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Conserved domains on  [gi|1789665|gb|AAC76297|]
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multidrug efflux pump membrane fusion lipoprotein AcrE [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

efflux RND transporter periplasmic adaptor subunit( domain architecture ID 1001665)

efflux RND transporter periplasmic adaptor subunit similar to Escherichia coli Multidrug export protein AcrE, part of the tripartite efflux system AcrEF-TolC, which is involved in the efflux of indole and organic solvents

CATH:  1.20.1600.10
Gene Ontology:  GO:0022857|GO:0055085
SCOP:  4003096
TCDB:  8.A.1

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK15030 super family cl33066
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
1-384 0e+00

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


The actual alignment was detected with superfamily member PRK15030:

Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 517.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665     1 MTKHARFFLLPSFILISAAL-IAGCNDKGEEKAHVGEPQVTVHIVKTAPLEVKTELPGRTNAYRIAEVRPQVSGIVLNRN 79
Cdd:PRK15030   1 MNKNRGFTPLAVVLMLSGSLaLTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    80 FTEGSDVQAGQSLYQIDPATYQANYDSAKGELAKSEAAAAIAHLTVKRYVPLVGTKYISQQEYDQAIADARQADAAVIAA 159
Cdd:PRK15030  81 FKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   160 KATVESARINLAYTKVTAPISGRIGKSTVTEGALVTNGQTTELATVQQLDPIYVDVTQSSNDFMRLKQSVEQGNLHKENA 239
Cdd:PRK15030 161 KAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQELANGTLKQENG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   240 TSNVELVMENGQTYPLKGTLQFSDVTVDESTGSITLRAVFPNPQHTLLPGMFVRARIDEGVQPDAILIPQQGVSRTPRGD 319
Cdd:PRK15030 241 KAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGD 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1789665   320 ATVLIVNDKSQVEARPVVASQAIGDKWLISEGLKSGDQVIVSGLQKARPGEQVKA---TTDTPADTAS 384
Cdd:PRK15030 321 ATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAqevTADNNQQAAS 388
 
Name Accession Description Interval E-value
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
1-384 0e+00

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 517.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665     1 MTKHARFFLLPSFILISAAL-IAGCNDKGEEKAHVGEPQVTVHIVKTAPLEVKTELPGRTNAYRIAEVRPQVSGIVLNRN 79
Cdd:PRK15030   1 MNKNRGFTPLAVVLMLSGSLaLTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    80 FTEGSDVQAGQSLYQIDPATYQANYDSAKGELAKSEAAAAIAHLTVKRYVPLVGTKYISQQEYDQAIADARQADAAVIAA 159
Cdd:PRK15030  81 FKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   160 KATVESARINLAYTKVTAPISGRIGKSTVTEGALVTNGQTTELATVQQLDPIYVDVTQSSNDFMRLKQSVEQGNLHKENA 239
Cdd:PRK15030 161 KAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQELANGTLKQENG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   240 TSNVELVMENGQTYPLKGTLQFSDVTVDESTGSITLRAVFPNPQHTLLPGMFVRARIDEGVQPDAILIPQQGVSRTPRGD 319
Cdd:PRK15030 241 KAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGD 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1789665   320 ATVLIVNDKSQVEARPVVASQAIGDKWLISEGLKSGDQVIVSGLQKARPGEQVKA---TTDTPADTAS 384
Cdd:PRK15030 321 ATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAqevTADNNQQAAS 388
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 44-380 4.43e-97

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: 292.23  E-value: 4.43e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   44 VKTAPLEVKTELPGRTNAYRIAEVRPQVSGIVLNRNFTEGSDVQAGQSLYQIDPATYQANYDSAKGELAKSEAAAAIAHL 123
Cdd:COG0845   3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665  124 TVKRYVPLVGTKYISQQEYDQAIADARQADAAVIAAKATVESARINLAYTKVTAPISGRIGKSTVTEGALVTNGQTteLA 203
Cdd:COG0845  83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTP--LF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665  204 TVQQLDPIYVDVTQSSNDFMRLKQSveqgnlhkenatSNVELVMENGQTYPLKGTLQFSDVTVDESTGSITLRAVFPNPQ 283
Cdd:COG0845 161 TIADLDPLEVEFDVPESDLARLKVG------------QPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPD 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665  284 HTLLPGMFVRARIDEGVQPDAILIPQQGVSRTPRGDaTVLIVNDKSQVEARPVVASQAIGDKWLISEGLKSGDQVIVSGL 363
Cdd:COG0845 229 GLLRPGMFVRVRIVLGERENALLVPASAVVRDGGGA-YVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGL 307

                       330
                ....*....|....*..
gi 1789665  364 QKARPGEQVKATTDTPA 380
Cdd:COG0845 308 QRLRDGAKVRVVEAAAP 324
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 46-360 5.31e-86

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: 263.90  E-value: 5.31e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665     46 TAPLEVKTELPGRTNAYRIAE-VRPQVSGIVLNRNFTEGSDVQAGQSLYQIDPATYQANYDSAKGELAKSEAAAAIAHLT 124
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    125 VKRYVPLVGTKYISQQEYDQAIADARQADAAVIAAKATVESARINLAYTKVTAPISGRIGKSTVTEGALVTNGQTTELAT 204
Cdd:pfam00529  81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    205 VQQLDPIYVDVTQSSNDFMRL-KQSVEQGNLHKENATSNVELVMENGQTYPLK----GTLQFSDVTVDESTGSITLRAVF 279
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAEvRSELSGAQLQIAEAEAELKLAKLDLERTEIRapvdGTVAFLSVTVDGGTVSAGLRLMF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    280 PNP-QHTLLPGMFVRARIDEGVQPDAILIPQQGVSRTPRGDATVLIVNDKSQVEARPVVASQAIGDKWLISEGLKSGDQV 358
Cdd:pfam00529 241 VVPeDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALV 320


                  ..
gi 1789665    359 IV 360
Cdd:pfam00529 321 RL 322
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 39-375 6.49e-82

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: 253.39  E-value: 6.49e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665     39 VTVHIVKTAPLEVKTELPGRTNAYRIAEVRPQVSGIVLNRNFTEGSDVQAGQSLYQIDPATYQANYDSAKGELAKSEAAA 118
Cdd:TIGR01730   1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    119 AIAHLTVKRYVPLVGTKYISQQEYDQAIADARQADAAVIAAKATVESARINLAYTKVTAPISGRIGKSTVTEGALVTNGQ 198
Cdd:TIGR01730  81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    199 TteLATVQQLDPIYVDVTQSSNDFMRLkqsveqgnlhKENATSNVELVMENGQTYplKGTLQFSDVTVDESTGSITLRAV 278
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLPQL----------RRGQTLTVELDALPGEEF--KGKLRFIDPRVDSGTGTVRVRAT 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    279 FPNPQHTLLPGMFVRARIDEGVQPDAILIPQQGVSRTPRGDAtVLIVNDKSQVEARPVVASQAIGDKWLISEGLKSGDQV 358
Cdd:TIGR01730 227 FPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKY-VYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQI 305

                         330
                  ....*....|....*..
gi 1789665    359 IVSGLQKARPGEQVKAT 375
Cdd:TIGR01730 306 VTAGVVKLRDGAKVKVV 322
 
Name Accession Description Interval E-value
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
1-384 0e+00

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 517.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665     1 MTKHARFFLLPSFILISAAL-IAGCNDKGEEKAHVGEPQVTVHIVKTAPLEVKTELPGRTNAYRIAEVRPQVSGIVLNRN 79
Cdd:PRK15030   1 MNKNRGFTPLAVVLMLSGSLaLTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    80 FTEGSDVQAGQSLYQIDPATYQANYDSAKGELAKSEAAAAIAHLTVKRYVPLVGTKYISQQEYDQAIADARQADAAVIAA 159
Cdd:PRK15030  81 FKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   160 KATVESARINLAYTKVTAPISGRIGKSTVTEGALVTNGQTTELATVQQLDPIYVDVTQSSNDFMRLKQSVEQGNLHKENA 239
Cdd:PRK15030 161 KAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQELANGTLKQENG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   240 TSNVELVMENGQTYPLKGTLQFSDVTVDESTGSITLRAVFPNPQHTLLPGMFVRARIDEGVQPDAILIPQQGVSRTPRGD 319
Cdd:PRK15030 241 KAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGD 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1789665   320 ATVLIVNDKSQVEARPVVASQAIGDKWLISEGLKSGDQVIVSGLQKARPGEQVKA---TTDTPADTAS 384
Cdd:PRK15030 321 ATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAqevTADNNQQAAS 388
PRK09859 PRK09859
multidrug transporter subunit MdtE;
6-385 1.82e-122

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 359.03  E-value: 1.82e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665     6 RFFLLPsfILISAALIAGCNDKGEEKAHVGEPQVTVHIVKTAPLEVKTELPGRTNAYRIAEVRPQVSGIVLNRNFTEGSD 85
Cdd:PRK09859   5 RKLLIP--LLFCGAMLTACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    86 VQAGQSLYQIDPATYQANYDSAKGELAKSEAAAAIAHLTVKRYVPLVGTKYISQQEYDQAIADARQADAAVIAAKATVES 165
Cdd:PRK09859  83 VNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQ 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   166 ARINLAYTKVTAPISGRIGKSTVTEGALVTNGQTTELATVQQLDPIYVDVTQSSNDFMRLKQSVEQGNLHKENATSNVEL 245
Cdd:PRK09859 163 ATINLQYANVTSPITGVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLRMKEEVASGQIKQVQGSTPVQL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   246 VMENGQTYPLKGTLQFSDVTVDESTGSITLRAVFPNPQHTLLPGMFVRARIDEGVQPDAILIPQQGVSRTPRGDATVLIV 325
Cdd:PRK09859 243 NLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAQGKATALIL 322

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1789665   326 NDKSQVEARPVVASQAIGDKWLISEGLKSGDQVIVSGLQKARPGEQVKA--TTDTPADTASK 385
Cdd:PRK09859 323 DKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAisSSQENASTESK 384
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
6-384 1.00e-100

MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 303.64  E-value: 1.00e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665     6 RFFLLPsFILISAALIAGCNDKGEEKAHVGEPQVTVHIVKTAPLEVKTELPGRTNAYRIAEVRPQVSGIVLNRNFTEGSD 85
Cdd:PRK09578   6 RRRLLL-AALVALFVLAGCGKGDSDAAAAAPREATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    86 VQAGQSLYQIDPATYQANYDSAKGELAKSEAAAAIAHLTVKRYVPLVGTKYISQQEYDQAIADARQADAAVIAAKATVES 165
Cdd:PRK09578  85 VKQGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVADERQAKAAVASAKAELAR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   166 ARINLAYTKVTAPISGRIGKSTVTEGALVTNGQTTELATVQQLDPIYVDVTQSSNDFMRLKQSVEQGNLH-KENATSNVE 244
Cdd:PRK09578 165 AQLQLDYATVTAPIDGRARRALVTEGALVGQDQATPLTTVEQLDPIYVNFSQPAADVEALRRAVKSGRATgIAQQDVAVT 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   245 LVMENGQTYPLKGTLQFSDVTVDESTGSITLRAVFPNPQHTLLPGMFVRARIDEGVQPDAILIPQQGVSRTPrGDATVLI 324
Cdd:PRK09578 245 LVRADGSEYPLKGKLLFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTA-DSASVKV 323

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   325 VNDKSQVEARPVVASQAIGDKWLISEGLKSGDQVIVSGLQKARPGEQVKATTDTPADTAS 384
Cdd:PRK09578 324 VGQNGKVRDVEVEADQMSGRDWIVTRGLAGGERVIVDNAAQFAPGTAVKAVERAPAAKPA 383
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 44-380 4.43e-97

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: 292.23  E-value: 4.43e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   44 VKTAPLEVKTELPGRTNAYRIAEVRPQVSGIVLNRNFTEGSDVQAGQSLYQIDPATYQANYDSAKGELAKSEAAAAIAHL 123
Cdd:COG0845   3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665  124 TVKRYVPLVGTKYISQQEYDQAIADARQADAAVIAAKATVESARINLAYTKVTAPISGRIGKSTVTEGALVTNGQTteLA 203
Cdd:COG0845  83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTP--LF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665  204 TVQQLDPIYVDVTQSSNDFMRLKQSveqgnlhkenatSNVELVMENGQTYPLKGTLQFSDVTVDESTGSITLRAVFPNPQ 283
Cdd:COG0845 161 TIADLDPLEVEFDVPESDLARLKVG------------QPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPD 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665  284 HTLLPGMFVRARIDEGVQPDAILIPQQGVSRTPRGDaTVLIVNDKSQVEARPVVASQAIGDKWLISEGLKSGDQVIVSGL 363
Cdd:COG0845 229 GLLRPGMFVRVRIVLGERENALLVPASAVVRDGGGA-YVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGL 307

                       330
                ....*....|....*..
gi 1789665  364 QKARPGEQVKATTDTPA 380
Cdd:COG0845 308 QRLRDGAKVRVVEAAAP 324
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 46-360 5.31e-86

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: 263.90  E-value: 5.31e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665     46 TAPLEVKTELPGRTNAYRIAE-VRPQVSGIVLNRNFTEGSDVQAGQSLYQIDPATYQANYDSAKGELAKSEAAAAIAHLT 124
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    125 VKRYVPLVGTKYISQQEYDQAIADARQADAAVIAAKATVESARINLAYTKVTAPISGRIGKSTVTEGALVTNGQTTELAT 204
Cdd:pfam00529  81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    205 VQQLDPIYVDVTQSSNDFMRL-KQSVEQGNLHKENATSNVELVMENGQTYPLK----GTLQFSDVTVDESTGSITLRAVF 279
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAEvRSELSGAQLQIAEAEAELKLAKLDLERTEIRapvdGTVAFLSVTVDGGTVSAGLRLMF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    280 PNP-QHTLLPGMFVRARIDEGVQPDAILIPQQGVSRTPRGDATVLIVNDKSQVEARPVVASQAIGDKWLISEGLKSGDQV 358
Cdd:pfam00529 241 VVPeDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALV 320


                  ..
gi 1789665    359 IV 360
Cdd:pfam00529 321 RL 322
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 39-375 6.49e-82

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: 253.39  E-value: 6.49e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665     39 VTVHIVKTAPLEVKTELPGRTNAYRIAEVRPQVSGIVLNRNFTEGSDVQAGQSLYQIDPATYQANYDSAKGELAKSEAAA 118
Cdd:TIGR01730   1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    119 AIAHLTVKRYVPLVGTKYISQQEYDQAIADARQADAAVIAAKATVESARINLAYTKVTAPISGRIGKSTVTEGALVTNGQ 198
Cdd:TIGR01730  81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    199 TteLATVQQLDPIYVDVTQSSNDFMRLkqsveqgnlhKENATSNVELVMENGQTYplKGTLQFSDVTVDESTGSITLRAV 278
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLPQL----------RRGQTLTVELDALPGEEF--KGKLRFIDPRVDSGTGTVRVRAT 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    279 FPNPQHTLLPGMFVRARIDEGVQPDAILIPQQGVSRTPRGDAtVLIVNDKSQVEARPVVASQAIGDKWLISEGLKSGDQV 358
Cdd:TIGR01730 227 FPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKY-VYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQI 305

                         330
                  ....*....|....*..
gi 1789665    359 IVSGLQKARPGEQVKAT 375
Cdd:TIGR01730 306 VTAGVVKLRDGAKVKVV 322
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
57-383 1.56e-47

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


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 166.89  E-value: 1.56e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    57 GRTNAYRIAEVRPQVSGIVLNRNFTEGSDVQAGQSLYQIDPATYQANYDSAKGELAKSEAAAAIAHLTVKRYVPLVGTKY 136
Cdd:PRK11556  80 GTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   137 ISQQEYDQAIADARQADAAVIAAKATVESARINLAYTKVTAPISGRIGKSTVTEGALVTNGQTTELATVQQLDPIYVDVT 216
Cdd:PRK11556 160 VSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLVFT 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   217 QSSNDFMRLKQSveqgnlHKENATSNVELVMENGQTYPLKGTLQFSDVTVDESTGSITLRAVFPNPQHTLLPGMFVRARI 296
Cdd:PRK11556 240 LPESDIATVVQA------QKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFVNARM 313

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   297 DEGVQPDAILIPQQGVSRTPRGDaTVLIVNDKSQVEARPVVASQAIGDKWLISEGLKSGDQVIVSGLQKARPGEQVKATT 376
Cdd:PRK11556 314 LVDTLQNAVVIPTAALQMGNEGH-FVWVLNDENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEVVE 392


                 ....*..
gi 1789665   377 DTPADTA 383
Cdd:PRK11556 393 PQSATTP 399
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
57-299 9.54e-20

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 88.95  E-value: 9.54e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   57 GRTNAyRIAEVRPQVSGIVLNRNFTEGSDVQAGQSLYQIDPATYQANYDSAKGELAKSEAAAAIAHLTV----------- 125
Cdd:COG1566  39 GRVEA-RVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLEAELgaeaeiaaaea 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665  126 ----------------KRYVPLVGTKYISQQEYDQA-----------------IADARQADAAVIAAKAT---------- 162
Cdd:COG1566 118 qlaaaqaqldlaqrelERYQALYKKGAVSQQELDEAraaldaaqaqleaaqaqLAQAQAGLREEEELAAAqaqvaqaeaa 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665  163 VESARINLAYTKVTAPISGRIGKSTVTEGALVTNGQTteLATVQQLDPIYVDVTQSSND--FMRLKQSVEqgnlhkenat 240
Cdd:COG1566 198 LAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQP--LLTIVPLDDLWVEAYVPETDlgRVKPGQPVE---------- 265

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665  241 snVELVMENGQTYplKGTLQF------SDVTVDESTGSITL----RAVFPNPQ-HTLLPGMFVRARIDEG 299
Cdd:COG1566 266 --VRVDAYPDRVF--EGKVTSispgagFTSPPKNATGNVVQrypvRIRLDNPDpEPLRPGMSATVEIDTE 331
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
 6-361 2.31e-11

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 64.41  E-value: 2.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665     6 RFFLLPSFILISAALIAgcndkgeEKAHVGEPQVTVHIVKTAPLEVKTELPGRTNAYRIAEVRPQVSGIVLNRNFTEGSD 85
Cdd:PRK11578  10 RYLIALVIVLAGGITLW-------RILNAPVPTYQTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIGDK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    86 VQAGQSLYQIDPATYQ-------ANYDSAKGELAKSEAAAAIAHLTVKRYVPLVGTKYISQQEYDQAIAD--ARQADAAV 156
Cdd:PRK11578  83 VKKDQLLGVIDPEQAEnqikeveATLMELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDTAATElaVKQAQIGT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   157 -----IAAKATVESARINLAYTKVTAPISGRIGKSTVTEGALVTNGQTT-ELATVQQLDPIYVDVTQSSNDFMRLKQSve 230
Cdd:PRK11578 163 idaqiKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQApNILTLADMSTMLVKAQVSEADVIHLKPG-- 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   231 qgnlHKENATsnvelVMENGQTYpLKGTLQFSDVTVDESTGSITLRAVF--PNPQHTLLPGMFVRARIDEGVQPDAILIP 308
Cdd:PRK11578 241 ----QKAWFT-----VLGDPLTR-YEGVLKDILPTPEKVNDAIFYYARFevPNPNGLLRLDMTAQVHIQLTDVKNVLTIP 310

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1789665   309 QQGVSRTPRGDATVLIVNDKSQVEARPVVASQAIGDKWLISEGLKSGDQVIVS 361
Cdd:PRK11578 311 LSALGDPVGDNRYKVKLLRNGETREREVTIGARNDTDVEIVKGLEAGDEVIIG 363
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 48-292 3.37e-11

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: 62.14  E-value: 3.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665     48 PLEVKTELPGR--TNAYRIAEVRPQVSGIV--LNRNFTeGSDVQAGQSLYQIdpatyqanydsakgelakseaaaaiahl 123
Cdd:pfam16576   1 PLSRTIRAVGRvaYDERRLAHVHARVEGWIekLYVNAT-GDPVKKGQPLAEL---------------------------- 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    124 tvkrYVP-LVGTkyisQQEYDQAIADARQADAAVIaakatVESAR------------IN-LAYTK-------VTAPISGR 182
Cdd:pfam16576  52 ----YSPeLVAA----QQEYLLALRSGDALSKSEL-----LRAARqrlrllgmpeaqIAeLERTGkvqptvtVYAPISGV 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    183 IGKSTVTEGALVTNGQTteLATVQQLDP--IYVDVTQSSNDFMRLKQSVEqgnlhkenatsnVELVMENGQTYplKGTLQ 260
Cdd:pfam16576 119 VTELNVREGMYVQPGDT--LFTIADLSTvwVEADVPEQDLALVKVGQPAE------------VTLPALPGKTF--EGKVD 182

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1789665    261 FSDVTVDESTGSITLRAVFPNPQHTLLPGMFV 292
Cdd:pfam16576 183 YIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
53-213 5.53e-08

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 53.98  E-value: 5.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    53 TELPGRTNAYRIAEV---RPQVSGIVLNRNFTEGSDVQAGQSLYQIDPATYQANYDSAKGELAKSEAAAAIAHLTVKRYV 129
Cdd:PRK10559  33 TESPWTRDARFSADVvaiAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRN 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   130 PLvGTKYISQQEYDQAIADARQADAAVIAAKATVESARINLAYTKVTAPISGRIGKSTVTEGALVTNGqTTELATVQQlD 209
Cdd:PRK10559 113 RL-GVQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRG-STAVALVKQ-N 189


                 ....
gi 1789665   210 PIYV 213
Cdd:PRK10559 190 SFYV 193
PRK10476 PRK10476
multidrug transporter subunit MdtN;
64-199 3.63e-06

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 48.48  E-value: 3.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    64 IAEVRPQVSGIVLNRNFTEGSDVQAGQSLYQIDPATYQANYDSAKGELA----------------------------KSE 115
Cdd:PRK10476  48 VVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLAladaqimttqrsvdaersnaasaneqveRAR 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   116 AAAAIAHLTVKRYVPLVGTKYISQQEYDQA----------IADARQADAAVIAAKATVES--------------ARINLA 171
Cdd:PRK10476 128 ANAKLATRTLERLEPLLAKGYVSAQQVDQArtaqrdaevsLNQALLQAQAAAAAVGGVDAlvaqraareaalaiAELHLE 207

                        170       180
                 ....*....|....*....|....*...
gi 1789665   172 YTKVTAPISGRIGKSTVTEGALVTNGQT 199
Cdd:PRK10476 208 DTTVRAPFDGRVVGLKVSVGEFAAPMQP 235
PRK09783 PRK09783
copper/silver efflux system membrane fusion protein CusB; Provisional
 167-363 1.43e-05

copper/silver efflux system membrane fusion protein CusB; Provisional


Pssm-ID: 236625 [Multi-domain]  Cd Length: 409  Bit Score: 46.78  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   167 RINLAYTkVTAPISGRIGKSTVTEGALVTNGQTteLATVQQLDPIYVDVtqssndfmrlkqSVEQGNLHKENATSNVELV 246
Cdd:PRK09783 205 KIQTRFT-LKAPIDGVITAFDLRAGMNIAKDNV--VAKIQGMDPVWVTA------------AIPESIAWLVKDASQFTLT 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   247 MEngqTYPLKgTLQFSDVT----VDESTGSITLRAVFPNPQHTLLPGMFVRARIDEGVQPdAILIPQQGVSRTPRGDATV 322
Cdd:PRK09783 270 VP---ARPDK-TFTIRKWTllpsVDAATRTLQLRLEVDNADEALKPGMNAWLQLNTASEP-MLLIPSQALIDTGSEQRVI 344

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 1789665   323 LIVNDKSQVEARPVVASQAIGDKwLISEGLKSGDQVIVSGL 363
Cdd:PRK09783 345 TVDADGRFVPKRVAVFQESQGVT-AIRSGLAEGEKVVSSGL 384
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 174-289 7.31e-05

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: 41.58  E-value: 7.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    174 KVTAPISGRIGKSTVTEGALVTNGQttELATVQQLDPIYVDVTQSSNDFMRLKQSVEqgnlhkenatsnVELVMENGQTY 253
Cdd:pfam13437   1 TIRAPVDGVVAELNVEEGQVVQAGD--PLATIVPPDRLLVEAFVPAADLGSLKKGQK------------VTLKLDPGSDY 66

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1789665    254 PLKGTLQFSDVTVDESTGSITLRAVFPNPQH--TLLPG 289
Cdd:pfam13437  67 TLEGKVVRISPTVDPDTGVIPVRVSIENPKTpiPLLPG 104
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
65-112 2.29e-04

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 38.58  E-value: 2.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1789665     65 AEVRPQVSGIVLNRNFTEGSDVQAGQSLYQIDPATYQANYDSAKGELA 112
Cdd:pfam13533   3 VKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
 71-213 5.96e-04

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 41.49  E-value: 5.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665    71 VSGIVLNRNFTEGSDVQAGQSLYQIDPATY-------QANYDSAKGELAK-------------------SEAAAAIAHLT 124
Cdd:PRK03598  50 VGGRLASLAVDEGDAVKAGQVLGELDAAPYenalmqaKANVSVAQAQLDLmlagyrdeeiaqaraavkqAQAAYDYAQNF 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789665   125 VKRYVPLVGTKYISQQEYDQAI-----ADAR---------------------QADAAVIAAKATVESARINLAYTKVTAP 178
Cdd:PRK03598 130 YNRQQGLWKSRTISANDLENARssrdqAQATlksaqdklsqyregnrpqdiaQAKASLAQAQAALAQAELNLQDTELIAP 209

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 1789665   179 ISGRIGKSTVTEGALVTNGQTteLATVQQLDPIYV 213
Cdd:PRK03598 210 SDGTILTRAVEPGTMLNAGST--VFTLSLTRPVWV 242
 
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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