTAPDVFYV-DGPWVPEFASNGALLdL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 144 DGLMSHLGFEvDDFNKVFLDDYLYNGARYAVPYARSTPIFYYDKSIWQKAGLPDRAPDTWAELEEWAPAIMKVTGGNPAV 223
Cdd:cd13585   79 DDYIEKDGLD-DDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTDKKGGQYGF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 224 RLPQGSIGTWAMSNVLWGRGGQY--SDGWDLKLDQPETLEAAGYARGLVFDsKIANVAAASGDTAVD--FAGGLAPCTIA 299
Cdd:cd13585  158 ALRGGSGGQTQWYPFLWSNGGDLldEDDGKATLNSPEAVEALQFYVDLYKD-GVAPSSATTGGDEAVdlFASGKVAMMID 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 300 SAGAVGIVTAS-AKFPIGTGVLPGGPQGQFVPTGGTGLAVIGSKTKEQQlAAAMFIKHLTEVDQQVALAKKTGyaPSRTS 378
Cdd:cd13585  237 GPWALGTLKDSkVKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPE-AAWKFIKFLTSKENQLKLGGAAG--PAALA 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 147831352 379 AGESTDLTGFWASNPAFRTVYDSLEHVRSQDWARTLIPNGD---TYLQQPWSQILTQDADPAA 438
Cdd:cd13585  314 AAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPilsEALQEALLGALGKSPEEAL 376
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 66-446 3.24e-30

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: 120.56  E-value: 3.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  66 ITWWTTHPGQTSDLEAQFAADFLAKT-GITVNVVTggASYDEIAQKLQAAAGTDSMPDMVNASDTWWFRYMvnKQSI--A 142
Cdd:cd14751    2 ITFWHTSSDEEKVLYEKLIPAFEKEYpKIKVKAVR--VPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFA--KLGYlqP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 143 MDGLMShlGFEVDDFNKVFLDDYLYNGARYAVPYARSTPIFYYDKSIWQKAGLPdrAPDTWAELEEWAPAIMKVTGgnpA 222
Cdd:cd14751   78 LDGTPA--FDDIVDYLPGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTE--VPKTMDELVAAAKAIKKKKG---R 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 223 VRLPQGSIGTWAMSNVLWGRGGQYSDGWD--LKLDQPETLEAAGYARGLVfDSKIANVAAASG--DTAVDFAGGLAPCTI 298
Cdd:cd14751  151 YGLYISGDGPYWLLPFLWSFGGDLTDEKKatGYLNSPESVRALETIVDLY-DEGAITPCASGGypNMQDGFKSGRYAMIV 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 299 ASAGAVGIVTASAKFP----IGTGVLPGGPQGQFVPTGGTGLAVI-GSKTKEqqlAAAMFIKHLTEVDQQVALAKKTGYA 373
Cdd:cd14751  230 NGPWAYADILGGKEFKdpdnLGIAPVPAGPGGSGSPVGGEDLVIFkGSKNKD---AAWKFVKFMSSAEAQALTAAKLGLL 306

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 147831352 374 PSRTSAGESTDLTGfwasNPAFRTVYDSLEHVRSqdwaRTLIPNG---DTYLQQPWSQILTQDADPAAVFPAAATQ 446
Cdd:cd14751  307 PTRTSAYESPEVAN----NPMVAAFKPALETAVP----RPPIPEWgelFEPLTLAFAKVLRGEKSPREALDEAAKQ 374
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 66-407 1.39e-29

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: 118.95  E-value: 1.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  66 ITWWTTHPGQTSDLEAQFAADFLAKT-GITVNVVTggASYDEIAQKLQAAAGTDSMPDMVNASDTWWFRYMvnkqsiAMD 144
Cdd:cd14747    2 LTVWAMGNSAEAELLKELADEFEKENpGIEVKVQV--LPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFA------AMG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 145 GL--MSHLGFEVDDFNKVF---LDDYLYNGARYAVPYARSTPIFYYDKSIWQKAGlPDRAPDTWAELEEWAPAIMKVTGG 219
Cdd:cd14747   74 ALedLTPYLEDLGGDKDLFpglVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAG-GDEAPKTWDELEAAAKKIKADGPD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 220 NPAVRLPQGSIGT-WAMSNVlWGRGGQY--SDGWDLKLDQPETLEAAGYARGLVFDSKI-ANVAAASGDTAVDFAGGLAP 295
Cdd:cd14747  153 VSGFAIPGKNDVWhNALPFV-WGAGGDLatKDKWKATLDSPEAVAGLEFYTSLYQKGLSpKSTLENSADVEQAFANGKVA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 296 CTIASAGAVGIVTASAKFP---IGTGVLPGGP-QGQFVPTGGTGLAVI-GSKTKEqqlAAAMFIKHLTEVDQQVALAKKT 370
Cdd:cd14747  232 MIISGPWEIGAIREAGPDLagkWGVAPLPGGPgGGSPSFAGGSNLAVFkGSKNKD---LAWKFIEFLSSPENQAAYAKAT 308

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 147831352 371 GYAPSRTSAGESTDLtgfwASNPAFRTVYDSLEHVRS 407
Cdd:cd14747  309 GMLPANTSAWDDPSL----ANDPLLAVFAEQLKTGKA 341
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 57-445 4.87e-29

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: 117.48  E-value: 4.87e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  57 WDGIQPATDITWWTthpgqtsDLEAQFAAdflAKTGITVNVVTggASYDEIAQKLQAAAGTDSMPDMVNASDTWWFRYMV 136
Cdd:cd14749    5 WQYFTGDTKKKYMD-------ELIADFEK---ENPNIKVKVVV--FPYDNYKTKLKTAVAAGEGPDVFNLWPGGWLAEFV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 137 nKQSIAMD-GLMSHLGFEVDDFNKVFLDDYLYNGARYAVPYARSTPIFYYDKSIWQKAGlPDRAPDTWAELEEwapAIMK 215
Cdd:cd14749   73 -KAGLLLPlTDYLDPNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAG-GVKPPKTWDELIE---AAKK 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 216 VTGGNPAVR----LPQGSIGTWAMSNVLWGRGG-----QYSDGWdlKLDQPETLEAAGYARGLVFDSKIANVAAASGDTA 286
Cdd:cd14749  148 DKFKAKGQTgfglLLGAQGGHWYFQYLVRQAGGgplsdDGSGKA--TFNDPAFVQALQKLQDLVKAGAFQEGFEGIDYDD 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 287 V--DFAGGLAPCTIASAGAVG-IVTASAKFPIGTGVLPGGPQG-QFVPTGGTGLAVIGSKTKEQQLAAAMFIKHLTEVDQ 362
Cdd:cd14749  226 AgqAFAQGKAAMNIGGSWDLGaIKAGEPGGKIGVFPFPTVGKGaQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEV 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 363 QVALAKKTGYAPSRTSAGESTDLTGFWASNPAFrtvyDSLEHVRSQDWARTLIPNGDTYLQQPWSQILTQDADPAAVFPA 442
Cdd:cd14749  306 MKQYLEDVGLLPAKEVVAKDEDPDPVAILGPFA----DVLNAAGSTPFLDEYWPAAAQVHKDAVQKLLTGKIDPEQVVKQ 381


                 ...
gi 147831352 443 AAT 445
Cdd:cd14749  382 AQS 384
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 65-403 3.76e-21

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: 94.67  E-value: 3.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  65 DITWWTTHPGQTSDLEAQFAADFLAKT-GITVNVVTGGASYDEIAQKL-QAAAGTDSMPDMVNASDTWwfrymvnKQSIA 142
Cdd:cd14750    1 TITFAAGSDGQEGELLKKAIAAFEKKHpDIKVEIEELPASSDDQRQQLvTALAAGSSAPDVLGLDVIW-------IPEFA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 143 MDGLMSHLGfevDDFNKVFLDDYL--------YNGARYAVPYARSTPIFYYDKSIWQKAGLPdrAPDTWAELEEWAPAIM 214
Cdd:cd14750   74 EAGWLLPLT---EYLKEEEDDDFLpatveantYDGKLYALPWFTDAGLLYYRKDLLEKYGPE--PPKTWDELLEAAKKRK 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 215 KvTGGNPAVRLPQG-----SIGTWAMsnVLWGRGGQY--SDGWDLKLDQPETLEAAGYARGLV-----------FDSKIA 276
Cdd:cd14750  149 A-GEPGIWGYVFQGkqyegLVCNFLE--LLWSNGGDIfdDDSGKVTVDSPEALEALQFLRDLIgegispkgvltYGEEEA 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 277 NVAAASGDTAvdFAG----GLAPCTIASAGAVGIVTASAkfpigtgvLPGGPQGQFVPT-GGTGLAVigSKTKEQQLAAA 351
Cdd:cd14750  226 RAAFQAGKAA--FMRnwpyAYALLQGPESAVAGKVGVAP--------LPAGPGGGSASTlGGWNLAI--SANSKHKEAAW 293

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 147831352 352 MFIKHLTEVDQQVALAKKTGYAPSRTSAGESTDLTgfwASNPAFRTVYDSLE 403
Cdd:cd14750  294 EFVKFLTSPEVQKRRAINGGLPPTRRALYDDPEVL---EAYPFLPALLEALE 342
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 65-404 9.37e-18

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: 84.65  E-value: 9.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  65 DITWWTTHPGQTSDLEAQfAADFLAKTGITVNVVTGGAsyDEIAQKLQAAAGTDSMPDMVNASDTWWFRYMVNkqsiamd 144
Cdd:cd13586    1 TITVWTDEDGELEYLKEL-AEEFEKKYGIKVEVVYVDS--GDTREKFITAGPAGKGPDVFFGPHDWLGELAAA------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 145 GLMSHLGFEVDD---FNKVFLDDYLYNGARYAVPYARSTPIFYYDKSIwqkagLPDrAPDTWAELEEWAPAIMKVTGGNP 221
Cdd:cd13586   71 GLLAPIPEYLAVkikNLPVALAAVTYNGKLYGVPVSVETIALFYNKDL-----VPE-PPKTWEELIALAKKFNDKAGGKY 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 222 AVRLPQgsigTWAMSNVLW--GRGGQY--SDGWDLK---LDQPETLEAAGYARGLVFDSKIaNVAAASGDTAVD-FAGGL 293
Cdd:cd13586  145 GFAYDQ----TNPYFSYPFlaAFGGYVfgENGGDPTdigLNNEGAVKGLKFIKDLKKKYKV-LPPDLDYDIADAlFKEGK 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 294 APCTI------ASAGAVGIVTASAKFPigtgVLPGGPQGQfvPTGGTGLAVIGSKTKEQQLAAAmFIKHLTEVDQQVALA 367
Cdd:cd13586  220 AAMIIngpwdlADYKDAGINFGVAPLP----TLPGGKQAA--PFVGVQGAFVSAYSKNKEAAVE-FAEYLTSDEAQLLLF 292

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 147831352 368 KKTGYAPSRTSAGESTDLtgfwASNPAFRTVYDSLEH 404
Cdd:cd13586  293 EKTGRIPALKDALNDAAV----KNDPLVKAFAEQAQY 325
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 82-363 1.63e-16

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: 79.77  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352   82 QFAADFLAK-TGITVNVVTGGasYDEIAQKLQAAAGTDSMPDMVNASDTWWFRYMVNKqsiamdglmshlGFEVDDFNKV 160
Cdd:pfam01547  12 ALVKEFEKEhPGIKVEVESVG--SGSLAQKLTTAIAAGDGPADVFASDNDWIAELAKA------------GLLLPLDDYV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  161 FLDDYLYNGARYAVPYARSTPIFYYDKSIWQKAGLPdrAPDTWAELEEWAPAIMKVTGGNPAVRLPQGSIGTWAMSN-VL 239
Cdd:pfam01547  78 ANYLVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLD--PPKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGYFTLaLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  240 WGRGGQYSDGWDLKLDQPETLEAAGYARGLVFDSKI------ANVAAASGDTAVD-FAGGLAPCTIASAGAVG------- 305
Cdd:pfam01547 156 ASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLlkklknPGVAGADGREALAlFEQGKAAMGIVGPWAALaankvkl 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 147831352  306 -----IVTASAKFPIGTGVLPGGPQGqfvPTGGTGLAVIgSKTKEQQLAAAmFIKHLTEVDQQ 363
Cdd:pfam01547 236 kvafaAPAPDPKGDVGYAPLPAGKGG---KGGGYGLAIP-KGSKNKEAAKK-FLDFLTSPEAQ 293
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
168-393 2.81e-15

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


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 77.53  E-value: 2.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 168 NGARYAVPYARSTPIFYYDKSIWQKAGL-PDRAPDTWAELEEWAPAIMK-------VTGGNPAVRLPQGSigTWAMSNVL 239
Cdd:PRK10974 134 TGHLLSQPFNSSTPVLYYNKDAFKKAGLdPEQPPKTWQDLAAYAAKLRAagmkcgyASGWQGWIQLENFS--AWHGLPFA 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 240 WGRGGqySDGWD--LKLDQPETLEAAGYARGLVFDSKIANVAAASGDTAvDFAGGLAPCTIASAGAVGIVTASAKFPIGT 317
Cdd:PRK10974 212 SKNNG--FDGTDavLEFNKPEQVKHIALLEEMNKKGDFTYVGRKDESTE-KFYNGDCAITTASSGSLANIRKYAKFNYGV 288

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 318 GVLP------GGPQGQFVptGGTGLAVIGSKTKEQQLAAAMFIKHLTEVDQQVALAKKTGYAPSRTSAGESTDLTGFWAS 391
Cdd:PRK10974 289 GMMPydadvkGAPQNAII--GGASLWVMQGKDKETYKGVAKFLDFLAKPENAAEWHQKTGYLPITTAAYDLTREQGFYEK 366


                 ..
gi 147831352 392 NP 393
Cdd:PRK10974 367 NP 368
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 66-382 7.58e-15

The periplasmic-binding component of ABC transport systems specific for maltose and related oligosaccharides; possess type 2 periplasmic binding fold; This family represents the periplasmic binding component of ABC transport systems involved in uptake of oligosaccharides including maltose, trehalose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270240 [Multi-domain]  Cd Length: 368  Bit Score: 75.91  E-value: 7.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  66 ITWWTTHPGQTSDLEAQFAADFLAKT-GITVNVVTGGAsyDEIAQKLQAAAGTDSMPDMVNASDTWwfrymvNKQSIAMd 144
Cdd:cd13522    2 ITVWHQYDTGENQAVNELIAKFEKAYpGITVEVTYQDT--EARRQFFSTAAAGGKGPDVVFGPSDS------LGPFAAA- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 145 GLMSHLGFEVDDFNKV---FLDDYLYNGARYAVPYARSTPIFYYDKSIwqkagLPDRAPDTWAELEEWApAIMKVTGGNP 221
Cdd:cd13522   73 GLLAPLDEYVSKSGKYapnTIAAMKLNGKLYGVPVSVGAHLMYYNKKL-----VPKNPPKTWQELIALA-QGLKAKNVWG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 222 AVrlpqgSIGTWAMSNVLW--GRGGQY----SDGWDLKLDQPETLEAAGYARGLVFDSKIanVAAASGDTAVD--FAGGL 293
Cdd:cd13522  147 LV-----YNQNEPYFFAAWigGFGGQVfkanNGKNNPTLDTPGAVEALQFLVDLKSKYKI--MPPETDYSIADalFKAGK 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 294 APCTIASAGAVGIVTASAKFPIGTGVLPGGPQGQFVPTGGTGLAVIGSKTKEQQLAAAMFIKHLTEVDQQVALAKKTGYA 373
Cdd:cd13522  220 AAMIINGPWDLGDYRQALKINLGVAPLPTFSGTKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFDDAGDI 299


                 ....*....
gi 147831352 374 PSRTSAGES 382
Cdd:cd13522  300 PANLQAYES 308
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 66-447 1.67e-10

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: 62.39  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  66 ITWWttHPGQTSDLEA--QFAADFLAKTGIT-VNVVTGGASydEIAQKLQAAAGTDSMPDMVnasdtWWfrymvNKQSIA 142
Cdd:cd13657    2 ITIW--HALTGAEEDAlqQIIDEFEAKYPVPnVKVPFEKKP--DLQNKLLTAIPAGEGPDLF-----IW-----AHDWIG 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 143 MDGLMSHLGFEVDDFNKVFLDDYL--------YNGARYAVPYARSTPIFYYDKSIWqkaglpDRAPDTWAELEEWAPAIM 214
Cdd:cd13657   68 QFAEAGLLVPISDYLSEDDFENYLptaveavtYKGKVYGLPEAYETVALIYNKALV------DQPPETTDELLAIMKDHT 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 215 KVTGGNPAVRLPQGSigTWAMSNVLWGRGGQYSDGWDLK--LDQPETLEAAGYarglvFDSKIANVAAASGDTAVD---F 289
Cdd:cd13657  142 DPAAGSYGLAYQVSD--AYFVSAWIFGFGGYYFDDETDKpgLDTPETIKGIQF-----LKDFSWPYMPSDPSYNTQtslF 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 290 AGGLAPCTI------ASAGAVGIVTASAKFPIGTGVLP----GGPQGQFVptggtgLAVIGSKTKEqqlAAAMFIKHLTE 359
Cdd:cd13657  215 NEGKAAMIIngpwfiGGIKAAGIDLGVAPLPTVDGTNPprpySGVEGIYV------TKYAERKNKE---AALDFAKFFTT 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 360 VDQQVALAKKTGYAPSRTSAGESTDLtgfwASNPAFRTVYDSLEHVrsqdwarTLIPNgDTYLQQPWS-------QILTQ 432
Cdd:cd13657  286 AEASKILADENGYVPAATNAYDDAEV----AADPVIAAFKAQAEHG-------VPMPN-SPEMASVWGpvtlalaAVYQG 353

                        410
                 ....*....|....*
gi 147831352 433 DADPAAVFPAAATQL 447
Cdd:cd13657  354 GQDPQEALAAAQQEI 368
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 84-379 4.82e-10

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: 60.96  E-value: 4.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  84 AADFLAKTGITVNVVTGGASYDEIAQKLQAAAGtdSMPD-MVNASDtwwfrymvNKQSIAMDGLMSHLGF---EVDDFNK 159
Cdd:cd13658   19 AKQYTKKTGVKVKLVEVDQLDQLEKLSLDGPAG--KGPDvMVAPHD--------RIGSAVLQGLLSPIKLskdKKKGFTD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 160 VFLDDYLYNGARYAVPYARSTPIFYYDKSiwqkagLPDRAPDTWAELEEWAPAIMKVTGGNPAVRLPQGSI-GTW----A 234
Cdd:cd13658   89 QALKALTYDGKLYGLPAAVETLALYYNKD------LVKNAPKTFDELEALAKDLTKEKGKQYGFLADATNFyYSYgllaG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 235 MSNVLWGRGGQYSDGWDLKLDQPETLEAAGYARGLvFDSKIANvAAASGDT---------AVDFAGGlaPCTIASAGAVG 305
Cdd:cd13658  163 NGGYIFKKNGSDLDINDIGLNSPGAVKAVKFLKKW-YTEGYLP-KGMTGDViqglfkegkAAAVIDG--PWAIQEYQEAG 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 147831352 306 IVTASAKFPigtgVLPGG-PQGQFVptGGTGLaVIGSKTKEQQLAAAmFIKHLTEVDQQVALAKKTGYAPSRTSA 379
Cdd:cd13658  239 VNYGVAPLP----TLPNGkPMAPFL--GVKGW-YLSAYSKHKEWAQK-FMEFLTSKENLKKRYDETNEIPPRKDV 305
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
18-429 5.20e-06

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 48.37  E-value: 5.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  18 DRRSVLKLGAVlggtAMLAACSGPSvggdtAATAAPDT----DWDGiqpatditwwtthpgqtsDLEAQFAADFLAKTGI 93
Cdd:COG0687    2 SRRSLLGLAAA----ALAAALAGGA-----PAAAAEGTlnvyNWGG------------------YIDPDVLEPFEKETGI 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  94 TVNVVTGGASyDEIAQKLQAAAGTdsmPDMVNASDTWWFRYMVNK--QSIAMDgLMSHLgfevDDFNKVFLDDYLYNGAR 171
Cdd:COG0687   55 KVVYDTYDSN-EEMLAKLRAGGSG---YDVVVPSDYFVARLIKAGllQPLDKS-KLPNL----ANLDPRFKDPPFDPGNV 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 172 YAVPYARSTPIFYYDKSIWqkaglpDRAPDTWAELeeWAPAIM-KVTGGNPAvrlpqgsigTWAMSNVLWGRGGQYSDGW 250
Cdd:COG0687  126 YGVPYTWGTTGIAYNTDKV------KEPPTSWADL--WDPEYKgKVALLDDP---------REVLGAALLYLGYDPNSTD 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 251 DLKLDQPETL--EAAGYARGlvFDSKIANVAA--ASGDTAvdfagglapctIASAGAVGIVTASAK-FPIGTgVLP--GG 323
Cdd:COG0687  189 PADLDAAFELliELKPNVRA--FWSDGAEYIQllASGEVD-----------LAVGWSGDALALRAEgPPIAY-VIPkeGA 254

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 324 pqgqfvpTGGTGLAVIGSKTKEQQLAAAmFIKHLTEVDQQVALAKKTGYAPSRTSAGEstDLTGFWASNPAfrtVYDSLE 403
Cdd:COG0687  255 -------LLWFDNMAIPKGAPNPDLAYA-FINFMLSPEVAAALAEYVGYAPPNKAARE--LLPPELAANPA---IYPPEE 321

                        410       420
                 ....*....|....*....|....*.
gi 147831352 404 HVRSQDWARTLIPNGDTYLQQPWSQI 429
Cdd:COG0687  322 VLDKLEFWNPLPPENRELYTRRWTEI 347
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 90-359 3.34e-05

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  90 KTGITVNV-VTGGASYDEiaqKLQAAAGTDSMPDMVNASDTWWFRYMVnKQSIAMDgLMSHLGFEVDDFNKVFLDDYL-- 166
Cdd:cd13580   31 KTNIDVKVkWVPDSSYDE---KLNLALASGDLPDIVVVNDPQLSITLV-KQGALWD-LTDYLDKYYPNLKKIIEQEGWds 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 167 --YNGARYAVPYARSTPIfyyDKSIW------QKAGLPdrAPDTWAELEEWAPAI---------MKVTGGnpaVRLPQGS 229
Cdd:cd13580  106 asVDGKIYGIPRKRPLIG---RNGLWirkdwlDKLGLE--VPKTLDELYEVAKAFtekdpdgngKKDTYG---LTDTKDL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 230 IGtWAMSNVLWGrGGQYSDGW----DLKL----DQPETLEAAGYARGLvFDSKIAN--VAAASGDTAVDFagglapctiA 299
Cdd:cd13580  178 IG-SGFTGLFGA-FGAPPNNWwkdeDGKLvpgsIQPEMKEALKFLKKL-YKEGLIDpeFAVNDGTKANEK---------F 245

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 147831352 300 SAGAVGIVTA-----------------SAKF-PIGTGVLPGGPQGQFVPTGGTGLAVIGSKTKEQQLAAAMFIKHLTE 359
Cdd:cd13580  246 ISGKAGIFVGnwwdpawpqaslkkndpDAEWvAVPIPSGPDGKYGVWAESGVNGFFVIPKKSKKPEAILKLLDFLSDP 323
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 83-385 1.20e-04

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 43.77  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  83 FAADFLAKTGITVNVVTGGASydEIAQKLQAAAGtDSMPDMVNASDtwwfryMVNKQSIAMDGLMshLGFEVDDFNKVfl 162
Cdd:COG1840    1 LLEAFEKKTGIKVNVVRGGSG--ELLARLKAEGG-NPPADVVWSGD------ADALEQLANEGLL--QPYKSPELDAI-- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 163 DDYLYNGARYAVPYARSTPIFYYDKSIWQKAGlpdrAPDTWAEL--EEWApaiMKVTGGNPAvrlpQGSIGTWAMSNVLW 240
Cdd:COG1840   68 PAEFRDPDGYWFGFSVRARVIVYNTDLLKELG----VPKSWEDLldPEYK---GKIAMADPS----SSGTGYLLVAALLQ 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 241 GRGGQYsdGWDLkLDQpetLEAAGyARGLVFDSKIANvAAASGDTAV----DFAGGLApctIASAGAVGIVtasakFP-I 315
Cdd:COG1840  137 AFGEEK--GWEW-LKG---LAANG-ARVTGSSSAVAK-AVASGEVAIgivnSYYALRA---KAKGAPVEVV-----FPeD 200

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 316 GTGVLPGGpqgqfvptggtglAVIGSKTKEQQLAAAmFIKHLTEVDQQVALAKKTGYAPSRTSAGESTDL 385
Cdd:COG1840  201 GTLVNPSG-------------AAILKGAPNPEAAKL-FIDFLLSDEGQELLAEEGYEYPVRPDVEPPEGL 256
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 79-374 4.37e-04

The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. 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.


Pssm-ID: 270307 [Multi-domain]  Cd Length: 268  Bit Score: 41.83  E-value: 4.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352  79 LEAQFAADFLAKTGITVNVVTGGASydEIAQKLQAAAGTDSMpDMVNASDtwwfrymVNKQSIAMDGLmshlgFEVDDFN 158
Cdd:cd13589   15 QRKAVIEPFEKETGIKVVYDTGTSA--DRLAKLQAQAGNPQW-DVVDLDD-------GDAARAIAEGL-----LEPLDYS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 159 KVFLDDYLYNGARYAVPYArsTPIFYYDKSI-WQKAGLPDrAPDTWAELEEWAPAimKVTGGNPAVRLPqgsIGTWAMSN 237
Cdd:cd13589   80 KIPNAAKDKAPAALKTGYG--VGYTLYSTGIaYNTDKFKE-PPTSWWLADFWDVG--KFPGPRILNTSG---LALLEAAL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147831352 238 VLWGrGGQYSDGWDL---KLDqpetlEAAGYArgLVFDSKIANVAA--ASGDTAVdfagglapcTIASAGAVGIVTAsAK 312
Cdd:cd13589  152 LADG-VDPYPLDVDRafaKLK-----ELKPNV--VTWWTSGAQLAQllQSGEVDM---------APAWNGRAQALID-AG 213

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 147831352 313 FPIGTGVlpggPQGQFVPTGGTGLAVIGSKTKEqqlaAAM-FIKHLTEVDQQVALAKKTGYAP 374
Cdd:cd13589  214 APVAFVW----PKEGAILGPDTLAIVKGAPNKE----LAMkFINFALSPEVQAALAEALGYGP 268
 
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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