|
Name |
Accession |
Description |
Interval |
E-value |
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
44-374 |
3.56e-79 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 246.50 E-value: 3.56e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 44 FGAVAFAGVLLVLYAWQFPPFASPIESTENAQVKGQTTLIGPQLSGYVHEVPVQDFQFVKAGDLLVRLDDRIYRQRLDQA 123
Cdd:COG1566 9 LLALVLLLLALGLALWAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 124 VAQLAVQKASLAnNLQQRRSAEATIGQRQAELQNSIAQSRKSAADLRRNQALVTDGSVSKSELDVTQAADAQANAAVAEA 203
Cdd:COG1566 89 EAQLAAAEAQLA-RLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 204 KAVLLIAREDLQTvIVNRGSLEASVANAQAAIELARIDLDNTRIVAPRDGQLGQIGVRLGAYVNSGAQLMALVP-EQRWI 282
Cdd:COG1566 168 QAQLAQAQAGLRE-EEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPlDDLWV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 283 VANMKETQMANVRLGQPVSFTVDALDGREMHGHVQRISPAAGSEFsllPADNATGNfvkISQRIPVRIVVDADQPmlEHL 362
Cdd:COG1566 247 EAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTS---PPKNATGN---VVQRYPVRIRLDNPDP--EPL 318
|
330
....*....|..
gi 516280512 363 RPGMSVVVSIDT 374
Cdd:COG1566 319 RPGMSATVEIDT 330
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
13-380 |
1.80e-55 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 187.21 E-value: 1.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 13 LSSPAPAPAPlTSPVtsKPRSTRKRVVSS-----VIFGAVAFAGVLLVLYAWQfppfaspieSTENAQVKGQTTLIGPQL 87
Cdd:PRK15136 1 MSANAETQTP-QQPV--KKKGKRKRALLLltllfIIIGVAYGIYWFLVLRHHQ---------ETDDAYVAGNQVQIMSQV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 88 SGYVHEVPVQDFQFVKAGDLLVRLDDRIYRQRLDQAvaqlavqKASLANNLQQ-------RRSAEATIGQRQAELQnsia 160
Cdd:PRK15136 69 SGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKA-------KTALANSVRQthqlminSKQYQANIELQKTALA---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 161 qsrKSAADLRRNQALVTDGSVSKSELDVTQAADAQANAAvaeakavLLIAREDL---QTVIVNRgSLEASVANAQAAIEL 237
Cdd:PRK15136 138 ---QAQSDLNRRVPLGNANLIGREELQHARDAVASAQAQ-------LDVAIQQYnanQAMILNT-PLEDQPAVQQAATEV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 238 --ARIDLDNTRIVAPRDGQLGQIGVRLGAYVNSGAQLMALVP-EQRWIVANMKETQMANVRLGQPVSFTVDAL-DGREMH 313
Cdd:PRK15136 207 rnAWLALQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVPaTNLWVDANFKETQLANMRIGQPATITSDIYgDDVVYT 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516280512 314 GHVQRISPAAGSEFSLLPADNATGNFVKISQRIPVRIVVDADQPMLEHLRPGMSVVVSIDT-SVEGDV 380
Cdd:PRK15136 287 GKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRIELDAKQLAQHPLRIGLSTLVTVDTaNRDGQV 354
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
68-374 |
5.05e-28 |
|
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: 112.13 E-value: 5.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 68 IESTENAQVKGQTTLIGPQLSGYVHEVPVQDFQFVKAGDLLVRLDDRIYRQRLDQAVAQLAVQKASLANNLQQRRSAEAT 147
Cdd:pfam00529 8 VEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 148 IGQR-----------------QAELQNSIAQSRKSAADLRRNQALVTDGSVSKSELD--------VTQAADAQANAAVAE 202
Cdd:pfam00529 88 ESELaisrqdydgataqlraaQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVtagalvaqAQANLLATVAQLDQI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 203 AKAVLLIAREDLQTVIVNRGSLEASVANAQAAIELARIDLDNTRIVAPRDGQLGQIGVRL-GAYVNSGAQLMALVPEQR- 280
Cdd:pfam00529 168 YVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDNl 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 281 WIVANMKETQMANVRLGQPVSFTVDALDGREMHGHVQRISPAAGsefsllpadnatgnfvkisQRIPVRIVVDADQPMLE 360
Cdd:pfam00529 248 LVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISP-------------------DTGPVRVVVDKAQGPYY 308
|
330
....*....|....
gi 516280512 361 HLRPGMSVVVSIDT 374
Cdd:pfam00529 309 PLRIGLSAGALVRL 322
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
78-385 |
1.05e-27 |
|
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: 111.25 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 78 GQTTLIGPQLSGYVHEVPVQDFQFVKAGDLLVRLDDRIYRQRLDQAVAQLAVQKASLANnlqqrrsaeatigqrqaelqn 157
Cdd:TIGR01730 24 VDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLEL--------------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 158 siaqsrkSAADLRRNQALVTDGSVSKSELDvtqaadaqanaavaeakavllIAREDLQtvivnrgSLEASVANAQAAIEL 237
Cdd:TIGR01730 83 -------AQRSFERAERLVKRNAVSQADLD---------------------DAKAAVE-------AAQADLEAAKASLAS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 238 ARIDLDNTRIVAPRDGQLGQIGVRLGAYVNSGAQLMALVPEQR-WIVANMKETQMANVRLGQPVSFTVDALDGREMHGHV 316
Cdd:TIGR01730 128 AQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPlEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKL 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516280512 317 QRISPAagsefsllpADNATGNFvkisqriPVRIVVDADQPMlehLRPGMSVVVSIDTSVEGDVP--PDPA 385
Cdd:TIGR01730 208 RFIDPR---------VDSGTGTV-------RVRATFPNPDGR---LLPGMFGRVTISLKVRSSAIvvPTQA 259
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
44-374 |
3.56e-79 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 246.50 E-value: 3.56e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 44 FGAVAFAGVLLVLYAWQFPPFASPIESTENAQVKGQTTLIGPQLSGYVHEVPVQDFQFVKAGDLLVRLDDRIYRQRLDQA 123
Cdd:COG1566 9 LLALVLLLLALGLALWAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 124 VAQLAVQKASLAnNLQQRRSAEATIGQRQAELQNSIAQSRKSAADLRRNQALVTDGSVSKSELDVTQAADAQANAAVAEA 203
Cdd:COG1566 89 EAQLAAAEAQLA-RLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 204 KAVLLIAREDLQTvIVNRGSLEASVANAQAAIELARIDLDNTRIVAPRDGQLGQIGVRLGAYVNSGAQLMALVP-EQRWI 282
Cdd:COG1566 168 QAQLAQAQAGLRE-EEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPlDDLWV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 283 VANMKETQMANVRLGQPVSFTVDALDGREMHGHVQRISPAAGSEFsllPADNATGNfvkISQRIPVRIVVDADQPmlEHL 362
Cdd:COG1566 247 EAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTS---PPKNATGN---VVQRYPVRIRLDNPDP--EPL 318
|
330
....*....|..
gi 516280512 363 RPGMSVVVSIDT 374
Cdd:COG1566 319 RPGMSATVEIDT 330
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
13-380 |
1.80e-55 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 187.21 E-value: 1.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 13 LSSPAPAPAPlTSPVtsKPRSTRKRVVSS-----VIFGAVAFAGVLLVLYAWQfppfaspieSTENAQVKGQTTLIGPQL 87
Cdd:PRK15136 1 MSANAETQTP-QQPV--KKKGKRKRALLLltllfIIIGVAYGIYWFLVLRHHQ---------ETDDAYVAGNQVQIMSQV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 88 SGYVHEVPVQDFQFVKAGDLLVRLDDRIYRQRLDQAvaqlavqKASLANNLQQ-------RRSAEATIGQRQAELQnsia 160
Cdd:PRK15136 69 SGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKA-------KTALANSVRQthqlminSKQYQANIELQKTALA---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 161 qsrKSAADLRRNQALVTDGSVSKSELDVTQAADAQANAAvaeakavLLIAREDL---QTVIVNRgSLEASVANAQAAIEL 237
Cdd:PRK15136 138 ---QAQSDLNRRVPLGNANLIGREELQHARDAVASAQAQ-------LDVAIQQYnanQAMILNT-PLEDQPAVQQAATEV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 238 --ARIDLDNTRIVAPRDGQLGQIGVRLGAYVNSGAQLMALVP-EQRWIVANMKETQMANVRLGQPVSFTVDAL-DGREMH 313
Cdd:PRK15136 207 rnAWLALQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVPaTNLWVDANFKETQLANMRIGQPATITSDIYgDDVVYT 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516280512 314 GHVQRISPAAGSEFSLLPADNATGNFVKISQRIPVRIVVDADQPMLEHLRPGMSVVVSIDT-SVEGDV 380
Cdd:PRK15136 287 GKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRIELDAKQLAQHPLRIGLSTLVTVDTaNRDGQV 354
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
79-380 |
1.00e-43 |
|
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: 154.33 E-value: 1.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 79 QTTLIGPQLSGYVHEVPVQDFQFVKAGDLLVRLDDRIYRQRLDQAVAQLAVQKASLANnlqqrrsaeatigqrqaelqns 158
Cdd:COG0845 22 REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLEL---------------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 159 iaqsrkSAADLRRNQALVTDGSVSKSELDVTQAadaqanaavaeakavlliaredlqtvivNRGSLEASVANAQAAIELA 238
Cdd:COG0845 80 ------AKAELERYKALLKKGAVSQQELDQAKA----------------------------ALDQAQAALAAAQAALEQA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 239 RIDLDNTRIVAPRDGQLGQIGVRLGAYVNSGAQLMALV-PEQRWIVANMKETQMANVRLGQPVSFTVDALDGREMHGHVQ 317
Cdd:COG0845 126 RANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIAdLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVT 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516280512 318 RISPAagsefsllpADNATGNFvkisqriPVRIVVDADQPMlehLRPGMSVVVSIDTSVEGDV 380
Cdd:COG0845 206 FIDPA---------VDPATRTV-------RVRAELPNPDGL---LRPGMFVRVRIVLGERENA 249
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
27-372 |
3.09e-34 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 129.76 E-value: 3.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 27 VTSKPRSTRKRVVSSVIFGAVAFAGVLLVLYAWQFPpfaspieSTENAQVKGQTTLIGPQLSGYVHEVPVQDFQFVKAGD 106
Cdd:PRK10476 2 ESTPKKSPRKKLPALAIVALAIVALVFVIWRTDSAP-------STDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 107 LLVRLDDRIYRQRLDQAVAQLAVQKASLANnlqQRRS-----AEATIGQRQAElqNSIAQSRKSAADLRRNQALVTDGSV 181
Cdd:PRK10476 75 LLFRIDPRPYELTVAQAQADLALADAQIMT---TQRSvdaerSNAASANEQVE--RARANAKLATRTLERLEPLLAKGYV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 182 SKSELDVTQaadAQANAAVAEAKAVLLIAREDLQTViVNRGSLEASVANAQAAIELARIDLDNTRIVAPRDGQLGQIGVR 261
Cdd:PRK10476 150 SAQQVDQAR---TAQRDAEVSLNQALLQAQAAAAAV-GGVDALVAQRAAREAALAIAELHLEDTTVRAPFDGRVVGLKVS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 262 LGAYVNSGAQLMALVPEQRW-IVANMKETQMANVRLGQPVSFTVDALDGREMHGHVQRISPAAGSEFSL-----LPADNA 335
Cdd:PRK10476 226 VGEFAAPMQPIFTLIDTDHWyAIANFRETDLKNIRVGDCATVYSMIDRGRPFEGKVDSIGWGVLPDDGGnvprgLPYVPR 305
|
330 340 350
....*....|....*....|....*....|....*..
gi 516280512 336 TGNFVKISQRIPVRIVVDADQPMLehLRPGMSVVVSI 372
Cdd:PRK10476 306 SINWVRVAQRFPVRIMLDKPDPEL--FRIGASAVVEL 340
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
68-374 |
5.05e-28 |
|
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: 112.13 E-value: 5.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 68 IESTENAQVKGQTTLIGPQLSGYVHEVPVQDFQFVKAGDLLVRLDDRIYRQRLDQAVAQLAVQKASLANNLQQRRSAEAT 147
Cdd:pfam00529 8 VEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 148 IGQR-----------------QAELQNSIAQSRKSAADLRRNQALVTDGSVSKSELD--------VTQAADAQANAAVAE 202
Cdd:pfam00529 88 ESELaisrqdydgataqlraaQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVtagalvaqAQANLLATVAQLDQI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 203 AKAVLLIAREDLQTVIVNRGSLEASVANAQAAIELARIDLDNTRIVAPRDGQLGQIGVRL-GAYVNSGAQLMALVPEQR- 280
Cdd:pfam00529 168 YVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDNl 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 281 WIVANMKETQMANVRLGQPVSFTVDALDGREMHGHVQRISPAAGsefsllpadnatgnfvkisQRIPVRIVVDADQPMLE 360
Cdd:pfam00529 248 LVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISP-------------------DTGPVRVVVDKAQGPYY 308
|
330
....*....|....
gi 516280512 361 HLRPGMSVVVSIDT 374
Cdd:pfam00529 309 PLRIGLSAGALVRL 322
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
78-385 |
1.05e-27 |
|
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: 111.25 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 78 GQTTLIGPQLSGYVHEVPVQDFQFVKAGDLLVRLDDRIYRQRLDQAVAQLAVQKASLANnlqqrrsaeatigqrqaelqn 157
Cdd:TIGR01730 24 VDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLEL--------------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 158 siaqsrkSAADLRRNQALVTDGSVSKSELDvtqaadaqanaavaeakavllIAREDLQtvivnrgSLEASVANAQAAIEL 237
Cdd:TIGR01730 83 -------AQRSFERAERLVKRNAVSQADLD---------------------DAKAAVE-------AAQADLEAAKASLAS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 238 ARIDLDNTRIVAPRDGQLGQIGVRLGAYVNSGAQLMALVPEQR-WIVANMKETQMANVRLGQPVSFTVDALDGREMHGHV 316
Cdd:TIGR01730 128 AQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPlEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKL 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516280512 317 QRISPAagsefsllpADNATGNFvkisqriPVRIVVDADQPMlehLRPGMSVVVSIDTSVEGDVP--PDPA 385
Cdd:TIGR01730 208 RFIDPR---------VDSGTGTV-------RVRATFPNPDGR---LLPGMFGRVTISLKVRSSAIvvPTQA 259
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
36-356 |
3.80e-23 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 98.27 E-value: 3.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 36 KRVVSSVIFGAVAFAGVLLVLYAWQFPPfASPIesTENAQVKGQTTLIGPQLSGYVHEVPVQDFQFVKAGDLLVRLDDRI 115
Cdd:PRK10559 6 RKISRTAITLVLVILAFIAIFRAWVFYT-ESPW--TRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 116 YRQRLDQAVAQLAVQKAsLANnlQQRRSAEatigqrqaelqnsiaqsrksaadlRRNQALVTdgSVSKSELDVtqaadaq 195
Cdd:PRK10559 83 YQKALAEAEADVAYYQV-LAQ--EKRREAG------------------------RRNRLGVQ--AMSREEIDQ------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 196 anaavaeakavlliAREDLQTVivnrgslEASVANAQAAIELARIDLDNTRIVAPRDGQLGQIGVRLGAYVNSGAQLMAL 275
Cdd:PRK10559 127 --------------ANNVLQTV-------LHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVAL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 276 VPEQR-WIVANMKETQMANVRLGQPVSFTVDALDgREMHGHVQRIspAAGSEFSLLPADN---ATGN----FVKISQRIP 347
Cdd:PRK10559 186 VKQNSfYVLAYMEETKLEGVRPGYRAEITPLGSN-KVLKGTVDSV--AAGVTNSSSTRDSkgmATIDsnleWVRLAQRVP 262
|
....*....
gi 516280512 348 VRIVVDADQ 356
Cdd:PRK10559 263 VRIRLDNQQ 271
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
88-375 |
3.67e-18 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 84.63 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 88 SGYVHEVPVQDFQFVKAGDLLVRLDDRIYRQRLDQAVAQLAVQKASLANNLQQRRSAEatIGQRQAELQNSIAQSRKSAA 167
Cdd:PRK03598 51 GGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQLDLMLAGYRDEE--IAQARAAVKQAQAAYDYAQN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 168 DLRRNQALVTDGSVSKSELDVTQAADAQANAAVAEAKAVLLIAREDlqtvivNR----GSLEASVANAQAAIELARIDLD 243
Cdd:PRK03598 129 FYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQDKLSQYREG------NRpqdiAQAKASLAQAQAALAQAELNLQ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 244 NTRIVAPRDGQLGQIGVRLGAYVNSGAQLMAL-VPEQRWIVANMKETQMANVRLGQPVSFTVDALDGREMHGHVQRISPA 322
Cdd:PRK03598 203 DTELIAPSDGTILTRAVEPGTMLNAGSTVFTLsLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFVSPT 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 516280512 323 AgsEFSllPADNATGNF-VKISQRIpvRIVV-DADqpmlEHLRPGMSVVVSIDTS 375
Cdd:PRK03598 283 A--EFT--PKTVETPDLrTDLVYRL--RIVVtDAD----DALRQGMPVTVRFADE 327
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
40-375 |
1.44e-13 |
|
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: 71.58 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 40 SSVIFGAVAFAGVLLVLYAWQFppFAsPIESTENAQ----VKGQTTLIGPQLSGYVHEVPVQDFQFVKAGDLLVRLDDRI 115
Cdd:TIGR01843 2 RFARLITWLIAGLVVIFFLWAY--FA-PLDVVATATgkvvPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 116 YRQRLDQAVAQLAVQKASLA----------------------------------NNLQQRRSA--------EATIGQRQA 153
Cdd:TIGR01843 79 VEADAAELESQVLRLEAEVArlraeadsqaaiefpddllsaedpavpelikgqqSLFESRKSTlraqleliLAQIKQLEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 154 EL------QNSIAQSRKSAAD-LRRNQALVTDGSVSKSEL-------DVTQAADAQANAAVAEAKAVLLIAREDLQTVI- 218
Cdd:TIGR01843 159 ELaglqaqLQALRQQLEVISEeLEARRKLKEKGLVSRLELlelererAEAQGELGRLEAELEVLKRQIDELQLERQQIEq 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 219 -----VNRGSLEASVANAQAAIELARIDLDNTR--IVAPRDGQLGQIGVR-LGAYVNSGAQLMALVPEQRWIV--ANMKE 288
Cdd:TIGR01843 239 tfreeVLEELTEAQARLAELRERLNKARDRLQRliIRSPVDGTVQSLKVHtVGGVVQPGETLMEIVPEDDPLEieAKLSP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 289 TQMANVRLGQPVSFTVDALDGRE---MHGHVQRISPaagsefSLLPADNATGNFvkisqrIPVRIVVDA----DQPMLEH 361
Cdd:TIGR01843 319 KDIGFVHVGQPAEIKFSAFPYRRygiLNGKVKSISP------DTFTDERGGGPY------YRVRISIDQntlgIGPKGLE 386
|
410
....*....|....
gi 516280512 362 LRPGMSVVVSIDTS 375
Cdd:TIGR01843 387 LSPGMPVTADIKTG 400
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
97-347 |
1.03e-11 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 65.97 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 97 QDFQFVKAGDLLVRLDDRIYRQRLDQAVAQLAVQKASLANnlqQRRsaeatigqrqaelqnsiaqsrksaaDLRRNQALV 176
Cdd:PRK11556 104 QEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLAN---ARR-------------------------DLARYQQLA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 177 TDGSVSKSELDVtqaadaqanaavaeakavlliaredlQTVIVNRGslEASVANAQAAIELARIDLDNTRIVAPRDGQLG 256
Cdd:PRK11556 156 KTNLVSRQELDA--------------------------QQALVSET--EGTIKADEASVASAQLQLDYSRITAPISGRVG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 257 QIGVRLGAYVNSGAQLMALVPEQRW---IVANMKETQMANV----RLGQPVsfTVDALDgremhghvqRISPAAGSEFSL 329
Cdd:PRK11556 208 LKQVDVGNQISSGDTTGIVVITQTHpidLVFTLPESDIATVvqaqKAGKPL--VVEAWD---------RTNSKKLSEGTL 276
|
250 260
....*....|....*....|.
gi 516280512 330 LPADN---ATGNFVKISQRIP 347
Cdd:PRK11556 277 LSLDNqidATTGTIKLKARFN 297
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
233-368 |
1.15e-10 |
|
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.
Pssm-ID: 435440 [Multi-domain] Cd Length: 214 Bit Score: 60.60 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 233 AAIELARIDLDNTRIVAPRDGQLGQIGVRLGAYVNSGAQLMALVP-EQRWIVANMKETQMANVRLGQPVSFTVDALDGRE 311
Cdd:pfam16576 97 AELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADlSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKT 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 516280512 312 MHGHVQRISPAAGSEfsllpadnatgnfvkiSQRIPVRIVVD-ADQpmleHLRPGMSV 368
Cdd:pfam16576 177 FEGKVDYIYPTLDPK----------------TRTVRVRIELPnPDG----RLKPGMFA 214
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
83-321 |
4.29e-09 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 57.48 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 83 IGPQLSGYVHEVPVQDFQFVKAGDLLVRLDDriyrqrlDQAVAQLavqkaslannlqqrRSAEATIGQRQAELQNSIAQS 162
Cdd:PRK11578 64 VGAQVSGQLKTLSVAIGDKVKKDQLLGVIDP-------EQAENQI--------------KEVEATLMELRAQRQQAEAEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 163 RKSAADLRRNQALVTDGSVSKSELDVtqaadaqanaavaeakavlliAREDLQTVIVNRGSLEASVANAQAAIELARIDL 242
Cdd:PRK11578 123 KLARVTLSRQQRLAKTQAVSQQDLDT---------------------AATELAVKQAQIGTIDAQIKRNQASLDTAKTNL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 243 DNTRIVAPRDGQLGQIGVRLGAYVNSGAQ---LMALVPEQRWIV-ANMKETQMANVRLGQPVSFTVDALDGREMHGHVQR 318
Cdd:PRK11578 182 DYTRIVAPMAGEVTQITTLQGQTVIAAQQapnILTLADMSTMLVkAQVSEADVIHLKPGQKAWFTVLGDPLTRYEGVLKD 261
|
...
gi 516280512 319 ISP 321
Cdd:PRK11578 262 ILP 264
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
246-365 |
9.68e-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: 52.75 E-value: 9.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 246 RIVAPRDGQLGQIGVRLGAYVNSGAQLMALVPEQR-WIVANMKETQMANVRLGQPVSFTVDALDGREMHGHVQRISPAAG 324
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRlLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 516280512 325 SEfsllpadnatgnfvkiSQRIPVRIVVDaDQPMLEHLRPG 365
Cdd:pfam13437 81 PD----------------TGVIPVRVSIE-NPKTPIPLLPG 104
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
80-128 |
1.56e-06 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 44.74 E-value: 1.56e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 516280512 80 TTLIGPQLSGYVHEVPVQDFQFVKAGDLLVRLDDRIYRQRLDQAVAQLA 128
Cdd:pfam13533 2 VVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
209-368 |
2.53e-05 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 45.86 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 209 IAREDLQTVIVNRGSLEASVANAQAAIELARIDLDNTRIVAPRDGQLGQIGVRLGAYVNSGaQLMALVPEQRWIVANMKE 288
Cdd:PRK15030 138 ISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNG-QATALATVQQLDPIYVDV 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516280512 289 TQMAN--VRLGQPV-SFTVDALDGREMHGHVQRIS---PAAGS-EFSLLPADNATGNfvkisqripvrIVVDADQPMLEH 361
Cdd:PRK15030 217 TQSSNdfLRLKQELaNGTLKQENGKAKVSLITSDGikfPQDGTlEFSDVTVDQTTGS-----------ITLRAIFPNPDH 285
|
....*...
gi 516280512 362 -LRPGMSV 368
Cdd:PRK15030 286 tLLPGMFV 293
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
117-171 |
6.46e-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: 6.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 516280512 117 RQRLDQAVAQLAVQKASLANNLQQRRSAEATIGQRQAELQNSIAQSRKSAADLRR 171
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| |
