|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
69-406 |
2.96e-104 |
|
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: 311.49 E-value: 2.96e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 69 VVTDDVEIYGEYVGRIRAQQFVEIRARVEGFLEKMLFDEGTYVKKGQPLFIIDPKQYQARANKAKAQLNKNKALALKAER 148
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 149 DLERIRPLYQQNAASQLDLDNAIASYESAKAEVEMSEADLTQAETALGYTTVSSPISGYISERNVDIGTLVGPGgqSLLA 228
Cdd:COG0845 83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG--TPLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 229 TVVKSDTVRVDFSMTGLDYLKskarnVNLGQKdttrtwepyITITLPDNSPYPQRGIVDFADPQVDPQTGTFSVRAEMPN 308
Cdd:COG0845 161 TIADLDPLEVEFDVPESDLAR-----LKVGQP---------VTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 309 PEHILLPGQFTKVRLLLDVREAAVVVPNKAIAIEKGGAYIFVVRADSIAERRMVELGPEVGNNVIIERGLVPHENIVVEG 388
Cdd:COG0845 227 PDGLLRPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSG 306
|
330
....*....|....*...
gi 2436919897 389 FHKLTHGDKVIPSTYRAE 406
Cdd:COG0845 307 LQRLRDGAKVRVVEAAAP 324
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
64-398 |
4.93e-83 |
|
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: 257.24 E-value: 4.93e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 64 VEVEPVVTDDVEIYGEYVGRIRAQQFVEIRARVEGFLEKMLFDEGTYVKKGQPLFIIDPKQYQARANKAKAQLNKNKALA 143
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 144 LKAERDLERIRPLYQQNAASQLDLDNAIASYESAKAEVEMSEADLTQAETALGYTTVSSPISGYISERNVDIGTLVGPGG 223
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 224 QslLATVVKSDTVRVDFSMTGLDYLkskarNVNLGQKDttrtwepyiTITLPDNSPYPQRGIVDFADPQVDPQTGTFSVR 303
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLP-----QLRRGQTL---------TVELDALPGEEFKGKLRFIDPRVDSGTGTVRVR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 304 AEMPNPEHILLPGQFTKVRLLLDVREAAVVVPNKAIAIEKGGAYIFVVRADSIAERRMVELGPEVGNNVIIERGLVPHEN 383
Cdd:TIGR01730 225 ATFPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQ 304
|
330
....*....|....*
gi 2436919897 384 IVVEGFHKLTHGDKV 398
Cdd:TIGR01730 305 IVTAGVVKLRDGAKV 319
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
39-411 |
6.37e-59 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 197.24 E-value: 6.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 39 AGILLLSGGLYWL----LRPAPPGPDLPIVEVEPVVTDDVEIYGEYVGRIRAQQFVEIRARVEGFLEKMLFDEGTYVKKG 114
Cdd:PRK15030 11 AVVLMLSGSLALTgcddKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 115 QPLFIIDPKQYQARANKAKAQLNKNKALALKAERDLERIRPLYQQNAASQLDLDNAIASYESAKAEVEMSEADLTQAETA 194
Cdd:PRK15030 91 VSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARIN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 195 LGYTTVSSPISGYISERNVDIGTLVGPGGQSLLATVVKSDTVRVDFSMTGLDYLKSKAR--NVNLGQKDTtrtwEPYITI 272
Cdd:PRK15030 171 LAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQElaNGTLKQENG----KAKVSL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 273 TLPDNSPYPQRGIVDFADPQVDPQTGTFSVRAEMPNPEHILLPGQFTKVRLLLDVREAAVVVPNKAIA-IEKGGAYIFVV 351
Cdd:PRK15030 247 ITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTrTPRGDATVLVV 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 352 RADSIAERRMVELGPEVGNNVIIERGLVPHENIVVEGFHKLTHGDKVIPSTYRAEQEDHS 411
Cdd:PRK15030 327 GADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQEVTADNNQQA 386
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
64-386 |
6.15e-43 |
|
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: 152.96 E-value: 6.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 64 VEVEPVVTDDVEIYGEYVgriraqqfvEIRARVEGFLEKMLFDEGTYVKKGQPLFIIDPKQYQARANKAKAQLNKNKALA 143
Cdd:pfam00529 4 LTKGVEAPGRVVVSGNAK---------AVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 144 LKAERDLERIRPLYQQNAASQLDLDNAIASYESAKAEVEMSEADLTQAETALGYTTVSSPISGYISERNVDIGTLVGPGG 223
Cdd:pfam00529 75 ARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 224 QSLLATVVKSDTVRVDFSMTGLDYLKSkARNVNLGQKDTTRTWEPYITITLPDNSPYPQR----GIVDFADPQVDPQTGT 299
Cdd:pfam00529 155 ANLLATVAQLDQIYVQITQSAAENQAE-VRSELSGAQLQIAEAEAELKLAKLDLERTEIRapvdGTVAFLSVTVDGGTVS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 300 FSVRAEMPNPE-HILLPGQFtKVRLLLDVRE--AAVVVPNKAIAIEKGGAYIFVVRADSIAERRMVELGPEVGNNVIIER 376
Cdd:pfam00529 234 AGLRLMFVVPEdNLLVPGMF-VETQLDQVRVgqPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRI 312
|
330
....*....|
gi 2436919897 377 GLVPHENIVV 386
Cdd:pfam00529 313 GLSAGALVRL 322
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
69-406 |
2.96e-104 |
|
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: 311.49 E-value: 2.96e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 69 VVTDDVEIYGEYVGRIRAQQFVEIRARVEGFLEKMLFDEGTYVKKGQPLFIIDPKQYQARANKAKAQLNKNKALALKAER 148
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 149 DLERIRPLYQQNAASQLDLDNAIASYESAKAEVEMSEADLTQAETALGYTTVSSPISGYISERNVDIGTLVGPGgqSLLA 228
Cdd:COG0845 83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG--TPLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 229 TVVKSDTVRVDFSMTGLDYLKskarnVNLGQKdttrtwepyITITLPDNSPYPQRGIVDFADPQVDPQTGTFSVRAEMPN 308
Cdd:COG0845 161 TIADLDPLEVEFDVPESDLAR-----LKVGQP---------VTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 309 PEHILLPGQFTKVRLLLDVREAAVVVPNKAIAIEKGGAYIFVVRADSIAERRMVELGPEVGNNVIIERGLVPHENIVVEG 388
Cdd:COG0845 227 PDGLLRPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSG 306
|
330
....*....|....*...
gi 2436919897 389 FHKLTHGDKVIPSTYRAE 406
Cdd:COG0845 307 LQRLRDGAKVRVVEAAAP 324
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
64-398 |
4.93e-83 |
|
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: 257.24 E-value: 4.93e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 64 VEVEPVVTDDVEIYGEYVGRIRAQQFVEIRARVEGFLEKMLFDEGTYVKKGQPLFIIDPKQYQARANKAKAQLNKNKALA 143
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 144 LKAERDLERIRPLYQQNAASQLDLDNAIASYESAKAEVEMSEADLTQAETALGYTTVSSPISGYISERNVDIGTLVGPGG 223
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 224 QslLATVVKSDTVRVDFSMTGLDYLkskarNVNLGQKDttrtwepyiTITLPDNSPYPQRGIVDFADPQVDPQTGTFSVR 303
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLP-----QLRRGQTL---------TVELDALPGEEFKGKLRFIDPRVDSGTGTVRVR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 304 AEMPNPEHILLPGQFTKVRLLLDVREAAVVVPNKAIAIEKGGAYIFVVRADSIAERRMVELGPEVGNNVIIERGLVPHEN 383
Cdd:TIGR01730 225 ATFPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQ 304
|
330
....*....|....*
gi 2436919897 384 IVVEGFHKLTHGDKV 398
Cdd:TIGR01730 305 IVTAGVVKLRDGAKV 319
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
39-411 |
6.37e-59 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 197.24 E-value: 6.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 39 AGILLLSGGLYWL----LRPAPPGPDLPIVEVEPVVTDDVEIYGEYVGRIRAQQFVEIRARVEGFLEKMLFDEGTYVKKG 114
Cdd:PRK15030 11 AVVLMLSGSLALTgcddKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 115 QPLFIIDPKQYQARANKAKAQLNKNKALALKAERDLERIRPLYQQNAASQLDLDNAIASYESAKAEVEMSEADLTQAETA 194
Cdd:PRK15030 91 VSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARIN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 195 LGYTTVSSPISGYISERNVDIGTLVGPGGQSLLATVVKSDTVRVDFSMTGLDYLKSKAR--NVNLGQKDTtrtwEPYITI 272
Cdd:PRK15030 171 LAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQElaNGTLKQENG----KAKVSL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 273 TLPDNSPYPQRGIVDFADPQVDPQTGTFSVRAEMPNPEHILLPGQFTKVRLLLDVREAAVVVPNKAIA-IEKGGAYIFVV 351
Cdd:PRK15030 247 ITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTrTPRGDATVLVV 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 352 RADSIAERRMVELGPEVGNNVIIERGLVPHENIVVEGFHKLTHGDKVIPSTYRAEQEDHS 411
Cdd:PRK15030 327 GADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQEVTADNNQQA 386
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
30-411 |
1.44e-53 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 182.69 E-value: 1.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 30 SLRVWLYVGAGILLLSGGLYWLLRPAPPGPdlPIVEVEPVVTDDVEIYGEYVGRIRAQQFVEIRARVEGFLEKMLFDEGT 109
Cdd:PRK09578 6 RRRLLLAALVALFVLAGCGKGDSDAAAAAP--REATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 110 YVKKGQPLFIIDPKQYQARANKAKAQLNKNKALALKAERDLERIRPLYQQNAASQLDLDNAIASYESAKAEVEMSEADLT 189
Cdd:PRK09578 84 EVKQGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVADERQAKAAVASAKAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 190 QAETALGYTTVSSPISGYISERNVDIGTLVGPGGQSLLATVVKSDTVRVDFSMTGLDyLKSKARNVNLGQKDTTRTWEPY 269
Cdd:PRK09578 164 RAQLQLDYATVTAPIDGRARRALVTEGALVGQDQATPLTTVEQLDPIYVNFSQPAAD-VEALRRAVKSGRATGIAQQDVA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 270 ITITLPDNSPYPQRGIVDFADPQVDPQTGTFSVRAEMPNPEHILLPGQFTKVRLLLDVREAAVVVPNKAIAIEKGGAYIF 349
Cdd:PRK09578 243 VTLVRADGSEYPLKGKLLFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTADSASVK 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2436919897 350 VVRADSIAERRMVELGPEVGNNVIIERGLVPHENIVVEGFHKLTHGDKVIPsTYRAEQEDHS 411
Cdd:PRK09578 323 VVGQNGKVRDVEVEADQMSGRDWIVTRGLAGGERVIVDNAAQFAPGTAVKA-VERAPAAKPA 383
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
61-397 |
6.75e-50 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 172.98 E-value: 6.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 61 LPIVEVEPVVTDDVEIYGEYVGRIRAQQFVEIRARVEGFLEKMLFDEGTYVKKGQPLFIIDPKQYQARANKAKAQLNKNK 140
Cdd:PRK09859 33 TPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKAL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 141 ALALKAERDLERIRPLYQQNAASQLDLDNAIASYESAKAEVEMSEADLTQAETALGYTTVSSPISGYISERNVDIGTLVG 220
Cdd:PRK09859 113 STASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 221 PGGQSLLATVVKSDTVRVDFSMTGLDYLKSKaRNVNLGQKDTTRTWEPyITITLPDNSPYPQRGIVDFADPQVDPQTGTF 300
Cdd:PRK09859 193 ANQADSLVTVQRLDPIYVDLTQSVQDFLRMK-EEVASGQIKQVQGSTP-VQLNLENGKRYSQTGTLKFSDPTVDETTGSV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 301 SVRAEMPNPEHILLPGQFTKVRLLLDVREAAVVVPNKAIAIE-KGGAYIFVVRADSIAERRMVELGPEVGNNVIIERGLV 379
Cdd:PRK09859 271 TLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNaQGKATALILDKDDVVQLREIEASKAIGDQWVVTSGLQ 350
|
330
....*....|....*...
gi 2436919897 380 PHENIVVEGFHKLTHGDK 397
Cdd:PRK09859 351 AGDRVIVSGLQRIRPGIK 368
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
52-398 |
4.13e-49 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 171.90 E-value: 4.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 52 LRPAPPGPdlpiVEVEPVVTDDVEIYGEYVGRIRAQQFVEIRARVEGFLEKMLFDEGTYVKKGQPLFIIDPKQYQARANK 131
Cdd:PRK11556 54 MRSGPLAP----VQAATATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 132 AKAQLNKNKALALKAERDLERIRPLYQQNAASQLDLDNAIASYESAKAEVEMSEADLTQAETALGYTTVSSPISGYISER 211
Cdd:PRK11556 130 AQGQLAKDQATLANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 212 NVDIGTLVGPGGQSLLATVVKSDTVRVDFSMTGLD---YLKSKARnvnlGQKDTTRTWEpyititlPDNSPYPQRGIVDF 288
Cdd:PRK11556 210 QVDVGNQISSGDTTGIVVITQTHPIDLVFTLPESDiatVVQAQKA----GKPLVVEAWD-------RTNSKKLSEGTLLS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 289 ADPQVDPQTGTFSVRAEMPNPEHILLPGQFTKVRLLLDVREAAVVVPNKAIAIEKGGAYIFVVRADSIAERRMVELGPEV 368
Cdd:PRK11556 279 LDNQIDATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQNAVVIPTAALQMGNEGHFVWVLNDENKVSKHLVTPGIQD 358
|
330 340 350
....*....|....*....|....*....|
gi 2436919897 369 GNNVIIERGLVPHENIVVEGFHKLTHGDKV 398
Cdd:PRK11556 359 SQKVVISAGLSAGDRVVTDGIDRLTEGAKV 388
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
64-386 |
6.15e-43 |
|
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: 152.96 E-value: 6.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 64 VEVEPVVTDDVEIYGEYVgriraqqfvEIRARVEGFLEKMLFDEGTYVKKGQPLFIIDPKQYQARANKAKAQLNKNKALA 143
Cdd:pfam00529 4 LTKGVEAPGRVVVSGNAK---------AVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 144 LKAERDLERIRPLYQQNAASQLDLDNAIASYESAKAEVEMSEADLTQAETALGYTTVSSPISGYISERNVDIGTLVGPGG 223
Cdd:pfam00529 75 ARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 224 QSLLATVVKSDTVRVDFSMTGLDYLKSkARNVNLGQKDTTRTWEPYITITLPDNSPYPQR----GIVDFADPQVDPQTGT 299
Cdd:pfam00529 155 ANLLATVAQLDQIYVQITQSAAENQAE-VRSELSGAQLQIAEAEAELKLAKLDLERTEIRapvdGTVAFLSVTVDGGTVS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 300 FSVRAEMPNPE-HILLPGQFtKVRLLLDVRE--AAVVVPNKAIAIEKGGAYIFVVRADSIAERRMVELGPEVGNNVIIER 376
Cdd:pfam00529 234 AGLRLMFVVPEdNLLVPGMF-VETQLDQVRVgqPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRI 312
|
330
....*....|
gi 2436919897 377 GLVPHENIVV 386
Cdd:pfam00529 313 GLSAGALVRL 322
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
29-326 |
1.60e-35 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 133.25 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 29 ISLRVWLYVGAGILLLSGGLYWLLRPAPPGPdlpivevepvVTDDveiygeyvGRIRAQQfVEIRARVEGFLEKMLFDEG 108
Cdd:COG1566 4 LKKRRLLALVLLLLALGLALWAAGRNGPDEP----------VTAD--------GRVEARV-VTVAAKVSGRVTEVLVKEG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 109 TYVKKGQPLFIIDPKQYQARANKAKAQLN---------------------------KNKALALKAERDLERIRPLYQQNA 161
Cdd:COG1566 65 DRVKKGQVLARLDPTDLQAALAQAEAQLAaaeaqlarleaelgaeaeiaaaeaqlaAAQAQLDLAQRELERYQALYKKGA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 162 ASQLDLDNAIASYESAK---------------------------AEVEMSEADLTQAETALGYTTVSSPISGYISERNVD 214
Cdd:COG1566 145 VSQQELDEARAALDAAQaqleaaqaqlaqaqaglreeeelaaaqAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 215 IGTLVGPGGQslLATVVKSDTVRVDFsmtgldYLK-SKARNVNLGQKdttrtwepyITITLpDNSPYPQ-RGIVDFADPQ 292
Cdd:COG1566 225 PGEVVSAGQP--LLTIVPLDDLWVEA------YVPeTDLGRVKPGQP---------VEVRV-DAYPDRVfEGKVTSISPG 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2436919897 293 VDP----------QTGTFSVRAEMPNPE-HILLPGQFTKVRLLLD 326
Cdd:COG1566 287 AGFtsppknatgnVVQRYPVRIRLDNPDpEPLRPGMSATVEIDTE 331
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
81-318 |
7.65e-22 |
|
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: 92.95 E-value: 7.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 81 VGRIRA--QQFVEIRARVEGFLEKMLFD-EGTYVKKGQPLFIID-PKQYQARAN--KAKAQLNKNKALALkAERDLERIR 154
Cdd:pfam16576 9 VGRVAYdeRRLAHVHARVEGWIEKLYVNaTGDPVKKGQPLAELYsPELVAAQQEylLALRSGDALSKSEL-LRAARQRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 155 plyqqnaasQLDldnaiasyesakaeveMSEAD---LTQAETALGYTTVSSPISGYISERNVDIGTLVGPGgqSLLATVV 231
Cdd:pfam16576 88 ---------LLG----------------MPEAQiaeLERTGKVQPTVTVYAPISGVVTELNVREGMYVQPG--DTLFTIA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 232 KSDTVRVDFsmtglDYLKSKARNVNLGQKdttrtwepyITITLPdnsPYPQR---GIVDFADPQVDPQTGTFSVRAEMPN 308
Cdd:pfam16576 141 DLSTVWVEA-----DVPEQDLALVKVGQP---------AEVTLP---ALPGKtfeGKVDYIYPTLDPKTRTVRVRIELPN 203
|
250
....*....|
gi 2436919897 309 PEHILLPGQF 318
Cdd:pfam16576 204 PDGRLKPGMF 213
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
26-386 |
7.73e-18 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 84.44 E-value: 7.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 26 IRRISLRVWLYVGAGILLLSGGLYWLLRPAPpgpdLPIVEVEPVVTDDVEIYGEYVGRIRAQQFVEIRARVEGFLEKMLF 105
Cdd:PRK11578 2 KKRKKVKKRYLIALVIVLAGGITLWRILNAP----VPTYQTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 106 DEGTYVKKGQPLFIIDPKQYQARANKAKA---QLNKNKALAlKAERDLERIRPLYQQN-----AASQLDLDNAIASYESA 177
Cdd:PRK11578 78 AIGDKVKKDQLLGVIDPEQAENQIKEVEAtlmELRAQRQQA-EAELKLARVTLSRQQRlaktqAVSQQDLDTAATELAVK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 178 KAEVEM-------SEADLTQAETALGYTTVSSPISGYIsernVDIGTLvgpGGQSLLA--------TVVKSDTVRVDFSM 242
Cdd:PRK11578 157 QAQIGTidaqikrNQASLDTAKTNLDYTRIVAPMAGEV----TQITTL---QGQTVIAaqqapnilTLADMSTMLVKAQV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 243 TGLD--YLKS--KARNVNLGQKDTTrtwepyITITLPDNSPYPQRgIVD--FadpqvdpqtgtFSVRAEMPNPEHILLPG 316
Cdd:PRK11578 230 SEADviHLKPgqKAWFTVLGDPLTR------YEGVLKDILPTPEK-VNDaiF-----------YYARFEVPNPNGLLRLD 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2436919897 317 QFTKVRLLLDVREAAVVVPNKAIAIEKGGA-YIFVVRADSIAERRMVELGPEVGNNVIIERGLVPHENIVV 386
Cdd:PRK11578 292 MTAQVHIQLTDVKNVLTIPLSALGDPVGDNrYKVKLLRNGETREREVTIGARNDTDVEIVKGLEAGDEVII 362
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
90-223 |
2.11e-16 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 79.62 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 90 VEIRA-----RVEGFLEKMLFDEGTYVKKGQPLFIIDPKQY-----QARAN---------------------KAKAQLNK 138
Cdd:PRK03598 39 VDIRTvnlgfRVGGRLASLAVDEGDAVKAGQVLGELDAAPYenalmQAKANvsvaqaqldlmlagyrdeeiaQARAAVKQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 139 NKALALKAERDLERIRPLYQQNAASQLDLDNAIAS-----------------YES---------AKAEVEMSEADLTQAE 192
Cdd:PRK03598 119 AQAAYDYAQNFYNRQQGLWKSRTISANDLENARSSrdqaqatlksaqdklsqYREgnrpqdiaqAKASLAQAQAALAQAE 198
|
170 180 190
....*....|....*....|....*....|.
gi 2436919897 193 TALGYTTVSSPISGYISERNVDIGTLVGPGG 223
Cdd:PRK03598 199 LNLQDTELIAPSDGTILTRAVEPGTMLNAGS 229
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
19-235 |
7.80e-14 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 71.98 E-value: 7.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 19 ALRLSEKIRRISLRVWLYVGAGILLLsGGLYWLLRPAPpgpdlpivevepvVTDDVEIYGEyvgriraqqFVEIRARVEG 98
Cdd:PRK10476 1 MESTPKKSPRKKLPALAIVALAIVAL-VFVIWRTDSAP-------------STDDAYIDAD---------VVHVASEVGG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 99 FLEKMLFDEGTYVKKGQPLFIIDPKQYQARANKAKAQLN----------------------------KNKALALKAERDL 150
Cdd:PRK10476 58 RIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLAladaqimttqrsvdaersnaasaneqveRARANAKLATRTL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 151 ERIRPLYQQNAASQLDLDNA------------------------IASYESAKAEVEMSEADLTQAETALGYTTVSSPISG 206
Cdd:PRK10476 138 ERLEPLLAKGYVSAQQVDQArtaqrdaevslnqallqaqaaaaaVGGVDALVAQRAAREAALAIAELHLEDTTVRAPFDG 217
|
250 260
....*....|....*....|....*....
gi 2436919897 207 YISERNVDIGTLVGPgGQSLLaTVVKSDT 235
Cdd:PRK10476 218 RVVGLKVSVGEFAAP-MQPIF-TLIDTDH 244
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
90-262 |
1.80e-13 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 71.26 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 90 VEIRARVEGFLEKMLFDEGTYVKKGQPLF----------------------------IIDPKQYQARANKAKAQLNknka 141
Cdd:PRK15136 62 VQIMSQVSGSVTKVWADNTDFVKEGDVLVtldptdaeqafekaktalansvrqthqlMINSKQYQANIELQKTALA---- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 142 lalKAERDLERIRPLYQQN--------------AASQLDLDNAIASYESAKA-----------EVEMSEADLTQAETALG 196
Cdd:PRK15136 138 ---QAQSDLNRRVPLGNANligreelqhardavASAQAQLDVAIQQYNANQAmilntpledqpAVQQAATEVRNAWLALQ 214
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2436919897 197 YTTVSSPISGYISERNVDIGTLVGPGgqSLLATVVKSDTVRVD--FSMTGLdylkskaRNVNLGQKDT 262
Cdd:PRK15136 215 RTKIVSPMTGYVSRRSVQVGAQISPT--TPLMAVVPATNLWVDanFKETQL-------ANMRIGQPAT 273
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
90-238 |
5.30e-09 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 57.06 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 90 VEIRARVEGFLEKMLFDEGTYVKKGQPLFIIDPKQYQARANKAKAQLNKNKALALKAERDLERIRPLYQQnAASQLDLDN 169
Cdd:PRK10559 48 VAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNRLGVQ-AMSREEIDQ 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2436919897 170 AIASYESAKAEVEMSEADLTQAETALGYTTVSSPISGYISERNVDIGTLVGPGgqSLLATVVKSDTVRV 238
Cdd:PRK10559 127 ANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRG--STAVALVKQNSFYV 193
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
90-137 |
3.91e-07 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 46.28 E-value: 3.91e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2436919897 90 VEIRARVEGFLEKMLFDEGTYVKKGQPLFIIDPKQYQARANKAKAQLN 137
Cdd:pfam13533 3 VKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
199-316 |
2.21e-06 |
|
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: 45.82 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 199 TVSSPISGYISERNVDIGTLVGPGgqSLLATVVKSDTVRVDFSMTGLDylkskARNVNLGQKdttrtwepyITITLPDNS 278
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAG--DPLATIVPPDRLLVEAFVPAAD-----LGSLKKGQK---------VTLKLDPGS 64
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2436919897 279 PYPQRGIVDFADPQVDPQTGTFSVRAEMPNPEH--ILLPG 316
Cdd:pfam13437 65 DYTLEGKVVRISPTVDPDTGVIPVRVSIENPKTpiPLLPG 104
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
123-199 |
1.00e-04 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 42.89 E-value: 1.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2436919897 123 KQYQARANKAKAQLNKNKALALKAERDLERIRPLYQQNAASQLDLDNAIASYESAKAEVEMSEADLTQAETALGYTT 199
Cdd:pfam02321 104 AQAYLQLLAAKEQLELAEQALELAEEALELAEARYEAGLISLLDVLQAEVELLEARLELLNAEADLELALAQLEQLL 180
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
125-195 |
6.91e-04 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 41.56 E-value: 6.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2436919897 125 YQARANKAKAQLNKnKALALkAERDLERIRPLYQQNAASQLDLDNAIASYESAKAEVEMSEADLTQAETAL 195
Cdd:COG1538 83 FDLLAAQEQLALAE-ENLAL-AEELLELARARYEAGLASRLDVLQAEAQLAQARAQLAQAEAQLAQARNAL 151
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
90-205 |
8.27e-03 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 38.12 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2436919897 90 VEIRARVEGFLEKMLFDEGTYVKKGQPLFIID------PKQYQARANKAKAQLNKNKALALKAErdlerirplyqqnaAS 163
Cdd:PTZ00144 88 VDIRAPASGVITKIFAEEGDTVEVGAPLSEIDtggappAAAPAAAAAAKAEKTTPEKPKAAAPT--------------PE 153
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2436919897 164 QLDLDNAIASYESAKAEVEMSEADLTQAETALGYTTVSSPIS 205
Cdd:PTZ00144 154 PPAASKPTPPAAAKPPEPAPAAKPPPTPVARADPRETRVPMS 195
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
53-121 |
8.90e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 34.99 E-value: 8.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2436919897 53 RPAPPGPdlPIVEV-EPVVTDDVeiygeyVGRIRA-QQFVEIRARVEGFLEKMLFDEGTYVKKGQPLFIID 121
Cdd:PRK07051 17 RPSPDAP--PYVEVgDAVAAGDV------VGLIEVmKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
|
|
| |
