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Conserved domains on  [gi|490458057|ref|WP_004328773|]
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MULTISPECIES: efflux RND transporter periplasmic adaptor subunit [Alistipes]

Protein Classification

efflux RND transporter periplasmic adaptor subunit( domain architecture ID 11436533)

efflux RND (resistance-nodulation-division) transporter periplasmic adaptor subunit, similar to Bacillus subtilis YknX, which is part of an unusual four-component transporter with a role in protection against sporulation-delaying-protein-induced killing

CATH:  2.40.50.100|2.40.420.20|2.40.30.170|1.10.287.470
Gene Ontology:  GO:0016020|GO:0055085|GO:0022857|GO:0042802
PubMed:  32073314
TCDB:  2.A.6

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 44-360 2.79e-71

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


:

Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 225.59  E-value: 2.79e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  44 TIRQYVIASGKVEPRDEVLIKPQISGIISEVLCKAGDRVKQGDVIATVKVIPEMGTLNAAESRVTVARLSLDQTRKEFER 123
Cdd:COG0845    7 DVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAELER 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 124 TEALYAKGVVSQEEFEKGQTTLRQAEEEFQNAEDNLEIVKTgitnrykDLSNTQIRSTITGMILDVPIKVGNSViqantf 203
Cdd:COG0845   87 YKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARA-------NLAYTTIRAPFDGVVGERNVEPGQLV------ 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 204 NDGTTIATVADMGDMLFRGNVDETDIGRLHAGMPVVLTIGAMQGTVLQATLEYISPKAADVNGiiMFEVKAAAKIPESVF 283
Cdd:COG0845  154 SAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATR--TVRVRAELPNPDGLL 231

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490458057 284 vRAGYSANASIVTDSREGVLTLPESTIQFEEGKPCVYILTspeesPEQTFEKRDVTLGLSDGVNIEIVSGVTETDKV 360
Cdd:COG0845  232 -RPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVD-----ADGKVERRPVTLGRRDGDQVEVLSGLKAGDRV 302
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 44-360 2.79e-71

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 225.59  E-value: 2.79e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  44 TIRQYVIASGKVEPRDEVLIKPQISGIISEVLCKAGDRVKQGDVIATVKVIPEMGTLNAAESRVTVARLSLDQTRKEFER 123
Cdd:COG0845    7 DVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAELER 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 124 TEALYAKGVVSQEEFEKGQTTLRQAEEEFQNAEDNLEIVKTgitnrykDLSNTQIRSTITGMILDVPIKVGNSViqantf 203
Cdd:COG0845   87 YKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARA-------NLAYTTIRAPFDGVVGERNVEPGQLV------ 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 204 NDGTTIATVADMGDMLFRGNVDETDIGRLHAGMPVVLTIGAMQGTVLQATLEYISPKAADVNGiiMFEVKAAAKIPESVF 283
Cdd:COG0845  154 SAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATR--TVRVRAELPNPDGLL 231

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490458057 284 vRAGYSANASIVTDSREGVLTLPESTIQFEEGKPCVYILTspeesPEQTFEKRDVTLGLSDGVNIEIVSGVTETDKV 360
Cdd:COG0845  232 -RPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVD-----ADGKVERRPVTLGRRDGDQVEVLSGLKAGDRV 302
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 36-360 2.61e-46

RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273776 [Multi-domain]  Cd Length: 322  Bit Score: 160.56  E-value: 2.61e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057   36 TLATPVHDTIRQYVIASGKVEPRDEVLIKPQISGIISEVLCKAGDRVKQGDVIATVKVIPEMGTLNAAESRVTVARLSLD 115
Cdd:TIGR01730   2 TVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  116 QTRKEFERTEALYAKGVVSQEEFEKGQTTLRQAEEEFQNAEDNLEIVKtgitnryKDLSNTQIRSTITGMILDVPIKVGN 195
Cdd:TIGR01730  82 LAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQ-------LNLRYTEIRAPFDGTIGRRLVEVGA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  196 SViqantfNDGTTIATVADMGDMLFRGNVDETDIGRLHAGMPVVLTIGAMQGTVLQATLEYISPKAADVNGiiMFEVKAA 275
Cdd:TIGR01730 155 YV------TAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTG--TVRVRAT 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  276 AKIPESVFvRAGYSANASIVTDSREGVLTLPESTIQFEEGKPCVYILtspeeSPEQTFEKRDVTLGLSDGVNIEIVSGVT 355
Cdd:TIGR01730 227 FPNPDGRL-LPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVV-----KNDGKVSKRPVEVGLRNGGYVEIESGLK 300


                  ....*
gi 490458057  356 ETDKV 360
Cdd:TIGR01730 301 AGDQI 305
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
 2-360 9.78e-22

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 95.23  E-value: 9.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057   2 KKFLKIFLgILFLALLVGTFVFLWNKTRPVKVVYTLATpVHDTIRQYVIASGKVEPRDEVLIKPQISGIISEVLCKAGDR 81
Cdd:PRK11578   5 KKVKKRYL-IALVIVLAGGITLWRILNAPVPTYQTLIV-RPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIGDK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  82 VKQGDVIATVKviPEMGTLNAAESRVTVARLSLDQTRKEFE---------RTEALYAKGVVSQEEFEKGQTTL--RQAEE 150
Cdd:PRK11578  83 VKKDQLLGVID--PEQAENQIKEVEATLMELRAQRQQAEAElklarvtlsRQQRLAKTQAVSQQDLDTAATELavKQAQI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 151 EFQNAE--DNLEIVKTGITNrykdLSNTQIRSTITGMILDVPIKVGNSVIQANtfnDGTTIATVADMGDMLFRGNVDETD 228
Cdd:PRK11578 161 GTIDAQikRNQASLDTAKTN----LDYTRIVAPMAGEVTQITTLQGQTVIAAQ---QAPNILTLADMSTMLVKAQVSEAD 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 229 IGRLHAGMPVVLTIGAMQGTVLQATLEYISPKAADVNGIIMFEVKAAAKIPESVfVRAGYSANASIVTDSREGVLTLPES 308
Cdd:PRK11578 234 VIHLKPGQKAWFTVLGDPLTRYEGVLKDILPTPEKVNDAIFYYARFEVPNPNGL-LRLDMTAQVHIQLTDVKNVLTIPLS 312

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490458057 309 TI--QFEEGKPCVYILTSPEEspeqtfEKRDVTLGLSDGVNIEIVSGVTETDKV 360
Cdd:PRK11578 313 ALgdPVGDNRYKVKLLRNGET------REREVTIGARNDTDVEIVKGLEAGDEV 360
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 49-296 2.68e-17

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 81.70  E-value: 2.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057   49 VIASGKVEP-RDEVLIKPQISGIISEVLCKAGDRVKQGDVIATVKVIPEMGTLNAAES---------------------- 105
Cdd:pfam00529   8 VEAPGRVVVsGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAqlakaqaqvarlqaeldrlqal 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  106 -----------------------RVTVARLSLDQTRKEFERTEALYAKGVVSQEE-------FEKGQTTLRQAEEEF--- 152
Cdd:pfam00529  88 eselaisrqdydgataqlraaqaAVKAAQAQLAQAQIDLARRRVLAPIGGISRESlvtagalVAQAQANLLATVAQLdqi 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  153 -----QNAEDNLEIVKTG--------------ITNRYKDLSNTQIRSTITGMILDVPIKVGNSVIQAntfndGTTIATVA 213
Cdd:pfam00529 168 yvqitQSAAENQAEVRSElsgaqlqiaeaeaeLKLAKLDLERTEIRAPVDGTVAFLSVTVDGGTVSA-----GLRLMFVV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  214 DMGDMLFRGNVDETDIGRLHAGMPVVLTIGAMQGTV---LQATLEYISPKAADVngiimfEVKAAAKIPESVFVRAGYSA 290
Cdd:pfam00529 243 PEDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKtgrFTGVVVGISPDTGPV------RVVVDKAQGPYYPLRIGLSA 316


                  ....*.
gi 490458057  291 NASIVT 296
Cdd:pfam00529 317 GALVRL 322
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 44-360 2.79e-71

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 225.59  E-value: 2.79e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  44 TIRQYVIASGKVEPRDEVLIKPQISGIISEVLCKAGDRVKQGDVIATVKVIPEMGTLNAAESRVTVARLSLDQTRKEFER 123
Cdd:COG0845    7 DVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAELER 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 124 TEALYAKGVVSQEEFEKGQTTLRQAEEEFQNAEDNLEIVKTgitnrykDLSNTQIRSTITGMILDVPIKVGNSViqantf 203
Cdd:COG0845   87 YKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARA-------NLAYTTIRAPFDGVVGERNVEPGQLV------ 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 204 NDGTTIATVADMGDMLFRGNVDETDIGRLHAGMPVVLTIGAMQGTVLQATLEYISPKAADVNGiiMFEVKAAAKIPESVF 283
Cdd:COG0845  154 SAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATR--TVRVRAELPNPDGLL 231

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490458057 284 vRAGYSANASIVTDSREGVLTLPESTIQFEEGKPCVYILTspeesPEQTFEKRDVTLGLSDGVNIEIVSGVTETDKV 360
Cdd:COG0845  232 -RPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVD-----ADGKVERRPVTLGRRDGDQVEVLSGLKAGDRV 302
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
1-297 3.04e-47

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 163.30  E-value: 3.04e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057   1 MKKF-LKIFLGILFLALLVGTFVFLWNKTRPVKVVytlatpvhdtirqyvIASGKVEpRDEVLIKPQISGIISEVLCKAG 79
Cdd:COG1566    1 MKALkKRRLLALVLLLLALGLALWAAGRNGPDEPV---------------TADGRVE-ARVVTVAAKVSGRVTEVLVKEG 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  80 DRVKQGDVIATV---------------------------KVIPEMGTLNAAESRVTVARLSLDQTRKEFERTEALYAKGV 132
Cdd:COG1566   65 DRVKKGQVLARLdptdlqaalaqaeaqlaaaeaqlarleAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 133 VSQEEFEKGQTTLRQAEEEFQNAEDNLEIVKTGITNR--------------------YKDLSNTQIRSTITGMILDVPIK 192
Cdd:COG1566  145 VSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEeelaaaqaqvaqaeaalaqaELNLARTTIRAPVDGVVTNLNVE 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 193 VGnSVIQAntfndGTTIATVADMGDMLFRGNVDETDIGRLHAGMPVVLTIGAMQGTVLQATLEYISPKAADV-------- 264
Cdd:COG1566  225 PG-EVVSA-----GQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTsppknatg 298

                        330       340       350
                 ....*....|....*....|....*....|...
gi 490458057 265 NGIIMFEVKAAAKIPESVFVRAGYSANASIVTD 297
Cdd:COG1566  299 NVVQRYPVRIRLDNPDPEPLRPGMSATVEIDTE 331
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 36-360 2.61e-46

RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273776 [Multi-domain]  Cd Length: 322  Bit Score: 160.56  E-value: 2.61e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057   36 TLATPVHDTIRQYVIASGKVEPRDEVLIKPQISGIISEVLCKAGDRVKQGDVIATVKVIPEMGTLNAAESRVTVARLSLD 115
Cdd:TIGR01730   2 TVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  116 QTRKEFERTEALYAKGVVSQEEFEKGQTTLRQAEEEFQNAEDNLEIVKtgitnryKDLSNTQIRSTITGMILDVPIKVGN 195
Cdd:TIGR01730  82 LAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQ-------LNLRYTEIRAPFDGTIGRRLVEVGA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  196 SViqantfNDGTTIATVADMGDMLFRGNVDETDIGRLHAGMPVVLTIGAMQGTVLQATLEYISPKAADVNGiiMFEVKAA 275
Cdd:TIGR01730 155 YV------TAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTG--TVRVRAT 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  276 AKIPESVFvRAGYSANASIVTDSREGVLTLPESTIQFEEGKPCVYILtspeeSPEQTFEKRDVTLGLSDGVNIEIVSGVT 355
Cdd:TIGR01730 227 FPNPDGRL-LPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVV-----KNDGKVSKRPVEVGLRNGGYVEIESGLK 300


                  ....*
gi 490458057  356 ETDKV 360
Cdd:TIGR01730 301 AGDQI 305
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
 2-360 9.78e-22

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 95.23  E-value: 9.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057   2 KKFLKIFLgILFLALLVGTFVFLWNKTRPVKVVYTLATpVHDTIRQYVIASGKVEPRDEVLIKPQISGIISEVLCKAGDR 81
Cdd:PRK11578   5 KKVKKRYL-IALVIVLAGGITLWRILNAPVPTYQTLIV-RPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIGDK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  82 VKQGDVIATVKviPEMGTLNAAESRVTVARLSLDQTRKEFE---------RTEALYAKGVVSQEEFEKGQTTL--RQAEE 150
Cdd:PRK11578  83 VKKDQLLGVID--PEQAENQIKEVEATLMELRAQRQQAEAElklarvtlsRQQRLAKTQAVSQQDLDTAATELavKQAQI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 151 EFQNAE--DNLEIVKTGITNrykdLSNTQIRSTITGMILDVPIKVGNSVIQANtfnDGTTIATVADMGDMLFRGNVDETD 228
Cdd:PRK11578 161 GTIDAQikRNQASLDTAKTN----LDYTRIVAPMAGEVTQITTLQGQTVIAAQ---QAPNILTLADMSTMLVKAQVSEAD 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 229 IGRLHAGMPVVLTIGAMQGTVLQATLEYISPKAADVNGIIMFEVKAAAKIPESVfVRAGYSANASIVTDSREGVLTLPES 308
Cdd:PRK11578 234 VIHLKPGQKAWFTVLGDPLTRYEGVLKDILPTPEKVNDAIFYYARFEVPNPNGL-LRLDMTAQVHIQLTDVKNVLTIPLS 312

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490458057 309 TI--QFEEGKPCVYILTSPEEspeqtfEKRDVTLGLSDGVNIEIVSGVTETDKV 360
Cdd:PRK11578 313 ALgdPVGDNRYKVKLLRNGET------REREVTIGARNDTDVEIVKGLEAGDEV 360
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 49-296 2.68e-17

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 81.70  E-value: 2.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057   49 VIASGKVEP-RDEVLIKPQISGIISEVLCKAGDRVKQGDVIATVKVIPEMGTLNAAES---------------------- 105
Cdd:pfam00529   8 VEAPGRVVVsGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAqlakaqaqvarlqaeldrlqal 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  106 -----------------------RVTVARLSLDQTRKEFERTEALYAKGVVSQEE-------FEKGQTTLRQAEEEF--- 152
Cdd:pfam00529  88 eselaisrqdydgataqlraaqaAVKAAQAQLAQAQIDLARRRVLAPIGGISRESlvtagalVAQAQANLLATVAQLdqi 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  153 -----QNAEDNLEIVKTG--------------ITNRYKDLSNTQIRSTITGMILDVPIKVGNSVIQAntfndGTTIATVA 213
Cdd:pfam00529 168 yvqitQSAAENQAEVRSElsgaqlqiaeaeaeLKLAKLDLERTEIRAPVDGTVAFLSVTVDGGTVSA-----GLRLMFVV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  214 DMGDMLFRGNVDETDIGRLHAGMPVVLTIGAMQGTV---LQATLEYISPKAADVngiimfEVKAAAKIPESVFVRAGYSA 290
Cdd:pfam00529 243 PEDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKtgrFTGVVVGISPDTGPV------RVVVDKAQGPYYPLRIGLSA 316


                  ....*.
gi 490458057  291 NASIVT 296
Cdd:pfam00529 317 GALVRL 322
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
 1-261 5.27e-13

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 69.22  E-value: 5.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057   1 MKKFLKIFLGILFLALLVGTFVFLWNKTRPVKVVYtlatpvhdtirqyviasGKVEPRdEVLIKPQISGIISEVLCKAGD 80
Cdd:PRK03598   2 KKKVVIGLAVVVLAAAVAGGWWWYQSRQDNGLTLY-----------------GNVDIR-TVNLGFRVGGRLASLAVDEGD 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  81 RVKQGDVIATVKVIPEMGTLNAAESRVTVARLSLDQTRK--------------------------EFERTEALYAKGVVS 134
Cdd:PRK03598  64 AVKAGQVLGELDAAPYENALMQAKANVSVAQAQLDLMLAgyrdeeiaqaraavkqaqaaydyaqnFYNRQQGLWKSRTIS 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 135 QEEFEKGQTTLRQAEEEFQNAEDNLEIVKTGitNRYKD---------------------LSNTQIRSTITGMILDVPIKV 193
Cdd:PRK03598 144 ANDLENARSSRDQAQATLKSAQDKLSQYREG--NRPQDiaqakaslaqaqaalaqaelnLQDTELIAPSDGTILTRAVEP 221

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490458057 194 GnSVIQAntfndGTTIATVADMGDMLFRGNVDETDIGRLHAGMPVVLTIGAMQGTVLQATLEYISPKA 261
Cdd:PRK03598 222 G-TMLNA-----GSTVFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFVSPTA 283
PRK09859 PRK09859
multidrug transporter subunit MdtE;
53-354 1.82e-12

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 67.82  E-value: 1.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  53 GKVEPRDEVLIKPQISGIISEVLCKAGDRVKQGDVIATVKVIPEMGTLNAAESRVTVARLSLDQTRKEFERTEALYAKGV 132
Cdd:PRK09859  54 GRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNY 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 133 VSQEEFEKGQTTLRQAEEefqnaedNLEIVKTGITNRYKDLSNTQIRSTITGMILDVPIKVGNSViqanTFNDGTTIATV 212
Cdd:PRK09859 134 VSRQDYDTARTQLNEAEA-------NVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALV----TANQADSLVTV 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 213 ADMG-----------DML-FRGNVDETDIGRLHAGMPVVLTIGAMQGTVLQATLEYISPKAADVNGIIMfeVKAAAKIPE 280
Cdd:PRK09859 203 QRLDpiyvdltqsvqDFLrMKEEVASGQIKQVQGSTPVQLNLENGKRYSQTGTLKFSDPTVDETTGSVT--LRAIFPNPN 280

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 281 SVFVrAGYSANASIVTDSREGVLTLP-ESTIQFEEGKPCVYILTSPEESPEQTFEKRD-------VTLGLSDGVNIeIVS 352
Cdd:PRK09859 281 GDLL-PGMYVTALVDEGSRQNVLLVPqEGVTHNAQGKATALILDKDDVVQLREIEASKaigdqwvVTSGLQAGDRV-IVS 358


                 ..
gi 490458057 353 GV 354
Cdd:PRK09859 359 GL 360
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 178-277 2.35e-11

HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.


Pssm-ID: 433206 [Multi-domain]  Cd Length: 104  Bit Score: 60.07  E-value: 2.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  178 IRSTITGMILDVPIKVGNsVIQAntfndGTTIATVADMGDMLFRGNVDETDIGRLHAGMPVVLTIGAMQGTVLQATLEYI 257
Cdd:pfam13437   2 IRAPVDGVVAELNVEEGQ-VVQA-----GDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRI 75

                          90       100
                  ....*....|....*....|
gi 490458057  258 SPKAADVNGIIMFEVKAAAK 277
Cdd:pfam13437  76 SPTVDPDTGVIPVRVSIENP 95
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 40-259 3.70e-10

Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.


Pssm-ID: 435440 [Multi-domain]  Cd Length: 214  Bit Score: 59.06  E-value: 3.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057   40 PVHDTIRqyviASGKVEP--RDEVLIKPQISGIISEVLCKA-GDRVKQGDVIATVKViPEmgtLNAAESrvtvarlsldq 116
Cdd:pfam16576   1 PLSRTIR----AVGRVAYdeRRLAHVHARVEGWIEKLYVNAtGDPVKKGQPLAELYS-PE---LVAAQQ----------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  117 trkefERTEALYAKGVVSQEEFekgqttLRQAEEEFQN----AEDNLEIVKTGITNRykdlsNTQIRSTITGMILDVPIK 192
Cdd:pfam16576  62 -----EYLLALRSGDALSKSEL------LRAARQRLRLlgmpEAQIAELERTGKVQP-----TVTVYAPISGVVTELNVR 125

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490458057  193 VGnSVIQAntfndGTTIATVADMGDMLFRGNVDETDIGRLHAGMPVVLTIGAMQGTVLQATLEYISP 259
Cdd:pfam16576 126 EG-MYVQP-----GDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKTFEGKVDYIYP 186
PRK10476 PRK10476
multidrug transporter subunit MdtN;
59-298 6.93e-10

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 59.66  E-value: 6.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  59 DEVLIKPQISGIISEVLCKAGDRVKQGDVIATVKVIPEMGTLNAAESRVTVARLSLDQTR-------------------- 118
Cdd:PRK10476  47 DVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLALADAQIMTTQrsvdaersnaasaneqvera 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 119 --------KEFERTEALYAKGVVSQEEFEKGQTTLRQAEEEFQNA-------------EDNLEI----VKTGITNRYKDL 173
Cdd:PRK10476 127 ranaklatRTLERLEPLLAKGYVSAQQVDQARTAQRDAEVSLNQAllqaqaaaaavggVDALVAqraaREAALAIAELHL 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 174 SNTQIRSTITGMILDVPIKVGNSVIQANtfndgtTIATVADMGDMLFRGNVDETDIGRLHAGMPVVLTIGAMQGTVLQAT 253
Cdd:PRK10476 207 EDTTVRAPFDGRVVGLKVSVGEFAAPMQ------PIFTLIDTDHWYAIANFRETDLKNIRVGDCATVYSMIDRGRPFEGK 280

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490458057 254 LEYISPKAADVNGIIM-------------------FEVKAAAKIPESVFVRAGYSANASIVTDS 298
Cdd:PRK10476 281 VDSIGWGVLPDDGGNVprglpyvprsinwvrvaqrFPVRIMLDKPDPELFRIGASAVVELRPGA 344
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
30-360 1.29e-08

MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 56.34  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  30 PVKVvytlATPVHDTIRQYVIASGKVEPRDEVLIKPQISGIISEVLCKAGDRVKQGDVIATVKVIPEMGTLNAAESRVTV 109
Cdd:PRK11556  61 PVQA----ATATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAK 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 110 ARLSLDQTRKEFERTEALYAKGVVSQEEFEKGQTTLRQaeeefqnAEDNLEIVKTGITNRYKDLSNTQIRSTITGMILDV 189
Cdd:PRK11556 137 DQATLANARRDLARYQQLAKTNLVSRQELDAQQALVSE-------TEGTIKADEASVASAQLQLDYSRITAPISGRVGLK 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 190 PIKVGNSVIQANTfnDGTTIATVADMGDMLFrgNVDETDIGRL----HAGMPVVL-------TIGAMQGTVLQ------A 252
Cdd:PRK11556 210 QVDVGNQISSGDT--TGIVVITQTHPIDLVF--TLPESDIATVvqaqKAGKPLVVeawdrtnSKKLSEGTLLSldnqidA 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 253 TLEYISPKAadvngiiMFEVKAAAKIPESvFVragysaNASIVTDSREGVLTLPESTIQFEEGKPCVYILTSpeespEQT 332
Cdd:PRK11556 286 TTGTIKLKA-------RFNNQDDALFPNQ-FV------NARMLVDTLQNAVVIPTAALQMGNEGHFVWVLND-----ENK 346

                        330       340
                 ....*....|....*....|....*...
gi 490458057 333 FEKRDVTLGLSDGVNIEIVSGVTETDKV 360
Cdd:PRK11556 347 VSKHLVTPGIQDSQKVVISAGLSAGDRV 374
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
 9-299 6.88e-08

type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 130902 [Multi-domain]  Cd Length: 423  Bit Score: 53.86  E-value: 6.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057    9 LGILFLALLVGTFvFLWNKTRPVKVVytlatpvhdtirqyVIASGKVEPRDEV-LIKPQISGIISEVLCKAGDRVKQGDV 87
Cdd:TIGR01843   6 LITWLIAGLVVIF-FLWAYFAPLDVV--------------ATATGKVVPSGNVkVVQHLEGGIVREILVREGDRVKAGQV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057   88 IatVKVIPEMGTLNAAESRVTVARLSLDQTR------------------------------------------------- 118
Cdd:TIGR01843  71 L--VELDATDVEADAAELESQVLRLEAEVARlraeadsqaaiefpddllsaedpavpelikgqqslfesrkstlraqlel 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  119 ------------------------------KEFERTEALYAKGVVSQEEFEKGQTTLRQAEEEFQNAEDNLEIVKTGIT- 167
Cdd:TIGR01843 149 ilaqikqleaelaglqaqlqalrqqlevisEELEARRKLKEKGLVSRLELLELERERAEAQGELGRLEAELEVLKRQIDe 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  168 ---------NRYK--------------------------DLSNTQIRSTITGMILDVPIKVGNSVIQAntfndGTTIATV 212
Cdd:TIGR01843 229 lqlerqqieQTFReevleelteaqarlaelrerlnkardRLQRLIIRSPVDGTVQSLKVHTVGGVVQP-----GETLMEI 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  213 ADMGD-MLFRGNVDETDIGRLHAGMPVVLTIGAMQGT---VLQATLEYISPKA-------ADV-NGIIMFEVKAAAKIPE 280
Cdd:TIGR01843 304 VPEDDpLEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRrygILNGKVKSISPDTftderggGPYyRVRISIDQNTLGIGPK 383

                         410
                  ....*....|....*....
gi 490458057  281 SVFVRAGYSANASIVTDSR 299
Cdd:TIGR01843 384 GLELSPGMPVTADIKTGER 402
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
59-108 1.33e-05

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 42.04  E-value: 1.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 490458057   59 DEVLIKPQISGIISEVLCKAGDRVKQGDVIATVKVIPEMGTLNAAESRVT 108
Cdd:pfam13533   1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
59-202 3.13e-05

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 45.12  E-value: 3.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  59 DEVLIKPQISGIISEVLCKAGDRVKQGDVIATVKVIPEMGTLNAAESRVTVARLSLDQTRKEFERTEALyakGV--VSQE 136
Cdd:PRK10559  46 DVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNRL---GVqaMSRE 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490458057 137 EFEKGQTTLRQAEEEFQNAEDNLEIVKTgitnrykDLSNTQIRSTITGMILDVPIKVGNSVIQANT 202
Cdd:PRK10559 123 EIDQANNVLQTVLHQLAKAQATRDLAKL-------DLERTVIRAPADGWVTNLNVYTGEFITRGST 181
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
59-241 6.61e-03

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 38.14  E-value: 6.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057  59 DEVLIKPQISGIISEVLCKAGDRVKQGDVIATVKVIPEMGTLNAAESrvTVARlSLDQTRKEFERTEALYAKGVVSQEEF 138
Cdd:PRK15136  60 NQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKT--ALAN-SVRQTHQLMINSKQYQANIELQKTAL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 139 EKGQTTLRQAE----------EEFQNAEDNLEIVK--------------------------------TGITNRYKDLSNT 176
Cdd:PRK15136 137 AQAQSDLNRRVplgnanligrEELQHARDAVASAQaqldvaiqqynanqamilntpledqpavqqaaTEVRNAWLALQRT 216

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490458057 177 QIRSTITGMILDVPIKVGNSViqantfNDGTTIATVADMGDMLFRGNVDETDIGRLHAGMPVVLT 241
Cdd:PRK15136 217 KIVSPMTGYVSRRSVQVGAQI------SPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATIT 275
OEP pfam02321
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ...
 100-161 7.04e-03

Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.


Pssm-ID: 396757 [Multi-domain]  Cd Length: 181  Bit Score: 37.12  E-value: 7.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490458057  100 LNAAESRVTVARLSLDQTRKEFERTEALYAKGVVSQEEFEKGQTTLRQAEEEFQNAEDNLEI 161
Cdd:pfam02321 110 LLAAKEQLELAEQALELAEEALELAEARYEAGLISLLDVLQAEVELLEARLELLNAEADLEL 171
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
102-161 9.21e-03

Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 37.71  E-value: 9.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490458057 102 AAESRVTVARLSLDQTRKEFERTEALYAKGVVSQEEFEKGQTTLRQAEEEFQNAEDNLEI 161
Cdd:COG1538   87 AAQEQLALAEENLALAEELLELARARYEAGLASRLDVLQAEAQLAQARAQLAQAEAQLAQ 146
 
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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