|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
45-355 |
3.24e-63 |
|
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: 204.41 E-value: 3.24e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 45 QFSGSIRAGNTTGIGFELAGKLQKLLVDTGDRVKPGQLLAQLDTSLLEAEQTELQAALDQNQADISLARATLKRSLELSA 124
Cdd:COG0845 13 EATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAELERYKALLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 125 KQYLSEQQLDELKGKLASLEAGHARLEASLKANELKRQKSLLIAPFAGVIAAREHNLGEVIALGSPVFTLVQSDNLQALI 204
Cdd:COG0845 93 KGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 205 GVPLNIAEQLQPGAILNLRVA---EHYYQAQLQGISGQINPVTRTVQLRFSITHTSETTPInGELAYLQYRREVPREGYW 281
Cdd:COG0845 173 DVPESDLARLKVGQPVTVTLDagpGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRP-GMFVRVRIVLGERENALL 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792057359 282 VPVSALTDGIRGlwnLYVLKQDADEfKLQRRDVEILYTEGDNAFITGAISPGEQFVTTGLHKLVAGQRVVPGAA 355
Cdd:COG0845 252 VPASAVVRDGGG---AYVFVVDADG-KVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRVVEA 321
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
44-352 |
5.02e-50 |
|
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: 170.19 E-value: 5.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 44 QQFSGSIRAGNTTGIGFELAGKLQKLLVDTGDRVKPGQLLAQLDTSLLEAEQTELQAALDQNQADISLARATLKRSLELS 123
Cdd:TIGR01730 15 LTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELAQRSFERAERLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 124 AKQYLSEQQLDELKGKLASLEAGHARLEASLKANELKRQKSLLIAPFAGVIAAREHNLGEVIALGSPVFTLVQSDNLQAL 203
Cdd:TIGR01730 95 KRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 204 IGVPLNIAEQLQPGAILNLrVAEHY----YQAQLQGISGQINPVTRTVQLRFSITHTsETTPINGELAYLQYRREVPREG 279
Cdd:TIGR01730 175 FSVPERDLPQLRRGQTLTV-ELDALpgeeFKGKLRFIDPRVDSGTGTVRVRATFPNP-DGRLLPGMFGRVTISLKVRSSA 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2792057359 280 YWVPVSALTDGIRGLwNLYVLKQDAdefKLQRRDVEILYTEGDNAFITGAISPGEQFVTTGLHKLVAGQRVVP 352
Cdd:TIGR01730 253 IVVPTQAVIEDLNGK-YVYVVKNDG---KVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKLRDGAKVKV 321
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
40-284 |
9.15e-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: 80.16 E-value: 9.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 40 YTKLQQFSGSIRA-GNTTGIGFELAGKLQKLLVDTGDRVKPGQLLAQLDTSLLEAEQTELQAALDQNQADISLARATLKR 118
Cdd:pfam00529 4 LTKGVEAPGRVVVsGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 119 SLELSAKQYLSEQQLDELKGKLASLEAGHARLEASLKANELKRQKSLLIAPFAGVIAAREHNLGEVIALGSPVFTLVQSD 198
Cdd:pfam00529 84 LQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 199 NLQALIGVPLNIAEQLQpgailnlRVAEHYYQAQLQGISGQinpvTRTVQLRFSITHTSETTPINGELAYLQYRRE---- 274
Cdd:pfam00529 164 LDQIYVQITQSAAENQA-------EVRSELSGAQLQIAEAE----AELKLAKLDLERTEIRAPVDGTVAFLSVTVDggtv 232
|
250
....*....|....*....
gi 2792057359 275 ---------VPREGYWVPV 284
Cdd:pfam00529 233 saglrlmfvVPEDNLLVPG 251
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
14-353 |
6.08e-16 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 78.22 E-value: 6.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 14 CQPQPSEHSETKPPVVNSanLVLKPGYTK-LQQFSGSIRAGNTTGIGFELAGKLQKLLVDTGDRVKPGQLLAQLDTSLLE 92
Cdd:PRK09859 21 CDDKSAENAAAMTPEVGV--VTLSPGSVNvLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 93 AEQTELQAALDQNQADISLARATLKRSLELSAKQYLSEQQLDELKGKLASLEAGHARLEASLKANELKRQKSLLIAPFAG 172
Cdd:PRK09859 99 AELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 173 VIAAREHNLGEVIalgspvfTLVQSDNL---QALIGVPLNIAEQLQPgailNLRVAEHYYQAQLQGISGQiNPV------ 243
Cdd:PRK09859 179 VSGKSSVTVGALV-------TANQADSLvtvQRLDPIYVDLTQSVQD----FLRMKEEVASGQIKQVQGS-TPVqlnlen 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 244 ----TRTVQLRFSITHTSETT-----------PiNGELAYLQYRREVPREG-----YWVPVSALTDGIRGLWNLYVLKQD 303
Cdd:PRK09859 247 gkrySQTGTLKFSDPTVDETTgsvtlraifpnP-NGDLLPGMYVTALVDEGsrqnvLLVPQEGVTHNAQGKATALILDKD 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2792057359 304 AdefKLQRRDVEILYTEGDNAFITGAISPGEQFVTTGLhklvagQRVVPG 353
Cdd:PRK09859 326 D---VVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGL------QRIRPG 366
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
45-355 |
3.24e-63 |
|
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: 204.41 E-value: 3.24e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 45 QFSGSIRAGNTTGIGFELAGKLQKLLVDTGDRVKPGQLLAQLDTSLLEAEQTELQAALDQNQADISLARATLKRSLELSA 124
Cdd:COG0845 13 EATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAELERYKALLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 125 KQYLSEQQLDELKGKLASLEAGHARLEASLKANELKRQKSLLIAPFAGVIAAREHNLGEVIALGSPVFTLVQSDNLQALI 204
Cdd:COG0845 93 KGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 205 GVPLNIAEQLQPGAILNLRVA---EHYYQAQLQGISGQINPVTRTVQLRFSITHTSETTPInGELAYLQYRREVPREGYW 281
Cdd:COG0845 173 DVPESDLARLKVGQPVTVTLDagpGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRP-GMFVRVRIVLGERENALL 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2792057359 282 VPVSALTDGIRGlwnLYVLKQDADEfKLQRRDVEILYTEGDNAFITGAISPGEQFVTTGLHKLVAGQRVVPGAA 355
Cdd:COG0845 252 VPASAVVRDGGG---AYVFVVDADG-KVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRVVEA 321
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
44-352 |
5.02e-50 |
|
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: 170.19 E-value: 5.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 44 QQFSGSIRAGNTTGIGFELAGKLQKLLVDTGDRVKPGQLLAQLDTSLLEAEQTELQAALDQNQADISLARATLKRSLELS 123
Cdd:TIGR01730 15 LTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELAQRSFERAERLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 124 AKQYLSEQQLDELKGKLASLEAGHARLEASLKANELKRQKSLLIAPFAGVIAAREHNLGEVIALGSPVFTLVQSDNLQAL 203
Cdd:TIGR01730 95 KRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 204 IGVPLNIAEQLQPGAILNLrVAEHY----YQAQLQGISGQINPVTRTVQLRFSITHTsETTPINGELAYLQYRREVPREG 279
Cdd:TIGR01730 175 FSVPERDLPQLRRGQTLTV-ELDALpgeeFKGKLRFIDPRVDSGTGTVRVRATFPNP-DGRLLPGMFGRVTISLKVRSSA 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2792057359 280 YWVPVSALTDGIRGLwNLYVLKQDAdefKLQRRDVEILYTEGDNAFITGAISPGEQFVTTGLHKLVAGQRVVP 352
Cdd:TIGR01730 253 IVVPTQAVIEDLNGK-YVYVVKNDG---KVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKLRDGAKVKV 321
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
52-251 |
5.09e-24 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 100.89 E-value: 5.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 52 AGNTTGIGFELAGKLQKLLVDTGDRVKPGQLLAQLDTSLLEA---------------------------EQTELQAALDQ 104
Cdd:COG1566 42 EARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAalaqaeaqlaaaeaqlarleaelgaeaEIAAAEAQLAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 105 NQADISLARATLKRSLELSAKQYLSEQQLDELKGKLASLEAGH---------------------------ARLEASLKAN 157
Cdd:COG1566 122 AQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLeaaqaqlaqaqaglreeeelaaaqaqvAQAEAALAQA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 158 ELKRQKSLLIAPFAGVIAAREHNLGEVIALGSPVFTLVQSDNLQALIGVPLNIAEQLQPGAILNLRV---AEHYYQAQLQ 234
Cdd:COG1566 202 ELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVdayPDRVFEGKVT 281
|
250 260
....*....|....*....|...
gi 2792057359 235 GISGQINP------VTRTVQLRF 251
Cdd:COG1566 282 SISPGAGFtsppknATGNVVQRY 304
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
40-284 |
9.15e-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: 80.16 E-value: 9.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 40 YTKLQQFSGSIRA-GNTTGIGFELAGKLQKLLVDTGDRVKPGQLLAQLDTSLLEAEQTELQAALDQNQADISLARATLKR 118
Cdd:pfam00529 4 LTKGVEAPGRVVVsGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 119 SLELSAKQYLSEQQLDELKGKLASLEAGHARLEASLKANELKRQKSLLIAPFAGVIAAREHNLGEVIALGSPVFTLVQSD 198
Cdd:pfam00529 84 LQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 199 NLQALIGVPLNIAEQLQpgailnlRVAEHYYQAQLQGISGQinpvTRTVQLRFSITHTSETTPINGELAYLQYRRE---- 274
Cdd:pfam00529 164 LDQIYVQITQSAAENQA-------EVRSELSGAQLQIAEAE----AELKLAKLDLERTEIRAPVDGTVAFLSVTVDggtv 232
|
250
....*....|....*....
gi 2792057359 275 ---------VPREGYWVPV 284
Cdd:pfam00529 233 saglrlmfvVPEDNLLVPG 251
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
14-353 |
6.08e-16 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 78.22 E-value: 6.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 14 CQPQPSEHSETKPPVVNSanLVLKPGYTK-LQQFSGSIRAGNTTGIGFELAGKLQKLLVDTGDRVKPGQLLAQLDTSLLE 92
Cdd:PRK09859 21 CDDKSAENAAAMTPEVGV--VTLSPGSVNvLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 93 AEQTELQAALDQNQADISLARATLKRSLELSAKQYLSEQQLDELKGKLASLEAGHARLEASLKANELKRQKSLLIAPFAG 172
Cdd:PRK09859 99 AELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 173 VIAAREHNLGEVIalgspvfTLVQSDNL---QALIGVPLNIAEQLQPgailNLRVAEHYYQAQLQGISGQiNPV------ 243
Cdd:PRK09859 179 VSGKSSVTVGALV-------TANQADSLvtvQRLDPIYVDLTQSVQD----FLRMKEEVASGQIKQVQGS-TPVqlnlen 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 244 ----TRTVQLRFSITHTSETT-----------PiNGELAYLQYRREVPREG-----YWVPVSALTDGIRGLWNLYVLKQD 303
Cdd:PRK09859 247 gkrySQTGTLKFSDPTVDETTgsvtlraifpnP-NGDLLPGMYVTALVDEGsrqnvLLVPQEGVTHNAQGKATALILDKD 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2792057359 304 AdefKLQRRDVEILYTEGDNAFITGAISPGEQFVTTGLhklvagQRVVPG 353
Cdd:PRK09859 326 D---VVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGL------QRIRPG 366
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
48-350 |
3.41e-15 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 76.37 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 48 GSIRAGNTTGIGFELAGKLQKLLVDTGDRVKPGQLLAQLDTSLLEAEQTELQAALDQNQADISLARATLKRSLELSAKQY 127
Cdd:PRK11556 80 GTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 128 LSEQQLDELKGKLASLEAGHARLEASLKANELKRQKSLLIAPFAGVIAAREHNLGEVIALG--SPVFTLVQSDNLQALIG 205
Cdd:PRK11556 160 VSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGdtTGIVVITQTHPIDLVFT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 206 VPLN-IAEQLQP---GAILNLRVAEHYYQAQL-QG----ISGQINPVTRTVQLRFSITHTSETTPINgelAYLQYRREVP 276
Cdd:PRK11556 240 LPESdIATVVQAqkaGKPLVVEAWDRTNSKKLsEGtllsLDNQIDATTGTIKLKARFNNQDDALFPN---QFVNARMLVD 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2792057359 277 REGYWV--PVSALTDGIRG--LWNLyvlkqdADEFKLQRRDVEILYTEGDNAFITGAISPGEQFVTTGLHKLVAGQRV 350
Cdd:PRK11556 317 TLQNAVviPTAALQMGNEGhfVWVL------NDENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKV 388
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
50-194 |
1.58e-14 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 73.46 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 50 IRagnTTGIGFELAGKLQKLLVDTGDRVKPGQLLAQLDT---------------------SLLEA-----EQTELQAALD 103
Cdd:PRK03598 41 IR---TVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAapyenalmqakanvsvaqaqlDLMLAgyrdeEIAQARAAVK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 104 QNQADISLARATLKRSLELSAKQYLSEQQLDEL--------------KGKLASLEAGH---------ARL---EASLKAN 157
Cdd:PRK03598 118 QAQAAYDYAQNFYNRQQGLWKSRTISANDLENArssrdqaqatlksaQDKLSQYREGNrpqdiaqakASLaqaQAALAQA 197
|
170 180 190
....*....|....*....|....*....|....*..
gi 2792057359 158 ELKRQKSLLIAPFAGVIAAREHNLGEVIALGSPVFTL 194
Cdd:PRK03598 198 ELNLQDTELIAPSDGTILTRAVEPGTMLNAGSTVFTL 234
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
27-174 |
1.54e-13 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 70.96 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 27 PVVNSANLVLKPGytKLQQ---FSGSIRAGNTTGIGFELAGKLQKLLVDTGDRVKPGQLLAQLD-----TSLLEAEQT-- 96
Cdd:PRK11578 32 PVPTYQTLIVRPG--DLQQsvlATGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDpeqaeNQIKEVEATlm 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 97 ELQAALDQNQADISLARATLKRSLELSAKQYLSEQQLDELKGKLA-------SLEAGHARLEASLKANELKRQKSLLIAP 169
Cdd:PRK11578 110 ELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDTAATELAvkqaqigTIDAQIKRNQASLDTAKTNLDYTRIVAP 189
|
....*
gi 2792057359 170 FAGVI 174
Cdd:PRK11578 190 MAGEV 194
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
62-250 |
6.28e-12 |
|
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: 64.06 E-value: 6.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 62 LAGKLQKLLVD-TGDRVKPGQLLAQLDTSLLEAEQTELQAALDQN--QADISLARATLKRsLELSAkqyLSEQQLdelkg 138
Cdd:pfam16576 26 VEGWIEKLYVNaTGDPVKKGQPLAELYSPELVAAQQEYLLALRSGdaLSKSELLRAARQR-LRLLG---MPEAQI----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 139 klasleaghARLEASLKAnelkRQKSLLIAPFAGVIAAREHNLGEVIALGSPVFTLVQSDNLQALIGVPLNIAEQLQPGA 218
Cdd:pfam16576 97 ---------AELERTGKV----QPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQ 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 2792057359 219 ILNLRVaEHY----YQAQLQGISGQINPVTRTVQLR 250
Cdd:pfam16576 164 PAEVTL-PALpgktFEGKVDYIYPTLDPKTRTVRVR 198
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
47-198 |
1.27e-08 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 55.80 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 47 SGSIRAgNTTGIGFELAGKLQKLLVDTGDRVKPGQLLAQLDTslleaeqTELQAALDQNQADISLARATL---KRSLE-- 121
Cdd:PRK10476 41 DAYIDA-DVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDP-------RPYELTVAQAQADLALADAQImttQRSVDae 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 122 ------------------------------LSAKQYLSEQQLD-----------ELK-------------GKLASLEAGH 147
Cdd:PRK10476 113 rsnaasaneqveraranaklatrtlerlepLLAKGYVSAQQVDqartaqrdaevSLNqallqaqaaaaavGGVDALVAQR 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2792057359 148 ARLEASLKANELKRQKSLLIAPFAGVIAAREHNLGEVIALGSPVFTLVQSD 198
Cdd:PRK10476 193 AAREAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTD 243
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
166-262 |
5.92e-08 |
|
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: 50.05 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 166 LIAPFAGVIAAREHNLGEVIALGSPVFTLVQSDNLQALIGVPLNIAEQLQPGAILNLRV---AEHYYQAQLQGISGQINP 242
Cdd:pfam13437 2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLdpgSDYTLEGKVVRISPTVDP 81
|
90 100
....*....|....*....|
gi 2792057359 243 VTRTVQLRFSITHTSETTPI 262
Cdd:pfam13437 82 DTGVIPVRVSIENPKTPIPL 101
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
54-102 |
1.32e-05 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 42.04 E-value: 1.32e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2792057359 54 NTTGIGFELAGKLQKLLVDTGDRVKPGQLLAQLDTSLLEAEQTELQAAL 102
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQL 49
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
61-350 |
2.17e-05 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 45.86 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 61 ELAGKLQKLLVDTGDRVKPGQLLAQLDTSLLEAEQTELQAALDQNQADISLARATLKRSLELSAKQYLSEQQLDElkgKL 140
Cdd:PRK15030 71 QVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQ---AL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 141 ASLEAGHARLEASLKANELKR---QKSLLIAPFAGVIAAREHNLGEVIALG--SPVFTLVQSDNLQALIGVP----LNIA 211
Cdd:PRK15030 148 ADAQQANAAVTAAKAAVETARinlAYTKVTSPISGRIGKSNVTEGALVQNGqaTALATVQQLDPIYVDVTQSsndfLRLK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 212 EQLQPGAI--------LNLRVAEHYYQAQ---LQGISGQINPVTRTVQLRfSITHTSETTPINGELAYLQYRREVPREGY 280
Cdd:PRK15030 228 QELANGTLkqengkakVSLITSDGIKFPQdgtLEFSDVTVDQTTGSITLR-AIFPNPDHTLLPGMFVRARLEEGLNPNAI 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 281 WVPVSALTDGIRGlwNLYVLKQDADEfKLQRRDVEILYTEGDNAFITGAISPGEQFVTTGLHKLVAGQRV 350
Cdd:PRK15030 307 LVPQQGVTRTPRG--DATVLVVGADD-KVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQV 373
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
81-168 |
2.84e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 81 QLLAQLDTslLEAEQTELQ----AALDQNQADisLARATLKRSLELSAKQYLSEQQLDELKGKLASLEAGHARLEAslKA 156
Cdd:COG1842 55 RLERQLEE--LEAEAEKWEekarLALEKGRED--LAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLES--KL 128
|
90
....*....|..
gi 2792057359 157 NELKRQKSLLIA 168
Cdd:COG1842 129 EELKAKKDTLKA 140
|
|
| TIGR02828 |
TIGR02828 |
putative membrane fusion protein; Members of this family show similarity to the members of ... |
182-338 |
9.37e-04 |
|
putative membrane fusion protein; Members of this family show similarity to the members of TIGR00999, the membrane fusion protein (MFP) cluster 2 family, which is linked to RND transport systems. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 131875 Cd Length: 188 Bit Score: 39.85 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 182 GEVIAlGSPVFTLVQSDNLQALIGVPLNIAEQLQPGAILNLRVAEHYYQAQLQGISGQINPVTRTVQLRFSITHTSEttp 261
Cdd:TIGR02828 40 GPVEE-GQPLFKIVDNLSLMLLVISADSLSESLLEGQEVELQVSGRDLELTARVVRLAAGGPDLLVHLEAPIPSYPD--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 262 ingelAYLQYRREV-----PREGYWVPVSALtDGIRGLWNLYVLKQDADEFKlqrrDVEILYTEGDNAFITGAISPGEQF 336
Cdd:TIGR02828 116 -----ALRLRKMRVsiklkEYEGIILPVSAI-DVEQGKTGVWILKNGGYVFV----PVRVLGSTADEVAVEGDKPPDAQL 185
|
..
gi 2792057359 337 VT 338
Cdd:TIGR02828 186 LT 187
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
61-88 |
1.41e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 37.30 E-value: 1.41e-03
10 20
....*....|....*....|....*...
gi 2792057359 61 ELAGKLQKLLVDTGDRVKPGQLLAQLDT 88
Cdd:PRK07051 53 EAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
40-203 |
1.68e-03 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 39.72 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 40 YTKLQQFSGSIRAgnttgIGFELAGKLQKLLVDTGDRVKPGQLLAQLDtslleaeQTELQAALDQNQADISLARATLKRS 119
Cdd:PRK10559 37 WTRDARFSADVVA-----IAPDVSGLITQVNVHDNQLVKKGQVLFTID-------QPRYQKALAEAEADVAYYQVLAQEK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 120 LELSAK------QYLSEQQLDELKGKLASLEAGHARLEASLKANELKRQKSLLIAPFAGVIAAREHNLGEVIALGSPVFT 193
Cdd:PRK10559 105 RREAGRrnrlgvQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVA 184
|
170
....*....|
gi 2792057359 194 LVQSDNLQAL 203
Cdd:PRK10559 185 LVKQNSFYVL 194
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
52-200 |
3.80e-03 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 38.91 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 52 AGNTTGIGFELAGKLQKLLVDTGDRVKPGQLLAQLDTS----LLEAEQTEL-----------------QAALDQNQADIS 110
Cdd:PRK15136 58 AGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTdaeqAFEKAKTALansvrqthqlminskqyQANIELQKTALA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 111 LARATLKRSLELSAKQYLSEQQLDELKGKLASleaGHARLEASL---KANE-------------------------LKRQ 162
Cdd:PRK15136 138 QAQSDLNRRVPLGNANLIGREELQHARDAVAS---AQAQLDVAIqqyNANQamilntpledqpavqqaatevrnawLALQ 214
|
170 180 190
....*....|....*....|....*....|....*...
gi 2792057359 163 KSLLIAPFAGVIAAREHNLGEVIALGSPVFTLVQSDNL 200
Cdd:PRK15136 215 RTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNL 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
61-177 |
5.93e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.21 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 61 ELAGKLQKLlvdtgDRVKPGQLLAQLDTSLLEAEQTELQAALDQNQADISLARATLKRSLELSAKQYLS-EQQLDELKGK 139
Cdd:COG4942 154 ELRADLAEL-----AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAElQQEAEELEAL 228
|
90 100 110
....*....|....*....|....*....|....*...
gi 2792057359 140 LASLEAGHARLEASLKANELKRQKSLLIAPFAGVIAAR 177
Cdd:COG4942 229 IARLEAEAAAAAERTPAAGFAALKGKLPWPVSGRVVRR 266
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
80-164 |
9.93e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 37.64 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2792057359 80 GQLLAQLDTSllEAEQTELQAALDQNQADISLA--RATLKRSlELSAKQYLSEQ---QLDELKGKLASLEAGHARLEASL 154
Cdd:PRK09039 84 ANLRASLSAA--EAERSRLQALLAELAGAGAAAegRAGELAQ-ELDSEKQVSARalaQVELLNQQIAALRRQLAALEAAL 160
|
90
....*....|
gi 2792057359 155 KANELKRQKS 164
Cdd:PRK09039 161 DASEKRDRES 170
|
|
| |
