NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2290489425|gb|UVP15083|]
View 

efflux RND transporter periplasmic adaptor subunit [Bacteroides fragilis]

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
47-356 1.70e-64

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: 207.49  E-value: 1.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425  47 MTLKKQIFNHELVSNGKISARGMADLRFESGEVIAHIWVKNGDRVRKGQKLAELDKFKLDNQLSQSEDALKKSELELRDV 126
Cdd:COG0845     1 MKVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 127 ---------LISQGYpaddISQVPEETMK--LAKVKSGYDQSKSQYEMSKYNAEHATLTAPFDGVVANLFSKPYNLASTS 195
Cdd:COG0845    81 kaelerykaLLKKGA----VSQQELDQAKaaLDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 196 DVFCTVIDMQGMEVDFTVLESELPLIKNGDKVVIKPYSDAATVHEGSISEINPLVDDK-GMVKVKARV-NGAGKLFSGMN 273
Cdd:COG0845   157 TPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPAtRTVRVRAELpNPDGLLRPGMF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 274 VRVSVH-RSLGEQLVIPKSAVVLRSGKQVVFTLKDGKMAQWNYIHTALENADSYSVADGLTEGDTVIVSGNINLAHEAPV 352
Cdd:COG0845   237 VRVRIVlGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKV 316

                  ....
gi 2290489425 353 TIIE 356
Cdd:COG0845   317 RVVE 320
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
47-356 1.70e-64

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: 207.49  E-value: 1.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425  47 MTLKKQIFNHELVSNGKISARGMADLRFESGEVIAHIWVKNGDRVRKGQKLAELDKFKLDNQLSQSEDALKKSELELRDV 126
Cdd:COG0845     1 MKVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 127 ---------LISQGYpaddISQVPEETMK--LAKVKSGYDQSKSQYEMSKYNAEHATLTAPFDGVVANLFSKPYNLASTS 195
Cdd:COG0845    81 kaelerykaLLKKGA----VSQQELDQAKaaLDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 196 DVFCTVIDMQGMEVDFTVLESELPLIKNGDKVVIKPYSDAATVHEGSISEINPLVDDK-GMVKVKARV-NGAGKLFSGMN 273
Cdd:COG0845   157 TPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPAtRTVRVRAELpNPDGLLRPGMF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 274 VRVSVH-RSLGEQLVIPKSAVVLRSGKQVVFTLKDGKMAQWNYIHTALENADSYSVADGLTEGDTVIVSGNINLAHEAPV 352
Cdd:COG0845   237 VRVRIVlGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKV 316

                  ....
gi 2290489425 353 TIIE 356
Cdd:COG0845   317 RVVE 320
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
44-355 8.05e-44

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: 153.62  E-value: 8.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425  44 VSVMTLKKQIFNHELVSNGKISARGMADLRFESGEVIAHIWVKNGDRVRKGQKLAELD--KFKLDNQLSQSEDALKKSEL 121
Cdd:TIGR01730   1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDddDYQLALQAALAQLAAAEAQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 122 ELRDV------------LISQgypADDISQVPEETMKLAKVKSgydqSKSQYEMSKYNAEHATLTAPFDGVVANLFSKPY 189
Cdd:TIGR01730  81 ELAQRsferaerlvkrnAVSQ---ADLDDAKAAVEAAQADLEA----AKASLASAQLNLRYTEIRAPFDGTIGRRLVEVG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 190 NLASTSDVFCTVIDMQGMEVDFTVLESELPLIKNGDKVVIKPYSDAATVHEGSISEINPLVDDK-GMVKVKARV-NGAGK 267
Cdd:TIGR01730 154 AYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGtGTVRVRATFpNPDGR 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 268 LFSGMNVRVSVH-RSLGEQLVIPKSAVVLRSGKQVVFTLKDGKMAQWNYIHTALENADSYSVADGLTEGDTVIVSGNINL 346
Cdd:TIGR01730 234 LLPGMFGRVTISlKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKL 313

                  ....*....
gi 2290489425 347 AHEAPVTII 355
Cdd:TIGR01730 314 RDGAKVKVV 322
PRK09859 PRK09859
multidrug transporter subunit MdtE;
10-342 1.23e-12

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 68.20  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425  10 LCLALTMLTACSGEEKESAS----EKGVETVLPDTKNEVSVMTlkkqifnhelvsnGKISARGMADLRFESGEVIAHIWV 85
Cdd:PRK09859   11 LLFCGAMLTACDDKSAENAAamtpEVGVVTLSPGSVNVLSELP-------------GRTVPYEVAEIRPQVGGIIIKRNF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425  86 KNGDRVRKGQKLAELDKFKLDNQLSQSEDALKKSELELRDVLISQGYPA-----DDISQVPEETMK--LAKVKSGYDQSK 158
Cdd:PRK09859   78 IEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQAsllktNYVSRQDYDTARtqLNEAEANVTVAK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 159 SQYEMSKYNAEHATLTAPFDGVV--ANLFSKPYNLASTSDVFCTVIDMQGMEVDFT------------VLESELPLIKNG 224
Cdd:PRK09859  158 AAVEQATINLQYANVTSPITGVSgkSSVTVGALVTANQADSLVTVQRLDPIYVDLTqsvqdflrmkeeVASGQIKQVQGS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 225 DKVVIKPYSDAATVHEGSISEINPLVDDK-GMVKVKARV-NGAGKLFSGMNVRVSVHR-SLGEQLVIPKSAVVLRS-GKQ 300
Cdd:PRK09859  238 TPVQLNLENGKRYSQTGTLKFSDPTVDETtGSVTLRAIFpNPNGDLLPGMYVTALVDEgSRQNVLLVPQEGVTHNAqGKA 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2290489425 301 VVFTLKDGKMAQWNYIHTALENADSYSVADGLTEGDTVIVSG 342
Cdd:PRK09859  318 TALILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSG 359
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
172-262 4.33e-09

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: 53.52  E-value: 4.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 172 TLTAPFDGVVANLFSKPYNLASTSDVFCTVIDMQGMEVDFTVLESELPLIKNGDKVVIKPYSDAATVHEGSISEINPLVD 251
Cdd:pfam13437   1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVD 80
                          90
                  ....*....|..
gi 2290489425 252 -DKGMVKVKARV 262
Cdd:pfam13437  81 pDTGVIPVRVSI 92
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
47-356 1.70e-64

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: 207.49  E-value: 1.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425  47 MTLKKQIFNHELVSNGKISARGMADLRFESGEVIAHIWVKNGDRVRKGQKLAELDKFKLDNQLSQSEDALKKSELELRDV 126
Cdd:COG0845     1 MKVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 127 ---------LISQGYpaddISQVPEETMK--LAKVKSGYDQSKSQYEMSKYNAEHATLTAPFDGVVANLFSKPYNLASTS 195
Cdd:COG0845    81 kaelerykaLLKKGA----VSQQELDQAKaaLDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 196 DVFCTVIDMQGMEVDFTVLESELPLIKNGDKVVIKPYSDAATVHEGSISEINPLVDDK-GMVKVKARV-NGAGKLFSGMN 273
Cdd:COG0845   157 TPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPAtRTVRVRAELpNPDGLLRPGMF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 274 VRVSVH-RSLGEQLVIPKSAVVLRSGKQVVFTLKDGKMAQWNYIHTALENADSYSVADGLTEGDTVIVSGNINLAHEAPV 352
Cdd:COG0845   237 VRVRIVlGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKV 316

                  ....
gi 2290489425 353 TIIE 356
Cdd:COG0845   317 RVVE 320
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
44-355 8.05e-44

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: 153.62  E-value: 8.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425  44 VSVMTLKKQIFNHELVSNGKISARGMADLRFESGEVIAHIWVKNGDRVRKGQKLAELD--KFKLDNQLSQSEDALKKSEL 121
Cdd:TIGR01730   1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDddDYQLALQAALAQLAAAEAQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 122 ELRDV------------LISQgypADDISQVPEETMKLAKVKSgydqSKSQYEMSKYNAEHATLTAPFDGVVANLFSKPY 189
Cdd:TIGR01730  81 ELAQRsferaerlvkrnAVSQ---ADLDDAKAAVEAAQADLEA----AKASLASAQLNLRYTEIRAPFDGTIGRRLVEVG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 190 NLASTSDVFCTVIDMQGMEVDFTVLESELPLIKNGDKVVIKPYSDAATVHEGSISEINPLVDDK-GMVKVKARV-NGAGK 267
Cdd:TIGR01730 154 AYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGtGTVRVRATFpNPDGR 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 268 LFSGMNVRVSVH-RSLGEQLVIPKSAVVLRSGKQVVFTLKDGKMAQWNYIHTALENADSYSVADGLTEGDTVIVSGNINL 346
Cdd:TIGR01730 234 LLPGMFGRVTISlKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKL 313

                  ....*....
gi 2290489425 347 AHEAPVTII 355
Cdd:TIGR01730 314 RDGAKVKVV 322
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
55-279 7.77e-24

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 100.12  E-value: 7.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425  55 NHELVSNGKISARgMADLRFESGEVIAHIWVKNGDRVRKGQKLAELDKFKLDNQLSQSEDALKKSELELRDVLISQGYPA 134
Cdd:COG1566    32 DEPVTADGRVEAR-VVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGAEA 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 135 D------DISQVpEETMKLAK---------VKSG------YDQSKSQYEMSK---------------------------- 165
Cdd:COG1566   111 EiaaaeaQLAAA-QAQLDLAQreleryqalYKKGavsqqeLDEARAALDAAQaqleaaqaqlaqaqaglreeeelaaaqa 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 166 -------------YNAEHATLTAPFDGVVANLFSKPYNLASTSDVFCTVIDMQGMEVDFTVLESELPLIKNGDKVVIKPY 232
Cdd:COG1566   190 qvaqaeaalaqaeLNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVD 269
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 233 SDAATVHEGSISEINPLVD-----------DKGMVKVKARVNGA--GKLFSGMNVRVSVH 279
Cdd:COG1566   270 AYPDRVFEGKVTSISPGAGftsppknatgnVVQRYPVRIRLDNPdpEPLRPGMSATVEID 329
PRK09859 PRK09859
multidrug transporter subunit MdtE;
10-342 1.23e-12

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 68.20  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425  10 LCLALTMLTACSGEEKESAS----EKGVETVLPDTKNEVSVMTlkkqifnhelvsnGKISARGMADLRFESGEVIAHIWV 85
Cdd:PRK09859   11 LLFCGAMLTACDDKSAENAAamtpEVGVVTLSPGSVNVLSELP-------------GRTVPYEVAEIRPQVGGIIIKRNF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425  86 KNGDRVRKGQKLAELDKFKLDNQLSQSEDALKKSELELRDVLISQGYPA-----DDISQVPEETMK--LAKVKSGYDQSK 158
Cdd:PRK09859   78 IEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQAsllktNYVSRQDYDTARtqLNEAEANVTVAK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 159 SQYEMSKYNAEHATLTAPFDGVV--ANLFSKPYNLASTSDVFCTVIDMQGMEVDFT------------VLESELPLIKNG 224
Cdd:PRK09859  158 AAVEQATINLQYANVTSPITGVSgkSSVTVGALVTANQADSLVTVQRLDPIYVDLTqsvqdflrmkeeVASGQIKQVQGS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 225 DKVVIKPYSDAATVHEGSISEINPLVDDK-GMVKVKARV-NGAGKLFSGMNVRVSVHR-SLGEQLVIPKSAVVLRS-GKQ 300
Cdd:PRK09859  238 TPVQLNLENGKRYSQTGTLKFSDPTVDETtGSVTLRAIFpNPNGDLLPGMYVTALVDEgSRQNVLLVPQEGVTHNAqGKA 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2290489425 301 VVFTLKDGKMAQWNYIHTALENADSYSVADGLTEGDTVIVSG 342
Cdd:PRK09859  318 TALILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSG 359
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
44-356 1.14e-11

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


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 65.58  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425  44 VSVMTLKKQIFNHELVSNGKISARGMADLRFE-SGEVIAhIWVKNGDRVRKGQKLAELDKFKLDNQLSQSEDALKKSELE 122
Cdd:PRK11556   62 VQAATATEQAVPRYLTGLGTVTAANTVTVRSRvDGQLMA-LHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQAT 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 123 L----RDV----------LISQGYPADDISQVPEETMKLAKVKSGYDQSKSQYEMSKynaehatLTAPFDGVVANLFSKP 188
Cdd:PRK11556  141 LanarRDLaryqqlaktnLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSR-------ITAPISGRVGLKQVDV 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 189 YNLASTSDVFCTVIDMQGMEVD--FTVLESELPLI----KNGDKVVIKPY--SDAATVHEGSISEINPLVD-DKGMVKVK 259
Cdd:PRK11556  214 GNQISSGDTTGIVVITQTHPIDlvFTLPESDIATVvqaqKAGKPLVVEAWdrTNSKKLSEGTLLSLDNQIDaTTGTIKLK 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 260 ARV-NGAGKLFSG--MNVRVSVHrSLGEQLVIPKSAVVLRSGKQVVFTLKDGKMAQWNYIHTALENADSYSVADGLTEGD 336
Cdd:PRK11556  294 ARFnNQDDALFPNqfVNARMLVD-TLQNAVVIPTAALQMGNEGHFVWVLNDENKVSKHLVTPGIQDSQKVVISAGLSAGD 372
                         330       340
                  ....*....|....*....|
gi 2290489425 337 TVIVSGNINLAHEAPVTIIE 356
Cdd:PRK11556  373 RVVTDGIDRLTEGAKVEVVE 392
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
172-262 4.33e-09

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: 53.52  E-value: 4.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 172 TLTAPFDGVVANLFSKPYNLASTSDVFCTVIDMQGMEVDFTVLESELPLIKNGDKVVIKPYSDAATVHEGSISEINPLVD 251
Cdd:pfam13437   1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVD 80
                          90
                  ....*....|..
gi 2290489425 252 -DKGMVKVKARV 262
Cdd:pfam13437  81 pDTGVIPVRVSI 92
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
76-341 2.73e-08

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 54.78  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425  76 SGEvIAHIWVKNGDRVRKGQKLAELDKFKLDNQLSQSEDALK---------KSELELRDVLIS--------QGYPADDIS 138
Cdd:PRK11578   69 SGQ-LKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATLMelraqrqqaEAELKLARVTLSrqqrlaktQAVSQQDLD 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 139 QVPEE-TMKLAKV---KSGYDQSKSQYEMSKYNAEHATLTAPFDGVVAN---LFSKPYNLASTSDVFCTVIDMQGMEVDF 211
Cdd:PRK11578  148 TAATElAVKQAQIgtiDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQittLQGQTVIAAQQAPNILTLADMSTMLVKA 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 212 TVLESELPLIKNGDKVVIKPYSDAATVHEGSISEINPL---VDDKGMVKVKARV-NGAGKLFSGMNVRVSVH-RSLGEQL 286
Cdd:PRK11578  228 QVSEADVIHLKPGQKAWFTVLGDPLTRYEGVLKDILPTpekVNDAIFYYARFEVpNPNGLLRLDMTAQVHIQlTDVKNVL 307
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2290489425 287 VIPKSAVvlrsGKQV------VFTLKDGKMAQWNYIHTALENADSySVADGLTEGDTVIVS 341
Cdd:PRK11578  308 TIPLSAL----GDPVgdnrykVKLLRNGETREREVTIGARNDTDV-EIVKGLEAGDEVIIG 363
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
57-278 1.57e-07

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: 52.43  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425  57 ELVSNGKISARGMAD-LRFESGEVIAHIWVKNGDRVRKGQKLAELDK-------FKLDNQLSQSEDALKKSELELR---- 124
Cdd:pfam00529   7 GVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPtdyqaalDSAEAQLAKAQAQVARLQAELDrlqa 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 125 ---DVLISQGYPADDISQVPEETMKLAKVKSGYDQSKSQY---------------------------------------- 161
Cdd:pfam00529  87 lesELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLarrrvlapiggisreslvtagalvaqaqanllatvaqldq 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 162 ----------------------------------EMSKYNAEHATLTAPFDGVVANLFSKPY-NLASTSDVFCTVIDMQG 206
Cdd:pfam00529 167 iyvqitqsaaenqaevrselsgaqlqiaeaeaelKLAKLDLERTEIRAPVDGTVAFLSVTVDgGTVSAGLRLMFVVPEDN 246
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2290489425 207 MEVDFTVLESELPLIKNGDKVVIKPYSDAATVHEGSISEINPLVDDKGMVKVKARVNGAGKlfsgMNVRVSV 278
Cdd:pfam00529 247 LLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPY----YPLRIGL 314
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
88-274 2.04e-07

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: 50.97  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425  88 GDRVRKGQKLAELDKFKLDN------QLSQSEDALKKSELEL--RDVLISQGYPADDISQVpeetmklakVKSGydqsKS 159
Cdd:pfam16576  39 GDPVKKGQPLAELYSPELVAaqqeylLALRSGDALSKSELLRaaRQRLRLLGMPEAQIAEL---------ERTG----KV 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 160 QYEMskynaehaTLTAPFDGVVANL------FSKP----YNLASTSDVFctvidmqgmeVDFTVLESELPLIKNGDKVVI 229
Cdd:pfam16576 106 QPTV--------TVYAPISGVVTELnvregmYVQPgdtlFTIADLSTVW----------VEADVPEQDLALVKVGQPAEV 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2290489425 230 KPYSDAATVHEGSISEINPLVDDKGMVkVKARV---NGAGKLFSGMNV 274
Cdd:pfam16576 168 TLPALPGKTFEGKVDYIYPTLDPKTRT-VRVRIelpNPDGRLKPGMFA 214
PRK09783 PRK09783
copper/silver efflux system membrane fusion protein CusB; Provisional
172-353 3.92e-06

copper/silver efflux system membrane fusion protein CusB; Provisional


Pssm-ID: 236625 [Multi-domain]  Cd Length: 409  Bit Score: 48.33  E-value: 3.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 172 TLTAPFDGVVANL-FSKPYNLASTSdvfcTVIDMQGME---VDFTVLESELPLIKNGDKVVIK-PYSDAATVHegsISEI 246
Cdd:PRK09783  211 TLKAPIDGVITAFdLRAGMNIAKDN----VVAKIQGMDpvwVTAAIPESIAWLVKDASQFTLTvPARPDKTFT---IRKW 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 247 N--PLVDDKG-MVKVKARVNGA-GKLFSGMNVRVSVHRSLGEQLVIPKSAVVLRSGKQVVFTL-KDGKMAQwNYIHTALE 321
Cdd:PRK09783  284 TllPSVDAATrTLQLRLEVDNAdEALKPGMNAWLQLNTASEPMLLIPSQALIDTGSEQRVITVdADGRFVP-KRVAVFQE 362
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2290489425 322 NADSYSVADGLTEGDTVIVSGNINLAHEAPVT 353
Cdd:PRK09783  363 SQGVTAIRSGLAEGEKVVSSGLFLIDSEANIS 394
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
79-117 1.06e-04

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 39.35  E-value: 1.06e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2290489425  79 VIAHIWVKNGDRVRKGQKLAELDKFKLDNQLSQSEDALK 117
Cdd:pfam13533  12 KVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
PRK10476 PRK10476
multidrug transporter subunit MdtN;
108-298 4.35e-04

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 41.94  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 108 QLSQSEDALKKSELELRDVLISQGYPADDISQVPEEtmkLAKVksgyDQSKSQYEMSKYNAEHATLTAPFDGVVANLFSK 187
Cdd:PRK10476  153 QVDQARTAQRDAEVSLNQALLQAQAAAAAVGGVDAL---VAQR----AAREAALAIAELHLEDTTVRAPFDGRVVGLKVS 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425 188 PYNLASTSDVFCTVIDMQGMEVDFTVLESELPLIKNGDKVVIKPYSDAATVHEGSISEINPLV--DDKGMV-----KVKA 260
Cdd:PRK10476  226 VGEFAAPMQPIFTLIDTDHWYAIANFRETDLKNIRVGDCATVYSMIDRGRPFEGKVDSIGWGVlpDDGGNVprglpYVPR 305
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2290489425 261 RVN--GAGKLFSgmnVRVSVHRSLGEQLVIPKSAVV-LRSG 298
Cdd:PRK10476  306 SINwvRVAQRFP---VRIMLDKPDPELFRIGASAVVeLRPG 343
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
76-175 2.49e-03

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: 39.61  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425  76 SGEVIAHIWVKNGDRVRKGQKLAELD-------KFKLDNQLSQSE------DALKKSEL--ELRDVLISQGYPADDiSQV 140
Cdd:TIGR01843  50 EGGIVREILVREGDRVKAGQVLVELDatdveadAAELESQVLRLEaevarlRAEADSQAaiEFPDDLLSAEDPAVP-ELI 128
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2290489425 141 PEETMKLAKVKSGYDQSKSQY--EMSKYNAEHATLTA 175
Cdd:TIGR01843 129 KGQQSLFESRKSTLRAQLELIlaQIKQLEAELAGLQA 165
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
71-162 5.20e-03

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 38.40  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290489425  71 DLRFESGEVIAHIWVKNGDRVRKGQKLAELDKFKLDNQLSQSEDALKKSELELrdVLISQGYPADDISQVPEEtmkLAKV 150
Cdd:PRK03598   45 NLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQL--DLMLAGYRDEEIAQARAA---VKQA 119
                          90
                  ....*....|..
gi 2290489425 151 KSGYDQSKSQYE 162
Cdd:PRK03598  120 QAAYDYAQNFYN 131
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH